---
_id: '8456'
abstract:
- lang: eng
text: The large majority of three-dimensional structures of biological macromolecules
have been determined by X-ray diffraction of crystalline samples. High-resolution
structure determination crucially depends on the homogeneity of the protein crystal.
Overall ‘rocking’ motion of molecules in the crystal is expected to influence
diffraction quality, and such motion may therefore affect the process of solving
crystal structures. Yet, so far overall molecular motion has not directly been
observed in protein crystals, and the timescale of such dynamics remains unclear.
Here we use solid-state NMR, X-ray diffraction methods and μs-long molecular dynamics
simulations to directly characterize the rigid-body motion of a protein in different
crystal forms. For ubiquitin crystals investigated in this study we determine
the range of possible correlation times of rocking motion, 0.1–100 μs. The amplitude
of rocking varies from one crystal form to another and is correlated with the
resolution obtainable in X-ray diffraction experiments.
article_number: '8361'
article_processing_charge: No
article_type: original
author:
- first_name: Peixiang
full_name: Ma, Peixiang
last_name: Ma
- first_name: Yi
full_name: Xue, Yi
last_name: Xue
- first_name: Nicolas
full_name: Coquelle, Nicolas
last_name: Coquelle
- first_name: Jens D.
full_name: Haller, Jens D.
last_name: Haller
- first_name: Tairan
full_name: Yuwen, Tairan
last_name: Yuwen
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Oleg
full_name: Mikhailovskii, Oleg
last_name: Mikhailovskii
- first_name: Dieter
full_name: Willbold, Dieter
last_name: Willbold
- first_name: Jacques-Philippe
full_name: Colletier, Jacques-Philippe
last_name: Colletier
- first_name: Nikolai R.
full_name: Skrynnikov, Nikolai R.
last_name: Skrynnikov
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Ma P, Xue Y, Coquelle N, et al. Observing the overall rocking motion of a protein
in a crystal. Nature Communications. 2015;6. doi:10.1038/ncomms9361
apa: Ma, P., Xue, Y., Coquelle, N., Haller, J. D., Yuwen, T., Ayala, I., … Schanda,
P. (2015). Observing the overall rocking motion of a protein in a crystal. Nature
Communications. Springer Nature. https://doi.org/10.1038/ncomms9361
chicago: Ma, Peixiang, Yi Xue, Nicolas Coquelle, Jens D. Haller, Tairan Yuwen, Isabel
Ayala, Oleg Mikhailovskii, et al. “Observing the Overall Rocking Motion of a Protein
in a Crystal.” Nature Communications. Springer Nature, 2015. https://doi.org/10.1038/ncomms9361.
ieee: P. Ma et al., “Observing the overall rocking motion of a protein in
a crystal,” Nature Communications, vol. 6. Springer Nature, 2015.
ista: Ma P, Xue Y, Coquelle N, Haller JD, Yuwen T, Ayala I, Mikhailovskii O, Willbold
D, Colletier J-P, Skrynnikov NR, Schanda P. 2015. Observing the overall rocking
motion of a protein in a crystal. Nature Communications. 6, 8361.
mla: Ma, Peixiang, et al. “Observing the Overall Rocking Motion of a Protein in
a Crystal.” Nature Communications, vol. 6, 8361, Springer Nature, 2015,
doi:10.1038/ncomms9361.
short: P. Ma, Y. Xue, N. Coquelle, J.D. Haller, T. Yuwen, I. Ayala, O. Mikhailovskii,
D. Willbold, J.-P. Colletier, N.R. Skrynnikov, P. Schanda, Nature Communications
6 (2015).
date_created: 2020-09-18T10:07:36Z
date_published: 2015-10-05T00:00:00Z
date_updated: 2021-01-12T08:19:24Z
day: '05'
doi: 10.1038/ncomms9361
extern: '1'
intvolume: ' 6'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
month: '10'
oa_version: Published Version
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Observing the overall rocking motion of a protein in a crystal
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 6
year: '2015'
...
---
_id: '14016'
abstract:
- lang: eng
text: All attosecond time-resolved measurements have so far relied on the use of
intense near-infrared laser pulses. In particular, attosecond streaking, laser-induced
electron diffraction and high-harmonic generation all make use of non-perturbative
light–matter interactions. Remarkably, the effect of the strong laser field on
the studied sample has often been neglected in previous studies. Here we use high-harmonic
spectroscopy to measure laser-induced modifications of the electronic structure
of molecules. We study high-harmonic spectra of spatially oriented CH3F and CH3Br
as generic examples of polar polyatomic molecules. We accurately measure intensity
ratios of even and odd-harmonic orders, and of the emission from aligned and unaligned
molecules. We show that these robust observables reveal a substantial modification
of the molecular electronic structure by the external laser field. Our insights
offer new challenges and opportunities for a range of emerging strong-field attosecond
spectroscopies.
article_number: '7039'
article_processing_charge: No
article_type: original
author:
- first_name: P. M.
full_name: Kraus, P. M.
last_name: Kraus
- first_name: O. I.
full_name: Tolstikhin, O. I.
last_name: Tolstikhin
- first_name: Denitsa Rangelova
full_name: Baykusheva, Denitsa Rangelova
id: 71b4d059-2a03-11ee-914d-dfa3beed6530
last_name: Baykusheva
- first_name: A.
full_name: Rupenyan, A.
last_name: Rupenyan
- first_name: J.
full_name: Schneider, J.
last_name: Schneider
- first_name: C. Z.
full_name: Bisgaard, C. Z.
last_name: Bisgaard
- first_name: T.
full_name: Morishita, T.
last_name: Morishita
- first_name: F.
full_name: Jensen, F.
last_name: Jensen
- first_name: L. B.
full_name: Madsen, L. B.
last_name: Madsen
- first_name: H. J.
full_name: Wörner, H. J.
last_name: Wörner
citation:
ama: Kraus PM, Tolstikhin OI, Baykusheva DR, et al. Observation of laser-induced
electronic structure in oriented polyatomic molecules. Nature Communications.
2015;6. doi:10.1038/ncomms8039
apa: Kraus, P. M., Tolstikhin, O. I., Baykusheva, D. R., Rupenyan, A., Schneider,
J., Bisgaard, C. Z., … Wörner, H. J. (2015). Observation of laser-induced electronic
structure in oriented polyatomic molecules. Nature Communications. Springer
Nature. https://doi.org/10.1038/ncomms8039
chicago: Kraus, P. M., O. I. Tolstikhin, Denitsa Rangelova Baykusheva, A. Rupenyan,
J. Schneider, C. Z. Bisgaard, T. Morishita, F. Jensen, L. B. Madsen, and H. J.
Wörner. “Observation of Laser-Induced Electronic Structure in Oriented Polyatomic
Molecules.” Nature Communications. Springer Nature, 2015. https://doi.org/10.1038/ncomms8039.
ieee: P. M. Kraus et al., “Observation of laser-induced electronic structure
in oriented polyatomic molecules,” Nature Communications, vol. 6. Springer
Nature, 2015.
ista: Kraus PM, Tolstikhin OI, Baykusheva DR, Rupenyan A, Schneider J, Bisgaard
CZ, Morishita T, Jensen F, Madsen LB, Wörner HJ. 2015. Observation of laser-induced
electronic structure in oriented polyatomic molecules. Nature Communications.
6, 7039.
mla: Kraus, P. M., et al. “Observation of Laser-Induced Electronic Structure in
Oriented Polyatomic Molecules.” Nature Communications, vol. 6, 7039, Springer
Nature, 2015, doi:10.1038/ncomms8039.
short: P.M. Kraus, O.I. Tolstikhin, D.R. Baykusheva, A. Rupenyan, J. Schneider,
C.Z. Bisgaard, T. Morishita, F. Jensen, L.B. Madsen, H.J. Wörner, Nature Communications
6 (2015).
date_created: 2023-08-10T06:38:01Z
date_published: 2015-05-05T00:00:00Z
date_updated: 2023-08-22T08:52:56Z
day: '05'
doi: 10.1038/ncomms8039
extern: '1'
external_id:
pmid:
- '25940229'
intvolume: ' 6'
keyword:
- General Physics and Astronomy
- General Biochemistry
- Genetics and Molecular Biology
- General Chemistry
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/ncomms8039
month: '05'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
eissn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Observation of laser-induced electronic structure in oriented polyatomic molecules
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 6
year: '2015'
...
---
_id: '11080'
abstract:
- lang: eng
text: The spindle assembly checkpoint prevents separation of sister chromatids until
each kinetochore is attached to the mitotic spindle. Rodriguez-Bravo et al. report
that the nuclear pore complex scaffolds spindle assembly checkpoint signaling
in interphase, providing a store of inhibitory signals that limits the speed of
the subsequent mitosis.
article_processing_charge: No
article_type: original
author:
- first_name: Abigail
full_name: Buchwalter, Abigail
last_name: Buchwalter
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Buchwalter A, Hetzer M. Nuclear pores set the speed limit for mitosis. Cell.
2014;156(5):868-869. doi:10.1016/j.cell.2014.02.004
apa: Buchwalter, A., & Hetzer, M. (2014). Nuclear pores set the speed limit
for mitosis. Cell. Elsevier. https://doi.org/10.1016/j.cell.2014.02.004
chicago: Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit
for Mitosis.” Cell. Elsevier, 2014. https://doi.org/10.1016/j.cell.2014.02.004.
ieee: A. Buchwalter and M. Hetzer, “Nuclear pores set the speed limit for mitosis,”
Cell, vol. 156, no. 5. Elsevier, pp. 868–869, 2014.
ista: Buchwalter A, Hetzer M. 2014. Nuclear pores set the speed limit for mitosis.
Cell. 156(5), 868–869.
mla: Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit
for Mitosis.” Cell, vol. 156, no. 5, Elsevier, 2014, pp. 868–69, doi:10.1016/j.cell.2014.02.004.
short: A. Buchwalter, M. Hetzer, Cell 156 (2014) 868–869.
date_created: 2022-04-07T07:50:04Z
date_published: 2014-02-27T00:00:00Z
date_updated: 2022-07-18T08:44:33Z
day: '27'
doi: 10.1016/j.cell.2014.02.004
extern: '1'
external_id:
pmid:
- '24581486'
intvolume: ' 156'
issue: '5'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2014.02.004
month: '02'
oa: 1
oa_version: Published Version
page: 868-869
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nuclear pores set the speed limit for mitosis
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 156
year: '2014'
...
---
_id: '11082'
abstract:
- lang: eng
text: The nuclear pore complex (NPC) plays a critical role in gene expression by
mediating import of transcription regulators into the nucleus and export of RNA
transcripts to the cytoplasm. Emerging evidence suggests that in addition to mediating
transport, a subset of nucleoporins (Nups) engage in transcriptional activation
and elongation at genomic loci that are not associated with NPCs. The underlying
mechanism and regulation of Nup mobility on and off nuclear pores remain unclear.
Here we show that Nup50 is a mobile Nup with a pronounced presence both at the
NPC and in the nucleoplasm that can move between these different localizations.
Strikingly, the dynamic behavior of Nup50 in both locations is dependent on active
transcription by RNA polymerase II and requires the N-terminal half of the protein,
which contains importin α– and Nup153-binding domains. However, Nup50 dynamics
are independent of importin α, Nup153, and Nup98, even though the latter two proteins
also exhibit transcription-dependent mobility. Of interest, depletion of Nup50
from C2C12 myoblasts does not affect cell proliferation but inhibits differentiation
into myotubes. Taken together, our results suggest a transport-independent role
for Nup50 in chromatin biology that occurs away from the NPC.
article_processing_charge: No
article_type: original
author:
- first_name: Abigail L.
full_name: Buchwalter, Abigail L.
last_name: Buchwalter
- first_name: Yun
full_name: Liang, Yun
last_name: Liang
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Buchwalter AL, Liang Y, Hetzer M. Nup50 is required for cell differentiation
and exhibits transcription-dependent dynamics. Molecular Biology of the Cell.
2014;25(16):2472-2484. doi:10.1091/mbc.e14-04-0865
apa: Buchwalter, A. L., Liang, Y., & Hetzer, M. (2014). Nup50 is required for
cell differentiation and exhibits transcription-dependent dynamics. Molecular
Biology of the Cell. American Society for Cell Biology. https://doi.org/10.1091/mbc.e14-04-0865
chicago: Buchwalter, Abigail L., Yun Liang, and Martin Hetzer. “Nup50 Is Required
for Cell Differentiation and Exhibits Transcription-Dependent Dynamics.” Molecular
Biology of the Cell. American Society for Cell Biology, 2014. https://doi.org/10.1091/mbc.e14-04-0865.
ieee: A. L. Buchwalter, Y. Liang, and M. Hetzer, “Nup50 is required for cell differentiation
and exhibits transcription-dependent dynamics,” Molecular Biology of the Cell,
vol. 25, no. 16. American Society for Cell Biology, pp. 2472–2484, 2014.
ista: Buchwalter AL, Liang Y, Hetzer M. 2014. Nup50 is required for cell differentiation
and exhibits transcription-dependent dynamics. Molecular Biology of the Cell.
25(16), 2472–2484.
mla: Buchwalter, Abigail L., et al. “Nup50 Is Required for Cell Differentiation
and Exhibits Transcription-Dependent Dynamics.” Molecular Biology of the Cell,
vol. 25, no. 16, American Society for Cell Biology, 2014, pp. 2472–84, doi:10.1091/mbc.e14-04-0865.
short: A.L. Buchwalter, Y. Liang, M. Hetzer, Molecular Biology of the Cell 25 (2014)
2472–2484.
date_created: 2022-04-07T07:50:24Z
date_published: 2014-08-15T00:00:00Z
date_updated: 2022-07-18T08:45:20Z
day: '15'
doi: 10.1091/mbc.e14-04-0865
extern: '1'
intvolume: ' 25'
issue: '16'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1091/mbc.e14-04-0865
month: '08'
oa: 1
oa_version: Published Version
page: 2472-2484
publication: Molecular Biology of the Cell
publication_identifier:
issn:
- 1059-1524
- 1939-4586
publication_status: published
publisher: American Society for Cell Biology
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nup50 is required for cell differentiation and exhibits transcription-dependent
dynamics
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 25
year: '2014'
...
---
_id: '8459'
abstract:
- lang: eng
text: Nuclear magnetic resonance (NMR) is a powerful tool for observing the motion
of biomolecules at the atomic level. One technique, the analysis of relaxation
dispersion phenomenon, is highly suited for studying the kinetics and thermodynamics
of biological processes. Built on top of the relax computational environment for
NMR dynamics is a new dispersion analysis designed to be comprehensive, accurate
and easy-to-use. The software supports more models, both numeric and analytic,
than current solutions. An automated protocol, available for scripting and driving
the graphical user interface (GUI), is designed to simplify the analysis of dispersion
data for NMR spectroscopists. Decreases in optimization time are granted by parallelization
for running on computer clusters and by skipping an initial grid search by using
parameters from one solution as the starting point for another —using analytic
model results for the numeric models, taking advantage of model nesting, and using
averaged non-clustered results for the clustered analysis.
article_processing_charge: No
article_type: original
author:
- first_name: Sébastien
full_name: Morin, Sébastien
last_name: Morin
- first_name: Troels E
full_name: Linnet, Troels E
last_name: Linnet
- first_name: Mathilde
full_name: Lescanne, Mathilde
last_name: Lescanne
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Gary S
full_name: Thompson, Gary S
last_name: Thompson
- first_name: Martin
full_name: Tollinger, Martin
last_name: Tollinger
- first_name: Kaare
full_name: Teilum, Kaare
last_name: Teilum
- first_name: Stéphane
full_name: Gagné, Stéphane
last_name: Gagné
- first_name: Dominique
full_name: Marion, Dominique
last_name: Marion
- first_name: Christian
full_name: Griesinger, Christian
last_name: Griesinger
- first_name: Martin
full_name: Blackledge, Martin
last_name: Blackledge
- first_name: Edward J
full_name: d’Auvergne, Edward J
last_name: d’Auvergne
citation:
ama: 'Morin S, Linnet TE, Lescanne M, et al. Relax: The analysis of biomolecular
kinetics and thermodynamics using NMR relaxation dispersion data. Bioinformatics.
2014;30(15):2219-2220. doi:10.1093/bioinformatics/btu166'
apa: 'Morin, S., Linnet, T. E., Lescanne, M., Schanda, P., Thompson, G. S., Tollinger,
M., … d’Auvergne, E. J. (2014). Relax: The analysis of biomolecular kinetics and
thermodynamics using NMR relaxation dispersion data. Bioinformatics. Oxford
University Press. https://doi.org/10.1093/bioinformatics/btu166'
chicago: 'Morin, Sébastien, Troels E Linnet, Mathilde Lescanne, Paul Schanda, Gary
S Thompson, Martin Tollinger, Kaare Teilum, et al. “Relax: The Analysis of Biomolecular
Kinetics and Thermodynamics Using NMR Relaxation Dispersion Data.” Bioinformatics.
Oxford University Press, 2014. https://doi.org/10.1093/bioinformatics/btu166.'
ieee: 'S. Morin et al., “Relax: The analysis of biomolecular kinetics and
thermodynamics using NMR relaxation dispersion data,” Bioinformatics, vol.
30, no. 15. Oxford University Press, pp. 2219–2220, 2014.'
ista: 'Morin S, Linnet TE, Lescanne M, Schanda P, Thompson GS, Tollinger M, Teilum
K, Gagné S, Marion D, Griesinger C, Blackledge M, d’Auvergne EJ. 2014. Relax:
The analysis of biomolecular kinetics and thermodynamics using NMR relaxation
dispersion data. Bioinformatics. 30(15), 2219–2220.'
mla: 'Morin, Sébastien, et al. “Relax: The Analysis of Biomolecular Kinetics and
Thermodynamics Using NMR Relaxation Dispersion Data.” Bioinformatics, vol.
30, no. 15, Oxford University Press, 2014, pp. 2219–20, doi:10.1093/bioinformatics/btu166.'
short: S. Morin, T.E. Linnet, M. Lescanne, P. Schanda, G.S. Thompson, M. Tollinger,
K. Teilum, S. Gagné, D. Marion, C. Griesinger, M. Blackledge, E.J. d’Auvergne,
Bioinformatics 30 (2014) 2219–2220.
date_created: 2020-09-18T10:08:07Z
date_published: 2014-08-01T00:00:00Z
date_updated: 2021-01-12T08:19:25Z
day: '01'
doi: 10.1093/bioinformatics/btu166
extern: '1'
intvolume: ' 30'
issue: '15'
keyword:
- Statistics and Probability
- Computational Theory and Mathematics
- Biochemistry
- Molecular Biology
- Computational Mathematics
- Computer Science Applications
language:
- iso: eng
month: '08'
oa_version: None
page: 2219-2220
publication: Bioinformatics
publication_identifier:
issn:
- 1367-4803
- 1460-2059
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1093/bioinformatics/btz397
status: public
title: 'Relax: The analysis of biomolecular kinetics and thermodynamics using NMR
relaxation dispersion data'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 30
year: '2014'
...
---
_id: '13402'
abstract:
- lang: eng
text: Nanoporous frameworks are polymeric materials built from rigid molecules,
which give rise to their nanoporous structures with applications in gas sorption
and storage, catalysis and others. Conceptually new applications could emerge,
should these beneficial properties be manipulated by external stimuli in a reversible
manner. One approach to render nanoporous frameworks responsive to external signals
would be to immobilize molecular switches within their nanopores. Although the
majority of molecular switches require conformational freedom to isomerize, and
switching in the solid state is prohibited, the nanopores may provide enough room
for the switches to efficiently isomerize. Here we describe two families of nanoporous
materials incorporating the spiropyran molecular switch. These materials exhibit
a variety of interesting properties, including reversible photochromism and acidochromism
under solvent-free conditions, light-controlled capture and release of metal ions,
as well reversible chromism induced by solvation/desolvation.
article_number: '3588'
article_processing_charge: No
article_type: original
author:
- first_name: Pintu K.
full_name: Kundu, Pintu K.
last_name: Kundu
- first_name: Gregory L.
full_name: Olsen, Gregory L.
last_name: Olsen
- first_name: Vladimir
full_name: Kiss, Vladimir
last_name: Kiss
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Kundu PK, Olsen GL, Kiss V, Klajn R. Nanoporous frameworks exhibiting multiple
stimuli responsiveness. Nature Communications. 2014;5. doi:10.1038/ncomms4588
apa: Kundu, P. K., Olsen, G. L., Kiss, V., & Klajn, R. (2014). Nanoporous frameworks
exhibiting multiple stimuli responsiveness. Nature Communications. Springer
Nature. https://doi.org/10.1038/ncomms4588
chicago: Kundu, Pintu K., Gregory L. Olsen, Vladimir Kiss, and Rafal Klajn. “Nanoporous
Frameworks Exhibiting Multiple Stimuli Responsiveness.” Nature Communications.
Springer Nature, 2014. https://doi.org/10.1038/ncomms4588.
ieee: P. K. Kundu, G. L. Olsen, V. Kiss, and R. Klajn, “Nanoporous frameworks exhibiting
multiple stimuli responsiveness,” Nature Communications, vol. 5. Springer
Nature, 2014.
ista: Kundu PK, Olsen GL, Kiss V, Klajn R. 2014. Nanoporous frameworks exhibiting
multiple stimuli responsiveness. Nature Communications. 5, 3588.
mla: Kundu, Pintu K., et al. “Nanoporous Frameworks Exhibiting Multiple Stimuli
Responsiveness.” Nature Communications, vol. 5, 3588, Springer Nature,
2014, doi:10.1038/ncomms4588.
short: P.K. Kundu, G.L. Olsen, V. Kiss, R. Klajn, Nature Communications 5 (2014).
date_created: 2023-08-01T09:46:27Z
date_published: 2014-04-07T00:00:00Z
date_updated: 2023-08-08T07:28:10Z
day: '07'
doi: 10.1038/ncomms4588
extern: '1'
external_id:
pmid:
- '24709950'
intvolume: ' 5'
keyword:
- General Physics and Astronomy
- General Biochemistry
- Genetics and Molecular Biology
- General Chemistry
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/ncomms4588
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
eissn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nanoporous frameworks exhibiting multiple stimuli responsiveness
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2014'
...
---
_id: '11084'
abstract:
- lang: eng
text: Protein turnover is an effective way of maintaining a functional proteome,
as old and potentially damaged polypeptides are destroyed and replaced by newly
synthesized copies. An increasing number of intracellular proteins, however, have
been identified that evade this turnover process and instead are maintained over
a cell's lifetime. This diverse group of long-lived proteins might be particularly
prone to accumulation of damage and thus have a crucial role in the functional
deterioration of key regulatory processes during ageing.
article_processing_charge: No
article_type: original
author:
- first_name: Brandon H.
full_name: Toyama, Brandon H.
last_name: Toyama
- 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: 'Toyama BH, Hetzer M. Protein homeostasis: Live long, won’t prosper. Nature
Reviews Molecular Cell Biology. 2013;14:55-61. doi:10.1038/nrm3496'
apa: 'Toyama, B. H., & Hetzer, M. (2013). Protein homeostasis: Live long, won’t
prosper. Nature Reviews Molecular Cell Biology. Springer Nature. https://doi.org/10.1038/nrm3496'
chicago: 'Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long,
Won’t Prosper.” Nature Reviews Molecular Cell Biology. Springer Nature,
2013. https://doi.org/10.1038/nrm3496.'
ieee: 'B. H. Toyama and M. Hetzer, “Protein homeostasis: Live long, won’t prosper,”
Nature Reviews Molecular Cell Biology, vol. 14. Springer Nature, pp. 55–61,
2013.'
ista: 'Toyama BH, Hetzer M. 2013. Protein homeostasis: Live long, won’t prosper.
Nature Reviews Molecular Cell Biology. 14, 55–61.'
mla: 'Toyama, Brandon H., and Martin Hetzer. “Protein Homeostasis: Live Long, Won’t
Prosper.” Nature Reviews Molecular Cell Biology, vol. 14, Springer Nature,
2013, pp. 55–61, doi:10.1038/nrm3496.'
short: B.H. Toyama, M. Hetzer, Nature Reviews Molecular Cell Biology 14 (2013) 55–61.
date_created: 2022-04-07T07:50:43Z
date_published: 2013-01-01T00:00:00Z
date_updated: 2022-07-18T08:37:53Z
day: '01'
doi: 10.1038/nrm3496
extern: '1'
external_id:
pmid:
- '23258296'
intvolume: ' 14'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
month: '01'
oa_version: None
page: 55-61
pmid: 1
publication: Nature Reviews Molecular Cell Biology
publication_identifier:
issn:
- 1471-0072
- 1471-0080
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Protein homeostasis: Live long, won''t prosper'
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 14
year: '2013'
...
---
_id: '11085'
abstract:
- lang: eng
text: During mitotic exit, missegregated chromosomes can recruit their own nuclear
envelope (NE) to form micronuclei (MN). MN have reduced functioning compared to
primary nuclei in the same cell, although the two compartments appear to be structurally
comparable. Here we show that over 60% of MN undergo an irreversible loss of compartmentalization
during interphase due to NE collapse. This disruption of the MN, which is induced
by defects in nuclear lamina assembly, drastically reduces nuclear functions and
can trigger massive DNA damage. MN disruption is associated with chromatin compaction
and invasion of endoplasmic reticulum (ER) tubules into the chromatin. We identified
disrupted MN in both major subtypes of human non-small-cell lung cancer, suggesting
that disrupted MN could be a useful objective biomarker for genomic instability
in solid tumors. Our study shows that NE collapse is a key event underlying MN
dysfunction and establishes a link between aberrant NE organization and aneuploidy.
article_processing_charge: No
article_type: original
author:
- first_name: Emily M.
full_name: Hatch, Emily M.
last_name: Hatch
- first_name: Andrew H.
full_name: Fischer, Andrew H.
last_name: Fischer
- first_name: Thomas J.
full_name: Deerinck, Thomas J.
last_name: Deerinck
- 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: Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. Catastrophic nuclear envelope
collapse in cancer cell micronuclei. Cell. 2013;154(1):47-60. doi:10.1016/j.cell.2013.06.007
apa: Hatch, E. M., Fischer, A. H., Deerinck, T. J., & Hetzer, M. (2013). Catastrophic
nuclear envelope collapse in cancer cell micronuclei. Cell. Elsevier. https://doi.org/10.1016/j.cell.2013.06.007
chicago: Hatch, Emily M., Andrew H. Fischer, Thomas J. Deerinck, and Martin Hetzer.
“Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” Cell.
Elsevier, 2013. https://doi.org/10.1016/j.cell.2013.06.007.
ieee: E. M. Hatch, A. H. Fischer, T. J. Deerinck, and M. Hetzer, “Catastrophic nuclear
envelope collapse in cancer cell micronuclei,” Cell, vol. 154, no. 1. Elsevier,
pp. 47–60, 2013.
ista: Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. 2013. Catastrophic nuclear envelope
collapse in cancer cell micronuclei. Cell. 154(1), 47–60.
mla: Hatch, Emily M., et al. “Catastrophic Nuclear Envelope Collapse in Cancer Cell
Micronuclei.” Cell, vol. 154, no. 1, Elsevier, 2013, pp. 47–60, doi:10.1016/j.cell.2013.06.007.
short: E.M. Hatch, A.H. Fischer, T.J. Deerinck, M. Hetzer, Cell 154 (2013) 47–60.
date_created: 2022-04-07T07:50:51Z
date_published: 2013-07-03T00:00:00Z
date_updated: 2022-07-18T08:45:47Z
day: '03'
doi: 10.1016/j.cell.2013.06.007
extern: '1'
external_id:
pmid:
- '23827674'
intvolume: ' 154'
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2013.06.007
month: '07'
oa: 1
oa_version: Published Version
page: 47-60
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Catastrophic nuclear envelope collapse in cancer cell micronuclei
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 154
year: '2013'
...
---
_id: '11086'
abstract:
- lang: eng
text: Faithful execution of developmental gene expression programs occurs at multiple
levels and involves many different components such as transcription factors, histone-modification
enzymes, and mRNA processing proteins. Recent evidence suggests that nucleoporins,
well known components that control nucleo-cytoplasmic trafficking, have wide-ranging
functions in developmental gene regulation that potentially extend beyond their
role in nuclear transport. Whether the unexpected role of nuclear pore proteins
in transcription regulation, which initially has been described in fungi and flies,
also applies to human cells is unknown. Here we show at a genome-wide level that
the nuclear pore protein NUP98 associates with developmentally regulated genes
active during human embryonic stem cell differentiation. Overexpression of a dominant
negative fragment of NUP98 levels decreases expression levels of NUP98-bound genes.
In addition, we identify two modes of developmental gene regulation by NUP98 that
are differentiated by the spatial localization of NUP98 target genes. Genes in
the initial stage of developmental induction can associate with NUP98 that is
embedded in the nuclear pores at the nuclear periphery. Alternatively, genes that
are highly induced can interact with NUP98 in the nuclear interior, away from
the nuclear pores. This work demonstrates for the first time that NUP98 dynamically
associates with the human genome during differentiation, revealing a role of a
nuclear pore protein in regulating developmental gene expression programs.
article_number: e1003308
article_processing_charge: No
article_type: original
author:
- first_name: Yun
full_name: Liang, Yun
last_name: Liang
- first_name: Tobias M.
full_name: Franks, Tobias M.
last_name: Franks
- first_name: Maria C.
full_name: Marchetto, Maria C.
last_name: Marchetto
- first_name: Fred H.
full_name: Gage, Fred H.
last_name: Gage
- 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: Liang Y, Franks TM, Marchetto MC, Gage FH, Hetzer M. Dynamic association of
NUP98 with the human genome. PLoS Genetics. 2013;9(2). doi:10.1371/journal.pgen.1003308
apa: Liang, Y., Franks, T. M., Marchetto, M. C., Gage, F. H., & Hetzer, M. (2013).
Dynamic association of NUP98 with the human genome. PLoS Genetics. Public
Library of Science. https://doi.org/10.1371/journal.pgen.1003308
chicago: Liang, Yun, Tobias M. Franks, Maria C. Marchetto, Fred H. Gage, and Martin
Hetzer. “Dynamic Association of NUP98 with the Human Genome.” PLoS Genetics.
Public Library of Science, 2013. https://doi.org/10.1371/journal.pgen.1003308.
ieee: Y. Liang, T. M. Franks, M. C. Marchetto, F. H. Gage, and M. Hetzer, “Dynamic
association of NUP98 with the human genome,” PLoS Genetics, vol. 9, no.
2. Public Library of Science, 2013.
ista: Liang Y, Franks TM, Marchetto MC, Gage FH, Hetzer M. 2013. Dynamic association
of NUP98 with the human genome. PLoS Genetics. 9(2), e1003308.
mla: Liang, Yun, et al. “Dynamic Association of NUP98 with the Human Genome.” PLoS
Genetics, vol. 9, no. 2, e1003308, Public Library of Science, 2013, doi:10.1371/journal.pgen.1003308.
short: Y. Liang, T.M. Franks, M.C. Marchetto, F.H. Gage, M. Hetzer, PLoS Genetics
9 (2013).
date_created: 2022-04-07T07:50:59Z
date_published: 2013-02-28T00:00:00Z
date_updated: 2022-07-18T08:45:58Z
day: '28'
doi: 10.1371/journal.pgen.1003308
extern: '1'
external_id:
pmid:
- '23468646'
intvolume: ' 9'
issue: '2'
keyword:
- Cancer Research
- Genetics (clinical)
- Genetics
- Molecular Biology
- Ecology
- Evolution
- Behavior and Systematics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1371/journal.pgen.1003308
month: '02'
oa: 1
oa_version: Published Version
pmid: 1
publication: PLoS Genetics
publication_identifier:
issn:
- 1553-7404
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Dynamic association of NUP98 with the human genome
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 9
year: '2013'
...
---
_id: '11087'
abstract:
- lang: eng
text: Intracellular proteins with long lifespans have recently been linked to age-dependent
defects, ranging from decreased fertility to the functional decline of neurons.
Why long-lived proteins exist in metabolically active cellular environments and
how they are maintained over time remains poorly understood. Here, we provide
a system-wide identification of proteins with exceptional lifespans in the rat
brain. These proteins are inefficiently replenished despite being translated robustly
throughout adulthood. Using nucleoporins as a paradigm for long-term protein persistence,
we found that nuclear pore complexes (NPCs) are maintained over a cell’s life
through slow but finite exchange of even its most stable subcomplexes. This maintenance
is limited, however, as some nucleoporin levels decrease during aging, providing
a rationale for the previously observed age-dependent deterioration of NPC function.
Our identification of a long-lived proteome reveals cellular components that are
at increased risk for damage accumulation, linking long-term protein persistence
to the cellular aging process.
article_processing_charge: No
article_type: original
author:
- first_name: Brandon H.
full_name: Toyama, Brandon H.
last_name: Toyama
- first_name: Jeffrey N.
full_name: Savas, Jeffrey N.
last_name: Savas
- first_name: Sung Kyu
full_name: Park, Sung Kyu
last_name: Park
- first_name: Michael S.
full_name: Harris, Michael S.
last_name: Harris
- first_name: Nicholas T.
full_name: Ingolia, Nicholas T.
last_name: Ingolia
- 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: Toyama BH, Savas JN, Park SK, et al. Identification of long-lived proteins
reveals exceptional stability of essential cellular structures. Cell. 2013;154(5):971-982.
doi:10.1016/j.cell.2013.07.037
apa: Toyama, B. H., Savas, J. N., Park, S. K., Harris, M. S., Ingolia, N. T., Yates,
J. R., & Hetzer, M. (2013). Identification of long-lived proteins reveals
exceptional stability of essential cellular structures. Cell. Elsevier.
https://doi.org/10.1016/j.cell.2013.07.037
chicago: Toyama, Brandon H., Jeffrey N. Savas, Sung Kyu Park, Michael S. Harris,
Nicholas T. Ingolia, John R. Yates, and Martin Hetzer. “Identification of Long-Lived
Proteins Reveals Exceptional Stability of Essential Cellular Structures.” Cell.
Elsevier, 2013. https://doi.org/10.1016/j.cell.2013.07.037.
ieee: B. H. Toyama et al., “Identification of long-lived proteins reveals
exceptional stability of essential cellular structures,” Cell, vol. 154,
no. 5. Elsevier, pp. 971–982, 2013.
ista: Toyama BH, Savas JN, Park SK, Harris MS, Ingolia NT, Yates JR, Hetzer M. 2013.
Identification of long-lived proteins reveals exceptional stability of essential
cellular structures. Cell. 154(5), 971–982.
mla: Toyama, Brandon H., et al. “Identification of Long-Lived Proteins Reveals Exceptional
Stability of Essential Cellular Structures.” Cell, vol. 154, no. 5, Elsevier,
2013, pp. 971–82, doi:10.1016/j.cell.2013.07.037.
short: B.H. Toyama, J.N. Savas, S.K. Park, M.S. Harris, N.T. Ingolia, J.R. Yates,
M. Hetzer, Cell 154 (2013) 971–982.
date_created: 2022-04-07T07:51:08Z
date_published: 2013-08-29T00:00:00Z
date_updated: 2022-07-18T08:50:47Z
day: '29'
doi: 10.1016/j.cell.2013.07.037
extern: '1'
external_id:
pmid:
- '23993091'
intvolume: ' 154'
issue: '5'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2013.07.037
month: '08'
oa: 1
oa_version: Published Version
page: 971-982
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Identification of long-lived proteins reveals exceptional stability of essential
cellular structures
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 154
year: '2013'
...
---
_id: '8462'
abstract:
- lang: eng
text: The transition of proteins from their soluble functional state to amyloid
fibrils and aggregates is associated with the onset of several human diseases.
Protein aggregation often requires some structural reshaping and the subsequent
formation of intermolecular contacts. Therefore, the study of the conformation
of excited protein states and their ability to form oligomers is of primary importance
for understanding the molecular basis of amyloid fibril formation. Here, we investigated
the oligomerization processes that occur along the folding of the amyloidogenic
human protein β2-microglobulin. The combination of real-time two-dimensional NMR
data with real-time small-angle X-ray scattering measurements allowed us to derive
thermodynamic and kinetic information on protein oligomerization of different
conformational states populated along the folding pathways. In particular, we
could demonstrate that a long-lived folding intermediate (I-state) has a higher
propensity to oligomerize compared to the native state. Our data agree well with
a simple five-state kinetic model that involves only monomeric and dimeric species.
The dimers have an elongated shape with the dimerization interface located at
the apical side of β2-microglobulin close to Pro32, the residue that has a trans
conformation in the I-state and a cis conformation in the native (N) state. Our
experimental data suggest that partial unfolding in the apical half of the protein
close to Pro32 leads to an excited state conformation with enhanced propensity
for oligomerization. This excited state becomes more populated in the transient
I-state due to the destabilization of the native conformation by the trans-Pro32
configuration.
article_processing_charge: No
article_type: original
author:
- first_name: E.
full_name: Rennella, E.
last_name: Rennella
- first_name: T.
full_name: Cutuil, T.
last_name: Cutuil
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: I.
full_name: Ayala, I.
last_name: Ayala
- first_name: F.
full_name: Gabel, F.
last_name: Gabel
- first_name: V.
full_name: Forge, V.
last_name: Forge
- first_name: A.
full_name: Corazza, A.
last_name: Corazza
- first_name: G.
full_name: Esposito, G.
last_name: Esposito
- first_name: B.
full_name: Brutscher, B.
last_name: Brutscher
citation:
ama: 'Rennella E, Cutuil T, Schanda P, et al. Oligomeric states along the folding
pathways of β2-microglobulin: Kinetics, thermodynamics, and structure. Journal
of Molecular Biology. 2013;425(15):2722-2736. doi:10.1016/j.jmb.2013.04.028'
apa: 'Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Gabel, F., Forge, V., …
Brutscher, B. (2013). Oligomeric states along the folding pathways of β2-microglobulin:
Kinetics, thermodynamics, and structure. Journal of Molecular Biology.
Elsevier. https://doi.org/10.1016/j.jmb.2013.04.028'
chicago: 'Rennella, E., T. Cutuil, Paul Schanda, I. Ayala, F. Gabel, V. Forge, A.
Corazza, G. Esposito, and B. Brutscher. “Oligomeric States along the Folding Pathways
of Β2-Microglobulin: Kinetics, Thermodynamics, and Structure.” Journal of Molecular
Biology. Elsevier, 2013. https://doi.org/10.1016/j.jmb.2013.04.028.'
ieee: 'E. Rennella et al., “Oligomeric states along the folding pathways
of β2-microglobulin: Kinetics, thermodynamics, and structure,” Journal of Molecular
Biology, vol. 425, no. 15. Elsevier, pp. 2722–2736, 2013.'
ista: 'Rennella E, Cutuil T, Schanda P, Ayala I, Gabel F, Forge V, Corazza A, Esposito
G, Brutscher B. 2013. Oligomeric states along the folding pathways of β2-microglobulin:
Kinetics, thermodynamics, and structure. Journal of Molecular Biology. 425(15),
2722–2736.'
mla: 'Rennella, E., et al. “Oligomeric States along the Folding Pathways of Β2-Microglobulin:
Kinetics, Thermodynamics, and Structure.” Journal of Molecular Biology,
vol. 425, no. 15, Elsevier, 2013, pp. 2722–36, doi:10.1016/j.jmb.2013.04.028.'
short: E. Rennella, T. Cutuil, P. Schanda, I. Ayala, F. Gabel, V. Forge, A. Corazza,
G. Esposito, B. Brutscher, Journal of Molecular Biology 425 (2013) 2722–2736.
date_created: 2020-09-18T10:09:12Z
date_published: 2013-08-09T00:00:00Z
date_updated: 2022-08-25T14:56:24Z
day: '09'
doi: 10.1016/j.jmb.2013.04.028
extern: '1'
intvolume: ' 425'
issue: '15'
keyword:
- Molecular Biology
language:
- iso: eng
month: '08'
oa_version: None
page: 2722-2736
publication: Journal of Molecular Biology
publication_identifier:
issn:
- 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: 'Oligomeric states along the folding pathways of β2-microglobulin: Kinetics,
thermodynamics, and structure'
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 425
year: '2013'
...
---
_id: '11090'
abstract:
- lang: eng
text: Nuclear export of mRNAs is thought to occur exclusively through nuclear pore
complexes. In this issue of Cell, Speese et al. identify an alternate pathway
for mRNA export in muscle cells where ribonucleoprotein complexes involved in
forming neuromuscular junctions transit the nuclear envelope by fusing with and
budding through the nuclear membrane.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Emily M.
full_name: Hatch, Emily M.
last_name: Hatch
- 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: Hatch EM, Hetzer M. RNP export by nuclear envelope budding. Cell. 2012;149(4):733-735.
doi:10.1016/j.cell.2012.04.018
apa: Hatch, E. M., & Hetzer, M. (2012). RNP export by nuclear envelope budding.
Cell. Elsevier. https://doi.org/10.1016/j.cell.2012.04.018
chicago: Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.”
Cell. Elsevier, 2012. https://doi.org/10.1016/j.cell.2012.04.018.
ieee: E. M. Hatch and M. Hetzer, “RNP export by nuclear envelope budding,” Cell,
vol. 149, no. 4. Elsevier, pp. 733–735, 2012.
ista: Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4),
733–735.
mla: Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.”
Cell, vol. 149, no. 4, Elsevier, 2012, pp. 733–35, doi:10.1016/j.cell.2012.04.018.
short: E.M. Hatch, M. Hetzer, Cell 149 (2012) 733–735.
date_created: 2022-04-07T07:51:45Z
date_published: 2012-05-11T00:00:00Z
date_updated: 2022-07-18T08:58:48Z
day: '11'
doi: 10.1016/j.cell.2012.04.018
extern: '1'
external_id:
pmid:
- '22579277'
intvolume: ' 149'
issue: '4'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2012.04.018
month: '05'
oa: 1
oa_version: Published Version
page: 733-735
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: RNP export by nuclear envelope budding
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 149
year: '2012'
...
---
_id: '11093'
abstract:
- lang: eng
text: Nuclear pore complexes (NPCs) are built from ∼30 different proteins called
nucleoporins or Nups. Previous studies have shown that several Nups exhibit cell-type-specific
expression and that mutations in NPC components result in tissue-specific diseases.
Here we show that a specific change in NPC composition is required for both myogenic
and neuronal differentiation. The transmembrane nucleoporin Nup210 is absent in
proliferating myoblasts and embryonic stem cells (ESCs) but becomes expressed
and incorporated into NPCs during cell differentiation. Preventing Nup210 production
by RNAi blocks myogenesis and the differentiation of ESCs into neuroprogenitors.
We found that the addition of Nup210 to NPCs does not affect nuclear transport
but is required for the induction of genes that are essential for cell differentiation.
Our results identify a single change in NPC composition as an essential step in
cell differentiation and establish a role for Nup210 in gene expression regulation
and cell fate determination.
article_processing_charge: No
article_type: original
author:
- first_name: Maximiliano A.
full_name: D'Angelo, Maximiliano A.
last_name: D'Angelo
- first_name: J. Sebastian
full_name: Gomez-Cavazos, J. Sebastian
last_name: Gomez-Cavazos
- first_name: Arianna
full_name: Mei, Arianna
last_name: Mei
- first_name: Daniel H.
full_name: Lackner, Daniel H.
last_name: Lackner
- 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, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. A change in nuclear
pore complex composition regulates cell differentiation. Developmental Cell.
2012;22(2):446-458. doi:10.1016/j.devcel.2011.11.021
apa: D’Angelo, M. A., Gomez-Cavazos, J. S., Mei, A., Lackner, D. H., & Hetzer,
M. (2012). A change in nuclear pore complex composition regulates cell differentiation.
Developmental Cell. Elsevier. https://doi.org/10.1016/j.devcel.2011.11.021
chicago: D’Angelo, Maximiliano A., J. Sebastian Gomez-Cavazos, Arianna Mei, Daniel H.
Lackner, and Martin Hetzer. “A Change in Nuclear Pore Complex Composition Regulates
Cell Differentiation.” Developmental Cell. Elsevier, 2012. https://doi.org/10.1016/j.devcel.2011.11.021.
ieee: M. A. D’Angelo, J. S. Gomez-Cavazos, A. Mei, D. H. Lackner, and M. Hetzer,
“A change in nuclear pore complex composition regulates cell differentiation,”
Developmental Cell, vol. 22, no. 2. Elsevier, pp. 446–458, 2012.
ista: D’Angelo MA, Gomez-Cavazos JS, Mei A, Lackner DH, Hetzer M. 2012. A change
in nuclear pore complex composition regulates cell differentiation. Developmental
Cell. 22(2), 446–458.
mla: D’Angelo, Maximiliano A., et al. “A Change in Nuclear Pore Complex Composition
Regulates Cell Differentiation.” Developmental Cell, vol. 22, no. 2, Elsevier,
2012, pp. 446–58, doi:10.1016/j.devcel.2011.11.021.
short: M.A. D’Angelo, J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, M. Hetzer, Developmental
Cell 22 (2012) 446–458.
date_created: 2022-04-07T07:52:10Z
date_published: 2012-01-19T00:00:00Z
date_updated: 2022-07-18T08:53:16Z
day: '19'
doi: 10.1016/j.devcel.2011.11.021
extern: '1'
external_id:
pmid:
- '22264802'
intvolume: ' 22'
issue: '2'
keyword:
- Developmental Biology
- Cell Biology
- General Biochemistry
- Genetics and Molecular Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.devcel.2011.11.021
month: '01'
oa: 1
oa_version: Published Version
page: 446-458
pmid: 1
publication: Developmental Cell
publication_identifier:
issn:
- 1534-5807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: A change in nuclear pore complex composition regulates cell differentiation
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 22
year: '2012'
...
---
_id: '11100'
abstract:
- lang: eng
text: Eukaryotic cell function depends on the physical separation of nucleoplasmic
and cytoplasmic components by the nuclear envelope (NE). Molecular communication
between the two compartments involves active, signal-mediated trafficking, a function
that is exclusively performed by nuclear pore complexes (NPCs). The individual
NPC components and the mechanisms that are involved in nuclear trafficking are
well documented and have become textbook knowledge. However, in addition to their
roles as nuclear gatekeepers, NPC components-nucleoporins-have been shown to have
critical roles in chromatin organization and gene regulation. These findings have
sparked new enthusiasm to study the roles of this multiprotein complex in nuclear
organization and explore novel functions that in some cases appear to go beyond
a role in transport. Here, we discuss our present view of NPC biogenesis, which
is tightly linked to proper cell cycle progression and cell differentiation. In
addition, we summarize new data suggesting that NPCs represent dynamic hubs for
the integration of gene regulation and nuclear transport processes.
article_processing_charge: No
article_type: original
author:
- first_name: M.
full_name: Capelson, M.
last_name: Capelson
- first_name: C.
full_name: Doucet, C.
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: 'Capelson M, Doucet C, Hetzer M. Nuclear pore complexes: Guardians of the nuclear
genome. Cold Spring Harbor Symposia on Quantitative Biology. 2011;75:585-597.
doi:10.1101/sqb.2010.75.059'
apa: 'Capelson, M., Doucet, C., & Hetzer, M. (2011). Nuclear pore complexes:
Guardians of the nuclear genome. Cold Spring Harbor Symposia on Quantitative
Biology. Cold Spring Harbor Laboratory Press. https://doi.org/10.1101/sqb.2010.75.059'
chicago: 'Capelson, M., C. Doucet, and Martin Hetzer. “Nuclear Pore Complexes: Guardians
of the Nuclear Genome.” Cold Spring Harbor Symposia on Quantitative Biology.
Cold Spring Harbor Laboratory Press, 2011. https://doi.org/10.1101/sqb.2010.75.059.'
ieee: 'M. Capelson, C. Doucet, and M. Hetzer, “Nuclear pore complexes: Guardians
of the nuclear genome,” Cold Spring Harbor Symposia on Quantitative Biology,
vol. 75. Cold Spring Harbor Laboratory Press, pp. 585–597, 2011.'
ista: 'Capelson M, Doucet C, Hetzer M. 2011. Nuclear pore complexes: Guardians of
the nuclear genome. Cold Spring Harbor Symposia on Quantitative Biology. 75, 585–597.'
mla: 'Capelson, M., et al. “Nuclear Pore Complexes: Guardians of the Nuclear Genome.”
Cold Spring Harbor Symposia on Quantitative Biology, vol. 75, Cold Spring
Harbor Laboratory Press, 2011, pp. 585–97, doi:10.1101/sqb.2010.75.059.'
short: M. Capelson, C. Doucet, M. Hetzer, Cold Spring Harbor Symposia on Quantitative
Biology 75 (2011) 585–597.
date_created: 2022-04-07T07:53:18Z
date_published: 2011-04-18T00:00:00Z
date_updated: 2022-07-18T08:54:23Z
day: '18'
doi: 10.1101/sqb.2010.75.059
extern: '1'
external_id:
pmid:
- '21502404'
intvolume: ' 75'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
month: '04'
oa_version: None
page: 585-597
pmid: 1
publication: Cold Spring Harbor Symposia on Quantitative Biology
publication_identifier:
isbn:
- '9781936113071'
issn:
- 0091-7451
- 1943-4456
publication_status: published
publisher: Cold Spring Harbor Laboratory Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Nuclear pore complexes: Guardians of the nuclear genome'
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 75
year: '2011'
...
---
_id: '11097'
abstract:
- lang: eng
text: The nuclear envelope (NE) is a highly regulated membrane barrier that separates
the nucleus from the cytoplasm in eukaryotic cells. It contains a large number
of different proteins that have been implicated in chromatin organization and
gene regulation. Although the nuclear membrane enables complex levels of gene
expression, it also poses a challenge when it comes to cell division. To allow
access of the mitotic spindle to chromatin, the nucleus of metazoans must completely
disassemble during mitosis, generating the need to re-establish the nuclear compartment
at the end of each cell division. Here, I summarize our current understanding
of the dynamic remodeling of the NE during the cell cycle.
article_processing_charge: No
article_type: original
author:
- 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: Hetzer M. The nuclear envelope. Cold Spring Harbor Perspectives in Biology.
2010;2(3):a000539-a000539. doi:10.1101/cshperspect.a000539
apa: Hetzer, M. (2010). The nuclear envelope. Cold Spring Harbor Perspectives
in Biology. Cold Spring Harbor Laboratory. https://doi.org/10.1101/cshperspect.a000539
chicago: Hetzer, Martin. “The Nuclear Envelope.” Cold Spring Harbor Perspectives
in Biology. Cold Spring Harbor Laboratory, 2010. https://doi.org/10.1101/cshperspect.a000539.
ieee: M. Hetzer, “The nuclear envelope,” Cold Spring Harbor Perspectives in Biology,
vol. 2, no. 3. Cold Spring Harbor Laboratory, pp. a000539–a000539, 2010.
ista: Hetzer M. 2010. The nuclear envelope. Cold Spring Harbor Perspectives in Biology.
2(3), a000539–a000539.
mla: Hetzer, Martin. “The Nuclear Envelope.” Cold Spring Harbor Perspectives
in Biology, vol. 2, no. 3, Cold Spring Harbor Laboratory, 2010, pp. a000539–a000539,
doi:10.1101/cshperspect.a000539.
short: M. Hetzer, Cold Spring Harbor Perspectives in Biology 2 (2010) a000539–a000539.
date_created: 2022-04-07T07:52:49Z
date_published: 2010-02-03T00:00:00Z
date_updated: 2022-07-18T08:53:50Z
day: '03'
doi: 10.1101/cshperspect.a000539
extern: '1'
external_id:
pmid:
- '20300205'
intvolume: ' 2'
issue: '3'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '02'
oa_version: None
page: a000539-a000539
pmid: 1
publication: Cold Spring Harbor Perspectives in Biology
publication_identifier:
issn:
- 1943-0264
publication_status: published
publisher: Cold Spring Harbor Laboratory
quality_controlled: '1'
scopus_import: '1'
status: public
title: The nuclear envelope
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 2
year: '2010'
...
---
_id: '11101'
abstract:
- lang: eng
text: In metazoa, nuclear pore complexes (NPCs) assemble from disassembled precursors
into a reforming nuclear envelope (NE) at the end of mitosis and into growing
intact NEs during interphase. Here, we show via RNAi-mediated knockdown that ELYS,
a nucleoporin critical for the recruitment of the essential Nup107/160 complex
to chromatin, is required for NPC assembly at the end of mitosis but not during
interphase. Conversely, the transmembrane nucleoporin POM121 is critical for the
incorporation of the Nup107/160 complex into new assembly sites specifically during
interphase. Strikingly, recruitment of the Nup107/160 complex to an intact NE
involves a membrane curvature-sensing domain of its constituent Nup133, which
is not required for postmitotic NPC formation. Our results suggest that in organisms
with open mitosis, NPCs assemble via two distinct mechanisms to accommodate cell
cycle-dependent differences in NE topology.
article_processing_charge: No
article_type: original
author:
- first_name: Christine M.
full_name: Doucet, Christine M.
last_name: Doucet
- first_name: Jessica A.
full_name: Talamas, Jessica A.
last_name: Talamas
- 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: Doucet CM, Talamas JA, Hetzer M. Cell cycle-dependent differences in nuclear
pore complex assembly in metazoa. Cell. 2010;141(6):1030-1041. doi:10.1016/j.cell.2010.04.036
apa: Doucet, C. M., Talamas, J. A., & Hetzer, M. (2010). Cell cycle-dependent
differences in nuclear pore complex assembly in metazoa. Cell. Elsevier.
https://doi.org/10.1016/j.cell.2010.04.036
chicago: Doucet, Christine M., Jessica A. Talamas, and Martin Hetzer. “Cell Cycle-Dependent
Differences in Nuclear Pore Complex Assembly in Metazoa.” Cell. Elsevier,
2010. https://doi.org/10.1016/j.cell.2010.04.036.
ieee: C. M. Doucet, J. A. Talamas, and M. Hetzer, “Cell cycle-dependent differences
in nuclear pore complex assembly in metazoa,” Cell, vol. 141, no. 6. Elsevier,
pp. 1030–1041, 2010.
ista: Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in
nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041.
mla: Doucet, Christine M., et al. “Cell Cycle-Dependent Differences in Nuclear Pore
Complex Assembly in Metazoa.” Cell, vol. 141, no. 6, Elsevier, 2010, pp.
1030–41, doi:10.1016/j.cell.2010.04.036.
short: C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 1030–1041.
date_created: 2022-04-07T07:53:29Z
date_published: 2010-06-11T00:00:00Z
date_updated: 2022-07-18T08:54:52Z
day: '11'
doi: 10.1016/j.cell.2010.04.036
extern: '1'
external_id:
pmid:
- '20550937'
intvolume: ' 141'
issue: '6'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2010.04.036
month: '06'
oa: 1
oa_version: Published Version
page: 1030-1041
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cell cycle-dependent differences in nuclear pore complex assembly in metazoa
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 141
year: '2010'
...
---
_id: '11102'
abstract:
- lang: eng
text: Nuclear pore complexes have recently been shown to play roles in gene activation;
however their potential involvement in metazoan transcription remains unclear.
Here we show that the nucleoporins Sec13, Nup98, and Nup88, as well as a group
of FG-repeat nucleoporins, bind to the Drosophila genome at functionally distinct
loci that often do not represent nuclear envelope contact sites. Whereas Nup88
localizes to silent loci, Sec13, Nup98, and a subset of FG-repeat nucleoporins
bind to developmentally regulated genes undergoing transcription induction. Strikingly,
RNAi-mediated knockdown of intranuclear Sec13 and Nup98 specifically inhibits
transcription of their target genes and prevents efficient reactivation of transcription
after heat shock, suggesting an essential role of NPC components in regulating
complex gene expression programs of multicellular organisms.
article_processing_charge: No
article_type: original
author:
- first_name: Maya
full_name: Capelson, Maya
last_name: Capelson
- first_name: Yun
full_name: Liang, Yun
last_name: Liang
- first_name: Roberta
full_name: Schulte, Roberta
last_name: Schulte
- first_name: William
full_name: Mair, William
last_name: Mair
- first_name: Ulrich
full_name: Wagner, Ulrich
last_name: Wagner
- 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: Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. Chromatin-bound
nuclear pore components regulate gene expression in higher eukaryotes. Cell.
2010;140(3):372-383. doi:10.1016/j.cell.2009.12.054
apa: Capelson, M., Liang, Y., Schulte, R., Mair, W., Wagner, U., & Hetzer, M.
(2010). Chromatin-bound nuclear pore components regulate gene expression in higher
eukaryotes. Cell. Elsevier. https://doi.org/10.1016/j.cell.2009.12.054
chicago: Capelson, Maya, Yun Liang, Roberta Schulte, William Mair, Ulrich Wagner,
and Martin Hetzer. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression
in Higher Eukaryotes.” Cell. Elsevier, 2010. https://doi.org/10.1016/j.cell.2009.12.054.
ieee: M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, and M. Hetzer, “Chromatin-bound
nuclear pore components regulate gene expression in higher eukaryotes,” Cell,
vol. 140, no. 3. Elsevier, pp. 372–383, 2010.
ista: Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. 2010. Chromatin-bound
nuclear pore components regulate gene expression in higher eukaryotes. Cell. 140(3),
372–383.
mla: Capelson, Maya, et al. “Chromatin-Bound Nuclear Pore Components Regulate Gene
Expression in Higher Eukaryotes.” Cell, vol. 140, no. 3, Elsevier, 2010,
pp. 372–83, doi:10.1016/j.cell.2009.12.054.
short: M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140
(2010) 372–383.
date_created: 2022-04-07T07:53:36Z
date_published: 2010-02-05T00:00:00Z
date_updated: 2022-07-18T08:55:03Z
day: '05'
doi: 10.1016/j.cell.2009.12.054
extern: '1'
external_id:
pmid:
- '20144761'
intvolume: ' 140'
issue: '3'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2009.12.054
month: '02'
oa: 1
oa_version: Published Version
page: 372-383
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Chromatin-bound nuclear pore components regulate gene expression in higher
eukaryotes
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 140
year: '2010'
...
---
_id: '8473'
abstract:
- lang: eng
text: β2-microglobulin (β2m), the light chain of class I major histocompatibility
complex, is responsible for the dialysis-related amyloidosis and, in patients
undergoing long term dialysis, the full-length and chemically unmodified β2m converts
into amyloid fibrils. The protein, belonging to the immunoglobulin superfamily,
in common to other members of this family, experiences during its folding a long-lived
intermediate associated to the trans-to-cis isomerization of Pro-32 that has been
addressed as the precursor of the amyloid fibril formation. In this respect, previous
studies on the W60G β2m mutant, showing that the lack of Trp-60 prevents fibril
formation in mild aggregating condition, prompted us to reinvestigate the refolding
kinetics of wild type and W60G β2m at atomic resolution by real-time NMR. The
analysis, conducted at ambient temperature by the band selective flip angle short
transient real-time two-dimensional NMR techniques and probing the β2m states
every 15 s, revealed a more complex folding energy landscape than previously reported
for wild type β2m, involving more than a single intermediate species, and shedding
new light into the fibrillogenic pathway. Moreover, a significant difference in
the kinetic scheme previously characterized by optical spectroscopic methods was
discovered for the W60G β2m mutant.
article_processing_charge: No
article_type: original
author:
- first_name: Alessandra
full_name: Corazza, Alessandra
last_name: Corazza
- first_name: Enrico
full_name: Rennella, Enrico
last_name: Rennella
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Maria Chiara
full_name: Mimmi, Maria Chiara
last_name: Mimmi
- first_name: Thomas
full_name: Cutuil, Thomas
last_name: Cutuil
- first_name: Sara
full_name: Raimondi, Sara
last_name: Raimondi
- first_name: Sofia
full_name: Giorgetti, Sofia
last_name: Giorgetti
- first_name: Federico
full_name: Fogolari, Federico
last_name: Fogolari
- first_name: Paolo
full_name: Viglino, Paolo
last_name: Viglino
- first_name: Lucio
full_name: Frydman, Lucio
last_name: Frydman
- first_name: Maayan
full_name: Gal, Maayan
last_name: Gal
- first_name: Vittorio
full_name: Bellotti, Vittorio
last_name: Bellotti
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Gennaro
full_name: Esposito, Gennaro
last_name: Esposito
citation:
ama: Corazza A, Rennella E, Schanda P, et al. Native-unlike long-lived intermediates
along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed
by real-time two-dimensional NMR. Journal of Biological Chemistry. 2010;285(8):5827-5835.
doi:10.1074/jbc.m109.061168
apa: Corazza, A., Rennella, E., Schanda, P., Mimmi, M. C., Cutuil, T., Raimondi,
S., … Esposito, G. (2010). Native-unlike long-lived intermediates along the folding
pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional
NMR. Journal of Biological Chemistry. American Society for Biochemistry
& Molecular Biology. https://doi.org/10.1074/jbc.m109.061168
chicago: Corazza, Alessandra, Enrico Rennella, Paul Schanda, Maria Chiara Mimmi,
Thomas Cutuil, Sara Raimondi, Sofia Giorgetti, et al. “Native-Unlike Long-Lived
Intermediates along the Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin
Revealed by Real-Time Two-Dimensional NMR.” Journal of Biological Chemistry.
American Society for Biochemistry & Molecular Biology, 2010. https://doi.org/10.1074/jbc.m109.061168.
ieee: A. Corazza et al., “Native-unlike long-lived intermediates along the
folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time
two-dimensional NMR,” Journal of Biological Chemistry, vol. 285, no. 8.
American Society for Biochemistry & Molecular Biology, pp. 5827–5835, 2010.
ista: Corazza A, Rennella E, Schanda P, Mimmi MC, Cutuil T, Raimondi S, Giorgetti
S, Fogolari F, Viglino P, Frydman L, Gal M, Bellotti V, Brutscher B, Esposito
G. 2010. Native-unlike long-lived intermediates along the folding pathway of the
amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR.
Journal of Biological Chemistry. 285(8), 5827–5835.
mla: Corazza, Alessandra, et al. “Native-Unlike Long-Lived Intermediates along the
Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin Revealed by Real-Time
Two-Dimensional NMR.” Journal of Biological Chemistry, vol. 285, no. 8,
American Society for Biochemistry & Molecular Biology, 2010, pp. 5827–35,
doi:10.1074/jbc.m109.061168.
short: A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi,
S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher,
G. Esposito, Journal of Biological Chemistry 285 (2010) 5827–5835.
date_created: 2020-09-18T10:11:23Z
date_published: 2010-02-19T00:00:00Z
date_updated: 2021-01-12T08:19:31Z
day: '19'
doi: 10.1074/jbc.m109.061168
extern: '1'
intvolume: ' 285'
issue: '8'
keyword:
- Cell Biology
- Biochemistry
- Molecular Biology
language:
- iso: eng
month: '02'
oa_version: None
page: 5827-5835
publication: Journal of Biological Chemistry
publication_identifier:
issn:
- 0021-9258
- 1083-351X
publication_status: published
publisher: American Society for Biochemistry & Molecular Biology
quality_controlled: '1'
status: public
title: Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic
protein β2-Microglobulin revealed by real-time two-dimensional NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 285
year: '2010'
...
---
_id: '12199'
abstract:
- lang: eng
text: The four microsporangia of the flowering plant anther develop from archesporial
cells in the L2 of the primordium. Within each microsporangium, developing microsporocytes
are surrounded by concentric monolayers of tapetal, middle layer and endothecial
cells. How this intricate array of tissues, each containing relatively few cells,
is established in an organ possessing no formal meristems is poorly understood.
We describe here the pivotal role of the LRR receptor kinase EXCESS MICROSPOROCYTES
1 (EMS1) in forming the monolayer of tapetal nurse cells in Arabidopsis. Unusually
for plants, tapetal cells are specified very early in development, and are subsequently
stimulated to proliferate by a receptor-like kinase (RLK) complex that includes
EMS1. Mutations in members of this EMS1 signalling complex and its putative ligand
result in male-sterile plants in which tapetal initials fail to proliferate. Surprisingly,
these cells continue to develop, isolated at the locular periphery. Mutant and
wild-type microsporangia expand at similar rates and the ‘tapetal’ space at the
periphery of mutant locules becomes occupied by microsporocytes. However, induction
of late expression of EMS1 in the few tapetal initials in ems1 plants results
in their proliferation to generate a functional tapetum, and this proliferation
suppresses microsporocyte number. Our experiments also show that integrity of
the tapetal monolayer is crucial for the maintenance of the polarity of divisions
within it. This unexpected autonomy of the tapetal ‘lineage’ is discussed in the
context of tissue development in complex plant organs, where constancy in size,
shape and cell number is crucial.
acknowledgement: 'We thank the following for providing mutant lines and reagents:
Hong Ma, De Ye, Sacco De Vries, and Rod Scott for providing the pA9::Barnase lines
and information on A9 expression patterns. Carla Galinha and Paolo Piazza gave valuable
help with in situ hybridisation and qRT-PCR, respectively, and we acknowledge Qing
Zhang, Helen Prescott and Matthew Dicks for providing excellent technical assistance.
We are indebted to Miltos Tsiantis and Angela Hay for helpful discussion, and the
research was funded by Oxford University through a Clarendon Scholarship to X.F.,
with additional financial support from Magdalen College (Oxford).'
article_processing_charge: No
article_type: original
author:
- first_name: Xiaoqi
full_name: Feng, Xiaoqi
id: e0164712-22ee-11ed-b12a-d80fcdf35958
last_name: Feng
orcid: 0000-0002-4008-1234
- first_name: Hugh G.
full_name: Dickinson, Hugh G.
last_name: Dickinson
citation:
ama: Feng X, Dickinson HG. Tapetal cell fate, lineage and proliferation in the Arabidopsis
anther. Development. 2010;137(14):2409-2416. doi:10.1242/dev.049320
apa: Feng, X., & Dickinson, H. G. (2010). Tapetal cell fate, lineage and proliferation
in the Arabidopsis anther. Development. The Company of Biologists. https://doi.org/10.1242/dev.049320
chicago: Feng, Xiaoqi, and Hugh G. Dickinson. “Tapetal Cell Fate, Lineage and Proliferation
in the Arabidopsis Anther.” Development. The Company of Biologists, 2010.
https://doi.org/10.1242/dev.049320.
ieee: X. Feng and H. G. Dickinson, “Tapetal cell fate, lineage and proliferation
in the Arabidopsis anther,” Development, vol. 137, no. 14. The Company
of Biologists, pp. 2409–2416, 2010.
ista: Feng X, Dickinson HG. 2010. Tapetal cell fate, lineage and proliferation in
the Arabidopsis anther. Development. 137(14), 2409–2416.
mla: Feng, Xiaoqi, and Hugh G. Dickinson. “Tapetal Cell Fate, Lineage and Proliferation
in the Arabidopsis Anther.” Development, vol. 137, no. 14, The Company
of Biologists, 2010, pp. 2409–16, doi:10.1242/dev.049320.
short: X. Feng, H.G. Dickinson, Development 137 (2010) 2409–2416.
date_created: 2023-01-16T09:21:54Z
date_published: 2010-07-15T00:00:00Z
date_updated: 2023-05-08T10:57:11Z
day: '15'
department:
- _id: XiFe
doi: 10.1242/dev.049320
extern: '1'
external_id:
pmid:
- '20570940'
intvolume: ' 137'
issue: '14'
keyword:
- Developmental Biology
- Molecular Biology
- Anther Tapetum
- Arabidopsis
- Cell Fate Establishment
- EMS1
- Reproductive Cell Lineage
language:
- iso: eng
month: '07'
oa_version: None
page: 2409-2416
pmid: 1
publication: Development
publication_identifier:
issn:
- 1477-9129
- 0950-1991
publication_status: published
publisher: The Company of Biologists
quality_controlled: '1'
scopus_import: '1'
status: public
title: Tapetal cell fate, lineage and proliferation in the Arabidopsis anther
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 137
year: '2010'
...
---
_id: '11103'
abstract:
- lang: eng
text: Over the last decade, the nuclear envelope (NE) has emerged as a key component
in the organization and function of the nuclear genome. As many as 100 different
proteins are thought to specifically localize to this double membrane that separates
the cytoplasm and the nucleoplasm of eukaryotic cells. Selective portals through
the NE are formed at sites where the inner and outer nuclear membranes are fused,
and the coincident assembly of ∼30 proteins into nuclear pore complexes occurs.
These nuclear pore complexes are essential for the control of nucleocytoplasmic
exchange. Many of the NE and nuclear pore proteins are thought to play crucial
roles in gene regulation and thus are increasingly linked to human diseases.
article_processing_charge: No
article_type: review
author:
- 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: Susan R.
full_name: Wente, Susan R.
last_name: Wente
citation:
ama: 'Hetzer M, Wente SR. Border control at the nucleus: Biogenesis and organization
of the nuclear membrane and pore complexes. Developmental Cell. 2009;17(5):606-616.
doi:10.1016/j.devcel.2009.10.007'
apa: 'Hetzer, M., & Wente, S. R. (2009). Border control at the nucleus: Biogenesis
and organization of the nuclear membrane and pore complexes. Developmental
Cell. Elsevier. https://doi.org/10.1016/j.devcel.2009.10.007'
chicago: 'Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis
and Organization of the Nuclear Membrane and Pore Complexes.” Developmental
Cell. Elsevier, 2009. https://doi.org/10.1016/j.devcel.2009.10.007.'
ieee: 'M. Hetzer and S. R. Wente, “Border control at the nucleus: Biogenesis and
organization of the nuclear membrane and pore complexes,” Developmental Cell,
vol. 17, no. 5. Elsevier, pp. 606–616, 2009.'
ista: 'Hetzer M, Wente SR. 2009. Border control at the nucleus: Biogenesis and organization
of the nuclear membrane and pore complexes. Developmental Cell. 17(5), 606–616.'
mla: 'Hetzer, Martin, and Susan R. Wente. “Border Control at the Nucleus: Biogenesis
and Organization of the Nuclear Membrane and Pore Complexes.” Developmental
Cell, vol. 17, no. 5, Elsevier, 2009, pp. 606–16, doi:10.1016/j.devcel.2009.10.007.'
short: M. Hetzer, S.R. Wente, Developmental Cell 17 (2009) 606–616.
date_created: 2022-04-07T07:53:45Z
date_published: 2009-11-17T00:00:00Z
date_updated: 2022-07-18T08:55:01Z
day: '17'
doi: 10.1016/j.devcel.2009.10.007
extern: '1'
external_id:
pmid:
- '19922866'
intvolume: ' 17'
issue: '5'
keyword:
- Developmental Biology
- Cell Biology
- General Biochemistry
- Genetics and Molecular Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.devcel.2009.10.007
month: '11'
oa: 1
oa_version: Published Version
page: 606-616
pmid: 1
publication: Developmental Cell
publication_identifier:
issn:
- 1534-5807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Border control at the nucleus: Biogenesis and organization of the nuclear
membrane and pore complexes'
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 17
year: '2009'
...