---
_id: '14782'
abstract:
- lang: eng
text: The actin cortex is a complex cytoskeletal machinery that drives and responds
to changes in cell shape. It must generate or adapt to plasma membrane curvature
to facilitate diverse functions such as cell division, migration, and phagocytosis.
Due to the complex molecular makeup of the actin cortex, it remains unclear whether
actin networks are inherently able to sense and generate membrane curvature, or
whether they rely on their diverse binding partners to accomplish this. Here,
we show that curvature sensing is an inherent capability of branched actin networks
nucleated by Arp2/3 and VCA. We develop a robust method to encapsulate actin inside
giant unilamellar vesicles (GUVs) and assemble an actin cortex at the inner surface
of the GUV membrane. We show that actin forms a uniform and thin cortical layer
when present at high concentration and distinct patches associated with negative
membrane curvature at low concentration. Serendipitously, we find that the GUV
production method also produces dumbbell-shaped GUVs, which we explain using mathematical
modeling in terms of membrane hemifusion of nested GUVs. We find that branched
actin networks preferentially assemble at the neck of the dumbbells, which possess
a micrometer-range convex curvature comparable with the curvature of the actin
patches found in spherical GUVs. Minimal branched actin networks can thus sense
membrane curvature, which may help mammalian cells to robustly recruit actin to
curved membranes to facilitate diverse cellular functions such as cytokinesis
and migration.
acknowledgement: We thank Jeffrey den Haan for protein purification, Kristina Ganzinger
(AMOLF) for providing the 10xHis VCA construct, David Kovar (University of Chicago)
for the CP constructs, and Michael Way (Crick Institute) for providing purified
human Arp2/3 proteins. We are grateful to Iris Lambert for early actin encapsulation
experiments that formed the basis for establishing the eDICE method, to Federico
Fanalista for acquiring images of dumbbell-shaped GUVs in samples produced by cDICE,
and to Tom Aarts for images of dumbbell-shaped GUVs produced by gel-assisted swelling.
Lennard van Buren is thanked for his help with image analysis to quantify actin
concentrations in GUVs. We thank Kristina Ganzinger (AMOLF) for hosting us to perform
pyrene assays in her lab, and Balász Antalicz (AMOLF) for technical assistance with
the spectrophotometer. The authors also thank Matthieu Piel and Daniel Fletcher
for insightful and inspiring discussions. We acknowledge financial support from
The Netherlands Organization of Scientific Research (NWO/OCW) Gravitation program
Building a Synthetic Cell (BaSyC) (024.003.019). F.F. gratefully acknowledges funding
from the Kavli Synergy program of the Kavli Institute of Nanoscience Delft.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Lucia
full_name: Baldauf, Lucia
last_name: Baldauf
- first_name: Felix F
full_name: Frey, Felix F
id: a0270b37-8f1a-11ec-95c7-8e710c59a4f3
last_name: Frey
- first_name: Marcos
full_name: Arribas Perez, Marcos
last_name: Arribas Perez
- first_name: Timon
full_name: Idema, Timon
last_name: Idema
- first_name: Gijsje H.
full_name: Koenderink, Gijsje H.
last_name: Koenderink
citation:
ama: Baldauf L, Frey FF, Arribas Perez M, Idema T, Koenderink GH. Branched actin
cortices reconstituted in vesicles sense membrane curvature. Biophysical Journal.
2023;122(11):2311-2324. doi:10.1016/j.bpj.2023.02.018
apa: Baldauf, L., Frey, F. F., Arribas Perez, M., Idema, T., & Koenderink, G.
H. (2023). Branched actin cortices reconstituted in vesicles sense membrane curvature.
Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2023.02.018
chicago: Baldauf, Lucia, Felix F Frey, Marcos Arribas Perez, Timon Idema, and Gijsje
H. Koenderink. “Branched Actin Cortices Reconstituted in Vesicles Sense Membrane
Curvature.” Biophysical Journal. Elsevier, 2023. https://doi.org/10.1016/j.bpj.2023.02.018.
ieee: L. Baldauf, F. F. Frey, M. Arribas Perez, T. Idema, and G. H. Koenderink,
“Branched actin cortices reconstituted in vesicles sense membrane curvature,”
Biophysical Journal, vol. 122, no. 11. Elsevier, pp. 2311–2324, 2023.
ista: Baldauf L, Frey FF, Arribas Perez M, Idema T, Koenderink GH. 2023. Branched
actin cortices reconstituted in vesicles sense membrane curvature. Biophysical
Journal. 122(11), 2311–2324.
mla: Baldauf, Lucia, et al. “Branched Actin Cortices Reconstituted in Vesicles Sense
Membrane Curvature.” Biophysical Journal, vol. 122, no. 11, Elsevier, 2023,
pp. 2311–24, doi:10.1016/j.bpj.2023.02.018.
short: L. Baldauf, F.F. Frey, M. Arribas Perez, T. Idema, G.H. Koenderink, Biophysical
Journal 122 (2023) 2311–2324.
date_created: 2024-01-10T09:45:48Z
date_published: 2023-06-06T00:00:00Z
date_updated: 2024-01-16T09:20:03Z
day: '06'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1016/j.bpj.2023.02.018
external_id:
isi:
- '001016792600001'
pmid:
- '36806830'
file:
- access_level: open_access
checksum: 70566e54cd95ea6df340909ad44c5cd5
content_type: application/pdf
creator: dernst
date_created: 2024-01-16T09:09:29Z
date_updated: 2024-01-16T09:09:29Z
file_id: '14807'
file_name: 2023_BiophysicalJournal_Baldauf.pdf
file_size: 3285810
relation: main_file
success: 1
file_date_updated: 2024-01-16T09:09:29Z
has_accepted_license: '1'
intvolume: ' 122'
isi: 1
issue: '11'
keyword:
- Biophysics
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
page: 2311-2324
pmid: 1
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
link:
- relation: software
url: https://github.com/BioSoftMatterGroup/actin-curvature-sensing
status: public
title: Branched actin cortices reconstituted in vesicles sense membrane curvature
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 122
year: '2023'
...
---
_id: '12163'
abstract:
- lang: eng
text: Small GTPases play essential roles in the organization of eukaryotic cells.
In recent years, it has become clear that their intracellular functions result
from intricate biochemical networks of the GTPase and their regulators that dynamically
bind to a membrane surface. Due to the inherent complexities of their interactions,
however, revealing the underlying mechanisms of action is often difficult to achieve
from in vivo studies. This review summarizes in vitro reconstitution approaches
developed to obtain a better mechanistic understanding of how small GTPase activities
are regulated in space and time.
acknowledgement: The authors acknowledge support from IST Austria and helpful comments
from the anonymous reviewers that helped to improve this manuscript. We apologize
to the authors of primary literature and outstanding research not cited here due
to space restraints.
article_processing_charge: Yes (via OA deal)
article_type: review
author:
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Albert
full_name: Auer, Albert
id: 3018E8C2-F248-11E8-B48F-1D18A9856A87
last_name: Auer
orcid: 0000-0002-3580-2906
- first_name: Gabriel
full_name: Brognara, Gabriel
id: D96FFDA0-A884-11E9-9968-DC26E6697425
last_name: Brognara
- first_name: Hanifatul R
full_name: Budiman, Hanifatul R
id: 55380f95-15b2-11ec-abd3-aff8e230696b
last_name: Budiman
- first_name: Lukasz M
full_name: Kowalski, Lukasz M
id: e3a512e2-4bbe-11eb-a68a-e3857a7844c2
last_name: Kowalski
- first_name: Ivana
full_name: Matijevic, Ivana
id: 83c17ce3-15b2-11ec-abd3-f486545870bd
last_name: Matijevic
citation:
ama: Loose M, Auer A, Brognara G, Budiman HR, Kowalski LM, Matijevic I. In vitro
reconstitution of small GTPase regulation. FEBS Letters. 2023;597(6):762-777.
doi:10.1002/1873-3468.14540
apa: Loose, M., Auer, A., Brognara, G., Budiman, H. R., Kowalski, L. M., & Matijevic,
I. (2023). In vitro reconstitution of small GTPase regulation. FEBS Letters.
Wiley. https://doi.org/10.1002/1873-3468.14540
chicago: Loose, Martin, Albert Auer, Gabriel Brognara, Hanifatul R Budiman, Lukasz
M Kowalski, and Ivana Matijevic. “In Vitro Reconstitution of Small GTPase Regulation.”
FEBS Letters. Wiley, 2023. https://doi.org/10.1002/1873-3468.14540.
ieee: M. Loose, A. Auer, G. Brognara, H. R. Budiman, L. M. Kowalski, and I. Matijevic,
“In vitro reconstitution of small GTPase regulation,” FEBS Letters, vol.
597, no. 6. Wiley, pp. 762–777, 2023.
ista: Loose M, Auer A, Brognara G, Budiman HR, Kowalski LM, Matijevic I. 2023. In
vitro reconstitution of small GTPase regulation. FEBS Letters. 597(6), 762–777.
mla: Loose, Martin, et al. “In Vitro Reconstitution of Small GTPase Regulation.”
FEBS Letters, vol. 597, no. 6, Wiley, 2023, pp. 762–77, doi:10.1002/1873-3468.14540.
short: M. Loose, A. Auer, G. Brognara, H.R. Budiman, L.M. Kowalski, I. Matijevic,
FEBS Letters 597 (2023) 762–777.
date_created: 2023-01-12T12:09:58Z
date_published: 2023-03-01T00:00:00Z
date_updated: 2023-08-16T08:32:29Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1002/1873-3468.14540
external_id:
isi:
- '000891573000001'
pmid:
- '36448231'
file:
- access_level: open_access
checksum: 7492244d3f9c5faa1347ef03f6e5bc84
content_type: application/pdf
creator: dernst
date_created: 2023-08-16T08:31:04Z
date_updated: 2023-08-16T08:31:04Z
file_id: '14063'
file_name: 2023_FEBSLetters_Loose.pdf
file_size: 3148143
relation: main_file
success: 1
file_date_updated: 2023-08-16T08:31:04Z
has_accepted_license: '1'
intvolume: ' 597'
isi: 1
issue: '6'
keyword:
- Cell Biology
- Genetics
- Molecular Biology
- Biochemistry
- Structural Biology
- Biophysics
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
page: 762-777
pmid: 1
publication: FEBS Letters
publication_identifier:
eissn:
- 1873-3468
issn:
- 0014-5793
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: In vitro reconstitution of small GTPase regulation
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 597
year: '2023'
...
---
_id: '10530'
abstract:
- lang: eng
text: "Cell dispersion from a confined area is fundamental in a number of biological
processes,\r\nincluding cancer metastasis. To date, a quantitative understanding
of the interplay of single\r\ncell motility, cell proliferation, and intercellular
contacts remains elusive. In particular, the role\r\nof E- and N-Cadherin junctions,
central components of intercellular contacts, is still\r\ncontroversial. Combining
theoretical modeling with in vitro observations, we investigate the\r\ncollective
spreading behavior of colonies of human cancer cells (T24). The spreading of these\r\ncolonies
is driven by stochastic single-cell migration with frequent transient cell-cell
contacts.\r\nWe find that inhibition of E- and N-Cadherin junctions decreases
colony spreading and average\r\nspreading velocities, without affecting the strength
of correlations in spreading velocities of\r\nneighboring cells. Based on a biophysical
simulation model for cell migration, we show that the\r\nbehavioral changes upon
disruption of these junctions can be explained by reduced repulsive\r\nexcluded
volume interactions between cells. This suggests that in cancer cell migration,\r\ncadherin-based
intercellular contacts sharpen cell boundaries leading to repulsive rather than\r\ncohesive
interactions between cells, thereby promoting efficient cell spreading during
collective\r\nmigration.\r\n"
acknowledgement: Funded by the Deutsche Forschungsgemeinschaft (DFG, German Research
Foundation) - Project-ID 201269156 - SFB 1032 (Projects B8 and B12). D.B.B. is supported
in part by a DFG fellowship within the Graduate School of Quantitative Biosciences
Munich (QBM) and by the Joachim Herz Stiftung.
article_processing_charge: No
article_type: original
author:
- first_name: Themistoklis
full_name: Zisis, Themistoklis
last_name: Zisis
- first_name: David
full_name: Brückner, David
id: e1e86031-6537-11eb-953a-f7ab92be508d
last_name: Brückner
orcid: 0000-0001-7205-2975
- first_name: Tom
full_name: Brandstätter, Tom
last_name: Brandstätter
- first_name: Wei Xiong
full_name: Siow, Wei Xiong
last_name: Siow
- first_name: Joseph
full_name: d’Alessandro, Joseph
last_name: d’Alessandro
- first_name: Angelika M.
full_name: Vollmar, Angelika M.
last_name: Vollmar
- first_name: Chase P.
full_name: Broedersz, Chase P.
last_name: Broedersz
- first_name: Stefan
full_name: Zahler, Stefan
last_name: Zahler
citation:
ama: Zisis T, Brückner D, Brandstätter T, et al. Disentangling cadherin-mediated
cell-cell interactions in collective cancer cell migration. Biophysical Journal.
2022;121(1):P44-60. doi:10.1016/j.bpj.2021.12.006
apa: Zisis, T., Brückner, D., Brandstätter, T., Siow, W. X., d’Alessandro, J., Vollmar,
A. M., … Zahler, S. (2022). Disentangling cadherin-mediated cell-cell interactions
in collective cancer cell migration. Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2021.12.006
chicago: Zisis, Themistoklis, David Brückner, Tom Brandstätter, Wei Xiong Siow,
Joseph d’Alessandro, Angelika M. Vollmar, Chase P. Broedersz, and Stefan Zahler.
“Disentangling Cadherin-Mediated Cell-Cell Interactions in Collective Cancer Cell
Migration.” Biophysical Journal. Elsevier, 2022. https://doi.org/10.1016/j.bpj.2021.12.006.
ieee: T. Zisis et al., “Disentangling cadherin-mediated cell-cell interactions
in collective cancer cell migration,” Biophysical Journal, vol. 121, no.
1. Elsevier, pp. P44-60, 2022.
ista: Zisis T, Brückner D, Brandstätter T, Siow WX, d’Alessandro J, Vollmar AM,
Broedersz CP, Zahler S. 2022. Disentangling cadherin-mediated cell-cell interactions
in collective cancer cell migration. Biophysical Journal. 121(1), P44-60.
mla: Zisis, Themistoklis, et al. “Disentangling Cadherin-Mediated Cell-Cell Interactions
in Collective Cancer Cell Migration.” Biophysical Journal, vol. 121, no.
1, Elsevier, 2022, pp. P44-60, doi:10.1016/j.bpj.2021.12.006.
short: T. Zisis, D. Brückner, T. Brandstätter, W.X. Siow, J. d’Alessandro, A.M.
Vollmar, C.P. Broedersz, S. Zahler, Biophysical Journal 121 (2022) P44-60.
date_created: 2021-12-10T09:48:19Z
date_published: 2022-01-04T00:00:00Z
date_updated: 2023-08-02T13:34:25Z
day: '04'
ddc:
- '570'
department:
- _id: EdHa
- _id: GaTk
doi: 10.1016/j.bpj.2021.12.006
external_id:
isi:
- '000740815400007'
file:
- access_level: open_access
checksum: 1aa7c3478e0c8256b973b632efd1f6b4
content_type: application/pdf
creator: dernst
date_created: 2022-07-29T10:17:10Z
date_updated: 2022-07-29T10:17:10Z
file_id: '11697'
file_name: 2022_BiophysicalJour_Zisis.pdf
file_size: 4475504
relation: main_file
success: 1
file_date_updated: 2022-07-29T10:17:10Z
has_accepted_license: '1'
intvolume: ' 121'
isi: 1
issue: '1'
keyword:
- Biophysics
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
page: P44-60
project:
- _id: 9B861AAC-BA93-11EA-9121-9846C619BF3A
name: NOMIS Fellowship Program
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Disentangling cadherin-mediated cell-cell interactions in collective cancer
cell migration
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 121
year: '2022'
...
---
_id: '10338'
abstract:
- lang: eng
text: In the nuclear pore complex, intrinsically disordered proteins (FG Nups),
along with their interactions with more globular proteins called nuclear transport
receptors (NTRs), are vital to the selectivity of transport into and out of the
cell nucleus. Although such interactions can be modeled at different levels of
coarse graining, in vitro experimental data have been quantitatively described
by minimal models that describe FG Nups as cohesive homogeneous polymers and NTRs
as uniformly cohesive spheres, in which the heterogeneous effects have been smeared
out. By definition, these minimal models do not account for the explicit heterogeneities
in FG Nup sequences, essentially a string of cohesive and noncohesive polymer
units, and at the NTR surface. Here, we develop computational and analytical models
that do take into account such heterogeneity in a minimal fashion and compare
them with experimental data on single-molecule interactions between FG Nups and
NTRs. Overall, we find that the heterogeneous nature of FG Nups and NTRs does
play a role in determining equilibrium binding properties but is of much greater
significance when it comes to unbinding and binding kinetics. Using our models,
we predict how binding equilibria and kinetics depend on the distribution of cohesive
blocks in the FG Nup sequences and of the binding pockets at the NTR surface,
with multivalency playing a key role. Finally, we observe that single-molecule
binding kinetics has a rather minor influence on the diffusion of NTRs in polymer
melts consisting of FG-Nup-like sequences.
article_processing_charge: No
article_type: original
author:
- first_name: Luke K.
full_name: Davis, Luke K.
last_name: Davis
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Bart W.
full_name: Hoogenboom, Bart W.
last_name: Hoogenboom
- first_name: Anton
full_name: Zilman, Anton
last_name: Zilman
citation:
ama: Davis LK, Šarić A, Hoogenboom BW, Zilman A. Physical modeling of multivalent
interactions in the nuclear pore complex. Biophysical Journal. 2021;120(9):1565-1577.
doi:10.1016/j.bpj.2021.01.039
apa: Davis, L. K., Šarić, A., Hoogenboom, B. W., & Zilman, A. (2021). Physical
modeling of multivalent interactions in the nuclear pore complex. Biophysical
Journal. Elsevier. https://doi.org/10.1016/j.bpj.2021.01.039
chicago: Davis, Luke K., Anđela Šarić, Bart W. Hoogenboom, and Anton Zilman. “Physical
Modeling of Multivalent Interactions in the Nuclear Pore Complex.” Biophysical
Journal. Elsevier, 2021. https://doi.org/10.1016/j.bpj.2021.01.039.
ieee: L. K. Davis, A. Šarić, B. W. Hoogenboom, and A. Zilman, “Physical modeling
of multivalent interactions in the nuclear pore complex,” Biophysical Journal,
vol. 120, no. 9. Elsevier, pp. 1565–1577, 2021.
ista: Davis LK, Šarić A, Hoogenboom BW, Zilman A. 2021. Physical modeling of multivalent
interactions in the nuclear pore complex. Biophysical Journal. 120(9), 1565–1577.
mla: Davis, Luke K., et al. “Physical Modeling of Multivalent Interactions in the
Nuclear Pore Complex.” Biophysical Journal, vol. 120, no. 9, Elsevier,
2021, pp. 1565–77, doi:10.1016/j.bpj.2021.01.039.
short: L.K. Davis, A. Šarić, B.W. Hoogenboom, A. Zilman, Biophysical Journal 120
(2021) 1565–1577.
date_created: 2021-11-25T15:36:36Z
date_published: 2021-02-19T00:00:00Z
date_updated: 2022-04-01T10:34:38Z
day: '19'
doi: 10.1016/j.bpj.2021.01.039
extern: '1'
external_id:
pmid:
- '33617830'
intvolume: ' 120'
issue: '9'
keyword:
- biophysics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2020.10.01.322156
month: '02'
oa: 1
oa_version: Preprint
page: 1565-1577
pmid: 1
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Physical modeling of multivalent interactions in the nuclear pore complex
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 120
year: '2021'
...
---
_id: '10340'
abstract:
- lang: eng
text: 'The cell membrane is an inhomogeneous system composed of phospholipids, sterols,
carbohydrates, and proteins that can be directly attached to underlying cytoskeleton.
The protein linkers between the membrane and the cytoskeleton are believed to
have a profound effect on the mechanical properties of the cell membrane and its
ability to reshape. Here, we investigate the role of membrane-cortex linkers on
the extrusion of membrane tubes using computer simulations and experiments. In
simulations, we find that the force for tube extrusion has a nonlinear dependence
on the density of membrane-cortex attachments: at a range of low and intermediate
linker densities, the force is not significantly influenced by the presence of
the membrane-cortex attachments and resembles that of the bare membrane. For large
concentrations of linkers, however, the force substantially increases compared
with the bare membrane. In both cases, the linkers provided membrane tubes with
increased stability against coalescence. We then pulled tubes from HEK cells using
optical tweezers for varying expression levels of the membrane-cortex attachment
protein Ezrin. In line with simulations, we observed that overexpression of Ezrin
led to an increased extrusion force, while Ezrin depletion had a negligible effect
on the force. Our results shed light on the importance of local protein rearrangements
for membrane reshaping at nanoscopic scales.'
acknowledgement: We thank Ewa Paluch, Alba Diz-Muñoz, Guillaume Salbreux, Guillaume
Charras, and Shiladitya Banerjee for helpful discussions. We acknowledge support
from the Engineering and Physical Sciences Research Council (A.P. and A.Š.), the
UCL Institute for the Physics of Living Systems (A.P., C.V.C., and A.Š.), the Royal
Society (C.V.C. and A.Š.), and the European Research Council (Starting grant EP/R011818/1
to A.Š.; E.C. and P.B. are partners of the advanced grant, project 339847) and from
Institut Curie (E.C. and P.B.) and Centre National de la Recherche Scientifique
(CNRS) (E.C. and P.B.). The P.B. and E.C. groups belong to Labex CelTisPhyBio (ANR-11-LABX0038)
and to Paris Sciences et Lettres (ANR-10-IDEX-0001-02). T.L. received a PhD grant
from Paris Sciences et Lettres Research University and support from the Institut
Curie.
article_processing_charge: No
article_type: original
author:
- first_name: Alexandru
full_name: Paraschiv, Alexandru
last_name: Paraschiv
- first_name: Thibaut J.
full_name: Lagny, Thibaut J.
last_name: Lagny
- first_name: Christian Vanhille
full_name: Campos, Christian Vanhille
last_name: Campos
- first_name: Evelyne
full_name: Coudrier, Evelyne
last_name: Coudrier
- first_name: Patricia
full_name: Bassereau, Patricia
last_name: Bassereau
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Paraschiv A, Lagny TJ, Campos CV, Coudrier E, Bassereau P, Šarić A. Influence
of membrane-cortex linkers on the extrusion of membrane tubes. Biophysical
Journal. 2021;120(4):598-606. doi:10.1016/j.bpj.2020.12.028
apa: Paraschiv, A., Lagny, T. J., Campos, C. V., Coudrier, E., Bassereau, P., &
Šarić, A. (2021). Influence of membrane-cortex linkers on the extrusion of membrane
tubes. Biophysical Journal. Cell Press. https://doi.org/10.1016/j.bpj.2020.12.028
chicago: Paraschiv, Alexandru, Thibaut J. Lagny, Christian Vanhille Campos, Evelyne
Coudrier, Patricia Bassereau, and Anđela Šarić. “Influence of Membrane-Cortex
Linkers on the Extrusion of Membrane Tubes.” Biophysical Journal. Cell
Press, 2021. https://doi.org/10.1016/j.bpj.2020.12.028.
ieee: A. Paraschiv, T. J. Lagny, C. V. Campos, E. Coudrier, P. Bassereau, and A.
Šarić, “Influence of membrane-cortex linkers on the extrusion of membrane tubes,”
Biophysical Journal, vol. 120, no. 4. Cell Press, pp. 598–606, 2021.
ista: Paraschiv A, Lagny TJ, Campos CV, Coudrier E, Bassereau P, Šarić A. 2021.
Influence of membrane-cortex linkers on the extrusion of membrane tubes. Biophysical
Journal. 120(4), 598–606.
mla: Paraschiv, Alexandru, et al. “Influence of Membrane-Cortex Linkers on the Extrusion
of Membrane Tubes.” Biophysical Journal, vol. 120, no. 4, Cell Press, 2021,
pp. 598–606, doi:10.1016/j.bpj.2020.12.028.
short: A. Paraschiv, T.J. Lagny, C.V. Campos, E. Coudrier, P. Bassereau, A. Šarić,
Biophysical Journal 120 (2021) 598–606.
date_created: 2021-11-25T16:18:23Z
date_published: 2021-01-16T00:00:00Z
date_updated: 2022-04-01T10:38:01Z
day: '16'
doi: 10.1016/j.bpj.2020.12.028
extern: '1'
external_id:
pmid:
- '33460596'
intvolume: ' 120'
issue: '4'
keyword:
- biophysics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2020.07.28.224741
month: '01'
oa: 1
oa_version: Preprint
page: 598-606
pmid: 1
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Influence of membrane-cortex linkers on the extrusion of membrane tubes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 120
year: '2021'
...
---
_id: '10406'
abstract:
- lang: eng
text: Multicellular organisms develop complex shapes from much simpler, single-celled
zygotes through a process commonly called morphogenesis. Morphogenesis involves
an interplay between several factors, ranging from the gene regulatory networks
determining cell fate and differentiation to the mechanical processes underlying
cell and tissue shape changes. Thus, the study of morphogenesis has historically
been based on multidisciplinary approaches at the interface of biology with physics
and mathematics. Recent technological advances have further improved our ability
to study morphogenesis by bridging the gap between the genetic and biophysical
factors through the development of new tools for visualizing, analyzing, and perturbing
these factors and their biochemical intermediaries. Here, we review how a combination
of genetic, microscopic, biophysical, and biochemical approaches has aided our
attempts to understand morphogenesis and discuss potential approaches that may
be beneficial to such an inquiry in the future.
acknowledgement: The authors would like to thank Feyza Nur Arslan, Suyash Naik, Diana
Pinheiro, Alexandra Schauer, and Shayan Shamipour for their comments on the draft.
N.M. is supported by an ISTplus postdoctoral fellowship (H2020 Marie-Sklodowska-Curie
COFUND Action).
article_processing_charge: No
article_type: original
author:
- first_name: Nikhil
full_name: Mishra, Nikhil
id: C4D70E82-1081-11EA-B3ED-9A4C3DDC885E
last_name: Mishra
orcid: 0000-0002-6425-5788
- first_name: Carl-Philipp J
full_name: Heisenberg, Carl-Philipp J
id: 39427864-F248-11E8-B48F-1D18A9856A87
last_name: Heisenberg
orcid: 0000-0002-0912-4566
citation:
ama: Mishra N, Heisenberg C-PJ. Dissecting organismal morphogenesis by bridging
genetics and biophysics. Annual Review of Genetics. 2021;55:209-233. doi:10.1146/annurev-genet-071819-103748
apa: Mishra, N., & Heisenberg, C.-P. J. (2021). Dissecting organismal morphogenesis
by bridging genetics and biophysics. Annual Review of Genetics. Annual
Reviews. https://doi.org/10.1146/annurev-genet-071819-103748
chicago: Mishra, Nikhil, and Carl-Philipp J Heisenberg. “Dissecting Organismal Morphogenesis
by Bridging Genetics and Biophysics.” Annual Review of Genetics. Annual
Reviews, 2021. https://doi.org/10.1146/annurev-genet-071819-103748.
ieee: N. Mishra and C.-P. J. Heisenberg, “Dissecting organismal morphogenesis by
bridging genetics and biophysics,” Annual Review of Genetics, vol. 55.
Annual Reviews, pp. 209–233, 2021.
ista: Mishra N, Heisenberg C-PJ. 2021. Dissecting organismal morphogenesis by bridging
genetics and biophysics. Annual Review of Genetics. 55, 209–233.
mla: Mishra, Nikhil, and Carl-Philipp J. Heisenberg. “Dissecting Organismal Morphogenesis
by Bridging Genetics and Biophysics.” Annual Review of Genetics, vol. 55,
Annual Reviews, 2021, pp. 209–33, doi:10.1146/annurev-genet-071819-103748.
short: N. Mishra, C.-P.J. Heisenberg, Annual Review of Genetics 55 (2021) 209–233.
date_created: 2021-12-05T23:01:41Z
date_published: 2021-08-30T00:00:00Z
date_updated: 2023-08-14T13:05:13Z
day: '30'
department:
- _id: CaHe
doi: 10.1146/annurev-genet-071819-103748
ec_funded: 1
external_id:
isi:
- '000747220900010'
pmid:
- '34460295'
intvolume: ' 55'
isi: 1
keyword:
- morphogenesis
- forward genetics
- high-resolution microscopy
- biophysics
- biochemistry
- patterning
language:
- iso: eng
month: '08'
oa_version: None
page: 209-233
pmid: 1
project:
- _id: 260C2330-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '754411'
name: ISTplus - Postdoctoral Fellowships
publication: Annual Review of Genetics
publication_identifier:
eissn:
- 1545-2948
issn:
- 0066-4197
publication_status: published
publisher: Annual Reviews
quality_controlled: '1'
scopus_import: '1'
status: public
title: Dissecting organismal morphogenesis by bridging genetics and biophysics
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 55
year: '2021'
...
---
_id: '10346'
abstract:
- lang: eng
text: One of the most robust examples of self-assembly in living organisms is the
formation of collagen architectures. Collagen type I molecules are a crucial component
of the extracellular matrix, where they self-assemble into fibrils of well-defined
axial striped patterns. This striped fibrillar pattern is preserved across the
animal kingdom and is important for the determination of cell phenotype, cell
adhesion, and tissue regulation and signaling. The understanding of the physical
processes that determine such a robust morphology of self-assembled collagen fibrils
is currently almost completely missing. Here, we develop a minimal coarse-grained
computational model to identify the physical principles of the assembly of collagen-mimetic
molecules. We find that screened electrostatic interactions can drive the formation
of collagen-like filaments of well-defined striped morphologies. The fibril axial
pattern is determined solely by the distribution of charges on the molecule and
is robust to the changes in protein concentration, monomer rigidity, and environmental
conditions. We show that the striped fibrillar pattern cannot be easily predicted
from the interactions between two monomers but is an emergent result of multibody
interactions. Our results can help address collagen remodeling in diseases and
aging and guide the design of collagen scaffolds for biotechnological applications.
acknowledgement: We thank Melinda Duer, Patrick Mesquida, Lucy Colwell, Lucie Liu,
Daan Frenkel, and Ivan Palaia for helpful discussions. We acknowledge support from
the Engineering and Physical Sciences Research Council (A.E.H., L.K.D., and A.Š.),
Biotechnology and Biological Sciences Research Council LIDo programme (N.G.G. and
C.A.B.), the Royal Society (A.Š.), and the UK Materials and Molecular Modelling
Hub for computational resources, which is partially funded by EPSRC ( EP/P020194/1).
article_processing_charge: No
article_type: original
author:
- first_name: Anne E.
full_name: Hafner, Anne E.
last_name: Hafner
- first_name: Noemi G.
full_name: Gyori, Noemi G.
last_name: Gyori
- first_name: Ciaran A.
full_name: Bench, Ciaran A.
last_name: Bench
- first_name: Luke K.
full_name: Davis, Luke K.
last_name: Davis
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Hafner AE, Gyori NG, Bench CA, Davis LK, Šarić A. Modeling fibrillogenesis
of collagen-mimetic molecules. Biophysical Journal. 2020;119(9):1791-1799.
doi:10.1016/j.bpj.2020.09.013
apa: Hafner, A. E., Gyori, N. G., Bench, C. A., Davis, L. K., & Šarić, A. (2020).
Modeling fibrillogenesis of collagen-mimetic molecules. Biophysical Journal.
Cell Press. https://doi.org/10.1016/j.bpj.2020.09.013
chicago: Hafner, Anne E., Noemi G. Gyori, Ciaran A. Bench, Luke K. Davis, and Anđela
Šarić. “Modeling Fibrillogenesis of Collagen-Mimetic Molecules.” Biophysical
Journal. Cell Press, 2020. https://doi.org/10.1016/j.bpj.2020.09.013.
ieee: A. E. Hafner, N. G. Gyori, C. A. Bench, L. K. Davis, and A. Šarić, “Modeling
fibrillogenesis of collagen-mimetic molecules,” Biophysical Journal, vol.
119, no. 9. Cell Press, pp. 1791–1799, 2020.
ista: Hafner AE, Gyori NG, Bench CA, Davis LK, Šarić A. 2020. Modeling fibrillogenesis
of collagen-mimetic molecules. Biophysical Journal. 119(9), 1791–1799.
mla: Hafner, Anne E., et al. “Modeling Fibrillogenesis of Collagen-Mimetic Molecules.”
Biophysical Journal, vol. 119, no. 9, Cell Press, 2020, pp. 1791–99, doi:10.1016/j.bpj.2020.09.013.
short: A.E. Hafner, N.G. Gyori, C.A. Bench, L.K. Davis, A. Šarić, Biophysical Journal
119 (2020) 1791–1799.
date_created: 2021-11-26T07:27:24Z
date_published: 2020-09-23T00:00:00Z
date_updated: 2021-11-26T07:45:24Z
day: '23'
doi: 10.1016/j.bpj.2020.09.013
extern: '1'
external_id:
pmid:
- '33049216'
intvolume: ' 119'
issue: '9'
keyword:
- biophysics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.06.08.140061v1
month: '09'
oa: 1
oa_version: Published Version
page: 1791-1799
pmid: 1
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Modeling fibrillogenesis of collagen-mimetic molecules
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 119
year: '2020'
...
---
_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: '6371'
abstract:
- lang: eng
text: "Decades of studies have revealed the mechanisms of gene regulation in molecular
detail. We make use of such well-described regulatory systems to explore how the
molecular mechanisms of protein-protein and protein-DNA interactions shape the
dynamics and evolution of gene regulation. \r\n\r\ni) We uncover how the biophysics
of protein-DNA binding determines the potential of regulatory networks to evolve
and adapt, which can be captured using a simple mathematical model. \r\nii) The
evolution of regulatory connections can lead to a significant amount of crosstalk
between binding proteins. We explore the effect of crosstalk on gene expression
from a target promoter, which seems to be modulated through binding competition
at non-specific DNA sites. \r\niii) We investigate how the very same biophysical
characteristics as in i) can generate significant fitness costs for cells through
global crosstalk, meaning non-specific DNA binding across the genomic background.
\r\niv) Binding competition between proteins at a target promoter is a prevailing
regulatory feature due to the prevalence of co-regulation at bacterial promoters.
However, the dynamics of these systems are not always straightforward to determine
even if the molecular mechanisms of regulation are known. A detailed model of
the biophysical interactions reveals that interference between the regulatory
proteins can constitute a new, generic form of system memory that records the
history of the input signals at the promoter. \r\n\r\nWe demonstrate how the biophysics
of protein-DNA binding can be harnessed to investigate the principles that shape
and ultimately limit cellular gene regulation. These results provide a basis for
studies of higher-level functionality, which arises from the underlying regulation.
\ \r\n"
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Claudia
full_name: Igler, Claudia
id: 46613666-F248-11E8-B48F-1D18A9856A87
last_name: Igler
citation:
ama: Igler C. On the nature of gene regulatory design - The biophysics of transcription
factor binding shapes gene regulation. 2019. doi:10.15479/AT:ISTA:6371
apa: Igler, C. (2019). On the nature of gene regulatory design - The biophysics
of transcription factor binding shapes gene regulation. Institute of Science
and Technology Austria. https://doi.org/10.15479/AT:ISTA:6371
chicago: Igler, Claudia. “On the Nature of Gene Regulatory Design - The Biophysics
of Transcription Factor Binding Shapes Gene Regulation.” Institute of Science
and Technology Austria, 2019. https://doi.org/10.15479/AT:ISTA:6371.
ieee: C. Igler, “On the nature of gene regulatory design - The biophysics of transcription
factor binding shapes gene regulation,” Institute of Science and Technology Austria,
2019.
ista: Igler C. 2019. On the nature of gene regulatory design - The biophysics of
transcription factor binding shapes gene regulation. Institute of Science and
Technology Austria.
mla: Igler, Claudia. On the Nature of Gene Regulatory Design - The Biophysics
of Transcription Factor Binding Shapes Gene Regulation. Institute of Science
and Technology Austria, 2019, doi:10.15479/AT:ISTA:6371.
short: C. Igler, On the Nature of Gene Regulatory Design - The Biophysics of Transcription
Factor Binding Shapes Gene Regulation, Institute of Science and Technology Austria,
2019.
date_created: 2019-05-03T11:55:51Z
date_published: 2019-05-03T00:00:00Z
date_updated: 2024-02-21T13:45:52Z
day: '03'
ddc:
- '576'
- '579'
degree_awarded: PhD
department:
- _id: CaGu
doi: 10.15479/AT:ISTA:6371
file:
- access_level: open_access
checksum: c0085d47c58c9cbcab1b0a783480f6da
content_type: application/pdf
creator: cigler
date_created: 2019-05-03T11:54:52Z
date_updated: 2021-02-11T11:17:13Z
embargo: 2020-05-02
file_id: '6373'
file_name: IglerClaudia_OntheNatureofGeneRegulatoryDesign.pdf
file_size: 12597663
relation: main_file
- access_level: closed
checksum: 2eac954de1c8bbf7e6fb35ed0221ae8c
content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document
creator: cigler
date_created: 2019-05-03T11:54:54Z
date_updated: 2020-07-14T12:47:28Z
embargo_to: open_access
file_id: '6374'
file_name: IglerClaudia_OntheNatureofGeneRegulatoryDesign.docx
file_size: 34644426
relation: source_file
file_date_updated: 2021-02-11T11:17:13Z
has_accepted_license: '1'
keyword:
- gene regulation
- biophysics
- transcription factor binding
- bacteria
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
page: '152'
project:
- _id: 251EE76E-B435-11E9-9278-68D0E5697425
grant_number: '24573'
name: Design principles underlying genetic switch architecture (DOC Fellowship)
publication_identifier:
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '67'
relation: part_of_dissertation
status: public
- id: '5585'
relation: popular_science
status: public
status: public
supervisor:
- first_name: Calin C
full_name: Guet, Calin C
id: 47F8433E-F248-11E8-B48F-1D18A9856A87
last_name: Guet
orcid: 0000-0001-6220-2052
title: On the nature of gene regulatory design - The biophysics of transcription factor
binding shapes gene regulation
type: dissertation
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
year: '2019'
...
---
_id: '8444'
abstract:
- lang: eng
text: Biophysical investigation of membrane proteins generally requires their extraction
from native sources using detergents, a step that can lead, possibly irreversibly,
to protein denaturation. The propensity of dodecylphosphocholine (DPC), a detergent
widely utilized in NMR studies of membrane proteins, to distort their structure
has been the subject of much controversy. It has been recently proposed that the
binding specificity of the yeast mitochondrial ADP/ATP carrier (yAAC3) toward
cardiolipins is preserved in DPC, thereby suggesting that DPC is a suitable environment
in which to study membrane proteins. In this communication, we used all-atom molecular
dynamics simulations to investigate the specific binding of cardiolipins to yAAC3.
Our data demonstrate that the interaction interface observed in a native-like
environment differs markedly from that inferred from an NMR investigation in DPC,
implying that in this detergent, the protein structure is distorted. We further
investigated yAAC3 solubilized in DPC and in the milder dodecylmaltoside with
thermal-shift assays. The loss of thermal transition observed in DPC confirms
that the protein is no longer properly folded in this environment.
article_processing_charge: No
article_type: original
author:
- first_name: François
full_name: Dehez, François
last_name: Dehez
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Martin S.
full_name: King, Martin S.
last_name: King
- first_name: Edmund R.S.
full_name: Kunji, Edmund R.S.
last_name: Kunji
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
citation:
ama: Dehez F, Schanda P, King MS, Kunji ERS, Chipot C. Mitochondrial ADP/ATP carrier
in dodecylphosphocholine binds cardiolipins with non-native affinity. Biophysical
Journal. 2017;113(11):2311-2315. doi:10.1016/j.bpj.2017.09.019
apa: Dehez, F., Schanda, P., King, M. S., Kunji, E. R. S., & Chipot, C. (2017).
Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with
non-native affinity. Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2017.09.019
chicago: Dehez, François, Paul Schanda, Martin S. King, Edmund R.S. Kunji, and Christophe
Chipot. “Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine Binds Cardiolipins
with Non-Native Affinity.” Biophysical Journal. Elsevier, 2017. https://doi.org/10.1016/j.bpj.2017.09.019.
ieee: F. Dehez, P. Schanda, M. S. King, E. R. S. Kunji, and C. Chipot, “Mitochondrial
ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with non-native affinity,”
Biophysical Journal, vol. 113, no. 11. Elsevier, pp. 2311–2315, 2017.
ista: Dehez F, Schanda P, King MS, Kunji ERS, Chipot C. 2017. Mitochondrial ADP/ATP
carrier in dodecylphosphocholine binds cardiolipins with non-native affinity.
Biophysical Journal. 113(11), 2311–2315.
mla: Dehez, François, et al. “Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine
Binds Cardiolipins with Non-Native Affinity.” Biophysical Journal, vol.
113, no. 11, Elsevier, 2017, pp. 2311–15, doi:10.1016/j.bpj.2017.09.019.
short: F. Dehez, P. Schanda, M.S. King, E.R.S. Kunji, C. Chipot, Biophysical Journal
113 (2017) 2311–2315.
date_created: 2020-09-18T10:05:54Z
date_published: 2017-12-05T00:00:00Z
date_updated: 2021-01-12T08:19:18Z
day: '05'
doi: 10.1016/j.bpj.2017.09.019
extern: '1'
intvolume: ' 113'
issue: '11'
keyword:
- Biophysics
language:
- iso: eng
month: '12'
oa_version: None
page: 2311-2315
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Mitochondrial ADP/ATP carrier in dodecylphosphocholine binds cardiolipins with
non-native affinity
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 113
year: '2017'
...
---
_id: '8448'
abstract:
- lang: eng
text: We present an improved fast mixing device based on the rapid mixing of two
solutions inside the NMR probe, as originally proposed by Hore and coworkers (J.
Am. Chem. Soc. 125 (2003) 12484–12492). Such a device is important for off-equilibrium
studies of molecular kinetics by multidimensional real-time NMR spectrsocopy.
The novelty of this device is that it allows removing the injector from the NMR
detection volume after mixing, and thus provides good magnetic field homogeneity
independently of the initial sample volume placed in the NMR probe. The apparatus
is simple to build, inexpensive, and can be used without any hardware modification
on any type of liquid-state NMR spectrometer. We demonstrate the performance of
our fast mixing device in terms of improved magnetic field homogeneity, and show
an application to the study of protein folding and the structural characterization
of transiently populated folding intermediates.
article_processing_charge: No
article_type: original
author:
- first_name: Rémi
full_name: Franco, Rémi
last_name: Franco
- first_name: Adrien
full_name: Favier, Adrien
last_name: Favier
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Franco R, Favier A, Schanda P, Brutscher B. Optimized fast mixing device for
real-time NMR applications. Journal of Magnetic Resonance. 2017;281(8):125-129.
doi:10.1016/j.jmr.2017.05.016
apa: Franco, R., Favier, A., Schanda, P., & Brutscher, B. (2017). Optimized
fast mixing device for real-time NMR applications. Journal of Magnetic Resonance.
Elsevier. https://doi.org/10.1016/j.jmr.2017.05.016
chicago: Franco, Rémi, Adrien Favier, Paul Schanda, and Bernhard Brutscher. “Optimized
Fast Mixing Device for Real-Time NMR Applications.” Journal of Magnetic Resonance.
Elsevier, 2017. https://doi.org/10.1016/j.jmr.2017.05.016.
ieee: R. Franco, A. Favier, P. Schanda, and B. Brutscher, “Optimized fast mixing
device for real-time NMR applications,” Journal of Magnetic Resonance,
vol. 281, no. 8. Elsevier, pp. 125–129, 2017.
ista: Franco R, Favier A, Schanda P, Brutscher B. 2017. Optimized fast mixing device
for real-time NMR applications. Journal of Magnetic Resonance. 281(8), 125–129.
mla: Franco, Rémi, et al. “Optimized Fast Mixing Device for Real-Time NMR Applications.”
Journal of Magnetic Resonance, vol. 281, no. 8, Elsevier, 2017, pp. 125–29,
doi:10.1016/j.jmr.2017.05.016.
short: R. Franco, A. Favier, P. Schanda, B. Brutscher, Journal of Magnetic Resonance
281 (2017) 125–129.
date_created: 2020-09-18T10:06:27Z
date_published: 2017-08-01T00:00:00Z
date_updated: 2021-01-12T08:19:20Z
day: '01'
doi: 10.1016/j.jmr.2017.05.016
extern: '1'
intvolume: ' 281'
issue: '8'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '08'
oa_version: None
page: 125-129
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Optimized fast mixing device for real-time NMR applications
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 281
year: '2017'
...
---
_id: '14308'
abstract:
- lang: eng
text: Here we describe an approach to bottom-up fabrication with nanometer-precision
that allows integrating the functional diversity of proteins in designed three-dimensional
structural frameworks. We reimagined the successful DNA origami design principle
using a set of custom staple proteins to fold a double-stranded DNA template into
a user-defined shape. Each staple protein recognizes two distinct double-helical
DNA sequences and can carry additional functionalities. The staple proteins we
present here are based on the transcription activator-like (TAL) effector proteins.
Due to their repetitive structure these proteins offer a unique programmability
that enables us to construct numerous staple proteins targeting any desired DNA
sequence. Our approach is general, meaning that many different objects may be
created using the same set of rules, and it is modular, because components can
be modified or exchanged individually. We present rules for constructing megadalton-scale
DNA-protein hybrid nanostructures; introduce important structural motifs, such
as curvature, corners, and vertices; describe principles for creating multi-layer
DNA-protein objects with enhanced rigidity; and demonstrate the possibility to
combine our DNA-protein hybrid origami with conventional DNA nanotechnology. Since
all components can be encoded genetically, our structures should be amenable to
biotechnological mass-production. Moreover, since the target objects can self-assemble
at room temperature in near-physiological buffer, our hybrid origami may also
provide an attractive method to realize positioning and scaffolding tasks in vivo.
We expect our method to find application both in scaffolding protein functionalities
and in manipulating the spatial arrangement of genomic DNA.
article_number: 25a
article_processing_charge: No
article_type: original
author:
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
citation:
ama: Praetorius FM, Dietz H. Genetically encoded DNA-protein hybrid origami. Biophysical
Journal. 2017;112(3). doi:10.1016/j.bpj.2016.11.171
apa: Praetorius, F. M., & Dietz, H. (2017). Genetically encoded DNA-protein
hybrid origami. Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2016.11.171
chicago: Praetorius, Florian M, and Hendrik Dietz. “Genetically Encoded DNA-Protein
Hybrid Origami.” Biophysical Journal. Elsevier, 2017. https://doi.org/10.1016/j.bpj.2016.11.171.
ieee: F. M. Praetorius and H. Dietz, “Genetically encoded DNA-protein hybrid origami,”
Biophysical Journal, vol. 112, no. 3. Elsevier, 2017.
ista: Praetorius FM, Dietz H. 2017. Genetically encoded DNA-protein hybrid origami.
Biophysical Journal. 112(3), 25a.
mla: Praetorius, Florian M., and Hendrik Dietz. “Genetically Encoded DNA-Protein
Hybrid Origami.” Biophysical Journal, vol. 112, no. 3, 25a, Elsevier, 2017,
doi:10.1016/j.bpj.2016.11.171.
short: F.M. Praetorius, H. Dietz, Biophysical Journal 112 (2017).
date_created: 2023-09-06T13:19:10Z
date_published: 2017-02-03T00:00:00Z
date_updated: 2023-11-07T11:28:58Z
day: '03'
doi: 10.1016/j.bpj.2016.11.171
extern: '1'
intvolume: ' 112'
issue: '3'
keyword:
- Biophysics
language:
- iso: eng
month: '02'
oa_version: None
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Genetically encoded DNA-protein hybrid origami
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 112
year: '2017'
...
---
_id: '10126'
article_number: 391a
article_processing_charge: No
article_type: letter_note
author:
- first_name: Afshin
full_name: Vahid Belarghou, Afshin
last_name: Vahid Belarghou
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Timon
full_name: Idema, Timon
last_name: Idema
citation:
ama: Vahid Belarghou A, Šarić A, Idema T. Curvature mediated interactions in highly
curved membranes. Biophysical Journal. 2017;112(3). doi:10.1016/j.bpj.2016.11.2123
apa: Vahid Belarghou, A., Šarić, A., & Idema, T. (2017). Curvature mediated
interactions in highly curved membranes. Biophysical Journal. Elsevier
. https://doi.org/10.1016/j.bpj.2016.11.2123
chicago: Vahid Belarghou, Afshin, Anđela Šarić, and Timon Idema. “Curvature Mediated
Interactions in Highly Curved Membranes.” Biophysical Journal. Elsevier
, 2017. https://doi.org/10.1016/j.bpj.2016.11.2123.
ieee: A. Vahid Belarghou, A. Šarić, and T. Idema, “Curvature mediated interactions
in highly curved membranes,” Biophysical Journal, vol. 112, no. 3. Elsevier
, 2017.
ista: Vahid Belarghou A, Šarić A, Idema T. 2017. Curvature mediated interactions
in highly curved membranes. Biophysical Journal. 112(3), 391a.
mla: Vahid Belarghou, Afshin, et al. “Curvature Mediated Interactions in Highly
Curved Membranes.” Biophysical Journal, vol. 112, no. 3, 391a, Elsevier
, 2017, doi:10.1016/j.bpj.2016.11.2123.
short: A. Vahid Belarghou, A. Šarić, T. Idema, Biophysical Journal 112 (2017).
date_created: 2021-10-12T07:47:55Z
date_published: 2017-02-03T00:00:00Z
date_updated: 2021-11-03T10:02:45Z
day: '03'
doi: 10.1016/j.bpj.2016.11.2123
extern: '1'
intvolume: ' 112'
issue: '3'
keyword:
- biophysics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.cell.com/biophysj/fulltext/S0006-3495(16)33153-8
month: '02'
oa: 1
oa_version: Published Version
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: 'Elsevier '
quality_controlled: '1'
status: public
title: Curvature mediated interactions in highly curved membranes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 112
year: '2017'
...
---
_id: '11088'
abstract:
- lang: eng
text: 'The crowded intracellular environment poses a formidable challenge to experimental
and theoretical analyses of intracellular transport mechanisms. Our measurements
of single-particle trajectories in cytoplasm and their random-walk interpretations
elucidate two of these mechanisms: molecular diffusion in crowded environments
and cytoskeletal transport along microtubules. We employed acousto-optic deflector
microscopy to map out the three-dimensional trajectories of microspheres migrating
in the cytosolic fraction of a cellular extract. Classical Brownian motion (BM),
continuous time random walk, and fractional BM were alternatively used to represent
these trajectories. The comparison of the experimental and numerical data demonstrates
that cytoskeletal transport along microtubules and diffusion in the cytosolic
fraction exhibit anomalous (nonFickian) behavior and posses statistically distinct
signatures. Among the three random-walk models used, continuous time random walk
provides the best representation of diffusion, whereas microtubular transport
is accurately modeled with fractional BM.'
article_processing_charge: No
article_type: original
author:
- first_name: Benjamin M.
full_name: Regner, Benjamin M.
last_name: Regner
- first_name: Dejan
full_name: Vučinić, Dejan
last_name: Vučinić
- first_name: Cristina
full_name: Domnisoru, Cristina
last_name: Domnisoru
- first_name: Thomas M.
full_name: Bartol, Thomas M.
last_name: Bartol
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
- first_name: Daniel M.
full_name: Tartakovsky, Daniel M.
last_name: Tartakovsky
- first_name: Terrence J.
full_name: Sejnowski, Terrence J.
last_name: Sejnowski
citation:
ama: Regner BM, Vučinić D, Domnisoru C, et al. Anomalous diffusion of single particles
in cytoplasm. Biophysical Journal. 2013;104(8):1652-1660. doi:10.1016/j.bpj.2013.01.049
apa: Regner, B. M., Vučinić, D., Domnisoru, C., Bartol, T. M., Hetzer, M., Tartakovsky,
D. M., & Sejnowski, T. J. (2013). Anomalous diffusion of single particles
in cytoplasm. Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2013.01.049
chicago: Regner, Benjamin M., Dejan Vučinić, Cristina Domnisoru, Thomas M. Bartol,
Martin Hetzer, Daniel M. Tartakovsky, and Terrence J. Sejnowski. “Anomalous Diffusion
of Single Particles in Cytoplasm.” Biophysical Journal. Elsevier, 2013.
https://doi.org/10.1016/j.bpj.2013.01.049.
ieee: B. M. Regner et al., “Anomalous diffusion of single particles in cytoplasm,”
Biophysical Journal, vol. 104, no. 8. Elsevier, pp. 1652–1660, 2013.
ista: Regner BM, Vučinić D, Domnisoru C, Bartol TM, Hetzer M, Tartakovsky DM, Sejnowski
TJ. 2013. Anomalous diffusion of single particles in cytoplasm. Biophysical Journal.
104(8), 1652–1660.
mla: Regner, Benjamin M., et al. “Anomalous Diffusion of Single Particles in Cytoplasm.”
Biophysical Journal, vol. 104, no. 8, Elsevier, 2013, pp. 1652–60, doi:10.1016/j.bpj.2013.01.049.
short: B.M. Regner, D. Vučinić, C. Domnisoru, T.M. Bartol, M. Hetzer, D.M. Tartakovsky,
T.J. Sejnowski, Biophysical Journal 104 (2013) 1652–1660.
date_created: 2022-04-07T07:51:26Z
date_published: 2013-04-16T00:00:00Z
date_updated: 2022-07-18T08:51:01Z
day: '16'
doi: 10.1016/j.bpj.2013.01.049
extern: '1'
external_id:
pmid:
- '23601312'
intvolume: ' 104'
issue: '8'
keyword:
- Biophysics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.bpj.2013.01.049
month: '04'
oa: 1
oa_version: Published Version
page: 1652-1660
pmid: 1
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Anomalous diffusion of single particles in cytoplasm
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 104
year: '2013'
...
---
_id: '8469'
abstract:
- lang: eng
text: The accurate experimental determination of dipolar-coupling constants for
one-bond heteronuclear dipolar couplings in solids is a key for the quantification
of the amplitudes of motional processes. Averaging of the dipolar coupling reports
on motions on time scales up to the inverse of the coupling constant, in our case
tens of microseconds. Combining dipolar-coupling derived order parameters that
characterize the amplitudes of the motion with relaxation data leads to a more
precise characterization of the dynamical parameters and helps to disentangle
the amplitudes and the time scales of the motional processes, which impact relaxation
rates in a highly correlated way. Here. we describe and characterize an improved
experimental protocol – based on REDOR – to measure these couplings in perdeuterated
proteins with a reduced sensitivity to experimental missettings. Because such
effects are presently the dominant source of systematic errors in experimental
dipolar-coupling measurements, these compensated experiments should help to significantly
improve the precision of such data. A detailed comparison with other commonly
used pulse sequences (T-MREV, phase-inverted CP,R18 5/2, and R18 7/1) is provided.
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
- first_name: Beat H.
full_name: Meier, Beat H.
last_name: Meier
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
citation:
ama: Schanda P, Meier BH, Ernst M. Accurate measurement of one-bond H–X heteronuclear
dipolar couplings in MAS solid-state NMR. Journal of Magnetic Resonance.
2011;210(2):246-259. doi:10.1016/j.jmr.2011.03.015
apa: Schanda, P., Meier, B. H., & Ernst, M. (2011). Accurate measurement of
one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR. Journal
of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2011.03.015
chicago: Schanda, Paul, Beat H. Meier, and Matthias Ernst. “Accurate Measurement
of One-Bond H–X Heteronuclear Dipolar Couplings in MAS Solid-State NMR.” Journal
of Magnetic Resonance. Elsevier, 2011. https://doi.org/10.1016/j.jmr.2011.03.015.
ieee: P. Schanda, B. H. Meier, and M. Ernst, “Accurate measurement of one-bond H–X
heteronuclear dipolar couplings in MAS solid-state NMR,” Journal of Magnetic
Resonance, vol. 210, no. 2. Elsevier, pp. 246–259, 2011.
ista: Schanda P, Meier BH, Ernst M. 2011. Accurate measurement of one-bond H–X heteronuclear
dipolar couplings in MAS solid-state NMR. Journal of Magnetic Resonance. 210(2),
246–259.
mla: Schanda, Paul, et al. “Accurate Measurement of One-Bond H–X Heteronuclear Dipolar
Couplings in MAS Solid-State NMR.” Journal of Magnetic Resonance, vol.
210, no. 2, Elsevier, 2011, pp. 246–59, doi:10.1016/j.jmr.2011.03.015.
short: P. Schanda, B.H. Meier, M. Ernst, Journal of Magnetic Resonance 210 (2011)
246–259.
date_created: 2020-09-18T10:10:50Z
date_published: 2011-06-01T00:00:00Z
date_updated: 2021-01-12T08:19:29Z
day: '01'
doi: 10.1016/j.jmr.2011.03.015
extern: '1'
intvolume: ' 210'
issue: '2'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '06'
oa_version: None
page: 246-259
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS
solid-state NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 210
year: '2011'
...
---
_id: '8482'
abstract:
- lang: eng
text: The SOFAST-HMQC experiment [P. Schanda, B. Brutscher, Very fast two-dimensional
NMR spectroscopy for real-time investigation of dynamic events in proteins on
the time scale of seconds, J. Am. Chem. Soc. 127 (2005) 8014–8015] allows recording
two-dimensional correlation spectra of macromolecules such as proteins in only
a few seconds acquisition time. To achieve the highest possible sensitivity, SOFAST-HMQC
experiments are preferably performed on high-field NMR spectrometers equipped
with cryogenically cooled probes. The duty cycle of over 80% in fast-pulsing SOFAST-HMQC
experiments, however, may cause problems when using a cryogenic probe. Here we
introduce SE-IPAP-SOFAST-HMQC, a new pulse sequence that provides comparable sensitivity
to standard SOFAST-HMQC, while avoiding heteronuclear decoupling during 1H detection,
and thus significantly reducing the radiofrequency load of the probe during the
experiment. The experiment is also attractive for fast and sensitive measurement
of heteronuclear one-bond spin coupling constants.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Thomas
full_name: Kern, Thomas
last_name: Kern
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Kern T, Schanda P, Brutscher B. Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing
2D NMR with reduced radiofrequency load. Journal of Magnetic Resonance.
2008;190(2):333-338. doi:10.1016/j.jmr.2007.11.015
apa: Kern, T., Schanda, P., & Brutscher, B. (2008). Sensitivity-enhanced IPAP-SOFAST-HMQC
for fast-pulsing 2D NMR with reduced radiofrequency load. Journal of Magnetic
Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2007.11.015
chicago: Kern, Thomas, Paul Schanda, and Bernhard Brutscher. “Sensitivity-Enhanced
IPAP-SOFAST-HMQC for Fast-Pulsing 2D NMR with Reduced Radiofrequency Load.” Journal
of Magnetic Resonance. Elsevier, 2008. https://doi.org/10.1016/j.jmr.2007.11.015.
ieee: T. Kern, P. Schanda, and B. Brutscher, “Sensitivity-enhanced IPAP-SOFAST-HMQC
for fast-pulsing 2D NMR with reduced radiofrequency load,” Journal of Magnetic
Resonance, vol. 190, no. 2. Elsevier, pp. 333–338, 2008.
ista: Kern T, Schanda P, Brutscher B. 2008. Sensitivity-enhanced IPAP-SOFAST-HMQC
for fast-pulsing 2D NMR with reduced radiofrequency load. Journal of Magnetic
Resonance. 190(2), 333–338.
mla: Kern, Thomas, et al. “Sensitivity-Enhanced IPAP-SOFAST-HMQC for Fast-Pulsing
2D NMR with Reduced Radiofrequency Load.” Journal of Magnetic Resonance,
vol. 190, no. 2, Elsevier, 2008, pp. 333–38, doi:10.1016/j.jmr.2007.11.015.
short: T. Kern, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 190 (2008)
333–338.
date_created: 2020-09-18T10:12:46Z
date_published: 2008-02-01T00:00:00Z
date_updated: 2021-01-12T08:19:35Z
day: '01'
doi: 10.1016/j.jmr.2007.11.015
extern: '1'
intvolume: ' 190'
issue: '2'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '02'
oa_version: None
page: 333-338
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced
radiofrequency load
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 190
year: '2008'
...
---
_id: '8490'
abstract:
- lang: eng
text: We demonstrate the feasibility of recording 1H–15N correlation spectra of
proteins in only one second of acquisition time. The experiment combines recently
proposed SOFAST-HMQC with Hadamard-type 15N frequency encoding. This allows site-resolved
real-time NMR studies of kinetic processes in proteins with an increased time
resolution. The sensitivity of the experiment is sufficient to be applicable to
a wide range of molecular systems available at millimolar concentration on a high
magnetic field spectrometer.
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
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Schanda P, Brutscher B. Hadamard frequency-encoded SOFAST-HMQC for ultrafast
two-dimensional protein NMR. Journal of Magnetic Resonance. 2006;178(2):334-339.
doi:10.1016/j.jmr.2005.10.007
apa: Schanda, P., & Brutscher, B. (2006). Hadamard frequency-encoded SOFAST-HMQC
for ultrafast two-dimensional protein NMR. Journal of Magnetic Resonance.
Elsevier. https://doi.org/10.1016/j.jmr.2005.10.007
chicago: Schanda, Paul, and Bernhard Brutscher. “Hadamard Frequency-Encoded SOFAST-HMQC
for Ultrafast Two-Dimensional Protein NMR.” Journal of Magnetic Resonance.
Elsevier, 2006. https://doi.org/10.1016/j.jmr.2005.10.007.
ieee: P. Schanda and B. Brutscher, “Hadamard frequency-encoded SOFAST-HMQC for ultrafast
two-dimensional protein NMR,” Journal of Magnetic Resonance, vol. 178,
no. 2. Elsevier, pp. 334–339, 2006.
ista: Schanda P, Brutscher B. 2006. Hadamard frequency-encoded SOFAST-HMQC for ultrafast
two-dimensional protein NMR. Journal of Magnetic Resonance. 178(2), 334–339.
mla: Schanda, Paul, and Bernhard Brutscher. “Hadamard Frequency-Encoded SOFAST-HMQC
for Ultrafast Two-Dimensional Protein NMR.” Journal of Magnetic Resonance,
vol. 178, no. 2, Elsevier, 2006, pp. 334–39, doi:10.1016/j.jmr.2005.10.007.
short: P. Schanda, B. Brutscher, Journal of Magnetic Resonance 178 (2006) 334–339.
date_created: 2020-09-18T10:13:51Z
date_published: 2006-02-01T00:00:00Z
date_updated: 2021-01-12T08:19:38Z
day: '01'
doi: 10.1016/j.jmr.2005.10.007
extern: '1'
intvolume: ' 178'
issue: '2'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '02'
oa_version: None
page: 334-339
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
status: public
title: Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein
NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 178
year: '2006'
...