---
_id: '8592'
abstract:
- lang: eng
text: Glioblastoma is the most malignant cancer in the brain and currently incurable.
It is urgent to identify effective targets for this lethal disease. Inhibition
of such targets should suppress the growth of cancer cells and, ideally also precancerous
cells for early prevention, but minimally affect their normal counterparts. Using
genetic mouse models with neural stem cells (NSCs) or oligodendrocyte precursor
cells (OPCs) as the cells‐of‐origin/mutation, it is shown that the susceptibility
of cells within the development hierarchy of glioma to the knockout of insulin‐like
growth factor I receptor (IGF1R) is determined not only by their oncogenic states,
but also by their cell identities/states. Knockout of IGF1R selectively disrupts
the growth of mutant and transformed, but not normal OPCs, or NSCs. The desirable
outcome of IGF1R knockout on cell growth requires the mutant cells to commit to
the OPC identity regardless of its development hierarchical status. At the molecular
level, oncogenic mutations reprogram the cellular network of OPCs and force them
to depend more on IGF1R for their growth. A new‐generation brain‐penetrable, orally
available IGF1R inhibitor harnessing tumor OPCs in the brain is also developed.
The findings reveal the cellular window of IGF1R targeting and establish IGF1R
as an effective target for the prevention and treatment of glioblastoma.
acknowledgement: The authors thank Drs. J. Eisen, QR. Lu, S. Duan, Z‐H. Li, W. Mo,
and Q. Wu for their critical comments on the manuscript. They also thank Dr. H.
Zong for providing the CKO_NG2‐CreER model. This work is supported by the National
Key Research and Development Program of China, Stem Cell and Translational Research
(2016YFA0101201 to C.L., 2016YFA0100303 to Y.J.W.), the National Natural Science
Foundation of China (81673035 and 81972915 to C.L., 81472722 to Y.J.W.), the Science
Foundation for Distinguished Young Scientists of Zhejiang Province (LR17H160001
to C.L.), Fundamental Research Funds for the Central Universities (2016QNA7023 and
2017QNA7028 to C.L.) and the Thousand Talent Program for Young Outstanding Scientists,
China (to C.L.), IST Austria institutional funds (to S.H.), European Research Council
(ERC) under the European Union's Horizon 2020 research and innovation programme
(725780 LinPro to S.H.). C.L. is a scholar of K. C. Wong Education Foundation.
article_number: '2001724'
article_processing_charge: No
article_type: original
author:
- first_name: Anhao
full_name: Tian, Anhao
last_name: Tian
- first_name: Bo
full_name: Kang, Bo
last_name: Kang
- first_name: Baizhou
full_name: Li, Baizhou
last_name: Li
- first_name: Biying
full_name: Qiu, Biying
last_name: Qiu
- first_name: Wenhong
full_name: Jiang, Wenhong
last_name: Jiang
- first_name: Fangjie
full_name: Shao, Fangjie
last_name: Shao
- first_name: Qingqing
full_name: Gao, Qingqing
last_name: Gao
- first_name: Rui
full_name: Liu, Rui
last_name: Liu
- first_name: Chengwei
full_name: Cai, Chengwei
last_name: Cai
- first_name: Rui
full_name: Jing, Rui
last_name: Jing
- first_name: Wei
full_name: Wang, Wei
last_name: Wang
- first_name: Pengxiang
full_name: Chen, Pengxiang
last_name: Chen
- first_name: Qinghui
full_name: Liang, Qinghui
last_name: Liang
- first_name: Lili
full_name: Bao, Lili
last_name: Bao
- first_name: Jianghong
full_name: Man, Jianghong
last_name: Man
- first_name: Yan
full_name: Wang, Yan
last_name: Wang
- first_name: Yu
full_name: Shi, Yu
last_name: Shi
- first_name: Jin
full_name: Li, Jin
last_name: Li
- first_name: Minmin
full_name: Yang, Minmin
last_name: Yang
- first_name: Lisha
full_name: Wang, Lisha
last_name: Wang
- first_name: Jianmin
full_name: Zhang, Jianmin
last_name: Zhang
- first_name: Simon
full_name: Hippenmeyer, Simon
id: 37B36620-F248-11E8-B48F-1D18A9856A87
last_name: Hippenmeyer
orcid: 0000-0003-2279-1061
- first_name: Junming
full_name: Zhu, Junming
last_name: Zhu
- first_name: Xiuwu
full_name: Bian, Xiuwu
last_name: Bian
- first_name: Ying‐Jie
full_name: Wang, Ying‐Jie
last_name: Wang
- first_name: Chong
full_name: Liu, Chong
last_name: Liu
citation:
ama: Tian A, Kang B, Li B, et al. Oncogenic state and cell identity combinatorially
dictate the susceptibility of cells within glioma development hierarchy to IGF1R
targeting. Advanced Science. 2020;7(21). doi:10.1002/advs.202001724
apa: Tian, A., Kang, B., Li, B., Qiu, B., Jiang, W., Shao, F., … Liu, C. (2020).
Oncogenic state and cell identity combinatorially dictate the susceptibility of
cells within glioma development hierarchy to IGF1R targeting. Advanced Science.
Wiley. https://doi.org/10.1002/advs.202001724
chicago: Tian, Anhao, Bo Kang, Baizhou Li, Biying Qiu, Wenhong Jiang, Fangjie Shao,
Qingqing Gao, et al. “Oncogenic State and Cell Identity Combinatorially Dictate
the Susceptibility of Cells within Glioma Development Hierarchy to IGF1R Targeting.”
Advanced Science. Wiley, 2020. https://doi.org/10.1002/advs.202001724.
ieee: A. Tian et al., “Oncogenic state and cell identity combinatorially
dictate the susceptibility of cells within glioma development hierarchy to IGF1R
targeting,” Advanced Science, vol. 7, no. 21. Wiley, 2020.
ista: Tian A, Kang B, Li B, Qiu B, Jiang W, Shao F, Gao Q, Liu R, Cai C, Jing R,
Wang W, Chen P, Liang Q, Bao L, Man J, Wang Y, Shi Y, Li J, Yang M, Wang L, Zhang
J, Hippenmeyer S, Zhu J, Bian X, Wang Y, Liu C. 2020. Oncogenic state and cell
identity combinatorially dictate the susceptibility of cells within glioma development
hierarchy to IGF1R targeting. Advanced Science. 7(21), 2001724.
mla: Tian, Anhao, et al. “Oncogenic State and Cell Identity Combinatorially Dictate
the Susceptibility of Cells within Glioma Development Hierarchy to IGF1R Targeting.”
Advanced Science, vol. 7, no. 21, 2001724, Wiley, 2020, doi:10.1002/advs.202001724.
short: A. Tian, B. Kang, B. Li, B. Qiu, W. Jiang, F. Shao, Q. Gao, R. Liu, C. Cai,
R. Jing, W. Wang, P. Chen, Q. Liang, L. Bao, J. Man, Y. Wang, Y. Shi, J. Li, M.
Yang, L. Wang, J. Zhang, S. Hippenmeyer, J. Zhu, X. Bian, Y. Wang, C. Liu, Advanced
Science 7 (2020).
date_created: 2020-10-01T09:44:13Z
date_published: 2020-11-04T00:00:00Z
date_updated: 2023-08-22T09:53:01Z
day: '04'
ddc:
- '570'
department:
- _id: SiHi
doi: 10.1002/advs.202001724
ec_funded: 1
external_id:
isi:
- '000573860700001'
file:
- access_level: open_access
checksum: 92818c23ecc70e35acfa671f3cfb9909
content_type: application/pdf
creator: dernst
date_created: 2020-12-10T14:07:24Z
date_updated: 2020-12-10T14:07:24Z
file_id: '8938'
file_name: 2020_AdvScience_Tian.pdf
file_size: 7835833
relation: main_file
success: 1
file_date_updated: 2020-12-10T14:07:24Z
has_accepted_license: '1'
intvolume: ' 7'
isi: 1
issue: '21'
keyword:
- General Engineering
- General Physics and Astronomy
- General Materials Science
- Medicine (miscellaneous)
- General Chemical Engineering
- Biochemistry
- Genetics and Molecular Biology (miscellaneous)
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
project:
- _id: 260018B0-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '725780'
name: Principles of Neural Stem Cell Lineage Progression in Cerebral Cortex Development
publication: Advanced Science
publication_identifier:
issn:
- 2198-3844
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Oncogenic state and cell identity combinatorially dictate the susceptibility
of cells within glioma development hierarchy to IGF1R targeting
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 7
year: '2020'
...
---
_id: '8744'
abstract:
- lang: eng
text: Understanding the conformational sampling of translation-arrested ribosome
nascent chain complexes is key to understand co-translational folding. Up to now,
coupling of cysteine oxidation, disulfide bond formation and structure formation
in nascent chains has remained elusive. Here, we investigate the eye-lens protein
γB-crystallin in the ribosomal exit tunnel. Using mass spectrometry, theoretical
simulations, dynamic nuclear polarization-enhanced solid-state nuclear magnetic
resonance and cryo-electron microscopy, we show that thiol groups of cysteine
residues undergo S-glutathionylation and S-nitrosylation and form non-native disulfide
bonds. Thus, covalent modification chemistry occurs already prior to nascent chain
release as the ribosome exit tunnel provides sufficient space even for disulfide
bond formation which can guide protein folding.
acknowledgement: 'We acknowledge help from Anja Seybert, Margot Frangakis, Diana Grewe,
Mikhail Eltsov, Utz Ermel, and Shintaro Aibara. The work was supported by Deutsche
Forschungsgemeinschaft in the CLiC graduate school. Work at the Center for Biomolecular
Magnetic Resonance (BMRZ) is supported by the German state of Hesse. The work at
BMRZ has been supported by the state of Hesse. L.S. has been supported by the DFG
graduate college: CLiC.'
article_number: '5569'
article_processing_charge: No
article_type: original
author:
- first_name: Linda
full_name: Schulte, Linda
last_name: Schulte
- first_name: Jiafei
full_name: Mao, Jiafei
last_name: Mao
- first_name: Julian
full_name: Reitz, Julian
last_name: Reitz
- first_name: Sridhar
full_name: Sreeramulu, Sridhar
last_name: Sreeramulu
- first_name: Denis
full_name: Kudlinzki, Denis
last_name: Kudlinzki
- first_name: Victor-Valentin
full_name: Hodirnau, Victor-Valentin
id: 3661B498-F248-11E8-B48F-1D18A9856A87
last_name: Hodirnau
- first_name: Jakob
full_name: Meier-Credo, Jakob
last_name: Meier-Credo
- first_name: Krishna
full_name: Saxena, Krishna
last_name: Saxena
- first_name: Florian
full_name: Buhr, Florian
last_name: Buhr
- first_name: Julian D.
full_name: Langer, Julian D.
last_name: Langer
- first_name: Martin
full_name: Blackledge, Martin
last_name: Blackledge
- first_name: Achilleas S.
full_name: Frangakis, Achilleas S.
last_name: Frangakis
- first_name: Clemens
full_name: Glaubitz, Clemens
last_name: Glaubitz
- first_name: Harald
full_name: Schwalbe, Harald
last_name: Schwalbe
citation:
ama: Schulte L, Mao J, Reitz J, et al. Cysteine oxidation and disulfide formation
in the ribosomal exit tunnel. Nature Communications. 2020;11. doi:10.1038/s41467-020-19372-x
apa: Schulte, L., Mao, J., Reitz, J., Sreeramulu, S., Kudlinzki, D., Hodirnau, V.-V.,
… Schwalbe, H. (2020). Cysteine oxidation and disulfide formation in the ribosomal
exit tunnel. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-020-19372-x
chicago: Schulte, Linda, Jiafei Mao, Julian Reitz, Sridhar Sreeramulu, Denis Kudlinzki,
Victor-Valentin Hodirnau, Jakob Meier-Credo, et al. “Cysteine Oxidation and Disulfide
Formation in the Ribosomal Exit Tunnel.” Nature Communications. Springer
Nature, 2020. https://doi.org/10.1038/s41467-020-19372-x.
ieee: L. Schulte et al., “Cysteine oxidation and disulfide formation in the
ribosomal exit tunnel,” Nature Communications, vol. 11. Springer Nature,
2020.
ista: Schulte L, Mao J, Reitz J, Sreeramulu S, Kudlinzki D, Hodirnau V-V, Meier-Credo
J, Saxena K, Buhr F, Langer JD, Blackledge M, Frangakis AS, Glaubitz C, Schwalbe
H. 2020. Cysteine oxidation and disulfide formation in the ribosomal exit tunnel.
Nature Communications. 11, 5569.
mla: Schulte, Linda, et al. “Cysteine Oxidation and Disulfide Formation in the Ribosomal
Exit Tunnel.” Nature Communications, vol. 11, 5569, Springer Nature, 2020,
doi:10.1038/s41467-020-19372-x.
short: L. Schulte, J. Mao, J. Reitz, S. Sreeramulu, D. Kudlinzki, V.-V. Hodirnau,
J. Meier-Credo, K. Saxena, F. Buhr, J.D. Langer, M. Blackledge, A.S. Frangakis,
C. Glaubitz, H. Schwalbe, Nature Communications 11 (2020).
date_created: 2020-11-09T07:49:36Z
date_published: 2020-11-04T00:00:00Z
date_updated: 2023-08-22T12:36:07Z
day: '04'
ddc:
- '570'
department:
- _id: EM-Fac
doi: 10.1038/s41467-020-19372-x
external_id:
isi:
- '000592028600001'
file:
- access_level: open_access
checksum: b2688f0347e69e6629bba582077278c5
content_type: application/pdf
creator: dernst
date_created: 2020-11-09T07:56:24Z
date_updated: 2020-11-09T07:56:24Z
file_id: '8745'
file_name: 2020_NatureComm_Schulte.pdf
file_size: 1670898
relation: main_file
success: 1
file_date_updated: 2020-11-09T07:56:24Z
has_accepted_license: '1'
intvolume: ' 11'
isi: 1
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cysteine oxidation and disulfide formation in the ribosomal exit tunnel
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 11
year: '2020'
...
---
_id: '8971'
abstract:
- lang: eng
text: The actin-related protein (Arp)2/3 complex nucleates branched actin filament
networks pivotal for cell migration, endocytosis and pathogen infection. Its activation
is tightly regulated and involves complex structural rearrangements and actin
filament binding, which are yet to be understood. Here, we report a 9.0 Å resolution
structure of the actin filament Arp2/3 complex branch junction in cells using
cryo-electron tomography and subtomogram averaging. This allows us to generate
an accurate model of the active Arp2/3 complex in the branch junction and its
interaction with actin filaments. Notably, our model reveals a previously undescribed
set of interactions of the Arp2/3 complex with the mother filament, significantly
different to the previous branch junction model. Our structure also indicates
a central role for the ArpC3 subunit in stabilizing the active conformation.
acknowledged_ssus:
- _id: ScienComp
- _id: LifeSc
- _id: Bio
- _id: EM-Fac
acknowledgement: "This research was supported by the Scientific Service Units (SSUs)
of IST Austria through resources provided by Scientific Computing (SciComp), the
Life Science Facility (LSF), the BioImaging Facility (BIF), and the Electron Microscopy
Facility (EMF). We also thank Dimitry Tegunov (MPI for Biophysical Chemistry) for
helpful discussions\r\nabout the M software, and Michael Sixt (IST Austria) and
Klemens Rottner (Technical University Braunschweig, HZI Braunschweig) for critical
reading of the manuscript. We also thank Gregory Voth (University of Chicago) for
providing us the MD-derived branch junction model for comparison. The authors acknowledge
support from IST Austria and from the Austrian Science Fund (FWF): M02495 to G.D.
and Austrian Science Fund (FWF): P33367 to F.K.M.S. "
article_number: '6437'
article_processing_charge: No
article_type: original
author:
- first_name: Florian
full_name: Fäßler, Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- first_name: Georgi A
full_name: Dimchev, Georgi A
id: 38C393BE-F248-11E8-B48F-1D18A9856A87
last_name: Dimchev
orcid: 0000-0001-8370-6161
- first_name: Victor-Valentin
full_name: Hodirnau, Victor-Valentin
id: 3661B498-F248-11E8-B48F-1D18A9856A87
last_name: Hodirnau
- first_name: William
full_name: Wan, William
last_name: Wan
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Fäßler F, Dimchev GA, Hodirnau V-V, Wan W, Schur FK. Cryo-electron tomography
structure of Arp2/3 complex in cells reveals new insights into the branch junction.
Nature Communications. 2020;11. doi:10.1038/s41467-020-20286-x
apa: Fäßler, F., Dimchev, G. A., Hodirnau, V.-V., Wan, W., & Schur, F. K. (2020).
Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights
into the branch junction. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-020-20286-x
chicago: Fäßler, Florian, Georgi A Dimchev, Victor-Valentin Hodirnau, William Wan,
and Florian KM Schur. “Cryo-Electron Tomography Structure of Arp2/3 Complex in
Cells Reveals New Insights into the Branch Junction.” Nature Communications.
Springer Nature, 2020. https://doi.org/10.1038/s41467-020-20286-x.
ieee: F. Fäßler, G. A. Dimchev, V.-V. Hodirnau, W. Wan, and F. K. Schur, “Cryo-electron
tomography structure of Arp2/3 complex in cells reveals new insights into the
branch junction,” Nature Communications, vol. 11. Springer Nature, 2020.
ista: Fäßler F, Dimchev GA, Hodirnau V-V, Wan W, Schur FK. 2020. Cryo-electron tomography
structure of Arp2/3 complex in cells reveals new insights into the branch junction.
Nature Communications. 11, 6437.
mla: Fäßler, Florian, et al. “Cryo-Electron Tomography Structure of Arp2/3 Complex
in Cells Reveals New Insights into the Branch Junction.” Nature Communications,
vol. 11, 6437, Springer Nature, 2020, doi:10.1038/s41467-020-20286-x.
short: F. Fäßler, G.A. Dimchev, V.-V. Hodirnau, W. Wan, F.K. Schur, Nature Communications
11 (2020).
date_created: 2020-12-23T08:25:45Z
date_published: 2020-12-22T00:00:00Z
date_updated: 2023-08-24T11:01:50Z
day: '22'
ddc:
- '570'
department:
- _id: FlSc
- _id: EM-Fac
doi: 10.1038/s41467-020-20286-x
external_id:
isi:
- '000603078000003'
file:
- access_level: open_access
checksum: 55d43ea0061cc4027ba45e966e1db8cc
content_type: application/pdf
creator: dernst
date_created: 2020-12-28T08:16:10Z
date_updated: 2020-12-28T08:16:10Z
file_id: '8975'
file_name: 2020_NatureComm_Faessler.pdf
file_size: 3958727
relation: main_file
success: 1
file_date_updated: 2020-12-28T08:16:10Z
has_accepted_license: '1'
intvolume: ' 11'
isi: 1
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
project:
- _id: 9B954C5C-BA93-11EA-9121-9846C619BF3A
grant_number: P33367
name: Structure and isoform diversity of the Arp2/3 complex
- _id: 2674F658-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: M02495
name: Protein structure and function in filopodia across scales
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- description: News on IST Homepage
relation: press_release
url: https://ist.ac.at/en/news/cutting-edge-technology-reveals-structures-within-cells/
scopus_import: '1'
status: public
title: Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights
into the branch junction
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 11
year: '2020'
...
---
_id: '13362'
abstract:
- lang: eng
text: Aggregation of organic molecules can drastically affect their physicochemical
properties. For instance, the optical properties of BODIPY dyes are inherently
related to the degree of aggregation and the mutual orientation of BODIPY units
within these aggregates. Whereas the noncovalent aggregation of various BODIPY
dyes has been studied in diverse media, the ill-defined nature of these aggregates
has made it difficult to elucidate the structure–property relationships. Here,
we studied the encapsulation of three structurally simple BODIPY derivatives within
the hydrophobic cavity of a water-soluble, flexible PdII6L4 coordination cage.
The cavity size allowed for the selective encapsulation of two dye molecules,
irrespective of the substitution pattern on the BODIPY core. Working with a model,
a pentamethyl-substituted derivative, we found that the mutual orientation of
two BODIPY units in the cage’s cavity was remarkably similar to that in the crystalline
state of the free dye, allowing us to isolate and characterize the smallest possible
noncovalent H-type BODIPY aggregate, namely, an H-dimer. Interestingly, a CF3-substituted
BODIPY, known for forming J-type aggregates, was also encapsulated as an H-dimer.
Taking advantage of the dynamic nature of encapsulation, we developed a system
in which reversible switching between H- and J-aggregates can be induced for multiple
cycles simply by addition and subsequent destruction of the cage. We expect that
the ability to rapidly and reversibly manipulate the optical properties of supramolecular
inclusion complexes in aqueous media will open up avenues for developing detection
systems that operate within biological environments.
article_processing_charge: No
article_type: original
author:
- first_name: Julius
full_name: Gemen, Julius
last_name: Gemen
- first_name: Johannes
full_name: Ahrens, Johannes
last_name: Ahrens
- first_name: Linda J. W.
full_name: Shimon, Linda J. W.
last_name: Shimon
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Gemen J, Ahrens J, Shimon LJW, Klajn R. Modulating the optical properties of
BODIPY dyes by noncovalent dimerization within a flexible coordination cage. Journal
of the American Chemical Society. 2020;142(41):17721-17729. doi:10.1021/jacs.0c08589
apa: Gemen, J., Ahrens, J., Shimon, L. J. W., & Klajn, R. (2020). Modulating
the optical properties of BODIPY dyes by noncovalent dimerization within a flexible
coordination cage. Journal of the American Chemical Society. American Chemical
Society. https://doi.org/10.1021/jacs.0c08589
chicago: Gemen, Julius, Johannes Ahrens, Linda J. W. Shimon, and Rafal Klajn. “Modulating
the Optical Properties of BODIPY Dyes by Noncovalent Dimerization within a Flexible
Coordination Cage.” Journal of the American Chemical Society. American
Chemical Society, 2020. https://doi.org/10.1021/jacs.0c08589.
ieee: J. Gemen, J. Ahrens, L. J. W. Shimon, and R. Klajn, “Modulating the optical
properties of BODIPY dyes by noncovalent dimerization within a flexible coordination
cage,” Journal of the American Chemical Society, vol. 142, no. 41. American
Chemical Society, pp. 17721–17729, 2020.
ista: Gemen J, Ahrens J, Shimon LJW, Klajn R. 2020. Modulating the optical properties
of BODIPY dyes by noncovalent dimerization within a flexible coordination cage.
Journal of the American Chemical Society. 142(41), 17721–17729.
mla: Gemen, Julius, et al. “Modulating the Optical Properties of BODIPY Dyes by
Noncovalent Dimerization within a Flexible Coordination Cage.” Journal of the
American Chemical Society, vol. 142, no. 41, American Chemical Society, 2020,
pp. 17721–29, doi:10.1021/jacs.0c08589.
short: J. Gemen, J. Ahrens, L.J.W. Shimon, R. Klajn, Journal of the American Chemical
Society 142 (2020) 17721–17729.
date_created: 2023-08-01T09:36:10Z
date_published: 2020-10-04T00:00:00Z
date_updated: 2023-08-07T10:09:54Z
day: '04'
doi: 10.1021/jacs.0c08589
extern: '1'
external_id:
pmid:
- '33006898'
intvolume: ' 142'
issue: '41'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1021/jacs.0c08589
month: '10'
oa: 1
oa_version: Published Version
page: 17721-17729
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Modulating the optical properties of BODIPY dyes by noncovalent dimerization
within a flexible coordination cage
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 142
year: '2020'
...
---
_id: '13364'
abstract:
- lang: eng
text: Photochromic molecules undergo reversible isomerization upon irradiation with
light at different wavelengths, a process that can alter their physical and chemical
properties. For instance, dihydropyrene (DHP) is a deep-colored compound that
isomerizes to light-brown cyclophanediene (CPD) upon irradiation with visible
light. CPD can then isomerize back to DHP upon irradiation with UV light or thermally
in the dark. Conversion between DHP and CPD is thought to proceed via a biradical
intermediate; bimolecular events involving this unstable intermediate thus result
in rapid decomposition and poor cycling performance. Here, we show that the reversible
isomerization of DHP can be stabilized upon confinement within a PdII6L4 coordination
cage. By protecting this reactive intermediate using the cage, each isomerization
reaction proceeds to higher yield, which significantly decreases the fatigue experienced
by the system upon repeated photocycling. Although molecular confinement is known
to help stabilize reactive species, this effect is not typically employed to protect
reactive intermediates and thus improve reaction yields. We envisage that performing
reactions under confinement will not only improve the cyclic performance of photochromic
molecules, but may also increase the amount of product obtainable from traditionally
low-yielding organic reactions.
article_processing_charge: No
article_type: original
author:
- first_name: Martina
full_name: Canton, Martina
last_name: Canton
- first_name: Angela B.
full_name: Grommet, Angela B.
last_name: Grommet
- first_name: Luca
full_name: Pesce, Luca
last_name: Pesce
- first_name: Julius
full_name: Gemen, Julius
last_name: Gemen
- first_name: Shiming
full_name: Li, Shiming
last_name: Li
- first_name: Yael
full_name: Diskin-Posner, Yael
last_name: Diskin-Posner
- first_name: Alberto
full_name: Credi, Alberto
last_name: Credi
- first_name: Giovanni M.
full_name: Pavan, Giovanni M.
last_name: Pavan
- first_name: Joakim
full_name: Andréasson, Joakim
last_name: Andréasson
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Canton M, Grommet AB, Pesce L, et al. Improving fatigue resistance of dihydropyrene
by encapsulation within a coordination cage. Journal of the American Chemical
Society. 2020;142(34):14557-14565. doi:10.1021/jacs.0c06146
apa: Canton, M., Grommet, A. B., Pesce, L., Gemen, J., Li, S., Diskin-Posner, Y.,
… Klajn, R. (2020). Improving fatigue resistance of dihydropyrene by encapsulation
within a coordination cage. Journal of the American Chemical Society. American
Chemical Society. https://doi.org/10.1021/jacs.0c06146
chicago: Canton, Martina, Angela B. Grommet, Luca Pesce, Julius Gemen, Shiming Li,
Yael Diskin-Posner, Alberto Credi, Giovanni M. Pavan, Joakim Andréasson, and Rafal
Klajn. “Improving Fatigue Resistance of Dihydropyrene by Encapsulation within
a Coordination Cage.” Journal of the American Chemical Society. American
Chemical Society, 2020. https://doi.org/10.1021/jacs.0c06146.
ieee: M. Canton et al., “Improving fatigue resistance of dihydropyrene by
encapsulation within a coordination cage,” Journal of the American Chemical
Society, vol. 142, no. 34. American Chemical Society, pp. 14557–14565, 2020.
ista: Canton M, Grommet AB, Pesce L, Gemen J, Li S, Diskin-Posner Y, Credi A, Pavan
GM, Andréasson J, Klajn R. 2020. Improving fatigue resistance of dihydropyrene
by encapsulation within a coordination cage. Journal of the American Chemical
Society. 142(34), 14557–14565.
mla: Canton, Martina, et al. “Improving Fatigue Resistance of Dihydropyrene by Encapsulation
within a Coordination Cage.” Journal of the American Chemical Society,
vol. 142, no. 34, American Chemical Society, 2020, pp. 14557–65, doi:10.1021/jacs.0c06146.
short: M. Canton, A.B. Grommet, L. Pesce, J. Gemen, S. Li, Y. Diskin-Posner, A.
Credi, G.M. Pavan, J. Andréasson, R. Klajn, Journal of the American Chemical Society
142 (2020) 14557–14565.
date_created: 2023-08-01T09:36:59Z
date_published: 2020-08-14T00:00:00Z
date_updated: 2023-08-07T10:15:38Z
day: '14'
doi: 10.1021/jacs.0c06146
extern: '1'
external_id:
pmid:
- '32791832'
intvolume: ' 142'
issue: '34'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1021/jacs.0c06146
month: '08'
oa: 1
oa_version: Published Version
page: 14557-14565
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Improving fatigue resistance of dihydropyrene by encapsulation within a coordination
cage
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 142
year: '2020'
...
---
_id: '13365'
abstract:
- lang: eng
text: Photoswitchable molecules are employed for many applications, from the development
of active materials to the design of stimuli-responsive molecular systems and
light-powered molecular machines. To fully exploit their potential, we must learn
ways to control the mechanism and kinetics of their photoinduced isomerization.
One possible strategy involves confinement of photoresponsive switches such as
azobenzenes or spiropyrans within crowded molecular environments, which may allow
control over their light-induced conversion. However, the molecular factors that
influence and control the switching process under realistic conditions and within
dynamic molecular regimes often remain difficult to ascertain. As a case study,
here we have employed molecular models to probe the isomerization of azobenzene
guests within a Pd(II)-based coordination cage host in water. Atomistic molecular
dynamics and metadynamics simulations allow us to characterize the flexibility
of the cage in the solvent, the (rare) guest encapsulation and release events,
and the relative probability/kinetics of light-induced isomerization of azobenzene
analogues in these host–guest systems. In this way, we can reconstruct the mechanism
of azobenzene switching inside the cage cavity and explore key molecular factors
that may control this event. We obtain a molecular-level insight on the effects
of crowding and host–guest interactions on azobenzene isomerization. The detailed
picture elucidated by this study may enable the rational design of photoswitchable
systems whose reactivity can be controlled via host–guest interactions.
article_processing_charge: No
article_type: original
author:
- first_name: Luca
full_name: Pesce, Luca
last_name: Pesce
- first_name: Claudio
full_name: Perego, Claudio
last_name: Perego
- first_name: Angela B.
full_name: Grommet, Angela B.
last_name: Grommet
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Giovanni M.
full_name: Pavan, Giovanni M.
last_name: Pavan
citation:
ama: Pesce L, Perego C, Grommet AB, Klajn R, Pavan GM. Molecular factors controlling
the isomerization of Azobenzenes in the cavity of a flexible coordination cage.
Journal of the American Chemical Society. 2020;142(21):9792-9802. doi:10.1021/jacs.0c03444
apa: Pesce, L., Perego, C., Grommet, A. B., Klajn, R., & Pavan, G. M. (2020).
Molecular factors controlling the isomerization of Azobenzenes in the cavity of
a flexible coordination cage. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/jacs.0c03444
chicago: Pesce, Luca, Claudio Perego, Angela B. Grommet, Rafal Klajn, and Giovanni
M. Pavan. “Molecular Factors Controlling the Isomerization of Azobenzenes in the
Cavity of a Flexible Coordination Cage.” Journal of the American Chemical Society.
American Chemical Society, 2020. https://doi.org/10.1021/jacs.0c03444.
ieee: L. Pesce, C. Perego, A. B. Grommet, R. Klajn, and G. M. Pavan, “Molecular
factors controlling the isomerization of Azobenzenes in the cavity of a flexible
coordination cage,” Journal of the American Chemical Society, vol. 142,
no. 21. American Chemical Society, pp. 9792–9802, 2020.
ista: Pesce L, Perego C, Grommet AB, Klajn R, Pavan GM. 2020. Molecular factors
controlling the isomerization of Azobenzenes in the cavity of a flexible coordination
cage. Journal of the American Chemical Society. 142(21), 9792–9802.
mla: Pesce, Luca, et al. “Molecular Factors Controlling the Isomerization of Azobenzenes
in the Cavity of a Flexible Coordination Cage.” Journal of the American Chemical
Society, vol. 142, no. 21, American Chemical Society, 2020, pp. 9792–802,
doi:10.1021/jacs.0c03444.
short: L. Pesce, C. Perego, A.B. Grommet, R. Klajn, G.M. Pavan, Journal of the American
Chemical Society 142 (2020) 9792–9802.
date_created: 2023-08-01T09:37:12Z
date_published: 2020-04-30T00:00:00Z
date_updated: 2023-08-07T10:18:53Z
day: '30'
doi: 10.1021/jacs.0c03444
extern: '1'
external_id:
pmid:
- '32353237'
intvolume: ' 142'
issue: '21'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1021/jacs.0c03444
month: '04'
oa: 1
oa_version: Published Version
page: 9792-9802
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Molecular factors controlling the isomerization of Azobenzenes in the cavity
of a flexible coordination cage
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 142
year: '2020'
...
---
_id: '14125'
abstract:
- lang: eng
text: "Motivation: Recent technological advances have led to an increase in the
production and availability of single-cell data. The ability to integrate a set
of multi-technology measurements would allow the identification of biologically
or clinically meaningful observations through the unification of the perspectives
afforded by each technology. In most cases, however, profiling technologies consume
the used cells and thus pairwise correspondences between datasets are lost. Due
to the sheer size single-cell datasets can acquire, scalable algorithms that are
able to universally match single-cell measurements carried out in one cell to
its corresponding sibling in another technology are needed.\r\nResults: We propose
Single-Cell data Integration via Matching (SCIM), a scalable approach to recover
such correspondences in two or more technologies. SCIM assumes that cells share
a common (low-dimensional) underlying structure and that the underlying cell distribution
is approximately constant across technologies. It constructs a technology-invariant
latent space using an autoencoder framework with an adversarial objective. Multi-modal
datasets are integrated by pairing cells across technologies using a bipartite
matching scheme that operates on the low-dimensional latent representations. We
evaluate SCIM on a simulated cellular branching process and show that the cell-to-cell
matches derived by SCIM reflect the same pseudotime on the simulated dataset.
Moreover, we apply our method to two real-world scenarios, a melanoma tumor sample
and a human bone marrow sample, where we pair cells from a scRNA dataset to their
sibling cells in a CyTOF dataset achieving 90% and 78% cell-matching accuracy
for each one of the samples, respectively."
article_processing_charge: No
article_type: original
author:
- first_name: Stefan G
full_name: Stark, Stefan G
last_name: Stark
- first_name: Joanna
full_name: Ficek, Joanna
last_name: Ficek
- first_name: Francesco
full_name: Locatello, Francesco
id: 26cfd52f-2483-11ee-8040-88983bcc06d4
last_name: Locatello
orcid: 0000-0002-4850-0683
- first_name: Ximena
full_name: Bonilla, Ximena
last_name: Bonilla
- first_name: Stéphane
full_name: Chevrier, Stéphane
last_name: Chevrier
- first_name: Franziska
full_name: Singer, Franziska
last_name: Singer
- first_name: Rudolf
full_name: Aebersold, Rudolf
last_name: Aebersold
- first_name: Faisal S
full_name: Al-Quaddoomi, Faisal S
last_name: Al-Quaddoomi
- first_name: Jonas
full_name: Albinus, Jonas
last_name: Albinus
- first_name: Ilaria
full_name: Alborelli, Ilaria
last_name: Alborelli
- first_name: Sonali
full_name: Andani, Sonali
last_name: Andani
- first_name: Per-Olof
full_name: Attinger, Per-Olof
last_name: Attinger
- first_name: Marina
full_name: Bacac, Marina
last_name: Bacac
- first_name: Daniel
full_name: Baumhoer, Daniel
last_name: Baumhoer
- first_name: Beatrice
full_name: Beck-Schimmer, Beatrice
last_name: Beck-Schimmer
- first_name: Niko
full_name: Beerenwinkel, Niko
last_name: Beerenwinkel
- first_name: Christian
full_name: Beisel, Christian
last_name: Beisel
- first_name: Lara
full_name: Bernasconi, Lara
last_name: Bernasconi
- first_name: Anne
full_name: Bertolini, Anne
last_name: Bertolini
- first_name: Bernd
full_name: Bodenmiller, Bernd
last_name: Bodenmiller
- first_name: Ximena
full_name: Bonilla, Ximena
last_name: Bonilla
- first_name: Ruben
full_name: Casanova, Ruben
last_name: Casanova
- first_name: Stéphane
full_name: Chevrier, Stéphane
last_name: Chevrier
- first_name: Natalia
full_name: Chicherova, Natalia
last_name: Chicherova
- first_name: Maya
full_name: D'Costa, Maya
last_name: D'Costa
- first_name: Esther
full_name: Danenberg, Esther
last_name: Danenberg
- first_name: Natalie
full_name: Davidson, Natalie
last_name: Davidson
- first_name: Monica-Andreea Dră
full_name: gan, Monica-Andreea Dră
last_name: gan
- first_name: Reinhard
full_name: Dummer, Reinhard
last_name: Dummer
- first_name: Stefanie
full_name: Engler, Stefanie
last_name: Engler
- first_name: Martin
full_name: Erkens, Martin
last_name: Erkens
- first_name: Katja
full_name: Eschbach, Katja
last_name: Eschbach
- first_name: Cinzia
full_name: Esposito, Cinzia
last_name: Esposito
- first_name: André
full_name: Fedier, André
last_name: Fedier
- first_name: Pedro
full_name: Ferreira, Pedro
last_name: Ferreira
- first_name: Joanna
full_name: Ficek, Joanna
last_name: Ficek
- first_name: Anja L
full_name: Frei, Anja L
last_name: Frei
- first_name: Bruno
full_name: Frey, Bruno
last_name: Frey
- first_name: Sandra
full_name: Goetze, Sandra
last_name: Goetze
- first_name: Linda
full_name: Grob, Linda
last_name: Grob
- first_name: Gabriele
full_name: Gut, Gabriele
last_name: Gut
- first_name: Detlef
full_name: Günther, Detlef
last_name: Günther
- first_name: Martina
full_name: Haberecker, Martina
last_name: Haberecker
- first_name: Pirmin
full_name: Haeuptle, Pirmin
last_name: Haeuptle
- first_name: Viola
full_name: Heinzelmann-Schwarz, Viola
last_name: Heinzelmann-Schwarz
- first_name: Sylvia
full_name: Herter, Sylvia
last_name: Herter
- first_name: Rene
full_name: Holtackers, Rene
last_name: Holtackers
- first_name: Tamara
full_name: Huesser, Tamara
last_name: Huesser
- first_name: Anja
full_name: Irmisch, Anja
last_name: Irmisch
- first_name: Francis
full_name: Jacob, Francis
last_name: Jacob
- first_name: Andrea
full_name: Jacobs, Andrea
last_name: Jacobs
- first_name: Tim M
full_name: Jaeger, Tim M
last_name: Jaeger
- first_name: Katharina
full_name: Jahn, Katharina
last_name: Jahn
- first_name: Alva R
full_name: James, Alva R
last_name: James
- first_name: Philip M
full_name: Jermann, Philip M
last_name: Jermann
- first_name: André
full_name: Kahles, André
last_name: Kahles
- first_name: Abdullah
full_name: Kahraman, Abdullah
last_name: Kahraman
- first_name: Viktor H
full_name: Koelzer, Viktor H
last_name: Koelzer
- first_name: Werner
full_name: Kuebler, Werner
last_name: Kuebler
- first_name: Jack
full_name: Kuipers, Jack
last_name: Kuipers
- first_name: Christian P
full_name: Kunze, Christian P
last_name: Kunze
- first_name: Christian
full_name: Kurzeder, Christian
last_name: Kurzeder
- first_name: Kjong-Van
full_name: Lehmann, Kjong-Van
last_name: Lehmann
- first_name: Mitchell
full_name: Levesque, Mitchell
last_name: Levesque
- first_name: Sebastian
full_name: Lugert, Sebastian
last_name: Lugert
- first_name: Gerd
full_name: Maass, Gerd
last_name: Maass
- first_name: Markus
full_name: Manz, Markus
last_name: Manz
- first_name: Philipp
full_name: Markolin, Philipp
last_name: Markolin
- first_name: Julien
full_name: Mena, Julien
last_name: Mena
- first_name: Ulrike
full_name: Menzel, Ulrike
last_name: Menzel
- first_name: Julian M
full_name: Metzler, Julian M
last_name: Metzler
- first_name: Nicola
full_name: Miglino, Nicola
last_name: Miglino
- first_name: Emanuela S
full_name: Milani, Emanuela S
last_name: Milani
- first_name: Holger
full_name: Moch, Holger
last_name: Moch
- first_name: Simone
full_name: Muenst, Simone
last_name: Muenst
- first_name: Riccardo
full_name: Murri, Riccardo
last_name: Murri
- first_name: Charlotte KY
full_name: Ng, Charlotte KY
last_name: Ng
- first_name: Stefan
full_name: Nicolet, Stefan
last_name: Nicolet
- first_name: Marta
full_name: Nowak, Marta
last_name: Nowak
- first_name: Patrick GA
full_name: Pedrioli, Patrick GA
last_name: Pedrioli
- first_name: Lucas
full_name: Pelkmans, Lucas
last_name: Pelkmans
- first_name: Salvatore
full_name: Piscuoglio, Salvatore
last_name: Piscuoglio
- first_name: Michael
full_name: Prummer, Michael
last_name: Prummer
- first_name: Mathilde
full_name: Ritter, Mathilde
last_name: Ritter
- first_name: Christian
full_name: Rommel, Christian
last_name: Rommel
- first_name: María L
full_name: Rosano-González, María L
last_name: Rosano-González
- first_name: Gunnar
full_name: Rätsch, Gunnar
last_name: Rätsch
- first_name: Natascha
full_name: Santacroce, Natascha
last_name: Santacroce
- first_name: Jacobo Sarabia del
full_name: Castillo, Jacobo Sarabia del
last_name: Castillo
- first_name: Ramona
full_name: Schlenker, Ramona
last_name: Schlenker
- first_name: Petra C
full_name: Schwalie, Petra C
last_name: Schwalie
- first_name: Severin
full_name: Schwan, Severin
last_name: Schwan
- first_name: Tobias
full_name: Schär, Tobias
last_name: Schär
- first_name: Gabriela
full_name: Senti, Gabriela
last_name: Senti
- first_name: Franziska
full_name: Singer, Franziska
last_name: Singer
- first_name: Sujana
full_name: Sivapatham, Sujana
last_name: Sivapatham
- first_name: Berend
full_name: Snijder, Berend
last_name: Snijder
- first_name: Bettina
full_name: Sobottka, Bettina
last_name: Sobottka
- first_name: Vipin T
full_name: Sreedharan, Vipin T
last_name: Sreedharan
- first_name: Stefan
full_name: Stark, Stefan
last_name: Stark
- first_name: Daniel J
full_name: Stekhoven, Daniel J
last_name: Stekhoven
- first_name: Alexandre PA
full_name: Theocharides, Alexandre PA
last_name: Theocharides
- first_name: Tinu M
full_name: Thomas, Tinu M
last_name: Thomas
- first_name: Markus
full_name: Tolnay, Markus
last_name: Tolnay
- first_name: Vinko
full_name: Tosevski, Vinko
last_name: Tosevski
- first_name: Nora C
full_name: Toussaint, Nora C
last_name: Toussaint
- first_name: Mustafa A
full_name: Tuncel, Mustafa A
last_name: Tuncel
- first_name: Marina
full_name: Tusup, Marina
last_name: Tusup
- first_name: Audrey Van
full_name: Drogen, Audrey Van
last_name: Drogen
- first_name: Marcus
full_name: Vetter, Marcus
last_name: Vetter
- first_name: Tatjana
full_name: Vlajnic, Tatjana
last_name: Vlajnic
- first_name: Sandra
full_name: Weber, Sandra
last_name: Weber
- first_name: Walter P
full_name: Weber, Walter P
last_name: Weber
- first_name: Rebekka
full_name: Wegmann, Rebekka
last_name: Wegmann
- first_name: Michael
full_name: Weller, Michael
last_name: Weller
- first_name: Fabian
full_name: Wendt, Fabian
last_name: Wendt
- first_name: Norbert
full_name: Wey, Norbert
last_name: Wey
- first_name: Andreas
full_name: Wicki, Andreas
last_name: Wicki
- first_name: Bernd
full_name: Wollscheid, Bernd
last_name: Wollscheid
- first_name: Shuqing
full_name: Yu, Shuqing
last_name: Yu
- first_name: Johanna
full_name: Ziegler, Johanna
last_name: Ziegler
- first_name: Marc
full_name: Zimmermann, Marc
last_name: Zimmermann
- first_name: Martin
full_name: Zoche, Martin
last_name: Zoche
- first_name: Gregor
full_name: Zuend, Gregor
last_name: Zuend
- first_name: Gunnar
full_name: Rätsch, Gunnar
last_name: Rätsch
- first_name: Kjong-Van
full_name: Lehmann, Kjong-Van
last_name: Lehmann
citation:
ama: 'Stark SG, Ficek J, Locatello F, et al. SCIM: Universal single-cell matching
with unpaired feature sets. Bioinformatics. 2020;36(Supplement_2):i919-i927.
doi:10.1093/bioinformatics/btaa843'
apa: 'Stark, S. G., Ficek, J., Locatello, F., Bonilla, X., Chevrier, S., Singer,
F., … Lehmann, K.-V. (2020). SCIM: Universal single-cell matching with unpaired
feature sets. Bioinformatics. Oxford University Press. https://doi.org/10.1093/bioinformatics/btaa843'
chicago: 'Stark, Stefan G, Joanna Ficek, Francesco Locatello, Ximena Bonilla, Stéphane
Chevrier, Franziska Singer, Rudolf Aebersold, et al. “SCIM: Universal Single-Cell
Matching with Unpaired Feature Sets.” Bioinformatics. Oxford University
Press, 2020. https://doi.org/10.1093/bioinformatics/btaa843.'
ieee: 'S. G. Stark et al., “SCIM: Universal single-cell matching with unpaired
feature sets,” Bioinformatics, vol. 36, no. Supplement_2. Oxford University
Press, pp. i919–i927, 2020.'
ista: 'Stark SG et al. 2020. SCIM: Universal single-cell matching with unpaired
feature sets. Bioinformatics. 36(Supplement_2), i919–i927.'
mla: 'Stark, Stefan G., et al. “SCIM: Universal Single-Cell Matching with Unpaired
Feature Sets.” Bioinformatics, vol. 36, no. Supplement_2, Oxford University
Press, 2020, pp. i919–27, doi:10.1093/bioinformatics/btaa843.'
short: S.G. Stark, J. Ficek, F. Locatello, X. Bonilla, S. Chevrier, F. Singer, R.
Aebersold, F.S. Al-Quaddoomi, J. Albinus, I. Alborelli, S. Andani, P.-O. Attinger,
M. Bacac, D. Baumhoer, B. Beck-Schimmer, N. Beerenwinkel, C. Beisel, L. Bernasconi,
A. Bertolini, B. Bodenmiller, X. Bonilla, R. Casanova, S. Chevrier, N. Chicherova,
M. D’Costa, E. Danenberg, N. Davidson, M.-A.D. gan, R. Dummer, S. Engler, M. Erkens,
K. Eschbach, C. Esposito, A. Fedier, P. Ferreira, J. Ficek, A.L. Frei, B. Frey,
S. Goetze, L. Grob, G. Gut, D. Günther, M. Haberecker, P. Haeuptle, V. Heinzelmann-Schwarz,
S. Herter, R. Holtackers, T. Huesser, A. Irmisch, F. Jacob, A. Jacobs, T.M. Jaeger,
K. Jahn, A.R. James, P.M. Jermann, A. Kahles, A. Kahraman, V.H. Koelzer, W. Kuebler,
J. Kuipers, C.P. Kunze, C. Kurzeder, K.-V. Lehmann, M. Levesque, S. Lugert, G.
Maass, M. Manz, P. Markolin, J. Mena, U. Menzel, J.M. Metzler, N. Miglino, E.S.
Milani, H. Moch, S. Muenst, R. Murri, C.K. Ng, S. Nicolet, M. Nowak, P.G. Pedrioli,
L. Pelkmans, S. Piscuoglio, M. Prummer, M. Ritter, C. Rommel, M.L. Rosano-González,
G. Rätsch, N. Santacroce, J.S. del Castillo, R. Schlenker, P.C. Schwalie, S. Schwan,
T. Schär, G. Senti, F. Singer, S. Sivapatham, B. Snijder, B. Sobottka, V.T. Sreedharan,
S. Stark, D.J. Stekhoven, A.P. Theocharides, T.M. Thomas, M. Tolnay, V. Tosevski,
N.C. Toussaint, M.A. Tuncel, M. Tusup, A.V. Drogen, M. Vetter, T. Vlajnic, S.
Weber, W.P. Weber, R. Wegmann, M. Weller, F. Wendt, N. Wey, A. Wicki, B. Wollscheid,
S. Yu, J. Ziegler, M. Zimmermann, M. Zoche, G. Zuend, G. Rätsch, K.-V. Lehmann,
Bioinformatics 36 (2020) i919–i927.
date_created: 2023-08-21T12:28:20Z
date_published: 2020-12-01T00:00:00Z
date_updated: 2023-09-11T10:21:00Z
day: '01'
department:
- _id: FrLo
doi: 10.1093/bioinformatics/btaa843
extern: '1'
external_id:
pmid:
- '33381818'
intvolume: ' 36'
issue: Supplement_2
keyword:
- Computational Mathematics
- Computational Theory and Mathematics
- Computer Science Applications
- Molecular Biology
- Biochemistry
- Statistics and Probability
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1093/bioinformatics/btaa843
month: '12'
oa: 1
oa_version: Published Version
page: i919-i927
pmid: 1
publication: Bioinformatics
publication_identifier:
eissn:
- 1367-4811
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
related_material:
link:
- relation: software
url: https://github.com/ratschlab/scim
scopus_import: '1'
status: public
title: 'SCIM: Universal single-cell matching with unpaired feature sets'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 36
year: '2020'
...
---
_id: '10348'
abstract:
- lang: eng
text: The endosomal sorting complex required for transport-III (ESCRT-III) catalyzes
membrane fission from within membrane necks, a process that is essential for many
cellular functions, from cell division to lysosome degradation and autophagy.
How it breaks membranes, though, remains unknown. Here, we characterize a sequential
polymerization of ESCRT-III subunits that, driven by a recruitment cascade and
by continuous subunit-turnover powered by the ATPase Vps4, induces membrane deformation
and fission. During this process, the exchange of Vps24 for Did2 induces a tilt
in the polymer-membrane interface, which triggers transition from flat spiral
polymers to helical filament to drive the formation of membrane protrusions, and
ends with the formation of a highly constricted Did2-Ist1 co-polymer that we show
is competent to promote fission when bound on the inside of membrane necks. Overall,
our results suggest a mechanism of stepwise changes in ESCRT-III filament structure
and mechanical properties via exchange of the filament subunits to catalyze ESCRT-III
activity.
acknowledgement: The authors thank Nicolas Chiaruttini, Jean Gruenberg, and Lena Harker-Kirschneck
for careful correction of this manuscript and helpful discussions. The authors want
to thank the NCCR Chemical Biology for constant support during this project. A.R.
acknowledges funding from the Swiss National Fund for Research (31003A_130520, 31003A_149975,
and 31003A_173087) and the European Research Council Consolidator (311536). A.Š.
acknowledges the European Research Council (802960). B.B. thanks the BBSRC (BB/K009001/1)
and Wellcome Trust (203276/Z/16/Z) for support. J.M.v.F. acknowledges funding through
an EMBO Long-Term Fellowship (ALTF 1065-2015), the European Commission FP7 (Marie
Curie Actions, LTFCOFUND2013, and GA-2013-609409), and a Transitional Postdoc fellowship
(2015/345) from the Swiss SystemsX.ch initiative, evaluated by the Swiss National
Science Foundation and Swiss National Science Foundation Research (SNSF SINERGIA
160728/1 [leader, Sophie Martin]).
article_processing_charge: No
article_type: original
author:
- first_name: Anna-Katharina
full_name: Pfitzner, Anna-Katharina
last_name: Pfitzner
- first_name: Vincent
full_name: Mercier, Vincent
last_name: Mercier
- first_name: Xiuyun
full_name: Jiang, Xiuyun
last_name: Jiang
- first_name: Joachim
full_name: Moser von Filseck, Joachim
last_name: Moser von Filseck
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Aurélien
full_name: Roux, Aurélien
last_name: Roux
citation:
ama: Pfitzner A-K, Mercier V, Jiang X, et al. An ESCRT-III polymerization sequence
drives membrane deformation and fission. Cell. 2020;182(5):1140-1155.e18.
doi:10.1016/j.cell.2020.07.021
apa: Pfitzner, A.-K., Mercier, V., Jiang, X., Moser von Filseck, J., Baum, B., Šarić,
A., & Roux, A. (2020). An ESCRT-III polymerization sequence drives membrane
deformation and fission. Cell. Elsevier. https://doi.org/10.1016/j.cell.2020.07.021
chicago: Pfitzner, Anna-Katharina, Vincent Mercier, Xiuyun Jiang, Joachim Moser
von Filseck, Buzz Baum, Anđela Šarić, and Aurélien Roux. “An ESCRT-III Polymerization
Sequence Drives Membrane Deformation and Fission.” Cell. Elsevier, 2020.
https://doi.org/10.1016/j.cell.2020.07.021.
ieee: A.-K. Pfitzner et al., “An ESCRT-III polymerization sequence drives
membrane deformation and fission,” Cell, vol. 182, no. 5. Elsevier, p.
1140–1155.e18, 2020.
ista: Pfitzner A-K, Mercier V, Jiang X, Moser von Filseck J, Baum B, Šarić A, Roux
A. 2020. An ESCRT-III polymerization sequence drives membrane deformation and
fission. Cell. 182(5), 1140–1155.e18.
mla: Pfitzner, Anna-Katharina, et al. “An ESCRT-III Polymerization Sequence Drives
Membrane Deformation and Fission.” Cell, vol. 182, no. 5, Elsevier, 2020,
p. 1140–1155.e18, doi:10.1016/j.cell.2020.07.021.
short: A.-K. Pfitzner, V. Mercier, X. Jiang, J. Moser von Filseck, B. Baum, A. Šarić,
A. Roux, Cell 182 (2020) 1140–1155.e18.
date_created: 2021-11-26T08:02:27Z
date_published: 2020-08-18T00:00:00Z
date_updated: 2021-11-26T08:58:37Z
day: '18'
doi: 10.1016/j.cell.2020.07.021
extern: '1'
external_id:
pmid:
- '32814015'
intvolume: ' 182'
issue: '5'
keyword:
- general biochemistry
- genetics and molecular biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.sciencedirect.com/science/article/pii/S0092867420309296
month: '08'
oa: 1
oa_version: Published Version
page: 1140-1155.e18
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: An ESCRT-III polymerization sequence drives membrane deformation and fission
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 182
year: '2020'
...
---
_id: '11060'
abstract:
- lang: eng
text: The inner nuclear membrane (INM) is a subdomain of the endoplasmic reticulum
(ER) that is gated by the nuclear pore complex. It is unknown whether proteins
of the INM and ER are degraded through shared or distinct pathways in mammalian
cells. We applied dynamic proteomics to profile protein half-lives and report
that INM and ER residents turn over at similar rates, indicating that the INM’s
unique topology is not a barrier to turnover. Using a microscopy approach, we
observed that the proteasome can degrade INM proteins in situ. However, we also
uncovered evidence for selective, vesicular transport-mediated turnover of a single
INM protein, emerin, that is potentiated by ER stress. Emerin is rapidly cleared
from the INM by a mechanism that requires emerin’s LEM domain to mediate vesicular
trafficking to lysosomes. This work demonstrates that the INM can be dynamically
remodeled in response to environmental inputs.
article_number: e49796
article_processing_charge: No
article_type: original
author:
- first_name: Abigail
full_name: Buchwalter, Abigail
last_name: Buchwalter
- first_name: Roberta
full_name: Schulte, Roberta
last_name: Schulte
- first_name: Hsiao
full_name: Tsai, Hsiao
last_name: Tsai
- first_name: Juliana
full_name: Capitanio, Juliana
last_name: Capitanio
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. Selective clearance
of the inner nuclear membrane protein emerin by vesicular transport during ER
stress. eLife. 2019;8. doi:10.7554/elife.49796
apa: Buchwalter, A., Schulte, R., Tsai, H., Capitanio, J., & Hetzer, M. (2019).
Selective clearance of the inner nuclear membrane protein emerin by vesicular
transport during ER stress. ELife. eLife Sciences Publications. https://doi.org/10.7554/elife.49796
chicago: Buchwalter, Abigail, Roberta Schulte, Hsiao Tsai, Juliana Capitanio, and
Martin Hetzer. “Selective Clearance of the Inner Nuclear Membrane Protein Emerin
by Vesicular Transport during ER Stress.” ELife. eLife Sciences Publications,
2019. https://doi.org/10.7554/elife.49796.
ieee: A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, and M. Hetzer, “Selective
clearance of the inner nuclear membrane protein emerin by vesicular transport
during ER stress,” eLife, vol. 8. eLife Sciences Publications, 2019.
ista: Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. 2019. Selective clearance
of the inner nuclear membrane protein emerin by vesicular transport during ER
stress. eLife. 8, e49796.
mla: Buchwalter, Abigail, et al. “Selective Clearance of the Inner Nuclear Membrane
Protein Emerin by Vesicular Transport during ER Stress.” ELife, vol. 8,
e49796, eLife Sciences Publications, 2019, doi:10.7554/elife.49796.
short: A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, M. Hetzer, ELife 8 (2019).
date_created: 2022-04-07T07:45:02Z
date_published: 2019-10-10T00:00:00Z
date_updated: 2023-05-31T06:36:22Z
day: '10'
ddc:
- '570'
doi: 10.7554/elife.49796
extern: '1'
external_id:
pmid:
- '31599721'
file:
- access_level: open_access
checksum: 1e8672a1e9c3dc0a2d3d0dad89673616
content_type: application/pdf
creator: dernst
date_created: 2022-04-08T08:18:01Z
date_updated: 2022-04-08T08:18:01Z
file_id: '11138'
file_name: 2019_eLife_Buchwalter.pdf
file_size: 6984654
relation: main_file
success: 1
file_date_updated: 2022-04-08T08:18:01Z
has_accepted_license: '1'
intvolume: ' 8'
keyword:
- General Immunology and Microbiology
- General Biochemistry
- Genetics and Molecular Biology
- General Medicine
- General Neuroscience
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
publication: eLife
publication_identifier:
issn:
- 2050-084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
related_material:
record:
- id: '13079'
relation: research_data
status: public
scopus_import: '1'
status: public
title: Selective clearance of the inner nuclear membrane protein emerin by vesicular
transport during ER stress
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 8
year: '2019'
...
---
_id: '8405'
abstract:
- lang: eng
text: Atomic-resolution structure determination is crucial for understanding protein
function. Cryo-EM and NMR spectroscopy both provide structural information, but
currently cryo-EM does not routinely give access to atomic-level structural data,
and, generally, NMR structure determination is restricted to small (<30 kDa) proteins.
We introduce an integrated structure determination approach that simultaneously
uses NMR and EM data to overcome the limits of each of these methods. The approach
enables structure determination of the 468 kDa large dodecameric aminopeptidase
TET2 to a precision and accuracy below 1 Å by combining secondary-structure information
obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large
subunits, distance restraints from backbone amides and ILV methyl groups, and
a 4.1 Å resolution EM map. The resulting structure exceeds current standards of
NMR and EM structure determination in terms of molecular weight and precision.
Importantly, the approach is successful even in cases where only medium-resolution
cryo-EM data are available.
article_number: '2697'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Leandro F.
full_name: Estrozi, Leandro F.
last_name: Estrozi
- first_name: Charles D.
full_name: Schwieters, Charles D.
last_name: Schwieters
- first_name: Gregory
full_name: Effantin, Gregory
last_name: Effantin
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Remy
full_name: Sounier, Remy
last_name: Sounier
- first_name: Astrid C.
full_name: Sivertsen, Astrid C.
last_name: Sivertsen
- first_name: Elena
full_name: Schmidt, Elena
last_name: Schmidt
- first_name: Rime
full_name: Kerfah, Rime
last_name: Kerfah
- first_name: Guillaume
full_name: Mas, Guillaume
last_name: Mas
- first_name: Jacques-Philippe
full_name: Colletier, Jacques-Philippe
last_name: Colletier
- first_name: Peter
full_name: Güntert, Peter
last_name: Güntert
- first_name: Adrien
full_name: Favier, Adrien
last_name: Favier
- first_name: Guy
full_name: Schoehn, Guy
last_name: Schoehn
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
citation:
ama: Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution
structure determination of a half-megadalton enzyme complex. Nature Communications.
2019;10. doi:10.1038/s41467-019-10490-9
apa: Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier,
R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex. Nature Communications.
Springer Nature. https://doi.org/10.1038/s41467-019-10490-9
chicago: Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin,
Pavel Macek, Remy Sounier, Astrid C. Sivertsen, et al. “Integrated NMR and Cryo-EM
Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.”
Nature Communications. Springer Nature, 2019. https://doi.org/10.1038/s41467-019-10490-9.
ieee: D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex,” Nature Communications,
vol. 10. Springer Nature, 2019.
ista: Gauto DF, Estrozi LF, Schwieters CD, Effantin G, Macek P, Sounier R, Sivertsen
AC, Schmidt E, Kerfah R, Mas G, Colletier J-P, Güntert P, Favier A, Schoehn G,
Schanda P, Boisbouvier J. 2019. Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex. Nature Communications. 10,
2697.
mla: Gauto, Diego F., et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure
Determination of a Half-Megadalton Enzyme Complex.” Nature Communications,
vol. 10, 2697, Springer Nature, 2019, doi:10.1038/s41467-019-10490-9.
short: D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier,
A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A.
Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019).
date_created: 2020-09-17T10:28:25Z
date_published: 2019-06-19T00:00:00Z
date_updated: 2021-01-12T08:19:03Z
day: '19'
doi: 10.1038/s41467-019-10490-9
extern: '1'
external_id:
pmid:
- '31217444'
intvolume: ' 10'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41467-019-10490-9
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton
enzyme complex
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 10
year: '2019'
...
---
_id: '8407'
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Schanda P. Relaxing with liquids and solids – A perspective on biomolecular
dynamics. Journal of Magnetic Resonance. 2019;306:180-186. doi:10.1016/j.jmr.2019.07.025
apa: Schanda, P. (2019). Relaxing with liquids and solids – A perspective on biomolecular
dynamics. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2019.07.025
chicago: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular
Dynamics.” Journal of Magnetic Resonance. Elsevier, 2019. https://doi.org/10.1016/j.jmr.2019.07.025.
ieee: P. Schanda, “Relaxing with liquids and solids – A perspective on biomolecular
dynamics,” Journal of Magnetic Resonance, vol. 306. Elsevier, pp. 180–186,
2019.
ista: Schanda P. 2019. Relaxing with liquids and solids – A perspective on biomolecular
dynamics. Journal of Magnetic Resonance. 306, 180–186.
mla: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular
Dynamics.” Journal of Magnetic Resonance, vol. 306, Elsevier, 2019, pp.
180–86, doi:10.1016/j.jmr.2019.07.025.
short: P. Schanda, Journal of Magnetic Resonance 306 (2019) 180–186.
date_created: 2020-09-17T10:28:47Z
date_published: 2019-09-01T00:00:00Z
date_updated: 2021-01-12T08:19:04Z
day: '01'
doi: 10.1016/j.jmr.2019.07.025
extern: '1'
external_id:
pmid:
- '31350165'
intvolume: ' 306'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '09'
oa_version: Submitted Version
page: 180-186
pmid: 1
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Relaxing with liquids and solids – A perspective on biomolecular dynamics
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 306
year: '2019'
...
---
_id: '8408'
abstract:
- lang: eng
text: Aromatic residues are located at structurally important sites of many proteins.
Probing their interactions and dynamics can provide important functional insight
but is challenging in large proteins. Here, we introduce approaches to characterize
dynamics of phenylalanine residues using 1H-detected fast magic-angle spinning
(MAS) NMR combined with a tailored isotope-labeling scheme. Our approach yields
isolated two-spin systems that are ideally suited for artefact-free dynamics measurements,
and allows probing motions effectively without molecular-weight limitations. The
application to the TET2 enzyme assembly of ~0.5 MDa size, the currently largest
protein assigned by MAS NMR, provides insights into motions occurring on a wide
range of time scales (ps-ms). We quantitatively probe ring flip motions, and show
the temperature dependence by MAS NMR measurements down to 100 K. Interestingly,
favorable line widths are observed down to 100 K, with potential implications
for DNP NMR. Furthermore, we report the first 13C R1ρ MAS NMR relaxation-dispersion
measurements and detect structural excursions occurring on a microsecond time
scale in the entry pore to the catalytic chamber and at a trimer interface that
was proposed as exit pore. We show that the labeling scheme with deuteration at
ca. 50 kHz MAS provides superior resolution compared to 100 kHz MAS experiments
with protonated, uniformly 13C-labeled samples.
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Alessandro
full_name: Barducci, Alessandro
last_name: Barducci
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Tsutomu
full_name: Terauchi, Tsutomu
last_name: Terauchi
- first_name: David
full_name: Gajan, David
last_name: Gajan
- first_name: Yohei
full_name: Miyanoiri, Yohei
last_name: Miyanoiri
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Masatsune
full_name: Kainosho, Masatsune
last_name: Kainosho
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Gauto DF, Macek P, Barducci A, et al. Aromatic ring dynamics, thermal activation,
and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and
fast magic-angle spinning NMR. Journal of the American Chemical Society.
2019;141(28):11183-11195. doi:10.1021/jacs.9b04219
apa: Gauto, D. F., Macek, P., Barducci, A., Fraga, H., Hessel, A., Terauchi, T.,
… Schanda, P. (2019). Aromatic ring dynamics, thermal activation, and transient
conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle
spinning NMR. Journal of the American Chemical Society. American Chemical
Society. https://doi.org/10.1021/jacs.9b04219
chicago: Gauto, Diego F., Pavel Macek, Alessandro Barducci, Hugo Fraga, Audrey Hessel,
Tsutomu Terauchi, David Gajan, et al. “Aromatic Ring Dynamics, Thermal Activation,
and Transient Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and
Fast Magic-Angle Spinning NMR.” Journal of the American Chemical Society.
American Chemical Society, 2019. https://doi.org/10.1021/jacs.9b04219.
ieee: D. F. Gauto et al., “Aromatic ring dynamics, thermal activation, and
transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast
magic-angle spinning NMR,” Journal of the American Chemical Society, vol.
141, no. 28. American Chemical Society, pp. 11183–11195, 2019.
ista: Gauto DF, Macek P, Barducci A, Fraga H, Hessel A, Terauchi T, Gajan D, Miyanoiri
Y, Boisbouvier J, Lichtenecker R, Kainosho M, Schanda P. 2019. Aromatic ring dynamics,
thermal activation, and transient conformations of a 468 kDa enzyme by specific
1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical
Society. 141(28), 11183–11195.
mla: Gauto, Diego F., et al. “Aromatic Ring Dynamics, Thermal Activation, and Transient
Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle
Spinning NMR.” Journal of the American Chemical Society, vol. 141, no.
28, American Chemical Society, 2019, pp. 11183–95, doi:10.1021/jacs.9b04219.
short: D.F. Gauto, P. Macek, A. Barducci, H. Fraga, A. Hessel, T. Terauchi, D. Gajan,
Y. Miyanoiri, J. Boisbouvier, R. Lichtenecker, M. Kainosho, P. Schanda, Journal
of the American Chemical Society 141 (2019) 11183–11195.
date_created: 2020-09-17T10:29:00Z
date_published: 2019-06-14T00:00:00Z
date_updated: 2021-01-12T08:19:04Z
day: '14'
doi: 10.1021/jacs.9b04219
extern: '1'
external_id:
pmid:
- '31199882'
intvolume: ' 141'
issue: '28'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '06'
oa_version: Submitted Version
page: 11183-11195
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Aromatic ring dynamics, thermal activation, and transient conformations of
a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '8413'
abstract:
- lang: eng
text: NMR relaxation dispersion methods provide a holistic way to observe microsecond
time-scale protein backbone motion both in solution and in the solid state. Different
nuclei (1H and 15N) and different relaxation dispersion techniques (Bloch–McConnell
and near-rotary-resonance) give complementary information about the amplitudes
and time scales of the conformational dynamics and provide comprehensive insights
into the mechanistic details of the structural rearrangements. In this paper,
we exemplify the benefits of the combination of various solution- and solid-state
relaxation dispersion methods on a microcrystalline protein (α-spectrin SH3 domain),
for which we are able to identify and model the functionally relevant conformational
rearrangements around the ligand recognition loop occurring on multiple microsecond
time scales. The observed loop motions suggest that the SH3 domain exists in a
binding-competent conformation in dynamic equilibrium with a sterically impaired
ground-state conformation both in solution and in crystalline form. This inherent
plasticity between the interconverting macrostates is compatible with a conformational-preselection
model and provides new insights into the recognition mechanisms of SH3 domains.
article_processing_charge: No
article_type: original
author:
- first_name: Petra
full_name: Rovó, Petra
last_name: Rovó
- first_name: Colin A.
full_name: Smith, Colin A.
last_name: Smith
- first_name: Diego
full_name: Gauto, Diego
last_name: Gauto
- first_name: Bert L.
full_name: de Groot, Bert L.
last_name: de Groot
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Rasmus
full_name: Linser, Rasmus
last_name: Linser
citation:
ama: Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. Mechanistic insights
into microsecond time-scale motion of solid proteins using complementary 15N and
1H relaxation dispersion techniques. Journal of the American Chemical Society.
2019;141(2):858-869. doi:10.1021/jacs.8b09258
apa: Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., & Linser,
R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins
using complementary 15N and 1H relaxation dispersion techniques. Journal of
the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09258
chicago: Rovó, Petra, Colin A. Smith, Diego Gauto, Bert L. de Groot, Paul Schanda,
and Rasmus Linser. “Mechanistic Insights into Microsecond Time-Scale Motion of
Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.”
Journal of the American Chemical Society. American Chemical Society, 2019.
https://doi.org/10.1021/jacs.8b09258.
ieee: P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, and R. Linser,
“Mechanistic insights into microsecond time-scale motion of solid proteins using
complementary 15N and 1H relaxation dispersion techniques,” Journal of the
American Chemical Society, vol. 141, no. 2. American Chemical Society, pp.
858–869, 2019.
ista: Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. 2019. Mechanistic
insights into microsecond time-scale motion of solid proteins using complementary
15N and 1H relaxation dispersion techniques. Journal of the American Chemical
Society. 141(2), 858–869.
mla: Rovó, Petra, et al. “Mechanistic Insights into Microsecond Time-Scale Motion
of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.”
Journal of the American Chemical Society, vol. 141, no. 2, American Chemical
Society, 2019, pp. 858–69, doi:10.1021/jacs.8b09258.
short: P. Rovó, C.A. Smith, D. Gauto, B.L. de Groot, P. Schanda, R. Linser, Journal
of the American Chemical Society 141 (2019) 858–869.
date_created: 2020-09-17T10:29:50Z
date_published: 2019-01-08T00:00:00Z
date_updated: 2021-01-12T08:19:07Z
day: '08'
doi: 10.1021/jacs.8b09258
extern: '1'
external_id:
pmid:
- '30620186'
intvolume: ' 141'
issue: '2'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '01'
oa_version: Submitted Version
page: 858-869
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Mechanistic insights into microsecond time-scale motion of solid proteins using
complementary 15N and 1H relaxation dispersion techniques
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '13371'
abstract:
- lang: eng
text: Diamondoid nanoporous crystals represent a synthetically challenging class
of materials that typically have been obtained from tetrahedral building blocks.
In this issue of Chem, Stoddart and coworkers demonstrate that it is possible
to generate diamondoid frameworks from a hexacationic building block lacking a
tetrahedral symmetry. These results highlight the great potential of self-assembly
for rapidly transforming small molecules into structurally complex functional
materials.
article_processing_charge: No
article_type: original
author:
- first_name: Michał J.
full_name: Białek, Michał J.
last_name: Białek
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Białek MJ, Klajn R. Diamond grows up. Chem. 2019;5(9):2283-2285. doi:10.1016/j.chempr.2019.08.012
apa: Białek, M. J., & Klajn, R. (2019). Diamond grows up. Chem. Elsevier.
https://doi.org/10.1016/j.chempr.2019.08.012
chicago: Białek, Michał J., and Rafal Klajn. “Diamond Grows Up.” Chem. Elsevier,
2019. https://doi.org/10.1016/j.chempr.2019.08.012.
ieee: M. J. Białek and R. Klajn, “Diamond grows up,” Chem, vol. 5, no. 9.
Elsevier, pp. 2283–2285, 2019.
ista: Białek MJ, Klajn R. 2019. Diamond grows up. Chem. 5(9), 2283–2285.
mla: Białek, Michał J., and Rafal Klajn. “Diamond Grows Up.” Chem, vol. 5,
no. 9, Elsevier, 2019, pp. 2283–85, doi:10.1016/j.chempr.2019.08.012.
short: M.J. Białek, R. Klajn, Chem 5 (2019) 2283–2285.
date_created: 2023-08-01T09:38:38Z
date_published: 2019-09-12T00:00:00Z
date_updated: 2023-08-07T10:46:50Z
day: '12'
doi: 10.1016/j.chempr.2019.08.012
extern: '1'
intvolume: ' 5'
issue: '9'
keyword:
- Materials Chemistry
- Biochemistry (medical)
- General Chemical Engineering
- Environmental Chemistry
- Biochemistry
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.chempr.2019.08.012
month: '09'
oa: 1
oa_version: Published Version
page: 2283-2285
publication: Chem
publication_identifier:
eissn:
- 2451-9294
issn:
- 2451-9308
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Diamond grows up
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2019'
...
---
_id: '13373'
abstract:
- lang: eng
text: The reversible photoisomerization of azobenzene has been utilized to construct
a plethora of systems in which optical, electronic, catalytic, and other properties
can be controlled by light. However, owing to azobenzene’s hydrophobic nature,
most of these examples have been realized only in organic solvents, and systems
operating in water are relatively scarce. Here, we show that by coadsorbing the
inherently hydrophobic azobenzenes with water-solubilizing ligands on the same
nanoparticulate platforms, it is possible to render them essentially water-soluble.
To this end, we developed a modified nanoparticle functionalization procedure
allowing us to precisely fine-tune the amount of azobenzene on the functionalized
nanoparticles. Molecular dynamics simulations helped us to identify two distinct
supramolecular architectures (depending on the length of the background ligand)
on these nanoparticles, which can explain their excellent aqueous solubilities.
Azobenzenes adsorbed on these water-soluble nanoparticles exhibit highly reversible
photoisomerization upon exposure to UV and visible light. Importantly, the mixed-monolayer
approach allowed us to systematically investigate how the background ligand affects
the switching properties of azobenzene. We found that the nature of the background
ligand has a profound effect on the kinetics of azobenzene switching. For example,
a hydroxy-terminated background ligand is capable of accelerating the back-isomerization
reaction by more than 6000-fold. These results pave the way toward the development
of novel light-responsive nanomaterials operating in aqueous media and, in the
long run, in biological environments.
article_processing_charge: No
article_type: original
author:
- first_name: Zonglin
full_name: Chu, Zonglin
last_name: Chu
- first_name: Yanxiao
full_name: Han, Yanxiao
last_name: Han
- first_name: Tong
full_name: Bian, Tong
last_name: Bian
- first_name: Soumen
full_name: De, Soumen
last_name: De
- first_name: Petr
full_name: Král, Petr
last_name: Král
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Chu Z, Han Y, Bian T, De S, Král P, Klajn R. Supramolecular control of azobenzene
switching on nanoparticles. Journal of the American Chemical Society. 2019;141(5):1949-1960.
doi:10.1021/jacs.8b09638
apa: Chu, Z., Han, Y., Bian, T., De, S., Král, P., & Klajn, R. (2019). Supramolecular
control of azobenzene switching on nanoparticles. Journal of the American Chemical
Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09638
chicago: Chu, Zonglin, Yanxiao Han, Tong Bian, Soumen De, Petr Král, and Rafal Klajn.
“Supramolecular Control of Azobenzene Switching on Nanoparticles.” Journal
of the American Chemical Society. American Chemical Society, 2019. https://doi.org/10.1021/jacs.8b09638.
ieee: Z. Chu, Y. Han, T. Bian, S. De, P. Král, and R. Klajn, “Supramolecular control
of azobenzene switching on nanoparticles,” Journal of the American Chemical
Society, vol. 141, no. 5. American Chemical Society, pp. 1949–1960, 2019.
ista: Chu Z, Han Y, Bian T, De S, Král P, Klajn R. 2019. Supramolecular control
of azobenzene switching on nanoparticles. Journal of the American Chemical Society.
141(5), 1949–1960.
mla: Chu, Zonglin, et al. “Supramolecular Control of Azobenzene Switching on Nanoparticles.”
Journal of the American Chemical Society, vol. 141, no. 5, American Chemical
Society, 2019, pp. 1949–60, doi:10.1021/jacs.8b09638.
short: Z. Chu, Y. Han, T. Bian, S. De, P. Král, R. Klajn, Journal of the American
Chemical Society 141 (2019) 1949–1960.
date_created: 2023-08-01T09:39:19Z
date_published: 2019-02-06T00:00:00Z
date_updated: 2023-08-07T10:51:12Z
day: '06'
doi: 10.1021/jacs.8b09638
extern: '1'
external_id:
pmid:
- '30595017'
intvolume: ' 141'
issue: '5'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '02'
oa_version: Published Version
page: 1949-1960
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Supramolecular control of azobenzene switching on nanoparticles
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '9018'
abstract:
- lang: eng
text: Anti-silencing function 1 (ASF1) is a conserved H3-H4 histone chaperone involved
in histone dynamics during replication, transcription, and DNA repair. Overexpressed
in proliferating tissues including many tumors, ASF1 has emerged as a promising
therapeutic target. Here, we combine structural, computational, and biochemical
approaches to design peptides that inhibit the ASF1-histone interaction. Starting
from the structure of the human ASF1-histone complex, we developed a rational
design strategy combining epitope tethering and optimization of interface contacts
to identify a potent peptide inhibitor with a dissociation constant of 3 nM. When
introduced into cultured cells, the inhibitors impair cell proliferation, perturb
cell-cycle progression, and reduce cell migration and invasion in a manner commensurate
with their affinity for ASF1. Finally, we find that direct injection of the most
potent ASF1 peptide inhibitor in mouse allografts reduces tumor growth. Our results
open new avenues to use ASF1 inhibitors as promising leads for cancer therapy.
article_processing_charge: No
article_type: original
author:
- first_name: May M
full_name: Bakail, May M
id: FB3C3F8E-522F-11EA-B186-22963DDC885E
last_name: Bakail
orcid: 0000-0002-9592-1587
- first_name: Albane
full_name: Gaubert, Albane
last_name: Gaubert
- first_name: Jessica
full_name: Andreani, Jessica
last_name: Andreani
- first_name: Gwenaëlle
full_name: Moal, Gwenaëlle
last_name: Moal
- first_name: Guillaume
full_name: Pinna, Guillaume
last_name: Pinna
- first_name: Ekaterina
full_name: Boyarchuk, Ekaterina
last_name: Boyarchuk
- first_name: Marie-Cécile
full_name: Gaillard, Marie-Cécile
last_name: Gaillard
- first_name: Regis
full_name: Courbeyrette, Regis
last_name: Courbeyrette
- first_name: Carl
full_name: Mann, Carl
last_name: Mann
- first_name: Jean-Yves
full_name: Thuret, Jean-Yves
last_name: Thuret
- first_name: Bérengère
full_name: Guichard, Bérengère
last_name: Guichard
- first_name: Brice
full_name: Murciano, Brice
last_name: Murciano
- first_name: Nicolas
full_name: Richet, Nicolas
last_name: Richet
- first_name: Adeline
full_name: Poitou, Adeline
last_name: Poitou
- first_name: Claire
full_name: Frederic, Claire
last_name: Frederic
- first_name: Marie-Hélène
full_name: Le Du, Marie-Hélène
last_name: Le Du
- first_name: Morgane
full_name: Agez, Morgane
last_name: Agez
- first_name: Caroline
full_name: Roelants, Caroline
last_name: Roelants
- first_name: Zachary A.
full_name: Gurard-Levin, Zachary A.
last_name: Gurard-Levin
- first_name: Geneviève
full_name: Almouzni, Geneviève
last_name: Almouzni
- first_name: Nadia
full_name: Cherradi, Nadia
last_name: Cherradi
- first_name: Raphael
full_name: Guerois, Raphael
last_name: Guerois
- first_name: Françoise
full_name: Ochsenbein, Françoise
last_name: Ochsenbein
citation:
ama: Bakail MM, Gaubert A, Andreani J, et al. Design on a rational basis of high-affinity
peptides inhibiting the histone chaperone ASF1. Cell Chemical Biology.
2019;26(11):1573-1585.e10. doi:10.1016/j.chembiol.2019.09.002
apa: Bakail, M. M., Gaubert, A., Andreani, J., Moal, G., Pinna, G., Boyarchuk, E.,
… Ochsenbein, F. (2019). Design on a rational basis of high-affinity peptides
inhibiting the histone chaperone ASF1. Cell Chemical Biology. Elsevier.
https://doi.org/10.1016/j.chembiol.2019.09.002
chicago: Bakail, May M, Albane Gaubert, Jessica Andreani, Gwenaëlle Moal, Guillaume
Pinna, Ekaterina Boyarchuk, Marie-Cécile Gaillard, et al. “Design on a Rational
Basis of High-Affinity Peptides Inhibiting the Histone Chaperone ASF1.” Cell
Chemical Biology. Elsevier, 2019. https://doi.org/10.1016/j.chembiol.2019.09.002.
ieee: M. M. Bakail et al., “Design on a rational basis of high-affinity peptides
inhibiting the histone chaperone ASF1,” Cell Chemical Biology, vol. 26,
no. 11. Elsevier, p. 1573–1585.e10, 2019.
ista: Bakail MM, Gaubert A, Andreani J, Moal G, Pinna G, Boyarchuk E, Gaillard M-C,
Courbeyrette R, Mann C, Thuret J-Y, Guichard B, Murciano B, Richet N, Poitou A,
Frederic C, Le Du M-H, Agez M, Roelants C, Gurard-Levin ZA, Almouzni G, Cherradi
N, Guerois R, Ochsenbein F. 2019. Design on a rational basis of high-affinity
peptides inhibiting the histone chaperone ASF1. Cell Chemical Biology. 26(11),
1573–1585.e10.
mla: Bakail, May M., et al. “Design on a Rational Basis of High-Affinity Peptides
Inhibiting the Histone Chaperone ASF1.” Cell Chemical Biology, vol. 26,
no. 11, Elsevier, 2019, p. 1573–1585.e10, doi:10.1016/j.chembiol.2019.09.002.
short: M.M. Bakail, A. Gaubert, J. Andreani, G. Moal, G. Pinna, E. Boyarchuk, M.-C.
Gaillard, R. Courbeyrette, C. Mann, J.-Y. Thuret, B. Guichard, B. Murciano, N.
Richet, A. Poitou, C. Frederic, M.-H. Le Du, M. Agez, C. Roelants, Z.A. Gurard-Levin,
G. Almouzni, N. Cherradi, R. Guerois, F. Ochsenbein, Cell Chemical Biology 26
(2019) 1573–1585.e10.
date_created: 2021-01-19T11:04:50Z
date_published: 2019-11-21T00:00:00Z
date_updated: 2023-02-23T13:46:53Z
day: '21'
doi: 10.1016/j.chembiol.2019.09.002
extern: '1'
external_id:
pmid:
- '31543461'
intvolume: ' 26'
issue: '11'
keyword:
- Clinical Biochemistry
- Molecular Medicine
- Biochemistry
- Molecular Biology
- Pharmacology
- Drug Discovery
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.chembiol.2019.09.002
month: '11'
oa: 1
oa_version: Published Version
page: 1573-1585.e10
pmid: 1
publication: Cell Chemical Biology
publication_identifier:
issn:
- 2451-9456
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Design on a rational basis of high-affinity peptides inhibiting the histone
chaperone ASF1
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 26
year: '2019'
...
---
_id: '9060'
abstract:
- lang: eng
text: Molecular motors are essential to the living, generating fluctuations that
boost transport and assist assembly. Active colloids, that consume energy to move,
hold similar potential for man-made materials controlled by forces generated from
within. Yet, their use as a powerhouse in materials science lacks. Here we show
a massive acceleration of the annealing of a monolayer of passive beads by moderate
addition of self-propelled microparticles. We rationalize our observations with
a model of collisions that drive active fluctuations and activate the annealing.
The experiment is quantitatively compared with Brownian dynamic simulations that
further unveil a dynamical transition in the mechanism of annealing. Active dopants
travel uniformly in the system or co-localize at the grain boundaries as a result
of the persistence of their motion. Our findings uncover the potential of internal
activity to control materials and lay the groundwork for the rise of materials
science beyond equilibrium.
article_number: '3380'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Sophie
full_name: Ramananarivo, Sophie
last_name: Ramananarivo
- first_name: Etienne
full_name: Ducrot, Etienne
last_name: Ducrot
- first_name: Jérémie A
full_name: Palacci, Jérémie A
id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d
last_name: Palacci
orcid: 0000-0002-7253-9465
citation:
ama: Ramananarivo S, Ducrot E, Palacci JA. Activity-controlled annealing of colloidal
monolayers. Nature Communications. 2019;10(1). doi:10.1038/s41467-019-11362-y
apa: Ramananarivo, S., Ducrot, E., & Palacci, J. A. (2019). Activity-controlled
annealing of colloidal monolayers. Nature Communications. Springer Nature.
https://doi.org/10.1038/s41467-019-11362-y
chicago: Ramananarivo, Sophie, Etienne Ducrot, and Jérémie A Palacci. “Activity-Controlled
Annealing of Colloidal Monolayers.” Nature Communications. Springer Nature,
2019. https://doi.org/10.1038/s41467-019-11362-y.
ieee: S. Ramananarivo, E. Ducrot, and J. A. Palacci, “Activity-controlled annealing
of colloidal monolayers,” Nature Communications, vol. 10, no. 1. Springer
Nature, 2019.
ista: Ramananarivo S, Ducrot E, Palacci JA. 2019. Activity-controlled annealing
of colloidal monolayers. Nature Communications. 10(1), 3380.
mla: Ramananarivo, Sophie, et al. “Activity-Controlled Annealing of Colloidal Monolayers.”
Nature Communications, vol. 10, no. 1, 3380, Springer Nature, 2019, doi:10.1038/s41467-019-11362-y.
short: S. Ramananarivo, E. Ducrot, J.A. Palacci, Nature Communications 10 (2019).
date_created: 2021-02-02T13:43:36Z
date_published: 2019-07-29T00:00:00Z
date_updated: 2023-02-23T13:47:59Z
day: '29'
ddc:
- '530'
doi: 10.1038/s41467-019-11362-y
extern: '1'
external_id:
arxiv:
- '1909.07382'
pmid:
- '31358762'
file:
- access_level: open_access
checksum: 70c6e5d6fbea0932b0669505ab6633ec
content_type: application/pdf
creator: cziletti
date_created: 2021-02-02T13:47:21Z
date_updated: 2021-02-02T13:47:21Z
file_id: '9061'
file_name: 2019_NatureComm_Ramananarivo.pdf
file_size: 2820337
relation: main_file
success: 1
file_date_updated: 2021-02-02T13:47:21Z
has_accepted_license: '1'
intvolume: ' 10'
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Activity-controlled annealing of colloidal monolayers
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 10
year: '2019'
...
---
_id: '12190'
abstract:
- lang: eng
text: Meiotic crossover frequency varies within genomes, which influences genetic
diversity and adaptation. In turn, genetic variation within populations can act
to modify crossover frequency in cis and trans. To identify genetic variation
that controls meiotic crossover frequency, we screened Arabidopsis accessions
using fluorescent recombination reporters. We mapped a genetic modifier of crossover
frequency in Col × Bur populations of Arabidopsis to a premature stop codon within
TBP-ASSOCIATED FACTOR 4b (TAF4b), which encodes a subunit of the RNA polymerase
II general transcription factor TFIID. The Arabidopsis taf4b mutation is a rare
variant found in the British Isles, originating in South-West Ireland. Using genetics,
genomics, and immunocytology, we demonstrate a genome-wide decrease in taf4b crossovers,
with strongest reduction in the sub-telomeric regions. Using RNA sequencing (RNA-seq)
from purified meiocytes, we show that TAF4b expression is meiocyte enriched, whereas
its paralog TAF4 is broadly expressed. Consistent with the role of TFIID in promoting
gene expression, RNA-seq of wild-type and taf4b meiocytes identified widespread
transcriptional changes, including in genes that regulate the meiotic cell cycle
and recombination. Therefore, TAF4b duplication is associated with acquisition
of meiocyte-specific expression and promotion of germline transcription, which
act directly or indirectly to elevate crossovers. This identifies a novel mode
of meiotic recombination control via a general transcription factor.
acknowledgement: "We thank Gregory Copenhaver (University of North Carolina), Avraham
Levy (The Weizmann Institute), and Scott Poethig (University of Pennsylvania) for
FTLs; Piotr Ziolkowski for Col-420/Bur seed; Sureshkumar Balasubramanian\r\n(Monash
University) for providing British and Irish Arabidopsis accessions; Mathilde Grelon
(INRA, Versailles) for providing the MLH1 antibody; and the Gurdon Institute for
access to microscopes. This work was supported by a BBSRC DTP studentship (E.J.L.),
European Research Area Network for Coordinating Action in Plant Sciences/BBSRC ‘‘DeCOP’’
(BB/M004937/1; C.L.), a BBSRC David Phillips Fellowship (BB/L025043/1; H.G. and
X.F.), the European Research Council (CoG ‘‘SynthHotspot,’’ A.J.T., C.L., and I.R.H.;
StG ‘‘SexMeth,’’ X.F.), and a Sainsbury Charitable Foundation Studentship (A.R.B.)."
article_processing_charge: No
article_type: original
author:
- first_name: Emma J.
full_name: Lawrence, Emma J.
last_name: Lawrence
- first_name: Hongbo
full_name: Gao, Hongbo
last_name: Gao
- first_name: Andrew J.
full_name: Tock, Andrew J.
last_name: Tock
- first_name: Christophe
full_name: Lambing, Christophe
last_name: Lambing
- first_name: Alexander R.
full_name: Blackwell, Alexander R.
last_name: Blackwell
- first_name: Xiaoqi
full_name: Feng, Xiaoqi
id: e0164712-22ee-11ed-b12a-d80fcdf35958
last_name: Feng
orcid: 0000-0002-4008-1234
- first_name: Ian R.
full_name: Henderson, Ian R.
last_name: Henderson
citation:
ama: Lawrence EJ, Gao H, Tock AJ, et al. Natural variation in TBP-ASSOCIATED FACTOR
4b controls meiotic crossover and germline transcription in Arabidopsis. Current
Biology. 2019;29(16):2676-2686.e3. doi:10.1016/j.cub.2019.06.084
apa: Lawrence, E. J., Gao, H., Tock, A. J., Lambing, C., Blackwell, A. R., Feng,
X., & Henderson, I. R. (2019). Natural variation in TBP-ASSOCIATED FACTOR
4b controls meiotic crossover and germline transcription in Arabidopsis. Current
Biology. Elsevier BV. https://doi.org/10.1016/j.cub.2019.06.084
chicago: Lawrence, Emma J., Hongbo Gao, Andrew J. Tock, Christophe Lambing, Alexander
R. Blackwell, Xiaoqi Feng, and Ian R. Henderson. “Natural Variation in TBP-ASSOCIATED
FACTOR 4b Controls Meiotic Crossover and Germline Transcription in Arabidopsis.”
Current Biology. Elsevier BV, 2019. https://doi.org/10.1016/j.cub.2019.06.084.
ieee: E. J. Lawrence et al., “Natural variation in TBP-ASSOCIATED FACTOR
4b controls meiotic crossover and germline transcription in Arabidopsis,” Current
Biology, vol. 29, no. 16. Elsevier BV, p. 2676–2686.e3, 2019.
ista: Lawrence EJ, Gao H, Tock AJ, Lambing C, Blackwell AR, Feng X, Henderson IR.
2019. Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover
and germline transcription in Arabidopsis. Current Biology. 29(16), 2676–2686.e3.
mla: Lawrence, Emma J., et al. “Natural Variation in TBP-ASSOCIATED FACTOR 4b Controls
Meiotic Crossover and Germline Transcription in Arabidopsis.” Current Biology,
vol. 29, no. 16, Elsevier BV, 2019, p. 2676–2686.e3, doi:10.1016/j.cub.2019.06.084.
short: E.J. Lawrence, H. Gao, A.J. Tock, C. Lambing, A.R. Blackwell, X. Feng, I.R.
Henderson, Current Biology 29 (2019) 2676–2686.e3.
date_created: 2023-01-16T09:16:33Z
date_published: 2019-08-19T00:00:00Z
date_updated: 2023-05-08T10:54:54Z
day: '19'
department:
- _id: XiFe
doi: 10.1016/j.cub.2019.06.084
extern: '1'
external_id:
pmid:
- '31378616'
intvolume: ' 29'
issue: '16'
keyword:
- General Agricultural and Biological Sciences
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '08'
oa_version: None
page: 2676-2686.e3
pmid: 1
publication: Current Biology
publication_identifier:
issn:
- 0960-9822
publication_status: published
publisher: Elsevier BV
quality_controlled: '1'
scopus_import: '1'
status: public
title: Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and
germline transcription in Arabidopsis
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 29
year: '2019'
...
---
_id: '12192'
abstract:
- lang: eng
text: Transposable elements (TEs), the movement of which can damage the genome,
are epigenetically silenced in eukaryotes. Intriguingly, TEs are activated in
the sperm companion cell – vegetative cell (VC) – of the flowering plant Arabidopsis
thaliana. However, the extent and mechanism of this activation are unknown. Here
we show that about 100 heterochromatic TEs are activated in VCs, mostly by DEMETER-catalyzed
DNA demethylation. We further demonstrate that DEMETER access to some of these
TEs is permitted by the natural depletion of linker histone H1 in VCs. Ectopically
expressed H1 suppresses TEs in VCs by reducing DNA demethylation and via a methylation-independent
mechanism. We demonstrate that H1 is required for heterochromatin condensation
in plant cells and show that H1 overexpression creates heterochromatic foci in
the VC progenitor cell. Taken together, our results demonstrate that the natural
depletion of H1 during male gametogenesis facilitates DEMETER-directed DNA demethylation,
heterochromatin relaxation, and TE activation.
acknowledgement: We thank David Twell for the pDONR-P4-P1R-pLAT52 and pDONR-P2R-P3-mRFP
vectors, the John Innes Centre Bioimaging Facility (Elaine Barclay and Grant Calder)
for their assistance with microscopy, and the Norwich BioScience Institute Partnership
Computing infrastructure for Science Group for High Performance Computing resources.
This work was funded by a Biotechnology and Biological Sciences Research Council
(BBSRC) David Phillips Fellowship (BB/L025043/1; SH, JZ and XF), a European Research
Council Starting Grant ('SexMeth' 804981; XF) and a Grant to Exceptional Researchers
by the Gatsby Charitable Foundation (SH and XF).
article_number: '42530'
article_processing_charge: No
article_type: original
author:
- first_name: Shengbo
full_name: He, Shengbo
last_name: He
- first_name: Martin
full_name: Vickers, Martin
last_name: Vickers
- first_name: Jingyi
full_name: Zhang, Jingyi
last_name: Zhang
- first_name: Xiaoqi
full_name: Feng, Xiaoqi
id: e0164712-22ee-11ed-b12a-d80fcdf35958
last_name: Feng
orcid: 0000-0002-4008-1234
citation:
ama: He S, Vickers M, Zhang J, Feng X. Natural depletion of histone H1 in sex cells
causes DNA demethylation, heterochromatin decondensation and transposon activation.
eLife. 2019;8. doi:10.7554/elife.42530
apa: He, S., Vickers, M., Zhang, J., & Feng, X. (2019). Natural depletion of
histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation
and transposon activation. ELife. eLife Sciences Publications, Ltd. https://doi.org/10.7554/elife.42530
chicago: He, Shengbo, Martin Vickers, Jingyi Zhang, and Xiaoqi Feng. “Natural Depletion
of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation
and Transposon Activation.” ELife. eLife Sciences Publications, Ltd, 2019.
https://doi.org/10.7554/elife.42530.
ieee: S. He, M. Vickers, J. Zhang, and X. Feng, “Natural depletion of histone H1
in sex cells causes DNA demethylation, heterochromatin decondensation and transposon
activation,” eLife, vol. 8. eLife Sciences Publications, Ltd, 2019.
ista: He S, Vickers M, Zhang J, Feng X. 2019. Natural depletion of histone H1 in
sex cells causes DNA demethylation, heterochromatin decondensation and transposon
activation. eLife. 8, 42530.
mla: He, Shengbo, et al. “Natural Depletion of Histone H1 in Sex Cells Causes DNA
Demethylation, Heterochromatin Decondensation and Transposon Activation.” ELife,
vol. 8, 42530, eLife Sciences Publications, Ltd, 2019, doi:10.7554/elife.42530.
short: S. He, M. Vickers, J. Zhang, X. Feng, ELife 8 (2019).
date_created: 2023-01-16T09:17:21Z
date_published: 2019-05-28T00:00:00Z
date_updated: 2023-05-08T10:54:12Z
day: '28'
ddc:
- '580'
department:
- _id: XiFe
doi: 10.7554/elife.42530
extern: '1'
external_id:
unknown:
- '31135340'
file:
- access_level: open_access
checksum: ea6b89c20d59e5eb3646916fe5d568ad
content_type: application/pdf
creator: alisjak
date_created: 2023-02-07T09:42:46Z
date_updated: 2023-02-07T09:42:46Z
file_id: '12525'
file_name: 2019_elife_He.pdf
file_size: 2493837
relation: main_file
success: 1
file_date_updated: 2023-02-07T09:42:46Z
has_accepted_license: '1'
intvolume: ' 8'
keyword:
- General Immunology and Microbiology
- General Biochemistry
- Genetics and Molecular Biology
- General Medicine
- General Neuroscience
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6594752/
month: '05'
oa: 1
oa_version: Published Version
publication: eLife
publication_identifier:
issn:
- 2050-084X
publication_status: published
publisher: eLife Sciences Publications, Ltd
quality_controlled: '1'
scopus_import: '1'
status: public
title: Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin
decondensation and transposon activation
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 8
year: '2019'
...
---
_id: '10880'
abstract:
- lang: eng
text: Acquisition of evolutionary novelties is a fundamental process for adapting
to the external environment and invading new niches and results in the diversification
of life, which we can see in the world today. How such novel phenotypic traits
are acquired in the course of evolution and are built up in developing embryos
has been a central question in biology. Whole-genome duplication (WGD) is a process
of genome doubling that supplies raw genetic materials and increases genome complexity.
Recently, it has been gradually revealed that WGD and subsequent fate changes
of duplicated genes can facilitate phenotypic evolution. Here, we review the current
understanding of the relationship between WGD and the acquisition of evolutionary
novelties. We show some examples of this link and discuss how WGD and subsequent
duplicated genes can facilitate phenotypic evolution as well as when such genomic
doubling can be advantageous for adaptation.
acknowledgement: This work was supported by JSPS overseas research fellowships (Y.M.)
and SENSHIN Medical Research Foundation (K.K.T.).
article_processing_charge: No
article_type: original
author:
- first_name: Moriyama
full_name: Yuuta, Moriyama
id: 4968E7C8-F248-11E8-B48F-1D18A9856A87
last_name: Yuuta
orcid: 0000-0002-2853-8051
- first_name: Kazuko
full_name: Koshiba-Takeuchi, Kazuko
last_name: Koshiba-Takeuchi
citation:
ama: Yuuta M, Koshiba-Takeuchi K. Significance of whole-genome duplications on the
emergence of evolutionary novelties. Briefings in Functional Genomics.
2018;17(5):329-338. doi:10.1093/bfgp/ely007
apa: Yuuta, M., & Koshiba-Takeuchi, K. (2018). Significance of whole-genome
duplications on the emergence of evolutionary novelties. Briefings in Functional
Genomics. Oxford University Press. https://doi.org/10.1093/bfgp/ely007
chicago: Yuuta, Moriyama, and Kazuko Koshiba-Takeuchi. “Significance of Whole-Genome
Duplications on the Emergence of Evolutionary Novelties.” Briefings in Functional
Genomics. Oxford University Press, 2018. https://doi.org/10.1093/bfgp/ely007.
ieee: M. Yuuta and K. Koshiba-Takeuchi, “Significance of whole-genome duplications
on the emergence of evolutionary novelties,” Briefings in Functional Genomics,
vol. 17, no. 5. Oxford University Press, pp. 329–338, 2018.
ista: Yuuta M, Koshiba-Takeuchi K. 2018. Significance of whole-genome duplications
on the emergence of evolutionary novelties. Briefings in Functional Genomics.
17(5), 329–338.
mla: Yuuta, Moriyama, and Kazuko Koshiba-Takeuchi. “Significance of Whole-Genome
Duplications on the Emergence of Evolutionary Novelties.” Briefings in Functional
Genomics, vol. 17, no. 5, Oxford University Press, 2018, pp. 329–38, doi:10.1093/bfgp/ely007.
short: M. Yuuta, K. Koshiba-Takeuchi, Briefings in Functional Genomics 17 (2018)
329–338.
date_created: 2022-03-18T12:40:35Z
date_published: 2018-09-01T00:00:00Z
date_updated: 2023-09-19T15:11:22Z
day: '01'
department:
- _id: CaHe
doi: 10.1093/bfgp/ely007
external_id:
isi:
- '000456054400004'
pmid:
- '29579140'
intvolume: ' 17'
isi: 1
issue: '5'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
- General Medicine
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1093/bfgp/ely007
month: '09'
oa: 1
oa_version: Published Version
page: 329-338
pmid: 1
publication: Briefings in Functional Genomics
publication_identifier:
eissn:
- 2041-2657
issn:
- 2041-2649
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Significance of whole-genome duplications on the emergence of evolutionary
novelties
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 17
year: '2018'
...