---
_id: '11092'
abstract:
- lang: eng
text: To combat the functional decline of the proteome, cells use the process of
protein turnover to replace potentially impaired polypeptides with new functional
copies. We found that extremely long-lived proteins (ELLPs) did not turn over
in postmitotic cells of the rat central nervous system. These ELLPs were associated
with chromatin and the nuclear pore complex, the central transport channels that
mediate all molecular trafficking in and out of the nucleus. The longevity of
these proteins would be expected to expose them to potentially harmful metabolites,
putting them at risk of accumulating damage over extended periods of time. Thus,
it is possible that failure to maintain proper levels and functional integrity
of ELLPs in nonproliferative cells might contribute to age-related deterioration
in cell and tissue function.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Jeffrey N.
full_name: Savas, Jeffrey N.
last_name: Savas
- first_name: Brandon H.
full_name: Toyama, Brandon H.
last_name: Toyama
- first_name: Tao
full_name: Xu, Tao
last_name: Xu
- first_name: John R.
full_name: Yates, John R.
last_name: Yates
- 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: Savas JN, Toyama BH, Xu T, Yates JR, Hetzer M. Extremely long-lived nuclear
pore proteins in the rat brain. Science. 2012;335(6071):942-942. doi:10.1126/science.1217421
apa: Savas, J. N., Toyama, B. H., Xu, T., Yates, J. R., & Hetzer, M. (2012).
Extremely long-lived nuclear pore proteins in the rat brain. Science. American
Association for the Advancement of Science. https://doi.org/10.1126/science.1217421
chicago: Savas, Jeffrey N., Brandon H. Toyama, Tao Xu, John R. Yates, and Martin
Hetzer. “Extremely Long-Lived Nuclear Pore Proteins in the Rat Brain.” Science.
American Association for the Advancement of Science, 2012. https://doi.org/10.1126/science.1217421.
ieee: J. N. Savas, B. H. Toyama, T. Xu, J. R. Yates, and M. Hetzer, “Extremely long-lived
nuclear pore proteins in the rat brain,” Science, vol. 335, no. 6071. American
Association for the Advancement of Science, pp. 942–942, 2012.
ista: Savas JN, Toyama BH, Xu T, Yates JR, Hetzer M. 2012. Extremely long-lived
nuclear pore proteins in the rat brain. Science. 335(6071), 942–942.
mla: Savas, Jeffrey N., et al. “Extremely Long-Lived Nuclear Pore Proteins in the
Rat Brain.” Science, vol. 335, no. 6071, American Association for the Advancement
of Science, 2012, pp. 942–942, doi:10.1126/science.1217421.
short: J.N. Savas, B.H. Toyama, T. Xu, J.R. Yates, M. Hetzer, Science 335 (2012)
942–942.
date_created: 2022-04-07T07:52:01Z
date_published: 2012-02-02T00:00:00Z
date_updated: 2022-07-18T08:53:06Z
day: '02'
doi: 10.1126/science.1217421
extern: '1'
external_id:
pmid:
- '22300851'
intvolume: ' 335'
issue: '6071'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '02'
oa_version: None
page: 942-942
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Extremely long-lived nuclear pore proteins in the rat brain
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 335
year: '2012'
...
---
_id: '12198'
abstract:
- lang: eng
text: The Arabidopsis thaliana central cell, the companion cell of the egg, undergoes
DNA demethylation before fertilization, but the targeting preferences, mechanism,
and biological significance of this process remain unclear. Here, we show that
active DNA demethylation mediated by the DEMETER DNA glycosylase accounts for
all of the demethylation in the central cell and preferentially targets small,
AT-rich, and nucleosome-depleted euchromatic transposable elements. The vegetative
cell, the companion cell of sperm, also undergoes DEMETER-dependent demethylation
of similar sequences, and lack of DEMETER in vegetative cells causes reduced small
RNA–directed DNA methylation of transposons in sperm. Our results demonstrate
that demethylation in companion cells reinforces transposon methylation in plant
gametes and likely contributes to stable silencing of transposable elements across
generations.
acknowledgement: We thank S. Harmer for assistance with the analysis of histone modifications,
the BioOptics team at the Vienna Biocenter Campus for sorting sperm and vegetative
cell nuclei, K. Slotkin for the LAT52p-amiRNA=GFP plasmid, and G. Drews for the
DD45p-GFP transgenic line. This work was partially funded by an NIH grant (GM69415)
to R.L.F., NSF grants (MCB-0918821 and IOS-1025890) to R.L.F. and D.Z., a Young
Investigator Grant from the Arnold and Mabel Beckman Foundation to D.Z., an Austrian
Science Fund (FWF) grant P21389-B03 to H.T., a Ruth L. Kirschstein NIH Predoctoral
Fellowship (GM093633) to C.A.I., a Fulbright Scholarship to J.A.R., a fellowship
from the Jane Coffin Childs Memorial Fund to A.Z., and a Robert and Colleen Haas
Scholarship to D.R. Sequencing data are deposited in GEO (GSE38935).
article_processing_charge: No
article_type: original
author:
- first_name: Christian A.
full_name: Ibarra, Christian A.
last_name: Ibarra
- first_name: Xiaoqi
full_name: Feng, Xiaoqi
id: e0164712-22ee-11ed-b12a-d80fcdf35958
last_name: Feng
orcid: 0000-0002-4008-1234
- first_name: Vera K.
full_name: Schoft, Vera K.
last_name: Schoft
- first_name: Tzung-Fu
full_name: Hsieh, Tzung-Fu
last_name: Hsieh
- first_name: Rie
full_name: Uzawa, Rie
last_name: Uzawa
- first_name: Jessica A.
full_name: Rodrigues, Jessica A.
last_name: Rodrigues
- first_name: Assaf
full_name: Zemach, Assaf
last_name: Zemach
- first_name: Nina
full_name: Chumak, Nina
last_name: Chumak
- first_name: Adriana
full_name: Machlicova, Adriana
last_name: Machlicova
- first_name: Toshiro
full_name: Nishimura, Toshiro
last_name: Nishimura
- first_name: Denisse
full_name: Rojas, Denisse
last_name: Rojas
- first_name: Robert L.
full_name: Fischer, Robert L.
last_name: Fischer
- first_name: Hisashi
full_name: Tamaru, Hisashi
last_name: Tamaru
- first_name: Daniel
full_name: Zilberman, Daniel
last_name: Zilberman
citation:
ama: Ibarra CA, Feng X, Schoft VK, et al. Active DNA demethylation in plant companion
cells reinforces transposon methylation in gametes. Science. 2012;337(6100):1360-1364.
doi:10.1126/science.1224839
apa: Ibarra, C. A., Feng, X., Schoft, V. K., Hsieh, T.-F., Uzawa, R., Rodrigues,
J. A., … Zilberman, D. (2012). Active DNA demethylation in plant companion cells
reinforces transposon methylation in gametes. Science. American Association
for the Advancement of Science. https://doi.org/10.1126/science.1224839
chicago: Ibarra, Christian A., Xiaoqi Feng, Vera K. Schoft, Tzung-Fu Hsieh, Rie
Uzawa, Jessica A. Rodrigues, Assaf Zemach, et al. “Active DNA Demethylation in
Plant Companion Cells Reinforces Transposon Methylation in Gametes.” Science.
American Association for the Advancement of Science, 2012. https://doi.org/10.1126/science.1224839.
ieee: C. A. Ibarra et al., “Active DNA demethylation in plant companion cells
reinforces transposon methylation in gametes,” Science, vol. 337, no. 6100.
American Association for the Advancement of Science, pp. 1360–1364, 2012.
ista: Ibarra CA, Feng X, Schoft VK, Hsieh T-F, Uzawa R, Rodrigues JA, Zemach A,
Chumak N, Machlicova A, Nishimura T, Rojas D, Fischer RL, Tamaru H, Zilberman
D. 2012. Active DNA demethylation in plant companion cells reinforces transposon
methylation in gametes. Science. 337(6100), 1360–1364.
mla: Ibarra, Christian A., et al. “Active DNA Demethylation in Plant Companion Cells
Reinforces Transposon Methylation in Gametes.” Science, vol. 337, no. 6100,
American Association for the Advancement of Science, 2012, pp. 1360–64, doi:10.1126/science.1224839.
short: C.A. Ibarra, X. Feng, V.K. Schoft, T.-F. Hsieh, R. Uzawa, J.A. Rodrigues,
A. Zemach, N. Chumak, A. Machlicova, T. Nishimura, D. Rojas, R.L. Fischer, H.
Tamaru, D. Zilberman, Science 337 (2012) 1360–1364.
date_created: 2023-01-16T09:21:24Z
date_published: 2012-09-14T00:00:00Z
date_updated: 2023-10-16T09:27:26Z
day: '14'
department:
- _id: XiFe
doi: 10.1126/science.1224839
external_id:
pmid:
- '22984074'
intvolume: ' 337'
issue: '6100'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4034762/
month: '09'
oa: 1
oa_version: Published Version
page: 1360-1364
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Active DNA demethylation in plant companion cells reinforces transposon methylation
in gametes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 337
year: '2012'
...
---
_id: '14305'
abstract:
- lang: eng
text: Understanding the mechanism of protein folding requires a detailed knowledge
of the structural properties of the barriers separating unfolded from native conformations.
The S-peptide from ribonuclease S forms its α-helical structure only upon binding
to the folded S-protein. We characterized the transition state for this binding-induced
folding reaction at high resolution by determining the effect of site-specific
backbone thioxylation and side-chain modifications on the kinetics and thermodynamics
of the reaction, which allows us to monitor formation of backbone hydrogen bonds
and side-chain interactions in the transition state. The experiments reveal that
α-helical structure in the S-peptide is absent in the transition state of binding.
Recognition between the unfolded S-peptide and the S-protein is mediated by loosely
packed hydrophobic side-chain interactions in two well defined regions on the
S-peptide. Close packing and helix formation occurs rapidly after binding. Introducing
hydrophobic residues at positions outside the recognition region can drastically
slow down association.
article_processing_charge: No
article_type: original
author:
- first_name: Annett
full_name: Bachmann, Annett
last_name: Bachmann
- first_name: Dirk
full_name: Wildemann, Dirk
last_name: Wildemann
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Gunter
full_name: Fischer, Gunter
last_name: Fischer
- first_name: Thomas
full_name: Kiefhaber, Thomas
last_name: Kiefhaber
citation:
ama: Bachmann A, Wildemann D, Praetorius FM, Fischer G, Kiefhaber T. Mapping backbone
and side-chain interactions in the transition state of a coupled protein folding
and binding reaction. PNAS. 2011;108(10):3952-3957. doi:10.1073/pnas.1012668108
apa: Bachmann, A., Wildemann, D., Praetorius, F. M., Fischer, G., & Kiefhaber,
T. (2011). Mapping backbone and side-chain interactions in the transition state
of a coupled protein folding and binding reaction. PNAS. Proceedings of
the National Academy of Sciences. https://doi.org/10.1073/pnas.1012668108
chicago: Bachmann, Annett, Dirk Wildemann, Florian M Praetorius, Gunter Fischer,
and Thomas Kiefhaber. “Mapping Backbone and Side-Chain Interactions in the Transition
State of a Coupled Protein Folding and Binding Reaction.” PNAS. Proceedings
of the National Academy of Sciences, 2011. https://doi.org/10.1073/pnas.1012668108.
ieee: A. Bachmann, D. Wildemann, F. M. Praetorius, G. Fischer, and T. Kiefhaber,
“Mapping backbone and side-chain interactions in the transition state of a coupled
protein folding and binding reaction,” PNAS, vol. 108, no. 10. Proceedings
of the National Academy of Sciences, pp. 3952–3957, 2011.
ista: Bachmann A, Wildemann D, Praetorius FM, Fischer G, Kiefhaber T. 2011. Mapping
backbone and side-chain interactions in the transition state of a coupled protein
folding and binding reaction. PNAS. 108(10), 3952–3957.
mla: Bachmann, Annett, et al. “Mapping Backbone and Side-Chain Interactions in the
Transition State of a Coupled Protein Folding and Binding Reaction.” PNAS,
vol. 108, no. 10, Proceedings of the National Academy of Sciences, 2011, pp. 3952–57,
doi:10.1073/pnas.1012668108.
short: A. Bachmann, D. Wildemann, F.M. Praetorius, G. Fischer, T. Kiefhaber, PNAS
108 (2011) 3952–3957.
date_created: 2023-09-06T12:54:36Z
date_published: 2011-01-12T00:00:00Z
date_updated: 2023-11-07T11:50:29Z
day: '12'
doi: 10.1073/pnas.1012668108
extern: '1'
external_id:
pmid:
- '21325613'
intvolume: ' 108'
issue: '10'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.1012668108
month: '01'
oa: 1
oa_version: Published Version
page: 3952-3957
pmid: 1
publication: PNAS
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mapping backbone and side-chain interactions in the transition state of a coupled
protein folding and binding reaction
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 108
year: '2011'
...
---
_id: '9452'
abstract:
- lang: eng
text: Eukaryotic cytosine methylation represses transcription but also occurs in
the bodies of active genes, and the extent of methylation biology conservation
is unclear. We quantified DNA methylation in 17 eukaryotic genomes and found that
gene body methylation is conserved between plants and animals, whereas selective
methylation of transposons is not. We show that methylation of plant transposons
in the CHG context extends to green algae and that exclusion of histone H2A.Z
from methylated DNA is conserved between plants and animals, and we present evidence
for RNA-directed DNA methylation of fungal genes. Our data demonstrate that extant
DNA methylation systems are mosaics of conserved and derived features, and indicate
that gene body methylation is an ancient property of eukaryotic genomes.
article_processing_charge: No
article_type: original
author:
- first_name: 'Assaf '
full_name: 'Zemach, Assaf '
last_name: Zemach
- first_name: Ivy E.
full_name: McDaniel, Ivy E.
last_name: McDaniel
- first_name: Pedro
full_name: Silva, Pedro
last_name: Silva
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
citation:
ama: Zemach A, McDaniel IE, Silva P, Zilberman D. Genome-wide evolutionary analysis
of eukaryotic DNA methylation. Science. 2010;328(5980):916-919. doi:10.1126/science.1186366
apa: Zemach, A., McDaniel, I. E., Silva, P., & Zilberman, D. (2010). Genome-wide
evolutionary analysis of eukaryotic DNA methylation. Science. American
Association for the Advancement of Science. https://doi.org/10.1126/science.1186366
chicago: Zemach, Assaf , Ivy E. McDaniel, Pedro Silva, and Daniel Zilberman. “Genome-Wide
Evolutionary Analysis of Eukaryotic DNA Methylation.” Science. American
Association for the Advancement of Science, 2010. https://doi.org/10.1126/science.1186366.
ieee: A. Zemach, I. E. McDaniel, P. Silva, and D. Zilberman, “Genome-wide evolutionary
analysis of eukaryotic DNA methylation,” Science, vol. 328, no. 5980. American
Association for the Advancement of Science, pp. 916–919, 2010.
ista: Zemach A, McDaniel IE, Silva P, Zilberman D. 2010. Genome-wide evolutionary
analysis of eukaryotic DNA methylation. Science. 328(5980), 916–919.
mla: Zemach, Assaf, et al. “Genome-Wide Evolutionary Analysis of Eukaryotic DNA
Methylation.” Science, vol. 328, no. 5980, American Association for the
Advancement of Science, 2010, pp. 916–19, doi:10.1126/science.1186366.
short: A. Zemach, I.E. McDaniel, P. Silva, D. Zilberman, Science 328 (2010) 916–919.
date_created: 2021-06-04T08:26:08Z
date_published: 2010-05-14T00:00:00Z
date_updated: 2021-12-14T08:35:37Z
day: '14'
department:
- _id: DaZi
doi: 10.1126/science.1186366
extern: '1'
external_id:
pmid:
- '20395474 '
intvolume: ' 328'
issue: '5980'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '05'
oa_version: None
page: 916-919
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Genome-wide evolutionary analysis of eukaryotic DNA methylation
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 328
year: '2010'
...
---
_id: '13418'
abstract:
- lang: eng
text: In traditional photoconductors1,2,3, the impinging light generates mobile
charge carriers in the valence and/or conduction bands, causing the material’s
conductivity to increase4. Such positive photoconductance is observed in both
bulk and nanostructured5,6 photoconductors. Here we describe a class of nanoparticle-based
materials whose conductivity can either increase or decrease on irradiation with
visible light of wavelengths close to the particles’ surface plasmon resonance.
The remarkable feature of these plasmonic materials is that the sign of the conductivity
change and the nature of the electron transport between the nanoparticles depend
on the molecules comprising the self-assembled monolayers (SAMs)7,8 stabilizing
the nanoparticles. For SAMs made of electrically neutral (polar and non-polar)
molecules, conductivity increases on irradiation. If, however, the SAMs contain
electrically charged (either negatively or positively) groups, conductivity decreases.
The optical and electrical characteristics of these previously undescribed inverse
photoconductors can be engineered flexibly by adjusting the material properties
of the nanoparticles and of the coating SAMs. In particular, in films comprising
mixtures of different nanoparticles or nanoparticles coated with mixed SAMs, the
overall photoconductance is a weighted average of the changes induced by the individual
components. These and other observations can be rationalized in terms of light-induced
creation of mobile charge carriers whose transport through the charged SAMs is
inhibited by carrier trapping in transient polaron-like states9,10. The nanoparticle-based
photoconductors we describe could have uses in chemical sensors and/or in conjunction
with flexible substrates.
article_processing_charge: No
article_type: original
author:
- first_name: Hideyuki
full_name: Nakanishi, Hideyuki
last_name: Nakanishi
- first_name: Kyle J. M.
full_name: Bishop, Kyle J. M.
last_name: Bishop
- first_name: Bartlomiej
full_name: Kowalczyk, Bartlomiej
last_name: Kowalczyk
- first_name: Abraham
full_name: Nitzan, Abraham
last_name: Nitzan
- first_name: Emily A.
full_name: Weiss, Emily A.
last_name: Weiss
- first_name: Konstantin V.
full_name: Tretiakov, Konstantin V.
last_name: Tretiakov
- first_name: Mario M.
full_name: Apodaca, Mario M.
last_name: Apodaca
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: J. Fraser
full_name: Stoddart, J. Fraser
last_name: Stoddart
- first_name: Bartosz A.
full_name: Grzybowski, Bartosz A.
last_name: Grzybowski
citation:
ama: Nakanishi H, Bishop KJM, Kowalczyk B, et al. Photoconductance and inverse photoconductance
in films of functionalized metal nanoparticles. Nature. 2009;460(7253):371-375.
doi:10.1038/nature08131
apa: Nakanishi, H., Bishop, K. J. M., Kowalczyk, B., Nitzan, A., Weiss, E. A., Tretiakov,
K. V., … Grzybowski, B. A. (2009). Photoconductance and inverse photoconductance
in films of functionalized metal nanoparticles. Nature. Springer Nature.
https://doi.org/10.1038/nature08131
chicago: Nakanishi, Hideyuki, Kyle J. M. Bishop, Bartlomiej Kowalczyk, Abraham Nitzan,
Emily A. Weiss, Konstantin V. Tretiakov, Mario M. Apodaca, Rafal Klajn, J. Fraser
Stoddart, and Bartosz A. Grzybowski. “Photoconductance and Inverse Photoconductance
in Films of Functionalized Metal Nanoparticles.” Nature. Springer Nature,
2009. https://doi.org/10.1038/nature08131.
ieee: H. Nakanishi et al., “Photoconductance and inverse photoconductance
in films of functionalized metal nanoparticles,” Nature, vol. 460, no.
7253. Springer Nature, pp. 371–375, 2009.
ista: Nakanishi H, Bishop KJM, Kowalczyk B, Nitzan A, Weiss EA, Tretiakov KV, Apodaca
MM, Klajn R, Stoddart JF, Grzybowski BA. 2009. Photoconductance and inverse photoconductance
in films of functionalized metal nanoparticles. Nature. 460(7253), 371–375.
mla: Nakanishi, Hideyuki, et al. “Photoconductance and Inverse Photoconductance
in Films of Functionalized Metal Nanoparticles.” Nature, vol. 460, no.
7253, Springer Nature, 2009, pp. 371–75, doi:10.1038/nature08131.
short: H. Nakanishi, K.J.M. Bishop, B. Kowalczyk, A. Nitzan, E.A. Weiss, K.V. Tretiakov,
M.M. Apodaca, R. Klajn, J.F. Stoddart, B.A. Grzybowski, Nature 460 (2009) 371–375.
date_created: 2023-08-01T10:29:50Z
date_published: 2009-07-16T00:00:00Z
date_updated: 2023-08-08T09:00:59Z
day: '16'
doi: 10.1038/nature08131
extern: '1'
external_id:
pmid:
- '19606145'
intvolume: ' 460'
issue: '7253'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '07'
oa_version: None
page: 371-375
pmid: 1
publication: Nature
publication_identifier:
eissn:
- 1476-4687
issn:
- 0028-0836
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Photoconductance and inverse photoconductance in films of functionalized metal
nanoparticles
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 460
year: '2009'
...
---
_id: '9453'
abstract:
- lang: eng
text: Parent-of-origin-specific (imprinted) gene expression is regulated in Arabidopsis
thaliana endosperm by cytosine demethylation of the maternal genome mediated by
the DNA glycosylase DEMETER, but the extent of the methylation changes is not
known. Here, we show that virtually the entire endosperm genome is demethylated,
coupled with extensive local non-CG hypermethylation of small interfering RNA–targeted
sequences. Mutation of DEMETER partially restores endosperm CG methylation to
levels found in other tissues, indicating that CG demethylation is specific to
maternal sequences. Endosperm demethylation is accompanied by CHH hypermethylation
of embryo transposable elements. Our findings demonstrate extensive reconfiguration
of the endosperm methylation landscape that likely reinforces transposon silencing
in the embryo.
article_processing_charge: No
article_type: original
author:
- first_name: Tzung-Fu
full_name: Hsieh, Tzung-Fu
last_name: Hsieh
- first_name: Christian A.
full_name: Ibarra, Christian A.
last_name: Ibarra
- first_name: Pedro
full_name: Silva, Pedro
last_name: Silva
- first_name: Assaf
full_name: Zemach, Assaf
last_name: Zemach
- first_name: Leor
full_name: Eshed-Williams, Leor
last_name: Eshed-Williams
- first_name: Robert L.
full_name: Fischer, Robert L.
last_name: Fischer
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
citation:
ama: Hsieh T-F, Ibarra CA, Silva P, et al. Genome-wide demethylation of Arabidopsis
endosperm. Science. 2009;324(5933):1451-1454. doi:10.1126/science.1172417
apa: Hsieh, T.-F., Ibarra, C. A., Silva, P., Zemach, A., Eshed-Williams, L., Fischer,
R. L., & Zilberman, D. (2009). Genome-wide demethylation of Arabidopsis endosperm.
Science. American Association for the Advancement of Science. https://doi.org/10.1126/science.1172417
chicago: Hsieh, Tzung-Fu, Christian A. Ibarra, Pedro Silva, Assaf Zemach, Leor Eshed-Williams,
Robert L. Fischer, and Daniel Zilberman. “Genome-Wide Demethylation of Arabidopsis
Endosperm.” Science. American Association for the Advancement of Science,
2009. https://doi.org/10.1126/science.1172417.
ieee: T.-F. Hsieh et al., “Genome-wide demethylation of Arabidopsis endosperm,”
Science, vol. 324, no. 5933. American Association for the Advancement of
Science, pp. 1451–1454, 2009.
ista: Hsieh T-F, Ibarra CA, Silva P, Zemach A, Eshed-Williams L, Fischer RL, Zilberman
D. 2009. Genome-wide demethylation of Arabidopsis endosperm. Science. 324(5933),
1451–1454.
mla: Hsieh, Tzung-Fu, et al. “Genome-Wide Demethylation of Arabidopsis Endosperm.”
Science, vol. 324, no. 5933, American Association for the Advancement of
Science, 2009, pp. 1451–54, doi:10.1126/science.1172417.
short: T.-F. Hsieh, C.A. Ibarra, P. Silva, A. Zemach, L. Eshed-Williams, R.L. Fischer,
D. Zilberman, Science 324 (2009) 1451–1454.
date_created: 2021-06-04T08:55:41Z
date_published: 2009-06-12T00:00:00Z
date_updated: 2021-12-14T08:53:26Z
day: '12'
department:
- _id: DaZi
doi: 10.1126/science.1172417
extern: '1'
external_id:
pmid:
- '19520962'
intvolume: ' 324'
issue: '5933'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4044190/
month: '06'
oa: 1
oa_version: Submitted Version
page: 1451-1454
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Genome-wide demethylation of Arabidopsis endosperm
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 324
year: '2009'
...
---
_id: '11114'
abstract:
- lang: eng
text: We present a miniaturized pull-down method for the detection of protein-protein
interactions using standard affinity chromatography reagents. Binding events between
different proteins, which are color-coded with quantum dots (QDs), are visualized
on single affinity chromatography beads by fluorescence microscopy. The use of
QDs for single molecule detection allows the simultaneous analysis of multiple
protein-protein binding events and reduces the amount of time and material needed
to perform a pull-down experiment.
article_number: e2061
article_processing_charge: No
article_type: original
author:
- first_name: Roberta
full_name: Schulte, Roberta
last_name: Schulte
- first_name: Jessica
full_name: Talamas, Jessica
last_name: Talamas
- first_name: Christine
full_name: Doucet, Christine
last_name: Doucet
- 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: Schulte R, Talamas J, Doucet C, Hetzer M. Single bead affinity detection (SINBAD)
for the analysis of protein-protein interactions. PLoS ONE. 2008;3(4).
doi:10.1371/journal.pone.0002061
apa: Schulte, R., Talamas, J., Doucet, C., & Hetzer, M. (2008). Single bead
affinity detection (SINBAD) for the analysis of protein-protein interactions.
PLoS ONE. Public Library of Science. https://doi.org/10.1371/journal.pone.0002061
chicago: Schulte, Roberta, Jessica Talamas, Christine Doucet, and Martin Hetzer.
“Single Bead Affinity Detection (SINBAD) for the Analysis of Protein-Protein Interactions.”
PLoS ONE. Public Library of Science, 2008. https://doi.org/10.1371/journal.pone.0002061.
ieee: R. Schulte, J. Talamas, C. Doucet, and M. Hetzer, “Single bead affinity detection
(SINBAD) for the analysis of protein-protein interactions,” PLoS ONE, vol.
3, no. 4. Public Library of Science, 2008.
ista: Schulte R, Talamas J, Doucet C, Hetzer M. 2008. Single bead affinity detection
(SINBAD) for the analysis of protein-protein interactions. PLoS ONE. 3(4), e2061.
mla: Schulte, Roberta, et al. “Single Bead Affinity Detection (SINBAD) for the Analysis
of Protein-Protein Interactions.” PLoS ONE, vol. 3, no. 4, e2061, Public
Library of Science, 2008, doi:10.1371/journal.pone.0002061.
short: R. Schulte, J. Talamas, C. Doucet, M. Hetzer, PLoS ONE 3 (2008).
date_created: 2022-04-07T07:55:57Z
date_published: 2008-04-30T00:00:00Z
date_updated: 2022-07-18T08:56:36Z
day: '30'
doi: 10.1371/journal.pone.0002061
extern: '1'
external_id:
pmid:
- '18446240'
intvolume: ' 3'
issue: '4'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: ' https://doi.org/10.1371/journal.pone.0002061'
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
publication: PLoS ONE
publication_identifier:
issn:
- 1932-6203
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Single bead affinity detection (SINBAD) for the analysis of protein-protein
interactions
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 3
year: '2008'
...
---
_id: '9457'
abstract:
- lang: eng
text: Eukaryotic chromatin is separated into functional domains differentiated by
posttranslational histone modifications, histone variants, and DNA methylation1–6.
Methylation is associated with repression of transcriptional initiation in plants
and animals, and is frequently found in transposable elements. Proper methylation
patterns are critical for eukaryotic development4,5, and aberrant methylation-induced
silencing of tumor suppressor genes is a common feature of human cancer7. In contrast
to methylation, the histone variant H2A.Z is preferentially deposited by the Swr1
ATPase complex near 5′ ends of genes where it promotes transcriptional competence8–20.
How DNA methylation and H2A.Z influence transcription remains largely unknown.
Here we show that in the plant Arabidopsis thaliana, regions of DNA methylation
are quantitatively deficient in H2A.Z. Exclusion of H2A.Z is seen at sites of
DNA methylation in the bodies of actively transcribed genes and in methylated
transposons. Mutation of the MET1 DNA methyltransferase, which causes both losses
and gains of DNA methylation4,5, engenders opposite changes in H2A.Z deposition,
while mutation of the PIE1 subunit of the Swr1 complex that deposits H2A.Z17 leads
to genome-wide hypermethylation. Our findings indicate that DNA methylation can
influence chromatin structure and effect gene silencing by excluding H2A.Z, and
that H2A.Z protects genes from DNA methylation.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
- first_name: Devin
full_name: Coleman-Derr, Devin
last_name: Coleman-Derr
- first_name: Tracy
full_name: Ballinger, Tracy
last_name: Ballinger
- first_name: Steven
full_name: Henikoff, Steven
last_name: Henikoff
citation:
ama: Zilberman D, Coleman-Derr D, Ballinger T, Henikoff S. Histone H2A.Z and DNA
methylation are mutually antagonistic chromatin marks. Nature. 2008;456(7218):125-129.
doi:10.1038/nature07324
apa: Zilberman, D., Coleman-Derr, D., Ballinger, T., & Henikoff, S. (2008).
Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks. Nature.
Springer Nature. https://doi.org/10.1038/nature07324
chicago: Zilberman, Daniel, Devin Coleman-Derr, Tracy Ballinger, and Steven Henikoff.
“Histone H2A.Z and DNA Methylation Are Mutually Antagonistic Chromatin Marks.”
Nature. Springer Nature, 2008. https://doi.org/10.1038/nature07324.
ieee: D. Zilberman, D. Coleman-Derr, T. Ballinger, and S. Henikoff, “Histone H2A.Z
and DNA methylation are mutually antagonistic chromatin marks,” Nature,
vol. 456, no. 7218. Springer Nature, pp. 125–129, 2008.
ista: Zilberman D, Coleman-Derr D, Ballinger T, Henikoff S. 2008. Histone H2A.Z
and DNA methylation are mutually antagonistic chromatin marks. Nature. 456(7218),
125–129.
mla: Zilberman, Daniel, et al. “Histone H2A.Z and DNA Methylation Are Mutually Antagonistic
Chromatin Marks.” Nature, vol. 456, no. 7218, Springer Nature, 2008, pp.
125–29, doi:10.1038/nature07324.
short: D. Zilberman, D. Coleman-Derr, T. Ballinger, S. Henikoff, Nature 456 (2008)
125–129.
date_created: 2021-06-04T11:49:32Z
date_published: 2008-11-06T00:00:00Z
date_updated: 2021-12-14T08:54:36Z
day: '06'
department:
- _id: DaZi
doi: 10.1038/nature07324
extern: '1'
external_id:
pmid:
- '18815594'
intvolume: ' 456'
issue: '7218'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2877514/
month: '11'
oa: 1
oa_version: Submitted Version
page: 125-129
pmid: 1
publication: Nature
publication_identifier:
eissn:
- 1476-4687
issn:
- 0028-0836
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 456
year: '2008'
...
---
_id: '8483'
abstract:
- lang: eng
text: Atom-resolved real-time studies of kinetic processes in proteins have been
hampered in the past by the lack of experimental techniques that yield sufficient
temporal and atomic resolution. Here we present band-selective optimized flip-angle
short transient (SOFAST) real-time 2D NMR spectroscopy, a method that allows simultaneous
observation of reaction kinetics for a large number of nuclear sites along the
polypeptide chain of a protein with an unprecedented time resolution of a few
seconds. SOFAST real-time 2D NMR spectroscopy combines fast NMR data acquisition
techniques with rapid sample mixing inside the NMR magnet to initiate the kinetic
event. We demonstrate the use of SOFAST real-time 2D NMR to monitor the conformational
transition of α-lactalbumin from a molten globular to the native state for a large
number of amide sites along the polypeptide chain. The kinetic behavior observed
for the disappearance of the molten globule and the appearance of the native state
is monoexponential and uniform along the polypeptide chain. This observation confirms
previous findings that a single transition state ensemble controls folding of
α-lactalbumin from the molten globule to the native state. In a second application,
the spontaneous unfolding of native ubiquitin under nondenaturing conditions is
characterized by amide hydrogen exchange rate constants measured at high pH by
using SOFAST real-time 2D NMR. Our data reveal that ubiquitin unfolds in a gradual
manner with distinct unfolding regimes.
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: V.
full_name: Forge, V.
last_name: Forge
- first_name: B.
full_name: Brutscher, B.
last_name: Brutscher
citation:
ama: Schanda P, Forge V, Brutscher B. Protein folding and unfolding studied at atomic
resolution by fast two-dimensional NMR spectroscopy. Proceedings of the National
Academy of Sciences. 2007;104(27):11257-11262. doi:10.1073/pnas.0702069104
apa: Schanda, P., Forge, V., & Brutscher, B. (2007). Protein folding and unfolding
studied at atomic resolution by fast two-dimensional NMR spectroscopy. Proceedings
of the National Academy of Sciences. National Academy of Sciences. https://doi.org/10.1073/pnas.0702069104
chicago: Schanda, Paul, V. Forge, and B. Brutscher. “Protein Folding and Unfolding
Studied at Atomic Resolution by Fast Two-Dimensional NMR Spectroscopy.” Proceedings
of the National Academy of Sciences. National Academy of Sciences, 2007. https://doi.org/10.1073/pnas.0702069104.
ieee: P. Schanda, V. Forge, and B. Brutscher, “Protein folding and unfolding studied
at atomic resolution by fast two-dimensional NMR spectroscopy,” Proceedings
of the National Academy of Sciences, vol. 104, no. 27. National Academy of
Sciences, pp. 11257–11262, 2007.
ista: Schanda P, Forge V, Brutscher B. 2007. Protein folding and unfolding studied
at atomic resolution by fast two-dimensional NMR spectroscopy. Proceedings of
the National Academy of Sciences. 104(27), 11257–11262.
mla: Schanda, Paul, et al. “Protein Folding and Unfolding Studied at Atomic Resolution
by Fast Two-Dimensional NMR Spectroscopy.” Proceedings of the National Academy
of Sciences, vol. 104, no. 27, National Academy of Sciences, 2007, pp. 11257–62,
doi:10.1073/pnas.0702069104.
short: P. Schanda, V. Forge, B. Brutscher, Proceedings of the National Academy of
Sciences 104 (2007) 11257–11262.
date_created: 2020-09-18T10:12:54Z
date_published: 2007-07-03T00:00:00Z
date_updated: 2021-01-12T08:19:35Z
day: '03'
doi: 10.1073/pnas.0702069104
extern: '1'
intvolume: ' 104'
issue: '27'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '07'
oa_version: None
page: 11257-11262
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
status: public
title: Protein folding and unfolding studied at atomic resolution by fast two-dimensional
NMR spectroscopy
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 104
year: '2007'
...
---
_id: '13425'
abstract:
- lang: eng
text: Nanoparticles (NPs) decorated with ligands combining photoswitchable dipoles
and covalent cross-linkers can be assembled by light into organized, three-dimensional
suprastructures of various types and sizes. NPs covered with only few photoactive
ligands form metastable crystals that can be assembled and disassembled “on demand”
by using light of different wavelengths. For higher surface concentrations, self-assembly
is irreversible, and the NPs organize into permanently cross-linked structures
including robust supracrystals and plastic spherical aggregates.
article_processing_charge: No
article_type: original
author:
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Kyle J. M.
full_name: Bishop, Kyle J. M.
last_name: Bishop
- first_name: Bartosz A.
full_name: Grzybowski, Bartosz A.
last_name: Grzybowski
citation:
ama: Klajn R, Bishop KJM, Grzybowski BA. Light-controlled self-assembly of reversible
and irreversible nanoparticle suprastructures. Proceedings of the National
Academy of Sciences. 2007;104(25):10305-10309. doi:10.1073/pnas.0611371104
apa: Klajn, R., Bishop, K. J. M., & Grzybowski, B. A. (2007). Light-controlled
self-assembly of reversible and irreversible nanoparticle suprastructures. Proceedings
of the National Academy of Sciences. Proceedings of the National Academy of
Sciences. https://doi.org/10.1073/pnas.0611371104
chicago: Klajn, Rafal, Kyle J. M. Bishop, and Bartosz A. Grzybowski. “Light-Controlled
Self-Assembly of Reversible and Irreversible Nanoparticle Suprastructures.” Proceedings
of the National Academy of Sciences. Proceedings of the National Academy of
Sciences, 2007. https://doi.org/10.1073/pnas.0611371104.
ieee: R. Klajn, K. J. M. Bishop, and B. A. Grzybowski, “Light-controlled self-assembly
of reversible and irreversible nanoparticle suprastructures,” Proceedings of
the National Academy of Sciences, vol. 104, no. 25. Proceedings of the National
Academy of Sciences, pp. 10305–10309, 2007.
ista: Klajn R, Bishop KJM, Grzybowski BA. 2007. Light-controlled self-assembly of
reversible and irreversible nanoparticle suprastructures. Proceedings of the National
Academy of Sciences. 104(25), 10305–10309.
mla: Klajn, Rafal, et al. “Light-Controlled Self-Assembly of Reversible and Irreversible
Nanoparticle Suprastructures.” Proceedings of the National Academy of Sciences,
vol. 104, no. 25, Proceedings of the National Academy of Sciences, 2007, pp. 10305–09,
doi:10.1073/pnas.0611371104.
short: R. Klajn, K.J.M. Bishop, B.A. Grzybowski, Proceedings of the National Academy
of Sciences 104 (2007) 10305–10309.
date_created: 2023-08-01T10:31:19Z
date_published: 2007-06-19T00:00:00Z
date_updated: 2023-08-08T11:24:51Z
day: '19'
doi: 10.1073/pnas.0611371104
extern: '1'
external_id:
pmid:
- '17563381'
intvolume: ' 104'
issue: '25'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.0611371104
month: '06'
oa: 1
oa_version: Published Version
page: 10305-10309
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Light-controlled self-assembly of reversible and irreversible nanoparticle
suprastructures
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 104
year: '2007'
...
---
_id: '13427'
abstract:
- lang: eng
text: Deformable, spherical aggregates of metal nanoparticles connected by long-chain
dithiol ligands self-assemble into nanostructured materials of macroscopic dimensions.
These materials are plastic and moldable against arbitrarily shaped masters and
can be thermally hardened into polycrystalline metal structures of controllable
porosity. In addition, in both plastic and hardened states, the assemblies are
electrically conductive and exhibit Ohmic characteristics down to ∼20 volts per
meter. The self-assembly method leading to such materials is applicable both to
pure metals and to bimetallic structures of various elemental compositions.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Kyle J. M.
full_name: Bishop, Kyle J. M.
last_name: Bishop
- first_name: Marcin
full_name: Fialkowski, Marcin
last_name: Fialkowski
- first_name: Maciej
full_name: Paszewski, Maciej
last_name: Paszewski
- first_name: Christopher J.
full_name: Campbell, Christopher J.
last_name: Campbell
- first_name: Timothy P.
full_name: Gray, Timothy P.
last_name: Gray
- first_name: Bartosz A.
full_name: Grzybowski, Bartosz A.
last_name: Grzybowski
citation:
ama: Klajn R, Bishop KJM, Fialkowski M, et al. Plastic and moldable metals by self-assembly
of sticky nanoparticle aggregates. Science. 2007;316(5822):261-264. doi:10.1126/science.1139131
apa: Klajn, R., Bishop, K. J. M., Fialkowski, M., Paszewski, M., Campbell, C. J.,
Gray, T. P., & Grzybowski, B. A. (2007). Plastic and moldable metals by self-assembly
of sticky nanoparticle aggregates. Science. American Association for the
Advancement of Science. https://doi.org/10.1126/science.1139131
chicago: Klajn, Rafal, Kyle J. M. Bishop, Marcin Fialkowski, Maciej Paszewski, Christopher
J. Campbell, Timothy P. Gray, and Bartosz A. Grzybowski. “Plastic and Moldable
Metals by Self-Assembly of Sticky Nanoparticle Aggregates.” Science. American
Association for the Advancement of Science, 2007. https://doi.org/10.1126/science.1139131.
ieee: R. Klajn et al., “Plastic and moldable metals by self-assembly of sticky
nanoparticle aggregates,” Science, vol. 316, no. 5822. American Association
for the Advancement of Science, pp. 261–264, 2007.
ista: Klajn R, Bishop KJM, Fialkowski M, Paszewski M, Campbell CJ, Gray TP, Grzybowski
BA. 2007. Plastic and moldable metals by self-assembly of sticky nanoparticle
aggregates. Science. 316(5822), 261–264.
mla: Klajn, Rafal, et al. “Plastic and Moldable Metals by Self-Assembly of Sticky
Nanoparticle Aggregates.” Science, vol. 316, no. 5822, American Association
for the Advancement of Science, 2007, pp. 261–64, doi:10.1126/science.1139131.
short: R. Klajn, K.J.M. Bishop, M. Fialkowski, M. Paszewski, C.J. Campbell, T.P.
Gray, B.A. Grzybowski, Science 316 (2007) 261–264.
date_created: 2023-08-01T10:36:08Z
date_published: 2007-04-13T00:00:00Z
date_updated: 2023-08-08T11:28:29Z
day: '13'
doi: 10.1126/science.1139131
extern: '1'
external_id:
pmid:
- '17431176'
intvolume: ' 316'
issue: '5822'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '04'
oa_version: None
page: 261-264
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Plastic and moldable metals by self-assembly of sticky nanoparticle aggregates
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 316
year: '2007'
...
---
_id: '11118'
abstract:
- lang: eng
text: Nuclear pore complexes are multiprotein channels that span the double lipid
bilayer of the nuclear envelope. How new pores are inserted into the intact nuclear
envelope of proliferating and differentiating eukaryotic cells is unknown. We
found that the Nup107-160 complex was incorporated into assembly sites in the
nuclear envelope from both the nucleoplasmic and the cytoplasmic sides. Nuclear
pore insertion required the generation of Ran guanosine triphosphate in the nuclear
and cytoplasmic compartments. Newly formed nuclear pore complexes did not contain
structural components of preexisting pores, suggesting that they can form de novo.
article_processing_charge: No
article_type: original
author:
- first_name: Maximiliano A.
full_name: D'Angelo, Maximiliano A.
last_name: D'Angelo
- first_name: Daniel J.
full_name: Anderson, Daniel J.
last_name: Anderson
- first_name: Erin
full_name: Richard, Erin
last_name: Richard
- 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: D’Angelo MA, Anderson DJ, Richard E, Hetzer M. Nuclear pores form de novo from
both sides of the nuclear envelope. Science. 2006;312(5772):440-443. doi:10.1126/science.1124196
apa: D’Angelo, M. A., Anderson, D. J., Richard, E., & Hetzer, M. (2006). Nuclear
pores form de novo from both sides of the nuclear envelope. Science. American
Association for the Advancement of Science. https://doi.org/10.1126/science.1124196
chicago: D’Angelo, Maximiliano A., Daniel J. Anderson, Erin Richard, and Martin
Hetzer. “Nuclear Pores Form de Novo from Both Sides of the Nuclear Envelope.”
Science. American Association for the Advancement of Science, 2006. https://doi.org/10.1126/science.1124196.
ieee: M. A. D’Angelo, D. J. Anderson, E. Richard, and M. Hetzer, “Nuclear pores
form de novo from both sides of the nuclear envelope,” Science, vol. 312,
no. 5772. American Association for the Advancement of Science, pp. 440–443, 2006.
ista: D’Angelo MA, Anderson DJ, Richard E, Hetzer M. 2006. Nuclear pores form de
novo from both sides of the nuclear envelope. Science. 312(5772), 440–443.
mla: D’Angelo, Maximiliano A., et al. “Nuclear Pores Form de Novo from Both Sides
of the Nuclear Envelope.” Science, vol. 312, no. 5772, American Association
for the Advancement of Science, 2006, pp. 440–43, doi:10.1126/science.1124196.
short: M.A. D’Angelo, D.J. Anderson, E. Richard, M. Hetzer, Science 312 (2006) 440–443.
date_created: 2022-04-07T07:56:32Z
date_published: 2006-04-21T00:00:00Z
date_updated: 2022-07-18T08:57:04Z
day: '21'
doi: 10.1126/science.1124196
extern: '1'
external_id:
pmid:
- '16627745'
intvolume: ' 312'
issue: '5772'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '04'
oa_version: None
page: 440-443
pmid: 1
publication: Science
publication_identifier:
issn:
- 0036-8075
- 1095-9203
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nuclear pores form de novo from both sides of the nuclear envelope
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 312
year: '2006'
...
---
_id: '9454'
article_processing_charge: No
article_type: original
author:
- first_name: Simon W.-L.
full_name: Chan, Simon W.-L.
last_name: Chan
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
- first_name: ' Zhixin'
full_name: Xie, Zhixin
last_name: Xie
- first_name: ' Lisa K.'
full_name: Johansen, Lisa K.
last_name: Johansen
- first_name: James C.
full_name: Carrington, James C.
last_name: Carrington
- first_name: Steven E.
full_name: Jacobsen, Steven E.
last_name: Jacobsen
citation:
ama: Chan SW-L, Zilberman D, Xie Zhixin, Johansen Lisa K., Carrington JC, Jacobsen
SE. RNA silencing genes control de novo DNA methylation. Science. 2004;303(5662):1336.
doi:10.1126/science.1095989
apa: Chan, S. W.-L., Zilberman, D., Xie, Zhixin, Johansen, Lisa K., Carrington,
J. C., & Jacobsen, S. E. (2004). RNA silencing genes control de novo DNA methylation.
Science. American Association for the Advancement of Science. https://doi.org/10.1126/science.1095989
chicago: Chan, Simon W.-L., Daniel Zilberman, Zhixin Xie, Lisa K. Johansen, James
C. Carrington, and Steven E. Jacobsen. “RNA Silencing Genes Control de Novo DNA
Methylation.” Science. American Association for the Advancement of Science,
2004. https://doi.org/10.1126/science.1095989.
ieee: S. W.-L. Chan, D. Zilberman, Zhixin Xie, Lisa K. Johansen, J. C. Carrington,
and S. E. Jacobsen, “RNA silencing genes control de novo DNA methylation,” Science,
vol. 303, no. 5662. American Association for the Advancement of Science, p. 1336,
2004.
ista: Chan SW-L, Zilberman D, Xie Zhixin, Johansen Lisa K., Carrington JC, Jacobsen
SE. 2004. RNA silencing genes control de novo DNA methylation. Science. 303(5662),
1336.
mla: Chan, Simon W. L., et al. “RNA Silencing Genes Control de Novo DNA Methylation.”
Science, vol. 303, no. 5662, American Association for the Advancement of
Science, 2004, p. 1336, doi:10.1126/science.1095989.
short: S.W.-L. Chan, D. Zilberman, Zhixin Xie, Lisa K. Johansen, J.C. Carrington,
S.E. Jacobsen, Science 303 (2004) 1336.
date_created: 2021-06-04T11:12:35Z
date_published: 2004-02-27T00:00:00Z
date_updated: 2021-12-14T09:13:53Z
day: '27'
department:
- _id: DaZi
doi: 10.1126/science.1095989
extern: '1'
external_id:
pmid:
- '14988555'
intvolume: ' 303'
issue: '5662'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '02'
oa_version: None
page: '1336'
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: RNA silencing genes control de novo DNA methylation
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 303
year: '2004'
...
---
_id: '11121'
abstract:
- lang: eng
text: In metazoa, the nuclear envelope breaks down and reforms during each cell
cycle. Nuclear pore complexes (NPCs), which serve as channels for transport between
the nucleus and cytoplasm1, assemble into the reforming nuclear envelope in a
sequential process involving association of a subset of NPC proteins, nucleoporins,
with chromatin followed by the formation of a closed nuclear envelope fenestrated
by NPCs2,3,4,5,6,7. How chromatin recruitment of nucleoporins and NPC assembly
are regulated is unknown. Here we demonstrate that RanGTP production is required
to dissociate nucleoporins Nup107, Nup153 and Nup358 from Importin β, to target
them to chromatin and to induce association between separate NPC subcomplexes.
Additionally, either an excess of RanGTP or removal of Importin β induces formation
of NPC-containing membrane structures—annulate lamellae—both in vitro in the absence
of chromatin and in vivo. Annulate lamellae formation is strongly and specifically
inhibited by an excess of Importin β. The data demonstrate that RanGTP triggers
distinct steps of NPC assembly, and suggest a mechanism for the spatial restriction
of NPC assembly to the surface of chromatin.
article_processing_charge: No
article_type: original
author:
- first_name: Tobias C.
full_name: Walther, Tobias C.
last_name: Walther
- first_name: Peter
full_name: Askjaer, Peter
last_name: Askjaer
- first_name: Marc
full_name: Gentzel, Marc
last_name: Gentzel
- first_name: Anja
full_name: Habermann, Anja
last_name: Habermann
- first_name: Gareth
full_name: Griffiths, Gareth
last_name: Griffiths
- first_name: Matthias
full_name: Wilm, Matthias
last_name: Wilm
- first_name: Iain W.
full_name: Mattaj, Iain W.
last_name: Mattaj
- 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: Walther TC, Askjaer P, Gentzel M, et al. RanGTP mediates nuclear pore complex
assembly. Nature. 2003;424(6949):689-694. doi:10.1038/nature01898
apa: Walther, T. C., Askjaer, P., Gentzel, M., Habermann, A., Griffiths, G., Wilm,
M., … Hetzer, M. (2003). RanGTP mediates nuclear pore complex assembly. Nature.
Springer Nature. https://doi.org/10.1038/nature01898
chicago: Walther, Tobias C., Peter Askjaer, Marc Gentzel, Anja Habermann, Gareth
Griffiths, Matthias Wilm, Iain W. Mattaj, and Martin Hetzer. “RanGTP Mediates
Nuclear Pore Complex Assembly.” Nature. Springer Nature, 2003. https://doi.org/10.1038/nature01898.
ieee: T. C. Walther et al., “RanGTP mediates nuclear pore complex assembly,”
Nature, vol. 424, no. 6949. Springer Nature, pp. 689–694, 2003.
ista: Walther TC, Askjaer P, Gentzel M, Habermann A, Griffiths G, Wilm M, Mattaj
IW, Hetzer M. 2003. RanGTP mediates nuclear pore complex assembly. Nature. 424(6949),
689–694.
mla: Walther, Tobias C., et al. “RanGTP Mediates Nuclear Pore Complex Assembly.”
Nature, vol. 424, no. 6949, Springer Nature, 2003, pp. 689–94, doi:10.1038/nature01898.
short: T.C. Walther, P. Askjaer, M. Gentzel, A. Habermann, G. Griffiths, M. Wilm,
I.W. Mattaj, M. Hetzer, Nature 424 (2003) 689–694.
date_created: 2022-04-07T07:57:02Z
date_published: 2003-07-30T00:00:00Z
date_updated: 2022-07-18T08:57:40Z
day: '30'
doi: 10.1038/nature01898
extern: '1'
external_id:
pmid:
- '12894213'
intvolume: ' 424'
issue: '6949'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '07'
oa_version: None
page: 689-694
pmid: 1
publication: Nature
publication_identifier:
eissn:
- 1476-4687
issn:
- 0028-0836
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: RanGTP mediates nuclear pore complex assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 424
year: '2003'
...
---
_id: '9455'
abstract:
- lang: eng
text: Proteins of the ARGONAUTE family are important in diverse posttranscriptional
RNA-mediated gene-silencing systems as well as in transcriptional gene silencing
in Drosophila and fission yeast and in programmed DNA elimination in Tetrahymena.
We cloned ARGONAUTE4 (AGO4) from a screen for mutants that suppress silencing
of the Arabidopsis SUPERMAN(SUP) gene. The ago4-1 mutant reactivated silentSUP
alleles and decreased CpNpG and asymmetric DNA methylation as well as histone
H3 lysine-9 methylation. In addition,ago4-1 blocked histone and DNA methylation
and the accumulation of 25-nucleotide small interfering RNAs (siRNAs) that correspond
to the retroelement AtSN1. These results suggest that AGO4 and long siRNAs direct
chromatin modifications, including histone methylation and non-CpG DNA methylation.
article_processing_charge: No
article_type: original
author:
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
- first_name: ' Xiaofeng'
full_name: Cao, Xiaofeng
last_name: Cao
- first_name: Steven E.
full_name: Jacobsen, Steven E.
last_name: Jacobsen
citation:
ama: Zilberman D, Cao Xiaofeng, Jacobsen SE. ARGONAUTE4 control of locus-specific
siRNA accumulation and DNA and histone methylation. Science. 2003;299(5607):716-719.
doi:10.1126/science.1079695
apa: Zilberman, D., Cao, Xiaofeng, & Jacobsen, S. E. (2003). ARGONAUTE4 control
of locus-specific siRNA accumulation and DNA and histone methylation. Science.
American Association for the Advancement of Science. https://doi.org/10.1126/science.1079695
chicago: Zilberman, Daniel, Xiaofeng Cao, and Steven E. Jacobsen. “ARGONAUTE4 Control
of Locus-Specific SiRNA Accumulation and DNA and Histone Methylation.” Science.
American Association for the Advancement of Science, 2003. https://doi.org/10.1126/science.1079695.
ieee: D. Zilberman, Xiaofeng Cao, and S. E. Jacobsen, “ARGONAUTE4 control of locus-specific
siRNA accumulation and DNA and histone methylation,” Science, vol. 299,
no. 5607. American Association for the Advancement of Science, pp. 716–719, 2003.
ista: Zilberman D, Cao Xiaofeng, Jacobsen SE. 2003. ARGONAUTE4 control of locus-specific
siRNA accumulation and DNA and histone methylation. Science. 299(5607), 716–719.
mla: Zilberman, Daniel, et al. “ARGONAUTE4 Control of Locus-Specific SiRNA Accumulation
and DNA and Histone Methylation.” Science, vol. 299, no. 5607, American
Association for the Advancement of Science, 2003, pp. 716–19, doi:10.1126/science.1079695.
short: D. Zilberman, Xiaofeng Cao, S.E. Jacobsen, Science 299 (2003) 716–719.
date_created: 2021-06-04T11:26:26Z
date_published: 2003-01-31T00:00:00Z
date_updated: 2021-12-14T08:43:30Z
day: '31'
department:
- _id: DaZi
doi: 10.1126/science.1079695
extern: '1'
external_id:
pmid:
- '12522258'
intvolume: ' 299'
issue: '5607'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '01'
oa_version: None
page: 716-719
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: ARGONAUTE4 control of locus-specific siRNA accumulation and DNA and histone
methylation
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 299
year: '2003'
...
---
_id: '9444'
abstract:
- lang: eng
text: Epigenetic silenced alleles of the Arabidopsis SUPERMANlocus (the clark kent
alleles) are associated with dense hypermethylation at noncanonical cytosines
(CpXpG and asymmetric sites, where X = A, T, C, or G). A genetic screen for suppressors
of a hypermethylated clark kent mutant identified nine loss-of-function alleles
of CHROMOMETHYLASE3(CMT3), a novel cytosine methyltransferase homolog. These cmt3
mutants display a wild-type morphology but exhibit decreased CpXpG methylation
of the SUP gene and of other sequences throughout the genome. They also show reactivated
expression of endogenous retrotransposon sequences. These results show that a
non-CpG DNA methyltransferase is responsible for maintaining epigenetic gene silencing.
article_processing_charge: No
article_type: original
author:
- first_name: A. M.
full_name: Lindroth, A. M.
last_name: Lindroth
- first_name: Xiaofeng
full_name: Cao, Xiaofeng
last_name: Cao
- first_name: James P.
full_name: Jackson, James P.
last_name: Jackson
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
- first_name: Claire M.
full_name: McCallum, Claire M.
last_name: McCallum
- first_name: Steven
full_name: Henikoff, Steven
last_name: Henikoff
- first_name: Steven E.
full_name: Jacobsen, Steven E.
last_name: Jacobsen
citation:
ama: Lindroth AM, Cao X, Jackson JP, et al. Requirement of CHROMOMETHYLASE3 for
maintenance of CpXpG methylation. Science. 2001;292(5524):2077-2080. doi:10.1126/science.1059745
apa: Lindroth, A. M., Cao, X., Jackson, J. P., Zilberman, D., McCallum, C. M., Henikoff,
S., & Jacobsen, S. E. (2001). Requirement of CHROMOMETHYLASE3 for maintenance
of CpXpG methylation. Science. American Association for the Advancement
of Science. https://doi.org/10.1126/science.1059745
chicago: Lindroth, A. M., Xiaofeng Cao, James P. Jackson, Daniel Zilberman, Claire
M. McCallum, Steven Henikoff, and Steven E. Jacobsen. “Requirement of CHROMOMETHYLASE3
for Maintenance of CpXpG Methylation.” Science. American Association for
the Advancement of Science, 2001. https://doi.org/10.1126/science.1059745.
ieee: A. M. Lindroth et al., “Requirement of CHROMOMETHYLASE3 for maintenance
of CpXpG methylation,” Science, vol. 292, no. 5524. American Association
for the Advancement of Science, pp. 2077–2080, 2001.
ista: Lindroth AM, Cao X, Jackson JP, Zilberman D, McCallum CM, Henikoff S, Jacobsen
SE. 2001. Requirement of CHROMOMETHYLASE3 for maintenance of CpXpG methylation.
Science. 292(5524), 2077–2080.
mla: Lindroth, A. M., et al. “Requirement of CHROMOMETHYLASE3 for Maintenance of
CpXpG Methylation.” Science, vol. 292, no. 5524, American Association for
the Advancement of Science, 2001, pp. 2077–80, doi:10.1126/science.1059745.
short: A.M. Lindroth, X. Cao, J.P. Jackson, D. Zilberman, C.M. McCallum, S. Henikoff,
S.E. Jacobsen, Science 292 (2001) 2077–2080.
date_created: 2021-06-02T13:35:16Z
date_published: 2001-06-15T00:00:00Z
date_updated: 2021-12-14T08:40:32Z
day: '15'
department:
- _id: DaZi
doi: 10.1126/science.1059745
extern: '1'
external_id:
pmid:
- '11349138'
intvolume: ' 292'
issue: '5524'
keyword:
- Multidisciplinary
language:
- iso: eng
month: '06'
oa_version: None
page: 2077-2080
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Requirement of CHROMOMETHYLASE3 for maintenance of CpXpG methylation
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 292
year: '2001'
...