---
_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: '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: '8461'
abstract:
- lang: eng
text: Solid-state NMR provides insight into protein motion over time scales ranging
from picoseconds to seconds. While in solution state the methodology to measure
protein dynamics is well established, there is currently no such consensus protocol
for measuring dynamics in solids. In this article, we perform a detailed investigation
of measurement protocols for fast motions, i.e. motions ranging from picoseconds
to a few microseconds, which is the range covered by dipolar coupling and relaxation
experiments. We perform a detailed theoretical investigation how dipolar couplings
and relaxation data can provide information about amplitudes and time scales of
local motion. We show that the measurement of dipolar couplings is crucial for
obtaining accurate motional parameters, while systematic errors are found when
only relaxation data are used. Based on this realization, we investigate how the
REDOR experiment can provide such data in a very accurate manner. We identify
that with accurate rf calibration, and explicit consideration of rf field inhomogeneities,
one can obtain highly accurate absolute order parameters. We then perform joint
model-free analyses of 6 relaxation data sets and dipolar couplings, based on
previously existing, as well as new data sets on microcrystalline ubiquitin. We
show that nanosecond motion can be detected primarily in loop regions, and compare
solid-state data to solution-state relaxation and RDC analyses. The protocols
investigated here will serve as a useful basis towards the establishment of a
routine protocol for the characterization of ps–μs motions in proteins by solid-state
NMR.
article_processing_charge: No
article_type: original
author:
- first_name: Jens D.
full_name: Haller, Jens D.
last_name: Haller
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Haller JD, Schanda P. Amplitudes and time scales of picosecond-to-microsecond
motion in proteins studied by solid-state NMR: a critical evaluation of experimental
approaches and application to crystalline ubiquitin. Journal of Biomolecular
NMR. 2013;57(3):263-280. doi:10.1007/s10858-013-9787-x'
apa: 'Haller, J. D., & Schanda, P. (2013). Amplitudes and time scales of picosecond-to-microsecond
motion in proteins studied by solid-state NMR: a critical evaluation of experimental
approaches and application to crystalline ubiquitin. Journal of Biomolecular
NMR. Springer Nature. https://doi.org/10.1007/s10858-013-9787-x'
chicago: 'Haller, Jens D., and Paul Schanda. “Amplitudes and Time Scales of Picosecond-to-Microsecond
Motion in Proteins Studied by Solid-State NMR: A Critical Evaluation of Experimental
Approaches and Application to Crystalline Ubiquitin.” Journal of Biomolecular
NMR. Springer Nature, 2013. https://doi.org/10.1007/s10858-013-9787-x.'
ieee: 'J. D. Haller and P. Schanda, “Amplitudes and time scales of picosecond-to-microsecond
motion in proteins studied by solid-state NMR: a critical evaluation of experimental
approaches and application to crystalline ubiquitin,” Journal of Biomolecular
NMR, vol. 57, no. 3. Springer Nature, pp. 263–280, 2013.'
ista: 'Haller JD, Schanda P. 2013. Amplitudes and time scales of picosecond-to-microsecond
motion in proteins studied by solid-state NMR: a critical evaluation of experimental
approaches and application to crystalline ubiquitin. Journal of Biomolecular NMR.
57(3), 263–280.'
mla: 'Haller, Jens D., and Paul Schanda. “Amplitudes and Time Scales of Picosecond-to-Microsecond
Motion in Proteins Studied by Solid-State NMR: A Critical Evaluation of Experimental
Approaches and Application to Crystalline Ubiquitin.” Journal of Biomolecular
NMR, vol. 57, no. 3, Springer Nature, 2013, pp. 263–80, doi:10.1007/s10858-013-9787-x.'
short: J.D. Haller, P. Schanda, Journal of Biomolecular NMR 57 (2013) 263–280.
date_created: 2020-09-18T10:09:05Z
date_published: 2013-10-09T00:00:00Z
date_updated: 2021-01-12T08:19:26Z
day: '09'
doi: 10.1007/s10858-013-9787-x
extern: '1'
intvolume: ' 57'
issue: '3'
keyword:
- Spectroscopy
- Biochemistry
language:
- iso: eng
month: '10'
oa_version: None
page: 263-280
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: 'Amplitudes and time scales of picosecond-to-microsecond motion in proteins
studied by solid-state NMR: a critical evaluation of experimental approaches and
application to crystalline ubiquitin'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 57
year: '2013'
...
---
_id: '9167'
abstract:
- lang: eng
text: We introduce a self-propelled colloidal hematite docker that can be steered
to a small particle cargo many times its size, dock, transport the cargo to a
remote location, and then release it. The self-propulsion and docking are reversible
and activated by visible light. The docker can be steered either by a weak uniform
magnetic field or by nanoscale tracks in a textured substrate. The light-activated
motion and docking originate from osmotic/phoretic particle transport in a concentration
gradient of fuel, hydrogen peroxide, induced by the photocatalytic activity of
the hematite. The docking mechanism is versatile and can be applied to various
materials and shapes. The hematite dockers are simple single-component particles
and are synthesized in bulk quantities. This system opens up new possibilities
for designing complex micrometer-size factories as well as new biomimetic systems.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Jérémie A
full_name: Palacci, Jérémie A
id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d
last_name: Palacci
orcid: 0000-0002-7253-9465
- first_name: Stefano
full_name: Sacanna, Stefano
last_name: Sacanna
- first_name: Adrian
full_name: Vatchinsky, Adrian
last_name: Vatchinsky
- first_name: Paul M.
full_name: Chaikin, Paul M.
last_name: Chaikin
- first_name: David J.
full_name: Pine, David J.
last_name: Pine
citation:
ama: Palacci JA, Sacanna S, Vatchinsky A, Chaikin PM, Pine DJ. Photoactivated colloidal
dockers for cargo transportation. Journal of the American Chemical Society.
2013;135(43):15978-15981. doi:10.1021/ja406090s
apa: Palacci, J. A., Sacanna, S., Vatchinsky, A., Chaikin, P. M., & Pine, D.
J. (2013). Photoactivated colloidal dockers for cargo transportation. Journal
of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja406090s
chicago: Palacci, Jérémie A, Stefano Sacanna, Adrian Vatchinsky, Paul M. Chaikin,
and David J. Pine. “Photoactivated Colloidal Dockers for Cargo Transportation.”
Journal of the American Chemical Society. American Chemical Society, 2013.
https://doi.org/10.1021/ja406090s.
ieee: J. A. Palacci, S. Sacanna, A. Vatchinsky, P. M. Chaikin, and D. J. Pine, “Photoactivated
colloidal dockers for cargo transportation,” Journal of the American Chemical
Society, vol. 135, no. 43. American Chemical Society, pp. 15978–15981, 2013.
ista: Palacci JA, Sacanna S, Vatchinsky A, Chaikin PM, Pine DJ. 2013. Photoactivated
colloidal dockers for cargo transportation. Journal of the American Chemical Society.
135(43), 15978–15981.
mla: Palacci, Jérémie A., et al. “Photoactivated Colloidal Dockers for Cargo Transportation.”
Journal of the American Chemical Society, vol. 135, no. 43, American Chemical
Society, 2013, pp. 15978–81, doi:10.1021/ja406090s.
short: J.A. Palacci, S. Sacanna, A. Vatchinsky, P.M. Chaikin, D.J. Pine, Journal
of the American Chemical Society 135 (2013) 15978–15981.
date_created: 2021-02-18T14:31:26Z
date_published: 2013-10-30T00:00:00Z
date_updated: 2021-02-22T10:10:41Z
day: '30'
doi: 10.1021/ja406090s
extern: '1'
external_id:
arxiv:
- '1310.5724'
pmid:
- '24131488'
intvolume: ' 135'
issue: '43'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1310.5724
month: '10'
oa: 1
oa_version: Preprint
page: 15978-15981
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- '15205126'
issn:
- '00027863'
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Photoactivated colloidal dockers for cargo transportation
type: journal_article
user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 135
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: '13407'
abstract:
- lang: eng
text: We show that diamagnetic particles can be remotely manipulated by a magnet
by the reversible adsorption of dual-responsive, light-switchable/superparamagnetic
nanoparticles down to their surface. Adsorption occurs upon exposure to UV light,
and can be reversed thermally or by ambient light. The dynamic self-assembly of
thin films of the dual-responsive nanoparticles induces attractive interactions
between diamagnetic particles. We demonstrate that catalytic amounts of the dual-responsive
nanoparticles are sufficient to magnetically guide and deliver the diamagnetic
particles to desired locations, where they can then be released by disassembling
the dynamic layers of superparamagnetic nanoparticles with visible light.
article_processing_charge: No
article_type: original
author:
- first_name: Olga
full_name: Chovnik, Olga
last_name: Chovnik
- first_name: Renata
full_name: Balgley, Renata
last_name: Balgley
- first_name: Joel R.
full_name: Goldman, Joel R.
last_name: Goldman
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Chovnik O, Balgley R, Goldman JR, Klajn R. Dynamically self-assembling carriers
enable guiding of diamagnetic particles by weak magnets. Journal of the American
Chemical Society. 2012;134(48):19564-19567. doi:10.1021/ja309633v
apa: Chovnik, O., Balgley, R., Goldman, J. R., & Klajn, R. (2012). Dynamically
self-assembling carriers enable guiding of diamagnetic particles by weak magnets.
Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja309633v
chicago: Chovnik, Olga, Renata Balgley, Joel R. Goldman, and Rafal Klajn. “Dynamically
Self-Assembling Carriers Enable Guiding of Diamagnetic Particles by Weak Magnets.”
Journal of the American Chemical Society. American Chemical Society, 2012.
https://doi.org/10.1021/ja309633v.
ieee: O. Chovnik, R. Balgley, J. R. Goldman, and R. Klajn, “Dynamically self-assembling
carriers enable guiding of diamagnetic particles by weak magnets,” Journal
of the American Chemical Society, vol. 134, no. 48. American Chemical Society,
pp. 19564–19567, 2012.
ista: Chovnik O, Balgley R, Goldman JR, Klajn R. 2012. Dynamically self-assembling
carriers enable guiding of diamagnetic particles by weak magnets. Journal of the
American Chemical Society. 134(48), 19564–19567.
mla: Chovnik, Olga, et al. “Dynamically Self-Assembling Carriers Enable Guiding
of Diamagnetic Particles by Weak Magnets.” Journal of the American Chemical
Society, vol. 134, no. 48, American Chemical Society, 2012, pp. 19564–67,
doi:10.1021/ja309633v.
short: O. Chovnik, R. Balgley, J.R. Goldman, R. Klajn, Journal of the American Chemical
Society 134 (2012) 19564–19567.
date_created: 2023-08-01T09:47:42Z
date_published: 2012-11-26T00:00:00Z
date_updated: 2023-08-08T07:51:10Z
day: '26'
doi: 10.1021/ja309633v
extern: '1'
external_id:
pmid:
- '23181449'
intvolume: ' 134'
issue: '48'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '11'
oa_version: Published Version
page: 19564-19567
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Dynamically self-assembling carriers enable guiding of diamagnetic particles
by weak magnets
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 134
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: '8469'
abstract:
- lang: eng
text: The accurate experimental determination of dipolar-coupling constants for
one-bond heteronuclear dipolar couplings in solids is a key for the quantification
of the amplitudes of motional processes. Averaging of the dipolar coupling reports
on motions on time scales up to the inverse of the coupling constant, in our case
tens of microseconds. Combining dipolar-coupling derived order parameters that
characterize the amplitudes of the motion with relaxation data leads to a more
precise characterization of the dynamical parameters and helps to disentangle
the amplitudes and the time scales of the motional processes, which impact relaxation
rates in a highly correlated way. Here. we describe and characterize an improved
experimental protocol – based on REDOR – to measure these couplings in perdeuterated
proteins with a reduced sensitivity to experimental missettings. Because such
effects are presently the dominant source of systematic errors in experimental
dipolar-coupling measurements, these compensated experiments should help to significantly
improve the precision of such data. A detailed comparison with other commonly
used pulse sequences (T-MREV, phase-inverted CP,R18 5/2, and R18 7/1) is provided.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Beat H.
full_name: Meier, Beat H.
last_name: Meier
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
citation:
ama: Schanda P, Meier BH, Ernst M. Accurate measurement of one-bond H–X heteronuclear
dipolar couplings in MAS solid-state NMR. Journal of Magnetic Resonance.
2011;210(2):246-259. doi:10.1016/j.jmr.2011.03.015
apa: Schanda, P., Meier, B. H., & Ernst, M. (2011). Accurate measurement of
one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR. Journal
of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2011.03.015
chicago: Schanda, Paul, Beat H. Meier, and Matthias Ernst. “Accurate Measurement
of One-Bond H–X Heteronuclear Dipolar Couplings in MAS Solid-State NMR.” Journal
of Magnetic Resonance. Elsevier, 2011. https://doi.org/10.1016/j.jmr.2011.03.015.
ieee: P. Schanda, B. H. Meier, and M. Ernst, “Accurate measurement of one-bond H–X
heteronuclear dipolar couplings in MAS solid-state NMR,” Journal of Magnetic
Resonance, vol. 210, no. 2. Elsevier, pp. 246–259, 2011.
ista: Schanda P, Meier BH, Ernst M. 2011. Accurate measurement of one-bond H–X heteronuclear
dipolar couplings in MAS solid-state NMR. Journal of Magnetic Resonance. 210(2),
246–259.
mla: Schanda, Paul, et al. “Accurate Measurement of One-Bond H–X Heteronuclear Dipolar
Couplings in MAS Solid-State NMR.” Journal of Magnetic Resonance, vol.
210, no. 2, Elsevier, 2011, pp. 246–59, doi:10.1016/j.jmr.2011.03.015.
short: P. Schanda, B.H. Meier, M. Ernst, Journal of Magnetic Resonance 210 (2011)
246–259.
date_created: 2020-09-18T10:10:50Z
date_published: 2011-06-01T00:00:00Z
date_updated: 2021-01-12T08:19:29Z
day: '01'
doi: 10.1016/j.jmr.2011.03.015
extern: '1'
intvolume: ' 210'
issue: '2'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '06'
oa_version: None
page: 246-259
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS
solid-state NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 210
year: '2011'
...
---
_id: '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: '13410'
abstract:
- lang: eng
text: A range (Au, Pt, Pd) of metal nanoparticles (MNPs) has been prepared and functionalized
with (a) redox-active stalks containing tetrathiafulvalene (TTF) units, (b) [2]pseudorotaxanes
formed between these stalks and cyclobis(paraquat-p-phenylene) (CBPQT4+) rings,
and (c) bistable [2]rotaxane molecules where the dumbbell component contains a
1,5-dioxynaphthalene (DNP) unit, as well as a TTF unit, encircled by a CBPQT4+
ring. It transpires that the molecules present in (a) and (c) and the supermolecules
described in (b) retain their switching characteristics, previously observed in
solution, when they are immobilized onto MNPs. Moreover, their oxidation potentials
depend on the fraction, χ, of the molecules or supermolecules on the surface of
the nanoparticles. A variation in χ affects the oxidation potentials of the TTF
units to the extent that switching can be subjected to fine tuning as a result.
Specifically, increasing χ results in positive shifts (i) in the oxidation potentials
of the TTF unit in (a)−(c) and (ii) the reduction potentials of the CBPQT4+ rings
in (c). These shifts can be attributed to an increase in the electrostatic potential
surrounding the MNPs. Both the magnitude and the direction of these shifts are
reproduced by a model, based on the Poisson−Boltzmann equation coupled with charge-regulating
boundary conditions. Furthermore, the kinetics of relaxation from the metastable
state coconformation (MSCC) to the ground-state coconformation (GSCC) of the bistable
[2]rotaxane molecules also depends on χ, as well as on the nanoparticle diameter.
Increasing either of these parameters accelerates the rate of relaxation from
the MSCC to the GSCC. This rate is a function of (i) the activation energy for
the relaxation process associated with the bistable [2]rotaxane molecules in solution
and (ii) the electrostatic potential surrounding the MNPs. The electrostatic potential
depends on (i) the diameter of the MNPs, (ii) the amount of the bistable [2]rotaxane
molecules on the surface of the MNPs, and (iii) the equilibrium distribution of
the CBPQT4+ rings between the DNP and TTF recognition sites in the GSCC. This
electrostatic potential has also been quantified using the Poisson−Boltzmann equation,
leading to faithful estimates of the rate constants.
article_processing_charge: No
article_type: original
author:
- first_name: Ali
full_name: Coskun, Ali
last_name: Coskun
- first_name: Paul J.
full_name: Wesson, Paul J.
last_name: Wesson
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Ali
full_name: Trabolsi, Ali
last_name: Trabolsi
- first_name: Lei
full_name: Fang, Lei
last_name: Fang
- first_name: Mark A.
full_name: Olson, Mark A.
last_name: Olson
- first_name: Sanjeev K.
full_name: Dey, Sanjeev K.
last_name: Dey
- first_name: Bartosz A.
full_name: Grzybowski, Bartosz A.
last_name: Grzybowski
- first_name: J. Fraser
full_name: Stoddart, J. Fraser
last_name: Stoddart
citation:
ama: 'Coskun A, Wesson PJ, Klajn R, et al. Molecular-mechanical switching at the
nanoparticle−solvent interface: Practice and theory. Journal of the American
Chemical Society. 2010;132(12):4310-4320. doi:10.1021/ja9102327'
apa: 'Coskun, A., Wesson, P. J., Klajn, R., Trabolsi, A., Fang, L., Olson, M. A.,
… Stoddart, J. F. (2010). Molecular-mechanical switching at the nanoparticle−solvent
interface: Practice and theory. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/ja9102327'
chicago: 'Coskun, Ali, Paul J. Wesson, Rafal Klajn, Ali Trabolsi, Lei Fang, Mark
A. Olson, Sanjeev K. Dey, Bartosz A. Grzybowski, and J. Fraser Stoddart. “Molecular-Mechanical
Switching at the Nanoparticle−solvent Interface: Practice and Theory.” Journal
of the American Chemical Society. American Chemical Society, 2010. https://doi.org/10.1021/ja9102327.'
ieee: 'A. Coskun et al., “Molecular-mechanical switching at the nanoparticle−solvent
interface: Practice and theory,” Journal of the American Chemical Society,
vol. 132, no. 12. American Chemical Society, pp. 4310–4320, 2010.'
ista: 'Coskun A, Wesson PJ, Klajn R, Trabolsi A, Fang L, Olson MA, Dey SK, Grzybowski
BA, Stoddart JF. 2010. Molecular-mechanical switching at the nanoparticle−solvent
interface: Practice and theory. Journal of the American Chemical Society. 132(12),
4310–4320.'
mla: 'Coskun, Ali, et al. “Molecular-Mechanical Switching at the Nanoparticle−solvent
Interface: Practice and Theory.” Journal of the American Chemical Society,
vol. 132, no. 12, American Chemical Society, 2010, pp. 4310–20, doi:10.1021/ja9102327.'
short: A. Coskun, P.J. Wesson, R. Klajn, A. Trabolsi, L. Fang, M.A. Olson, S.K.
Dey, B.A. Grzybowski, J.F. Stoddart, Journal of the American Chemical Society
132 (2010) 4310–4320.
date_created: 2023-08-01T09:48:27Z
date_published: 2010-03-31T00:00:00Z
date_updated: 2023-08-08T08:00:31Z
day: '31'
doi: 10.1021/ja9102327
extern: '1'
external_id:
pmid:
- '20218598'
intvolume: ' 132'
issue: '12'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '03'
oa_version: None
page: 4310-4320
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Molecular-mechanical switching at the nanoparticle−solvent interface: Practice
and theory'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 132
year: '2010'
...
---
_id: '12200'
abstract:
- lang: eng
text: Key steps in the evolution of the angiosperm anther include the patterning
of the concentrically organized microsporangium and the incorporation of four
such microsporangia into a leaf-like structure. Mutant studies in the model plant
Arabidopsis thaliana are leading to an increasingly accurate picture of (i) the
cell lineages culminating in the different cell types present in the microsporangium
(the microsporocytes, the tapetum, and the middle and endothecial layers), and
(ii) some of the genes responsible for specifying their fates. However, the processes
that confer polarity on the developing anther and position the microsporangia
within it remain unclear. Certainly, data from a range of experimental strategies
suggest that hormones play a central role in establishing polarity and the patterning
of the anther initial, and may be responsible for locating the microsporangia.
But the fact that microsporangia were originally positioned externally suggests
that their development is likely to be autonomous, perhaps with the reproductive
cells generating signals controlling the growth and division of the investing
anther epidermis. These possibilities are discussed in the context of the expression
of genes which initiate and maintain male and female reproductive development,
and in the perspective of our current views of anther evolution.
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. Cell–cell interactions during patterning of the Arabidopsis
anther. Biochemical Society Transactions. 2010;38(2):571-576. doi:10.1042/bst0380571
apa: Feng, X., & Dickinson, H. G. (2010). Cell–cell interactions during patterning
of the Arabidopsis anther. Biochemical Society Transactions. Portland
Press Ltd. https://doi.org/10.1042/bst0380571
chicago: Feng, Xiaoqi, and Hugh G. Dickinson. “Cell–Cell Interactions during Patterning
of the Arabidopsis Anther.” Biochemical Society Transactions. Portland
Press Ltd., 2010. https://doi.org/10.1042/bst0380571.
ieee: X. Feng and H. G. Dickinson, “Cell–cell interactions during patterning of
the Arabidopsis anther,” Biochemical Society Transactions, vol.
38, no. 2. Portland Press Ltd., pp. 571–576, 2010.
ista: Feng X, Dickinson HG. 2010. Cell–cell interactions during patterning of the
Arabidopsis anther. Biochemical Society Transactions. 38(2), 571–576.
mla: Feng, Xiaoqi, and Hugh G. Dickinson. “Cell–Cell Interactions during Patterning
of the Arabidopsis Anther.” Biochemical Society Transactions, vol.
38, no. 2, Portland Press Ltd., 2010, pp. 571–76, doi:10.1042/bst0380571.
short: X. Feng, H.G. Dickinson, Biochemical Society Transactions 38 (2010) 571–576.
date_created: 2023-01-16T09:22:18Z
date_published: 2010-03-22T00:00:00Z
date_updated: 2023-05-08T10:57:59Z
day: '22'
department:
- _id: XiFe
doi: 10.1042/bst0380571
extern: '1'
external_id:
pmid:
- '20298223'
intvolume: ' 38'
issue: '2'
keyword:
- Biochemistry
- Anther Development
- Arabidopsis
- Cell Fate
- Microsporangium
- Polarity
- Receptor Kinase
language:
- iso: eng
month: '03'
oa_version: None
page: 571-576
pmid: 1
publication: Biochemical Society Transactions
publication_identifier:
issn:
- 0300-5127
- 1470-8752
publication_status: published
publisher: Portland Press Ltd.
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cell–cell interactions during patterning of the Arabidopsis anther
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 38
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'
...
---
_id: '11105'
abstract:
- lang: eng
text: Nuclear-pore complexes (NPCs) are large protein channels that span the nuclear
envelope (NE), which is a double membrane that encloses the nuclear genome of
eukaryotes. Each of the typically 2,000–4,000 pores in the NE of vertebrate cells
is composed of multiple copies of 30 different proteins known as nucleoporins.
The evolutionarily conserved NPC proteins have the well-characterized function
of mediating the transport of molecules between the nucleoplasm and the cytoplasm.
Mutations in nucleoporins are often linked to specific developmental defects and
disease, and the resulting phenotypes are usually interpreted as the consequences
of perturbed nuclear transport activity. However, recent evidence suggests that
NPCs have additional functions in chromatin organization and gene regulation,
some of which might be independent of nuclear transport. Here, we review the transport-dependent
and transport-independent roles of NPCs in the regulation of nuclear function
and gene expression.
article_processing_charge: No
article_type: original
author:
- first_name: Maya
full_name: Capelson, Maya
last_name: Capelson
- 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, Hetzer M. The role of nuclear pores in gene regulation, development
and disease. EMBO reports. 2009;10(7):697-705. doi:10.1038/embor.2009.147
apa: Capelson, M., & Hetzer, M. (2009). The role of nuclear pores in gene regulation,
development and disease. EMBO Reports. EMBO. https://doi.org/10.1038/embor.2009.147
chicago: Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation,
Development and Disease.” EMBO Reports. EMBO, 2009. https://doi.org/10.1038/embor.2009.147.
ieee: M. Capelson and M. Hetzer, “The role of nuclear pores in gene regulation,
development and disease,” EMBO reports, vol. 10, no. 7. EMBO, pp. 697–705,
2009.
ista: Capelson M, Hetzer M. 2009. The role of nuclear pores in gene regulation,
development and disease. EMBO reports. 10(7), 697–705.
mla: Capelson, Maya, and Martin Hetzer. “The Role of Nuclear Pores in Gene Regulation,
Development and Disease.” EMBO Reports, vol. 10, no. 7, EMBO, 2009, pp.
697–705, doi:10.1038/embor.2009.147.
short: M. Capelson, M. Hetzer, EMBO Reports 10 (2009) 697–705.
date_created: 2022-04-07T07:54:06Z
date_published: 2009-07-01T00:00:00Z
date_updated: 2022-07-18T08:42:44Z
day: '01'
doi: 10.1038/embor.2009.147
extern: '1'
external_id:
pmid:
- '19543230'
intvolume: ' 10'
issue: '7'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/embor.2009.147
month: '07'
oa: 1
oa_version: Published Version
page: 697-705
pmid: 1
publication: EMBO reports
publication_identifier:
eissn:
- 1469-3178
issn:
- 1469-221X
publication_status: published
publisher: EMBO
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/embor.2009.176
scopus_import: '1'
status: public
title: The role of nuclear pores in gene regulation, development and disease
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 10
year: '2009'
...
---
_id: '11108'
abstract:
- lang: eng
text: In dividing cells, nuclear pore complexes (NPCs) disassemble during mitosis
and reassemble into the newly forming nuclei. However, the fate of nuclear pores
in postmitotic cells is unknown. Here, we show that NPCs, unlike other nuclear
structures, do not turn over in differentiated cells. While a subset of NPC components,
like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like
the Nup107/160 complex, are extremely long-lived and remain incorporated in the
nuclear membrane during the entire cellular life span. Besides the lack of nucleoporin
expression and NPC turnover, we discovered an age-related deterioration of NPCs,
leading to an increase in nuclear permeability and the leaking of cytoplasmic
proteins into the nucleus. Our finding that nuclear “leakiness” is dramatically
accelerated during aging and that a subset of nucleoporins is oxidatively damaged
in old cells suggests that the accumulation of damage at the NPC might be a crucial
aging event.
article_processing_charge: No
article_type: original
author:
- first_name: Maximiliano A.
full_name: D'Angelo, Maximiliano A.
last_name: D'Angelo
- first_name: Marcela
full_name: Raices, Marcela
last_name: Raices
- first_name: Siler H.
full_name: Panowski, Siler H.
last_name: Panowski
- 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, Raices M, Panowski SH, Hetzer M. Age-dependent deterioration of
nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells.
Cell. 2009;136(2):284-295. doi:10.1016/j.cell.2008.11.037
apa: D’Angelo, M. A., Raices, M., Panowski, S. H., & Hetzer, M. (2009). Age-dependent
deterioration of nuclear pore complexes causes a loss of nuclear integrity in
postmitotic cells. Cell. Elsevier. https://doi.org/10.1016/j.cell.2008.11.037
chicago: D’Angelo, Maximiliano A., Marcela Raices, Siler H. Panowski, and Martin
Hetzer. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of
Nuclear Integrity in Postmitotic Cells.” Cell. Elsevier, 2009. https://doi.org/10.1016/j.cell.2008.11.037.
ieee: M. A. D’Angelo, M. Raices, S. H. Panowski, and M. Hetzer, “Age-dependent deterioration
of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells,”
Cell, vol. 136, no. 2. Elsevier, pp. 284–295, 2009.
ista: D’Angelo MA, Raices M, Panowski SH, Hetzer M. 2009. Age-dependent deterioration
of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells.
Cell. 136(2), 284–295.
mla: D’Angelo, Maximiliano A., et al. “Age-Dependent Deterioration of Nuclear Pore
Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” Cell,
vol. 136, no. 2, Elsevier, 2009, pp. 284–95, doi:10.1016/j.cell.2008.11.037.
short: M.A. D’Angelo, M. Raices, S.H. Panowski, M. Hetzer, Cell 136 (2009) 284–295.
date_created: 2022-04-07T07:54:52Z
date_published: 2009-01-23T00:00:00Z
date_updated: 2022-07-18T08:55:29Z
day: '23'
doi: 10.1016/j.cell.2008.11.037
extern: '1'
external_id:
pmid:
- '19167330'
intvolume: ' 136'
issue: '2'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2008.11.037
month: '01'
oa: 1
oa_version: Published Version
page: 284-295
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear
integrity in postmitotic cells
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 136
year: '2009'
...
---
_id: '8479'
abstract:
- lang: eng
text: Multidimensional NMR spectroscopy is a well-established technique for the
characterization of structure and fast-time-scale dynamics of highly populated
ground states of biological macromolecules. The investigation of short-lived excited
states that are important for molecular folding, misfolding and function, however,
remains a challenge for modern biomolecular NMR techniques. Off-equilibrium real-time
kinetic NMR methods allow direct observation of conformational or chemical changes
by following peak positions and intensities in a series of spectra recorded during
a kinetic event. Because standard multidimensional NMR methods required to yield
sufficient atom-resolution are intrinsically time-consuming, many interesting
phenomena are excluded from real-time NMR analysis. Recently, spatially encoded
ultrafast 2D NMR techniques have been proposed that allow one to acquire a 2D
NMR experiment within a single transient. In addition, when combined with the
SOFAST technique, such ultrafast experiments can be repeated at high rates. One
of the problems detected for such ultrafast protein NMR experiments is related
to the heteronuclear decoupling during detection with interferences between the
pulses and the oscillatory magnetic field gradients arising in this scheme. Here
we present a method for improved ultrafast data acquisition yielding higher signal
to noise and sharper lines in single-scan 2D NMR spectra. In combination with
a fast-mixing device, the recording of 1H–15N correlation spectra with repetition
rates of up to a few Hertz becomes feasible, enabling real-time studies of protein
kinetics occurring on time scales down to a few seconds.
article_processing_charge: No
article_type: original
author:
- first_name: Maayan
full_name: Gal, Maayan
last_name: Gal
- first_name: Thomas
full_name: Kern, Thomas
last_name: Kern
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Lucio
full_name: Frydman, Lucio
last_name: Frydman
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: 'Gal M, Kern T, Schanda P, Frydman L, Brutscher B. An improved ultrafast 2D
NMR experiment: Towards atom-resolved real-time studies of protein kinetics at
multi-Hz rates. Journal of Biomolecular NMR. 2009;43:1-10. doi:10.1007/s10858-008-9284-9'
apa: 'Gal, M., Kern, T., Schanda, P., Frydman, L., & Brutscher, B. (2009). An
improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies
of protein kinetics at multi-Hz rates. Journal of Biomolecular NMR. Springer
Nature. https://doi.org/10.1007/s10858-008-9284-9'
chicago: 'Gal, Maayan, Thomas Kern, Paul Schanda, Lucio Frydman, and Bernhard Brutscher.
“An Improved Ultrafast 2D NMR Experiment: Towards Atom-Resolved Real-Time Studies
of Protein Kinetics at Multi-Hz Rates.” Journal of Biomolecular NMR. Springer
Nature, 2009. https://doi.org/10.1007/s10858-008-9284-9.'
ieee: 'M. Gal, T. Kern, P. Schanda, L. Frydman, and B. Brutscher, “An improved ultrafast
2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics
at multi-Hz rates,” Journal of Biomolecular NMR, vol. 43. Springer Nature,
pp. 1–10, 2009.'
ista: 'Gal M, Kern T, Schanda P, Frydman L, Brutscher B. 2009. An improved ultrafast
2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics
at multi-Hz rates. Journal of Biomolecular NMR. 43, 1–10.'
mla: 'Gal, Maayan, et al. “An Improved Ultrafast 2D NMR Experiment: Towards Atom-Resolved
Real-Time Studies of Protein Kinetics at Multi-Hz Rates.” Journal of Biomolecular
NMR, vol. 43, Springer Nature, 2009, pp. 1–10, doi:10.1007/s10858-008-9284-9.'
short: M. Gal, T. Kern, P. Schanda, L. Frydman, B. Brutscher, Journal of Biomolecular
NMR 43 (2009) 1–10.
date_created: 2020-09-18T10:12:20Z
date_published: 2009-01-01T00:00:00Z
date_updated: 2021-01-12T08:19:33Z
day: '01'
doi: 10.1007/s10858-008-9284-9
extern: '1'
intvolume: ' 43'
keyword:
- Spectroscopy
- Biochemistry
language:
- iso: eng
month: '01'
oa_version: None
page: 1-10
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: 'An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies
of protein kinetics at multi-Hz rates'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 43
year: '2009'
...
---
_id: '13420'
abstract:
- lang: eng
text: Weakly protected metal nanoparticles (MNPs) are used as precursors for the
preparation of catenane- and pseudorotaxane-decorated NPs of various compositions
(gold, palladium, platinum). When attached to the surface of MNPs, the molecular
switches retain their switching abilities. The redox potentials of these switches
depend on and can be regulated by the composition of the mixed self-assembled
monolayers covering the MNPs.
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: Lei
full_name: Fang, Lei
last_name: Fang
- first_name: Ali
full_name: Coskun, Ali
last_name: Coskun
- first_name: Mark A.
full_name: Olson, Mark A.
last_name: Olson
- first_name: Paul J.
full_name: Wesson, Paul J.
last_name: Wesson
- 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: Klajn R, Fang L, Coskun A, et al. Metal nanoparticles functionalized with molecular
and supramolecular switches. Journal of the American Chemical Society.
2009;131(12):4233-4235. doi:10.1021/ja9001585
apa: Klajn, R., Fang, L., Coskun, A., Olson, M. A., Wesson, P. J., Stoddart, J.
F., & Grzybowski, B. A. (2009). Metal nanoparticles functionalized with molecular
and supramolecular switches. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/ja9001585
chicago: Klajn, Rafal, Lei Fang, Ali Coskun, Mark A. Olson, Paul J. Wesson, J. Fraser
Stoddart, and Bartosz A. Grzybowski. “Metal Nanoparticles Functionalized with
Molecular and Supramolecular Switches.” Journal of the American Chemical Society.
American Chemical Society, 2009. https://doi.org/10.1021/ja9001585.
ieee: R. Klajn et al., “Metal nanoparticles functionalized with molecular
and supramolecular switches,” Journal of the American Chemical Society,
vol. 131, no. 12. American Chemical Society, pp. 4233–4235, 2009.
ista: Klajn R, Fang L, Coskun A, Olson MA, Wesson PJ, Stoddart JF, Grzybowski BA.
2009. Metal nanoparticles functionalized with molecular and supramolecular switches.
Journal of the American Chemical Society. 131(12), 4233–4235.
mla: Klajn, Rafal, et al. “Metal Nanoparticles Functionalized with Molecular and
Supramolecular Switches.” Journal of the American Chemical Society, vol.
131, no. 12, American Chemical Society, 2009, pp. 4233–35, doi:10.1021/ja9001585.
short: R. Klajn, L. Fang, A. Coskun, M.A. Olson, P.J. Wesson, J.F. Stoddart, B.A.
Grzybowski, Journal of the American Chemical Society 131 (2009) 4233–4235.
date_created: 2023-08-01T10:30:17Z
date_published: 2009-04-01T00:00:00Z
date_updated: 2023-08-08T09:06:00Z
day: '01'
doi: 10.1021/ja9001585
extern: '1'
external_id:
pmid:
- '19265400'
intvolume: ' 131'
issue: '12'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '04'
oa_version: None
page: 4233-4235
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Metal nanoparticles functionalized with molecular and supramolecular switches
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 131
year: '2009'
...