---
_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: '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: 2024-10-14T11:28:25Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: 2024-10-14T11:28:35Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
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: 2024-10-14T11:28:59Z
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 136
year: '2009'
...
---
_id: '8480'
abstract:
- lang: eng
text: The KIX domain of the transcription co-activator CBP is a three-helix bundle
protein that folds via rapid accumulation of an intermediate state, followed by
a slower folding phase. Recent NMR relaxation dispersion studies revealed the
presence of a low-populated (excited) state of KIX that exists in equilibrium
with the natively folded form under non-denaturing conditions, and likely represents
the equilibrium analog of the folding intermediate. Here, we combine amide hydrogen/deuterium
exchange measurements using rapid NMR data acquisition techniques with backbone
15N and 13C relaxation dispersion experiments to further investigate the equilibrium
folding of the KIX domain. Residual structure within the folding intermediate
is detected by both methods, and their combination enables reliable quantification
of the amount of persistent residual structure. Three well-defined folding subunits
are found, which display variable stability and correspond closely to the individual
helices in the native state. While two of the three helices (α2 and α3) are partially
formed in the folding intermediate (to ∼ 50% and ∼ 80%, respectively, at 20 °C),
the third helix is disordered. The observed helical content within the excited
state exceeds the helical propensities predicted for the corresponding peptide
regions, suggesting that the two helices are weakly mutually stabilized, while
methyl 13C relaxation dispersion data indicate that a defined packing arrangement
is unlikely. Temperature-dependent experiments reveal that the largest enthalpy
and entropy changes along the folding reaction occur during the final transition
from the intermediate to the native state. Our experimental data are consistent
with a folding mechanism where helices α2 and α3 form rapidly, although to different
extents, while helix α1 consolidates only as folding proceeds to complete the
native state-structure.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Robert
full_name: Konrat, Robert
last_name: Konrat
- first_name: Martin
full_name: Tollinger, Martin
last_name: Tollinger
citation:
ama: 'Schanda P, Brutscher B, Konrat R, Tollinger M. Folding of the KIX domain:
Characterization of the equilibrium analog of a folding intermediate using 15N/13C
relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. Journal
of Molecular Biology. 2008;380(4):726-741. doi:10.1016/j.jmb.2008.05.040'
apa: 'Schanda, P., Brutscher, B., Konrat, R., & Tollinger, M. (2008). Folding
of the KIX domain: Characterization of the equilibrium analog of a folding intermediate
using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy.
Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2008.05.040'
chicago: 'Schanda, Paul, Bernhard Brutscher, Robert Konrat, and Martin Tollinger.
“Folding of the KIX Domain: Characterization of the Equilibrium Analog of a Folding
Intermediate Using 15N/13C Relaxation Dispersion and Fast 1H/2H Amide Exchange
NMR Spectroscopy.” Journal of Molecular Biology. Elsevier, 2008. https://doi.org/10.1016/j.jmb.2008.05.040.'
ieee: 'P. Schanda, B. Brutscher, R. Konrat, and M. Tollinger, “Folding of the KIX
domain: Characterization of the equilibrium analog of a folding intermediate using
15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy,”
Journal of Molecular Biology, vol. 380, no. 4. Elsevier, pp. 726–741, 2008.'
ista: 'Schanda P, Brutscher B, Konrat R, Tollinger M. 2008. Folding of the KIX domain:
Characterization of the equilibrium analog of a folding intermediate using 15N/13C
relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. Journal
of Molecular Biology. 380(4), 726–741.'
mla: 'Schanda, Paul, et al. “Folding of the KIX Domain: Characterization of the
Equilibrium Analog of a Folding Intermediate Using 15N/13C Relaxation Dispersion
and Fast 1H/2H Amide Exchange NMR Spectroscopy.” Journal of Molecular Biology,
vol. 380, no. 4, Elsevier, 2008, pp. 726–41, doi:10.1016/j.jmb.2008.05.040.'
short: P. Schanda, B. Brutscher, R. Konrat, M. Tollinger, Journal of Molecular Biology
380 (2008) 726–741.
date_created: 2020-09-18T10:12:29Z
date_published: 2008-07-18T00:00:00Z
date_updated: 2021-01-12T08:19:34Z
day: '18'
doi: 10.1016/j.jmb.2008.05.040
extern: '1'
intvolume: ' 380'
issue: '4'
keyword:
- Molecular Biology
language:
- iso: eng
month: '07'
oa_version: None
page: 726-741
publication: Journal of Molecular Biology
publication_identifier:
issn:
- 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: 'Folding of the KIX domain: Characterization of the equilibrium analog of a
folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange
NMR spectroscopy'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 380
year: '2008'
...
---
_id: '8481'
abstract:
- lang: eng
text: 'The copK gene is localized on the pMOL30 plasmid of Cupriavidus metallidurans
CH34 within the complex cop cluster of genes, for which 21 genes have been identified.
The expression of the corresponding periplasmic CopK protein is strongly upregulated
in the presence of copper, leading to a high periplasmic accumulation. The structure
and metal-binding properties of CopK were investigated by NMR and mass spectrometry.
The protein is dimeric in the apo state with a dissociation constant in the range
of 10- 5 M estimated from analytical ultracentrifugation. Mass spectrometry revealed
that CopK has two high-affinity Cu(I)-binding sites per monomer with different
Cu(I) affinities. Binding of Cu(II) was observed but appeared to be non-specific.
The solution structure of apo-CopK revealed an all-β fold formed of two β-sheets
in perpendicular orientation with an unstructured C-terminal tail. The dimer interface
is formed by the surface of the C-terminal β-sheet. Binding of the first Cu(I)-ion
induces a major structural modification involving dissociation of the dimeric
apo-protein. Backbone chemical shifts determined for the 1Cu(I)-bound form confirm
the conservation of the N-terminal β-sheet, while the last strand of the C-terminal
sheet appears in slow conformational exchange. We hypothesize that the partial
disruption of the C-terminal β-sheet is related to dimer dissociation. NH-exchange
data acquired on the apo-protein are consistent with a lower thermodynamic stability
of the C-terminal sheet. CopK contains seven methionine residues, five of which
appear highly conserved. Chemical shift data suggest implication of two or three
methionines (Met54, Met38, Met28) in the first Cu(I) site. Addition of a second
Cu(I) ion further increases protein plasticity. Comparison of the structural and
metal-binding properties of CopK with other periplasmic copper-binding proteins
reveals two conserved features within these functionally related proteins: the
all-β fold and the methionine-rich Cu(I)-binding site.'
article_processing_charge: No
article_type: original
author:
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Adrien
full_name: Favier, Adrien
last_name: Favier
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Sébastien
full_name: van Aelst, Sébastien
last_name: van Aelst
- first_name: Tatiana
full_name: Vallaeys, Tatiana
last_name: Vallaeys
- first_name: Jacques
full_name: Covès, Jacques
last_name: Covès
- first_name: Max
full_name: Mergeay, Max
last_name: Mergeay
- first_name: Ruddy
full_name: Wattiez, Ruddy
last_name: Wattiez
citation:
ama: Bersch B, Favier A, Schanda P, et al. Molecular structure and metal-binding
properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans
CH34 during copper challenge. Journal of Molecular Biology. 2008;380(2):386-403.
doi:10.1016/j.jmb.2008.05.017
apa: Bersch, B., Favier, A., Schanda, P., van Aelst, S., Vallaeys, T., Covès, J.,
… Wattiez, R. (2008). Molecular structure and metal-binding properties of the
periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper
challenge. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2008.05.017
chicago: Bersch, Beate, Adrien Favier, Paul Schanda, Sébastien van Aelst, Tatiana
Vallaeys, Jacques Covès, Max Mergeay, and Ruddy Wattiez. “Molecular Structure
and Metal-Binding Properties of the Periplasmic CopK Protein Expressed in Cupriavidus
Metallidurans CH34 during Copper Challenge.” Journal of Molecular Biology.
Elsevier, 2008. https://doi.org/10.1016/j.jmb.2008.05.017.
ieee: B. Bersch et al., “Molecular structure and metal-binding properties
of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during
copper challenge,” Journal of Molecular Biology, vol. 380, no. 2. Elsevier,
pp. 386–403, 2008.
ista: Bersch B, Favier A, Schanda P, van Aelst S, Vallaeys T, Covès J, Mergeay M,
Wattiez R. 2008. Molecular structure and metal-binding properties of the periplasmic
CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge.
Journal of Molecular Biology. 380(2), 386–403.
mla: Bersch, Beate, et al. “Molecular Structure and Metal-Binding Properties of
the Periplasmic CopK Protein Expressed in Cupriavidus Metallidurans CH34 during
Copper Challenge.” Journal of Molecular Biology, vol. 380, no. 2, Elsevier,
2008, pp. 386–403, doi:10.1016/j.jmb.2008.05.017.
short: B. Bersch, A. Favier, P. Schanda, S. van Aelst, T. Vallaeys, J. Covès, M.
Mergeay, R. Wattiez, Journal of Molecular Biology 380 (2008) 386–403.
date_created: 2020-09-18T10:12:37Z
date_published: 2008-07-04T00:00:00Z
date_updated: 2021-01-12T08:19:34Z
day: '04'
doi: 10.1016/j.jmb.2008.05.017
extern: '1'
intvolume: ' 380'
issue: '2'
keyword:
- Molecular Biology
language:
- iso: eng
month: '07'
oa_version: None
page: 386-403
publication: Journal of Molecular Biology
publication_identifier:
issn:
- 0022-2836
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Molecular structure and metal-binding properties of the periplasmic CopK protein
expressed in Cupriavidus metallidurans CH34 during copper challenge
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 380
year: '2008'
...
---
_id: '11116'
abstract:
- lang: eng
text: The metazoan nuclear envelope (NE) breaks down and re-forms during each cell
cycle. Nuclear pore complexes (NPCs), which allow nucleocytoplasmic transport
during interphase, assemble into the re-forming NE at the end of mitosis. Using
in vitro NE assembly, we show that the vertebrate homologue of MEL-28 (maternal
effect lethal), a recently discovered NE component in Caenorhabditis elegans,
functions in postmitotic NPC assembly. MEL-28 interacts with the Nup107–160 complex
(Nup for nucleoporin), an important building block of the NPC, and is essential
for the recruitment of the Nup107–160 complex to chromatin. We suggest that MEL-28
acts as a seeding point for NPC assembly.
article_processing_charge: No
article_type: original
author:
- first_name: Cerstin
full_name: Franz, Cerstin
last_name: Franz
- first_name: Rudolf
full_name: Walczak, Rudolf
last_name: Walczak
- first_name: Sevil
full_name: Yavuz, Sevil
last_name: Yavuz
- first_name: Rachel
full_name: Santarella, Rachel
last_name: Santarella
- first_name: Marc
full_name: Gentzel, Marc
last_name: Gentzel
- first_name: Peter
full_name: Askjaer, Peter
last_name: Askjaer
- first_name: Vincent
full_name: Galy, Vincent
last_name: Galy
- 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: Iain W
full_name: Mattaj, Iain W
last_name: Mattaj
- first_name: Wolfram
full_name: Antonin, Wolfram
last_name: Antonin
citation:
ama: Franz C, Walczak R, Yavuz S, et al. MEL‐28/ELYS is required for the recruitment
of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO
reports. 2007;8(2):165-172. doi:10.1038/sj.embor.7400889
apa: Franz, C., Walczak, R., Yavuz, S., Santarella, R., Gentzel, M., Askjaer, P.,
… Antonin, W. (2007). MEL‐28/ELYS is required for the recruitment of nucleoporins
to chromatin and postmitotic nuclear pore complex assembly. EMBO Reports.
EMBO. https://doi.org/10.1038/sj.embor.7400889
chicago: Franz, Cerstin, Rudolf Walczak, Sevil Yavuz, Rachel Santarella, Marc Gentzel,
Peter Askjaer, Vincent Galy, Martin Hetzer, Iain W Mattaj, and Wolfram Antonin.
“MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins to Chromatin and
Postmitotic Nuclear Pore Complex Assembly.” EMBO Reports. EMBO, 2007. https://doi.org/10.1038/sj.embor.7400889.
ieee: C. Franz et al., “MEL‐28/ELYS is required for the recruitment of nucleoporins
to chromatin and postmitotic nuclear pore complex assembly,” EMBO reports,
vol. 8, no. 2. EMBO, pp. 165–172, 2007.
ista: Franz C, Walczak R, Yavuz S, Santarella R, Gentzel M, Askjaer P, Galy V, Hetzer
M, Mattaj IW, Antonin W. 2007. MEL‐28/ELYS is required for the recruitment of
nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO
reports. 8(2), 165–172.
mla: Franz, Cerstin, et al. “MEL‐28/ELYS Is Required for the Recruitment of Nucleoporins
to Chromatin and Postmitotic Nuclear Pore Complex Assembly.” EMBO Reports,
vol. 8, no. 2, EMBO, 2007, pp. 165–72, doi:10.1038/sj.embor.7400889.
short: C. Franz, R. Walczak, S. Yavuz, R. Santarella, M. Gentzel, P. Askjaer, V.
Galy, M. Hetzer, I.W. Mattaj, W. Antonin, EMBO Reports 8 (2007) 165–172.
date_created: 2022-04-07T07:56:13Z
date_published: 2007-01-19T00:00:00Z
date_updated: 2022-07-18T08:56:40Z
day: '19'
doi: 10.1038/sj.embor.7400889
extern: '1'
external_id:
pmid:
- '17235358'
intvolume: ' 8'
issue: '2'
keyword:
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/sj.embor.7400889
month: '01'
oa: 1
oa_version: Published Version
page: 165-172
pmid: 1
publication: EMBO reports
publication_identifier:
eissn:
- 1469-3178
issn:
- 1469-221X
publication_status: published
publisher: EMBO
quality_controlled: '1'
scopus_import: '1'
status: public
title: MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and
postmitotic nuclear pore complex assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 8
year: '2007'
...
---
_id: '11117'
abstract:
- lang: eng
text: Over the last years it has become evident that the nuclear envelope (NE) is
more than a passive membrane barrier that separates the nucleus from the cytoplasm.
The NE not only controls the trafficking of macromolecules between the nucleoplasm
and the cytosol, but also provides anchoring sites for chromosomes and cytoskeleton
to the nuclear periphery. Targeting of chromatin to the NE might actually be part
of gene expression regulation in eukaryotes. Mutations in certain NE proteins
are associated with a diversity of human diseases, including muscular dystrophy,
neuropathy, lipodistrophy, torsion dystonia and the premature aging condition
progeria. Despite the importance of the NE for cell division and differentiation,
relatively little is known about its biogenesis and its role in human diseases.
It is our goal to provide a comprehensive view of the NE and to discuss possible
implications of NE-associated changes for gene expression, chromatin organization
and signal transduction.
article_processing_charge: No
article_type: review
author:
- first_name: M. A.
full_name: D’Angelo, M. A.
last_name: D’Angelo
- 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, Hetzer M. The role of the nuclear envelope in cellular organization.
Cellular and Molecular Life Sciences. 2006;63(3):316-332. doi:10.1007/s00018-005-5361-3
apa: D’Angelo, M. A., & Hetzer, M. (2006). The role of the nuclear envelope
in cellular organization. Cellular and Molecular Life Sciences. Springer
Nature. https://doi.org/10.1007/s00018-005-5361-3
chicago: D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in
Cellular Organization.” Cellular and Molecular Life Sciences. Springer
Nature, 2006. https://doi.org/10.1007/s00018-005-5361-3.
ieee: M. A. D’Angelo and M. Hetzer, “The role of the nuclear envelope in cellular
organization,” Cellular and Molecular Life Sciences, vol. 63, no. 3. Springer
Nature, pp. 316–332, 2006.
ista: D’Angelo MA, Hetzer M. 2006. The role of the nuclear envelope in cellular
organization. Cellular and Molecular Life Sciences. 63(3), 316–332.
mla: D’Angelo, M. A., and Martin Hetzer. “The Role of the Nuclear Envelope in Cellular
Organization.” Cellular and Molecular Life Sciences, vol. 63, no. 3, Springer
Nature, 2006, pp. 316–32, doi:10.1007/s00018-005-5361-3.
short: M.A. D’Angelo, M. Hetzer, Cellular and Molecular Life Sciences 63 (2006)
316–332.
date_created: 2022-04-07T07:56:22Z
date_published: 2006-01-02T00:00:00Z
date_updated: 2024-10-14T11:30:38Z
day: '02'
doi: 10.1007/s00018-005-5361-3
extern: '1'
external_id:
pmid:
- '16389459'
intvolume: ' 63'
issue: '3'
keyword:
- Cell Biology
- Cellular and Molecular Neuroscience
- Pharmacology
- Molecular Biology
- Molecular Medicine
language:
- iso: eng
month: '01'
oa_version: None
page: 316-332
pmid: 1
publication: Cellular and Molecular Life Sciences
publication_identifier:
eissn:
- 1420-9071
issn:
- 1420-682X
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: The role of the nuclear envelope in cellular organization
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 63
year: '2006'
...
---
_id: '12203'
abstract:
- lang: eng
text: 'Geranylgeranyl diphosphate synthase (GGPPS, EC: 2.5.1.29) catalyzes the biosynthesis
of geranylgeranyl diphosphate (GGPP), which is a key precursor for ginkgolide
biosynthesis. Here we reported for the first time the cloning of a new full-length
cDNA encoding GGPPS from the living fossil plant Ginkgo biloba. The full-length
cDNA encoding G. biloba GGPPS (designated as GbGGPPS) was 1657bp long and contained
a 1176bp open reading frame encoding a 391 amino acid protein. Comparative analysis
showed that GbGGPPS possessed a 79 amino acid transit peptide at its N-terminal,
which directed GbGGPPS to target to the plastids. Bioinformatic analysis revealed
that GbGGPPS was a member of polyprenyltransferases with two highly conserved
aspartate-rich motifs like other plant GGPPSs. Phylogenetic tree analysis indicated
that plant GGPPSs could be classified into two groups, angiosperm and gymnosperm
GGPPSs, while GbGGPPS had closer relationship with gymnosperm plant GGPPSs.'
acknowledgement: This study was financially supported by China National High-Tech
“863” Program. The authors are very thankful to Dr Li Wang (School of Life Sciences,
Fudan University, Shanghai, China) for her kind help with constructing the phylogenetic
tree.
article_processing_charge: No
article_type: original
author:
- first_name: Zhihua
full_name: Liao, Zhihua
last_name: Liao
- first_name: Min
full_name: Chen, Min
last_name: Chen
- first_name: Yifu
full_name: Gong, Yifu
last_name: Gong
- first_name: Liang
full_name: Guo, Liang
last_name: Guo
- first_name: Qiumin
full_name: Tan, Qiumin
last_name: Tan
- first_name: Xiaoqi
full_name: Feng, Xiaoqi
id: e0164712-22ee-11ed-b12a-d80fcdf35958
last_name: Feng
orcid: 0000-0002-4008-1234
- first_name: Xiaofen
full_name: Sun, Xiaofen
last_name: Sun
- first_name: Feng
full_name: Tan, Feng
last_name: Tan
- first_name: Kexuan
full_name: Tang, Kexuan
last_name: Tang
citation:
ama: Liao Z, Chen M, Gong Y, et al. A new geranylgeranyl Diphosphate synthase gene
from Ginkgo biloba, which intermediates the biosynthesis of the key precursor
for ginkgolides. DNA Sequence. 2004;15(2):153-158. doi:10.1080/10425170410001667348
apa: Liao, Z., Chen, M., Gong, Y., Guo, L., Tan, Q., Feng, X., … Tang, K. (2004).
A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates
the biosynthesis of the key precursor for ginkgolides. DNA Sequence. Informa
UK Limited. https://doi.org/10.1080/10425170410001667348
chicago: Liao, Zhihua, Min Chen, Yifu Gong, Liang Guo, Qiumin Tan, Xiaoqi Feng,
Xiaofen Sun, Feng Tan, and Kexuan Tang. “A New Geranylgeranyl Diphosphate Synthase
Gene from Ginkgo Biloba, Which Intermediates the Biosynthesis of the Key Precursor
for Ginkgolides.” DNA Sequence. Informa UK Limited, 2004. https://doi.org/10.1080/10425170410001667348.
ieee: Z. Liao et al., “A new geranylgeranyl Diphosphate synthase gene from
Ginkgo biloba, which intermediates the biosynthesis of the key precursor for ginkgolides,”
DNA Sequence, vol. 15, no. 2. Informa UK Limited, pp. 153–158, 2004.
ista: Liao Z, Chen M, Gong Y, Guo L, Tan Q, Feng X, Sun X, Tan F, Tang K. 2004.
A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates
the biosynthesis of the key precursor for ginkgolides. DNA Sequence. 15(2), 153–158.
mla: Liao, Zhihua, et al. “A New Geranylgeranyl Diphosphate Synthase Gene from Ginkgo
Biloba, Which Intermediates the Biosynthesis of the Key Precursor for Ginkgolides.”
DNA Sequence, vol. 15, no. 2, Informa UK Limited, 2004, pp. 153–58, doi:10.1080/10425170410001667348.
short: Z. Liao, M. Chen, Y. Gong, L. Guo, Q. Tan, X. Feng, X. Sun, F. Tan, K. Tang,
DNA Sequence 15 (2004) 153–158.
date_created: 2023-01-16T09:24:50Z
date_published: 2004-01-01T00:00:00Z
date_updated: 2023-05-08T10:58:29Z
department:
- _id: XiFe
doi: 10.1080/10425170410001667348
extern: '1'
external_id:
pmid:
- '15352294'
intvolume: ' 15'
issue: '2'
keyword:
- Endocrinology
- Genetics
- Molecular Biology
- Biochemistry
language:
- iso: eng
oa_version: None
page: 153-158
pmid: 1
publication: DNA Sequence
publication_identifier:
issn:
- 1042-5179
publication_status: published
publisher: Informa UK Limited
quality_controlled: '1'
scopus_import: '1'
status: public
title: A new geranylgeranyl Diphosphate synthase gene from Ginkgo biloba, which intermediates
the biosynthesis of the key precursor for ginkgolides
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 15
year: '2004'
...
---
_id: '11122'
abstract:
- lang: eng
text: Nuclear pore complexes (NPCs) are large multiprotein assemblies that allow
traffic between the cytoplasm and the nucleus. During mitosis in higher eukaryotes,
the Nuclear Envelope (NE) breaks down and NPCs disassemble. How NPCs reassemble
and incorporate into the NE upon mitotic exit is poorly understood. We demonstrate
a function for the conserved Nup107-160 complex in this process. Partial in vivo
depletion of Nup133 or Nup107 via RNAi in HeLa cells resulted in reduced levels
of multiple nucleoporins and decreased NPC density in the NE. Immunodepletion
of the entire Nup107-160 complex from in vitro nuclear assembly reactions produced
nuclei with a continuous NE but no NPCs. This phenotype was reversible only if
Nup107-160 complex was readded before closed NE formation. Depletion also prevented
association of FG-repeat nucleoporins with chromatin. We propose a stepwise model
in which postmitotic NPC assembly initiates on chromatin via early recruitment
of the Nup107-160 complex.
article_processing_charge: No
article_type: original
author:
- first_name: Tobias C.
full_name: Walther, Tobias C.
last_name: Walther
- first_name: Annabelle
full_name: Alves, Annabelle
last_name: Alves
- first_name: Helen
full_name: Pickersgill, Helen
last_name: Pickersgill
- first_name: Isabelle
full_name: Loı̈odice, Isabelle
last_name: Loı̈odice
- 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: Vincent
full_name: Galy, Vincent
last_name: Galy
- first_name: Bastian B.
full_name: Hülsmann, Bastian B.
last_name: Hülsmann
- first_name: Thomas
full_name: Köcher, Thomas
last_name: Köcher
- first_name: Matthias
full_name: Wilm, Matthias
last_name: Wilm
- first_name: Terry
full_name: Allen, Terry
last_name: Allen
- first_name: Iain W.
full_name: Mattaj, Iain W.
last_name: Mattaj
- first_name: Valérie
full_name: Doye, Valérie
last_name: Doye
citation:
ama: Walther TC, Alves A, Pickersgill H, et al. The conserved Nup107-160 complex
is critical for nuclear pore complex assembly. Cell. 2003;113(2):195-206.
doi:10.1016/s0092-8674(03)00235-6
apa: Walther, T. C., Alves, A., Pickersgill, H., Loı̈odice, I., Hetzer, M., Galy,
V., … Doye, V. (2003). The conserved Nup107-160 complex is critical for nuclear
pore complex assembly. Cell. Elsevier. https://doi.org/10.1016/s0092-8674(03)00235-6
chicago: Walther, Tobias C., Annabelle Alves, Helen Pickersgill, Isabelle Loı̈odice,
Martin Hetzer, Vincent Galy, Bastian B. Hülsmann, et al. “The Conserved Nup107-160
Complex Is Critical for Nuclear Pore Complex Assembly.” Cell. Elsevier,
2003. https://doi.org/10.1016/s0092-8674(03)00235-6.
ieee: T. C. Walther et al., “The conserved Nup107-160 complex is critical
for nuclear pore complex assembly,” Cell, vol. 113, no. 2. Elsevier, pp.
195–206, 2003.
ista: Walther TC, Alves A, Pickersgill H, Loı̈odice I, Hetzer M, Galy V, Hülsmann
BB, Köcher T, Wilm M, Allen T, Mattaj IW, Doye V. 2003. The conserved Nup107-160
complex is critical for nuclear pore complex assembly. Cell. 113(2), 195–206.
mla: Walther, Tobias C., et al. “The Conserved Nup107-160 Complex Is Critical for
Nuclear Pore Complex Assembly.” Cell, vol. 113, no. 2, Elsevier, 2003,
pp. 195–206, doi:10.1016/s0092-8674(03)00235-6.
short: T.C. Walther, A. Alves, H. Pickersgill, I. Loı̈odice, M. Hetzer, V. Galy,
B.B. Hülsmann, T. Köcher, M. Wilm, T. Allen, I.W. Mattaj, V. Doye, Cell 113 (2003)
195–206.
date_created: 2022-04-07T07:57:10Z
date_published: 2003-04-17T00:00:00Z
date_updated: 2022-07-18T08:57:42Z
day: '17'
doi: 10.1016/s0092-8674(03)00235-6
extern: '1'
external_id:
pmid:
- '12705868'
intvolume: ' 113'
issue: '2'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '04'
oa_version: Published Version
page: 195-206
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: The conserved Nup107-160 complex is critical for nuclear pore complex assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 113
year: '2003'
...
---
_id: '13438'
abstract:
- lang: eng
text: ICln is an ion channel identified by expression cloning using a cDNA library
from Madin-Darby canine kidney cells. In all organisms tested so far, only one
transcript for the ICln protein could be identified. Here we show that two splice
variants of the ICln ion channel can be found in Caenorhabditis elegans. Moreover,
we show that these two splice variants of the ICln channel protein, which we termed
IClnN1 and IClnN2, can be functionally reconstituted and tested in an artificial
lipid bilayer. In these experiments, the IClnN1-induced currents showed no voltage-dependent
inactivation, whereas the IClnN2-induced currents fully inactivated at positive
potentials. The molecular entity responsible for the voltage-dependent inactivation
of IClnN2 is a cluster of positively charged amino acids encoded by exon 2a, which
is absent in IClnN1. Our experiments suggest a mechanism of channel inactivation
that is similar to the “ball and chain” model proposed for the Shaker potassium
channel,i.e. a cluster of positively charged amino acids hinders ion permeation
through the channel by a molecular and voltage-dependent interaction at the inner
vestibulum of the pore. This hypothesis is supported by the finding that synthetic
peptides with the same amino acid sequence as the positive cluster can transform
the IClnN1-induced current to the current observed after reconstitution of IClnN2.
Furthermore, we show that the nematode ICln gene is embedded in an operon harboring
two additional genes, which we termed Nx and Ny. Co-reconstitution of Nx and IClnN2
and functional analysis of the related currents revealed a functional interaction
between the two proteins, as evidenced by the fact that the IClnN2-induced current
in the presence of Nx was no longer voltage-sensitive. The experiments described
indicate that the genome organization in nematodes allows an effective approach
for the identification of functional partner proteins of ion channels.
acknowledgement: We are grateful to D. E. Clapham, E. Wöll, G. Meyer, and G. Botta
for helpful discussion and/or reading of the manuscript. We also thank T. Stiernagle
for providing the N2 strain of C. elegans and A. Wimmer and M. Frick for technical
assistance
article_processing_charge: No
article_type: original
author:
- first_name: Johannes
full_name: Fürst, Johannes
last_name: Fürst
- first_name: Markus
full_name: Ritter, Markus
last_name: Ritter
- first_name: Jakob
full_name: Rudzki, Jakob
last_name: Rudzki
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
- first_name: Martin
full_name: Gschwentner, Martin
last_name: Gschwentner
- first_name: Elke
full_name: Scandella, Elke
last_name: Scandella
- first_name: Martin
full_name: Jakab, Martin
last_name: Jakab
- first_name: Matthias
full_name: König, Matthias
last_name: König
- first_name: Bernhard
full_name: Oehl, Bernhard
last_name: Oehl
- first_name: Florian
full_name: Lang, Florian
last_name: Lang
- first_name: Peter
full_name: Deetjen, Peter
last_name: Deetjen
- first_name: Markus
full_name: Paulmichl, Markus
last_name: Paulmichl
citation:
ama: Fürst J, Ritter M, Rudzki J, et al. ICln Ion channel splice variants in Caenorhabditis
elegans. Journal of Biological Chemistry. 2002;277(6):4435-4445. doi:10.1074/jbc.m107372200
apa: Fürst, J., Ritter, M., Rudzki, J., Danzl, J. G., Gschwentner, M., Scandella,
E., … Paulmichl, M. (2002). ICln Ion channel splice variants in Caenorhabditis
elegans. Journal of Biological Chemistry. Elsevier. https://doi.org/10.1074/jbc.m107372200
chicago: Fürst, Johannes, Markus Ritter, Jakob Rudzki, Johann G Danzl, Martin Gschwentner,
Elke Scandella, Martin Jakab, et al. “ICln Ion Channel Splice Variants in Caenorhabditis
Elegans.” Journal of Biological Chemistry. Elsevier, 2002. https://doi.org/10.1074/jbc.m107372200.
ieee: J. Fürst et al., “ICln Ion channel splice variants in Caenorhabditis
elegans,” Journal of Biological Chemistry, vol. 277, no. 6. Elsevier, pp.
4435–4445, 2002.
ista: Fürst J, Ritter M, Rudzki J, Danzl JG, Gschwentner M, Scandella E, Jakab M,
König M, Oehl B, Lang F, Deetjen P, Paulmichl M. 2002. ICln Ion channel splice
variants in Caenorhabditis elegans. Journal of Biological Chemistry. 277(6), 4435–4445.
mla: Fürst, Johannes, et al. “ICln Ion Channel Splice Variants in Caenorhabditis
Elegans.” Journal of Biological Chemistry, vol. 277, no. 6, Elsevier, 2002,
pp. 4435–45, doi:10.1074/jbc.m107372200.
short: J. Fürst, M. Ritter, J. Rudzki, J.G. Danzl, M. Gschwentner, E. Scandella,
M. Jakab, M. König, B. Oehl, F. Lang, P. Deetjen, M. Paulmichl, Journal of Biological
Chemistry 277 (2002) 4435–4445.
date_created: 2023-08-01T12:37:50Z
date_published: 2002-02-08T00:00:00Z
date_updated: 2023-08-01T12:55:54Z
day: '08'
ddc:
- '570'
doi: 10.1074/jbc.m107372200
extern: '1'
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pmid:
- '11706026'
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has_accepted_license: '1'
intvolume: ' 277'
issue: '6'
keyword:
- Cell Biology
- Molecular Biology
- Biochemistry
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: 4435-4445
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
issn:
- 0021-9258
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: ICln Ion channel splice variants in Caenorhabditis elegans
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 277
year: '2002'
...
---
_id: '11124'
abstract:
- lang: eng
text: Ran GTPase plays important roles in nucleocytoplasmic transport in interphase
[1, 2] and in both spindle formation and nuclear envelope (NE) assembly during
mitosis [3, 4, 5]. The latter functions rely on the presence of high local concentrations
of GTP-bound Ran near mitotic chromatin [3, 4, 5]. RanGTP localization has been
proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1,
with chromatin [6, 7, 8, 9], but Ran is shown here to bind directly to chromatin
in two modes, either dependent or independent of RCC1, and, where bound, to increase
the affinity of chromatin for NE membranes. We propose that the Ran binding capacity
of chromatin contributes to localized spindle and NE assembly.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Daniel
full_name: Bilbao-Cortés, Daniel
last_name: Bilbao-Cortés
- 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: Gernot
full_name: Längst, Gernot
last_name: Längst
- first_name: Peter B.
full_name: Becker, Peter B.
last_name: Becker
- first_name: Iain W.
full_name: Mattaj, Iain W.
last_name: Mattaj
citation:
ama: Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. Ran binds to chromatin
by two distinct mechanisms. Current Biology. 2002;12(13):1151-1156. doi:10.1016/s0960-9822(02)00927-2
apa: Bilbao-Cortés, D., Hetzer, M., Längst, G., Becker, P. B., & Mattaj, I.
W. (2002). Ran binds to chromatin by two distinct mechanisms. Current Biology.
Elsevier BV. https://doi.org/10.1016/s0960-9822(02)00927-2
chicago: Bilbao-Cortés, Daniel, Martin Hetzer, Gernot Längst, Peter B. Becker, and
Iain W. Mattaj. “Ran Binds to Chromatin by Two Distinct Mechanisms.” Current
Biology. Elsevier BV, 2002. https://doi.org/10.1016/s0960-9822(02)00927-2.
ieee: D. Bilbao-Cortés, M. Hetzer, G. Längst, P. B. Becker, and I. W. Mattaj, “Ran
binds to chromatin by two distinct mechanisms,” Current Biology, vol. 12,
no. 13. Elsevier BV, pp. 1151–1156, 2002.
ista: Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW. 2002. Ran binds
to chromatin by two distinct mechanisms. Current Biology. 12(13), 1151–1156.
mla: Bilbao-Cortés, Daniel, et al. “Ran Binds to Chromatin by Two Distinct Mechanisms.”
Current Biology, vol. 12, no. 13, Elsevier BV, 2002, pp. 1151–56, doi:10.1016/s0960-9822(02)00927-2.
short: D. Bilbao-Cortés, M. Hetzer, G. Längst, P.B. Becker, I.W. Mattaj, Current
Biology 12 (2002) 1151–1156.
date_created: 2022-04-07T07:57:31Z
date_published: 2002-07-09T00:00:00Z
date_updated: 2022-07-18T08:58:05Z
day: '09'
doi: 10.1016/s0960-9822(02)00927-2
extern: '1'
external_id:
pmid:
- '12121625'
intvolume: ' 12'
issue: '13'
keyword:
- General Agricultural and Biological Sciences
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/S0960-9822(02)00927-2
month: '07'
oa: 1
oa_version: Published Version
page: 1151-1156
pmid: 1
publication: Current Biology
publication_identifier:
issn:
- 0960-9822
publication_status: published
publisher: Elsevier BV
quality_controlled: '1'
scopus_import: '1'
status: public
title: Ran binds to chromatin by two distinct mechanisms
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 12
year: '2002'
...
---
_id: '11127'
abstract:
- lang: eng
text: Nuclear formation in Xenopus egg extracts requires cytosol and is inhibited
by GTPγS, indicating a requirement for GTPase activity. Nuclear envelope (NE)
vesicle fusion is extensively inhibited by GTPγS and two mutant forms of the Ran
GTPase, Q69L and T24N. Depletion of either Ran or RCC1, the exchange factor for
Ran, from the assembly reaction also inhibits this step of NE formation. Ran depletion
can be complemented by the addition of Ran loaded with either GTP or GDP but not
with GTPγS. RCC1 depletion is only complemented by RCC1 itself or by RanGTP. Thus,
generation of RanGTP by RCC1 and GTP hydrolysis by Ran are both required for the
extensive membrane fusion events that lead to NE formation.
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
- first_name: Daniel
full_name: Bilbao-Cortés, Daniel
last_name: Bilbao-Cortés
- first_name: Tobias C
full_name: Walther, Tobias C
last_name: Walther
- first_name: Oliver J
full_name: Gruss, Oliver J
last_name: Gruss
- first_name: Iain W
full_name: Mattaj, Iain W
last_name: Mattaj
citation:
ama: Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. GTP hydrolysis
by Ran is required for nuclear envelope assembly. Molecular Cell. 2000;5(6):1013-1024.
doi:10.1016/s1097-2765(00)80266-x
apa: Hetzer, M., Bilbao-Cortés, D., Walther, T. C., Gruss, O. J., & Mattaj,
I. W. (2000). GTP hydrolysis by Ran is required for nuclear envelope assembly.
Molecular Cell. Elsevier. https://doi.org/10.1016/s1097-2765(00)80266-x
chicago: Hetzer, Martin, Daniel Bilbao-Cortés, Tobias C Walther, Oliver J Gruss,
and Iain W Mattaj. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.”
Molecular Cell. Elsevier, 2000. https://doi.org/10.1016/s1097-2765(00)80266-x.
ieee: M. Hetzer, D. Bilbao-Cortés, T. C. Walther, O. J. Gruss, and I. W. Mattaj,
“GTP hydrolysis by Ran is required for nuclear envelope assembly,” Molecular
Cell, vol. 5, no. 6. Elsevier, pp. 1013–1024, 2000.
ista: Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. 2000. GTP hydrolysis
by Ran is required for nuclear envelope assembly. Molecular Cell. 5(6), 1013–1024.
mla: Hetzer, Martin, et al. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope
Assembly.” Molecular Cell, vol. 5, no. 6, Elsevier, 2000, pp. 1013–24,
doi:10.1016/s1097-2765(00)80266-x.
short: M. Hetzer, D. Bilbao-Cortés, T.C. Walther, O.J. Gruss, I.W. Mattaj, Molecular
Cell 5 (2000) 1013–1024.
date_created: 2022-04-07T07:57:59Z
date_published: 2000-06-01T00:00:00Z
date_updated: 2022-07-18T08:58:31Z
day: '01'
doi: 10.1016/s1097-2765(00)80266-x
extern: '1'
external_id:
pmid:
- '10911995'
intvolume: ' 5'
issue: '6'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/S1097-2765(00)80266-X
month: '06'
oa: 1
oa_version: Published Version
page: 1013-1024
pmid: 1
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: GTP hydrolysis by Ran is required for nuclear envelope assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 5
year: '2000'
...