---
_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: '11106'
abstract:
- lang: eng
text: Formation of the nuclear envelope (NE) around segregated chromosomes occurs
by the reshaping of the endoplasmic reticulum (ER), a reservoir for disassembled
nuclear membrane components during mitosis. In this study, we show that inner
nuclear membrane proteins such as lamin B receptor (LBR), MAN1, Lap2β, and the
trans-membrane nucleoporins Ndc1 and POM121 drive the spreading of ER membranes
into the emerging NE via their capacity to bind chromatin in a collaborative manner.
Despite their redundant functions, decreasing the levels of any of these trans-membrane
proteins by RNAi-mediated knockdown delayed NE formation, whereas increasing the
levels of any of them had the opposite effect. Furthermore, acceleration of NE
formation interferes with chromosome separation during mitosis, indicating that
the time frame over which chromatin becomes membrane enclosed is physiologically
relevant and regulated. These data suggest that functionally distinct classes
of chromatin-interacting membrane proteins, which are present at nonsaturating
levels, collaborate to rapidly reestablish the nuclear compartment at the end
of mitosis.
article_processing_charge: No
article_type: original
author:
- first_name: Daniel J.
full_name: Anderson, Daniel J.
last_name: Anderson
- first_name: Jesse D.
full_name: Vargas, Jesse D.
last_name: Vargas
- first_name: Joshua P.
full_name: Hsiao, Joshua P.
last_name: Hsiao
- 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: Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. Recruitment of functionally distinct
membrane proteins to chromatin mediates nuclear envelope formation in vivo. Journal
of Cell Biology. 2009;186(2):183-191. doi:10.1083/jcb.200901106
apa: Anderson, D. J., Vargas, J. D., Hsiao, J. P., & Hetzer, M. (2009). Recruitment
of functionally distinct membrane proteins to chromatin mediates nuclear envelope
formation in vivo. Journal of Cell Biology. Rockefeller University Press.
https://doi.org/10.1083/jcb.200901106
chicago: Anderson, Daniel J., Jesse D. Vargas, Joshua P. Hsiao, and Martin Hetzer.
“Recruitment of Functionally Distinct Membrane Proteins to Chromatin Mediates
Nuclear Envelope Formation in Vivo.” Journal of Cell Biology. Rockefeller
University Press, 2009. https://doi.org/10.1083/jcb.200901106.
ieee: D. J. Anderson, J. D. Vargas, J. P. Hsiao, and M. Hetzer, “Recruitment of
functionally distinct membrane proteins to chromatin mediates nuclear envelope
formation in vivo,” Journal of Cell Biology, vol. 186, no. 2. Rockefeller
University Press, pp. 183–191, 2009.
ista: Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. 2009. Recruitment of functionally
distinct membrane proteins to chromatin mediates nuclear envelope formation in
vivo. Journal of Cell Biology. 186(2), 183–191.
mla: Anderson, Daniel J., et al. “Recruitment of Functionally Distinct Membrane
Proteins to Chromatin Mediates Nuclear Envelope Formation in Vivo.” Journal
of Cell Biology, vol. 186, no. 2, Rockefeller University Press, 2009, pp.
183–91, doi:10.1083/jcb.200901106.
short: D.J. Anderson, J.D. Vargas, J.P. Hsiao, M. Hetzer, Journal of Cell Biology
186 (2009) 183–191.
date_created: 2022-04-07T07:54:18Z
date_published: 2009-07-20T00:00:00Z
date_updated: 2022-07-18T08:58:35Z
day: '20'
doi: 10.1083/jcb.200901106
extern: '1'
external_id:
pmid:
- '19620630'
intvolume: ' 186'
issue: '2'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1083/jcb.200901106
month: '07'
oa: 1
oa_version: Published Version
page: 183-191
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1083/jcb.20090110620090903c
scopus_import: '1'
status: public
title: Recruitment of functionally distinct membrane proteins to chromatin mediates
nuclear envelope formation in vivo
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 186
year: '2009'
...
---
_id: '11107'
abstract:
- lang: eng
text: Nucleocytoplasmic transport occurs exclusively through nuclear pore complexes
(NPCs) embedded in pores formed by inner and outer nuclear membrane fusion. The
mechanism for de novo pore and NPC biogenesis remains unclear. Reticulons (RTNs)
and Yop1/DP1 are conserved membrane protein families required to form and maintain
the tubular endoplasmic reticulum (ER) and the postmitotic nuclear envelope. In
this study, we report that members of the RTN and Yop1/DP1 families are required
for nuclear pore formation. Analysis of Saccharomyces cerevisiae prp20-G282S and
nup133Δ NPC assembly mutants revealed perturbations in Rtn1–green fluorescent
protein (GFP) and Yop1-GFP ER distribution and colocalization to NPC clusters.
Combined deletion of RTN1 and YOP1 resulted in NPC clustering, nuclear import
defects, and synthetic lethality with the additional absence of Pom34, Pom152,
and Nup84 subcomplex members. We tested for a direct role in NPC biogenesis using
Xenopus laevis in vitro assays and found that anti-Rtn4a antibodies specifically
inhibited de novo nuclear pore formation. We hypothesize that these ER membrane–bending
proteins mediate early NPC assembly steps.
article_processing_charge: No
article_type: original
author:
- first_name: T. Renee
full_name: Dawson, T. Renee
last_name: Dawson
- first_name: Michelle D.
full_name: Lazarus, Michelle D.
last_name: Lazarus
- 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: Dawson TR, Lazarus MD, Hetzer M, Wente SR. ER membrane–bending proteins are
necessary for de novo nuclear pore formation. Journal of Cell Biology.
2009;184(5):659-675. doi:10.1083/jcb.200806174
apa: Dawson, T. R., Lazarus, M. D., Hetzer, M., & Wente, S. R. (2009). ER membrane–bending
proteins are necessary for de novo nuclear pore formation. Journal of Cell
Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.200806174
chicago: Dawson, T. Renee, Michelle D. Lazarus, Martin Hetzer, and Susan R. Wente.
“ER Membrane–Bending Proteins Are Necessary for de Novo Nuclear Pore Formation.”
Journal of Cell Biology. Rockefeller University Press, 2009. https://doi.org/10.1083/jcb.200806174.
ieee: T. R. Dawson, M. D. Lazarus, M. Hetzer, and S. R. Wente, “ER membrane–bending
proteins are necessary for de novo nuclear pore formation,” Journal of Cell
Biology, vol. 184, no. 5. Rockefeller University Press, pp. 659–675, 2009.
ista: Dawson TR, Lazarus MD, Hetzer M, Wente SR. 2009. ER membrane–bending proteins
are necessary for de novo nuclear pore formation. Journal of Cell Biology. 184(5),
659–675.
mla: Dawson, T. Renee, et al. “ER Membrane–Bending Proteins Are Necessary for de
Novo Nuclear Pore Formation.” Journal of Cell Biology, vol. 184, no. 5,
Rockefeller University Press, 2009, pp. 659–75, doi:10.1083/jcb.200806174.
short: T.R. Dawson, M.D. Lazarus, M. Hetzer, S.R. Wente, Journal of Cell Biology
184 (2009) 659–675.
date_created: 2022-04-07T07:54:44Z
date_published: 2009-03-09T00:00:00Z
date_updated: 2022-07-18T08:55:05Z
day: '09'
doi: 10.1083/jcb.200806174
extern: '1'
external_id:
pmid:
- '19273614'
intvolume: ' 184'
issue: '5'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1083/jcb.200806174
month: '03'
oa: 1
oa_version: Published Version
page: 659-675
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: ER membrane–bending proteins are necessary for de novo nuclear pore formation
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 184
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: '11752'
abstract:
- lang: eng
text: We propose a model which suggests that structural martensitic transitions
are related to significant changes in the electronic structure, and are effected
by high-magnetic fields. The magnetic field dependence is considered unusual as
many influential investigations of martensitic transitions have emphasized that
the structural transitions are primarily lattice dynamical and are driven by the
entropy due to the phonons. We provide a theoretical framework which can be used
to describe the effect of high magnetic field on the transition and lattice dynamics
in which the field dependence originates from the dielectric constant. The model
is compared with some recent experimental results.
alternative_title:
- JPCS
article_number: '032062'
article_processing_charge: No
author:
- first_name: Xiaodong
full_name: Yang, Xiaodong
last_name: Yang
- first_name: Peter S
full_name: Riseborough, Peter S
last_name: Riseborough
- first_name: Kimberly A
full_name: Modic, Kimberly A
id: 13C26AC0-EB69-11E9-87C6-5F3BE6697425
last_name: Modic
orcid: 0000-0001-9760-3147
- first_name: R A
full_name: Fisher, R A
last_name: Fisher
- first_name: C P
full_name: Oppeil, C P
last_name: Oppeil
- first_name: T R
full_name: Finlayson, T R
last_name: Finlayson
- first_name: J C
full_name: Cooley, J C
last_name: Cooley
- first_name: J L
full_name: Smith, J L
last_name: Smith
- first_name: P A
full_name: Goddard, P A
last_name: Goddard
- first_name: A V
full_name: Silhanek, A V
last_name: Silhanek
- first_name: J C
full_name: Lashley, J C
last_name: Lashley
citation:
ama: 'Yang X, Riseborough PS, Modic KA, et al. Influence of magnetic fields on structural
martensitic transitions. In: Journal of Physics: Conference Series. Vol
200. IOP Publishing; 2009. doi:10.1088/1742-6596/200/3/032062'
apa: 'Yang, X., Riseborough, P. S., Modic, K. A., Fisher, R. A., Oppeil, C. P.,
Finlayson, T. R., … Lashley, J. C. (2009). Influence of magnetic fields on structural
martensitic transitions. In Journal of Physics: Conference Series (Vol.
200). Karlsruhe, Germany: IOP Publishing. https://doi.org/10.1088/1742-6596/200/3/032062'
chicago: 'Yang, Xiaodong, Peter S Riseborough, Kimberly A Modic, R A Fisher, C P
Oppeil, T R Finlayson, J C Cooley, et al. “Influence of Magnetic Fields on Structural
Martensitic Transitions.” In Journal of Physics: Conference Series, Vol.
200. IOP Publishing, 2009. https://doi.org/10.1088/1742-6596/200/3/032062.'
ieee: 'X. Yang et al., “Influence of magnetic fields on structural martensitic
transitions,” in Journal of Physics: Conference Series, Karlsruhe, Germany,
2009, vol. 200, no. 3.'
ista: 'Yang X, Riseborough PS, Modic KA, Fisher RA, Oppeil CP, Finlayson TR, Cooley
JC, Smith JL, Goddard PA, Silhanek AV, Lashley JC. 2009. Influence of magnetic
fields on structural martensitic transitions. Journal of Physics: Conference Series.
ICM: International Conference on Magnetism, JPCS, vol. 200, 032062.'
mla: 'Yang, Xiaodong, et al. “Influence of Magnetic Fields on Structural Martensitic
Transitions.” Journal of Physics: Conference Series, vol. 200, no. 3, 032062,
IOP Publishing, 2009, doi:10.1088/1742-6596/200/3/032062.'
short: 'X. Yang, P.S. Riseborough, K.A. Modic, R.A. Fisher, C.P. Oppeil, T.R. Finlayson,
J.C. Cooley, J.L. Smith, P.A. Goddard, A.V. Silhanek, J.C. Lashley, in:, Journal
of Physics: Conference Series, IOP Publishing, 2009.'
conference:
end_date: 2009-07-31
location: Karlsruhe, Germany
name: 'ICM: International Conference on Magnetism'
start_date: 2009-07-26
date_created: 2022-08-08T08:43:04Z
date_published: 2009-07-01T00:00:00Z
date_updated: 2023-02-23T12:58:33Z
day: '01'
doi: 10.1088/1742-6596/200/3/032062
extern: '1'
intvolume: ' 200'
issue: '3'
language:
- iso: eng
month: '07'
oa_version: None
publication: 'Journal of Physics: Conference Series'
publication_identifier:
eissn:
- 1742-6596
issn:
- 1742-6588
publication_status: published
publisher: IOP Publishing
quality_controlled: '1'
related_material:
record:
- id: '7080'
relation: later_version
status: public
scopus_import: '1'
status: public
title: Influence of magnetic fields on structural martensitic transitions
type: conference
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 200
year: '2009'
...
---
_id: '8026'
abstract:
- lang: eng
text: Recent theoretical work has provided a basic understanding of signal propagation
in networks of spiking neurons, but mechanisms for gating and controlling these
signals have not been investigated previously. Here we introduce an idea for the
gating of multiple signals in cortical networks that combines principles of signal
propagation with aspects of balanced networks. Specifically, we studied networks
in which incoming excitatory signals are normally cancelled by locally evoked
inhibition, leaving the targeted layer unresponsive. Transmission can be gated
'on' by modulating excitatory and inhibitory gains to upset this detailed balance.
We illustrate gating through detailed balance in large networks of integrate-and-fire
neurons. We show successful gating of multiple signals and study failure modes
that produce effects reminiscent of clinically observed pathologies. Provided
that the individual signals are detectable, detailed balance has a large capacity
for gating multiple signals.
article_processing_charge: No
article_type: original
author:
- first_name: Tim P
full_name: Vogels, Tim P
id: CB6FF8D2-008F-11EA-8E08-2637E6697425
last_name: Vogels
orcid: 0000-0003-3295-6181
- first_name: L F
full_name: Abbott, L F
last_name: Abbott
citation:
ama: Vogels TP, Abbott LF. Gating multiple signals through detailed balance of excitation
and inhibition in spiking networks. Nature Neuroscience. 2009;12(4):483-491.
doi:10.1038/nn.2276
apa: Vogels, T. P., & Abbott, L. F. (2009). Gating multiple signals through
detailed balance of excitation and inhibition in spiking networks. Nature Neuroscience.
Springer Nature. https://doi.org/10.1038/nn.2276
chicago: Vogels, Tim P, and L F Abbott. “Gating Multiple Signals through Detailed
Balance of Excitation and Inhibition in Spiking Networks.” Nature Neuroscience.
Springer Nature, 2009. https://doi.org/10.1038/nn.2276.
ieee: T. P. Vogels and L. F. Abbott, “Gating multiple signals through detailed balance
of excitation and inhibition in spiking networks,” Nature Neuroscience,
vol. 12, no. 4. Springer Nature, pp. 483–491, 2009.
ista: Vogels TP, Abbott LF. 2009. Gating multiple signals through detailed balance
of excitation and inhibition in spiking networks. Nature Neuroscience. 12(4),
483–491.
mla: Vogels, Tim P., and L. F. Abbott. “Gating Multiple Signals through Detailed
Balance of Excitation and Inhibition in Spiking Networks.” Nature Neuroscience,
vol. 12, no. 4, Springer Nature, 2009, pp. 483–91, doi:10.1038/nn.2276.
short: T.P. Vogels, L.F. Abbott, Nature Neuroscience 12 (2009) 483–491.
date_created: 2020-06-25T13:10:55Z
date_published: 2009-04-01T00:00:00Z
date_updated: 2021-01-12T08:16:36Z
day: '01'
doi: 10.1038/nn.2276
extern: '1'
external_id:
pmid:
- '19305402'
intvolume: ' 12'
issue: '4'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2693069/
month: '04'
oa: 1
oa_version: Submitted Version
page: 483-491
pmid: 1
publication: Nature Neuroscience
publication_identifier:
issn:
- 1097-6256
- 1546-1726
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Gating multiple signals through detailed balance of excitation and inhibition
in spiking networks
type: journal_article
user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 12
year: '2009'
...
---
_id: '8474'
abstract:
- lang: eng
text: Hydrogen bonds are ubiquitous interactions in proteins, and are important
for their folding and functionality. Scalar coupling constants across hydrogen
bonds in the protein backbone, some as small as 0.5 Hz, can be directly measured
in the solid state by NMR spectroscopy (see figure). The nuclei on both sides
of the hydrogen bond can be identified and the size of the coupling constant can
be measured accurately.
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: Matthias
full_name: Huber, Matthias
last_name: Huber
- first_name: René
full_name: Verel, René
last_name: Verel
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
- first_name: "Beatâ\x80\NH."
full_name: "Meier, Beatâ\x80\NH."
last_name: Meier
citation:
ama: Schanda P, Huber M, Verel R, Ernst M, Meier B. Direct detection of 3hJN’ hydrogen-bond
scalar couplings in proteins by solid-state NMR spectroscopy. Angewandte Chemie
International Edition. 2009;48(49):9322-9325. doi:10.1002/anie.200904411
apa: Schanda, P., Huber, M., Verel, R., Ernst, M., & Meier, B. (2009). Direct
detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR
spectroscopy. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.200904411
chicago: "Schanda, Paul, Matthias Huber, René Verel, Matthias Ernst, and Beatâ\x80\NH.
Meier. “Direct Detection of 3hJN’ Hydrogen-Bond Scalar Couplings in Proteins by
Solid-State NMR Spectroscopy.” Angewandte Chemie International Edition.
Wiley, 2009. https://doi.org/10.1002/anie.200904411."
ieee: P. Schanda, M. Huber, R. Verel, M. Ernst, and B. Meier, “Direct detection
of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy,”
Angewandte Chemie International Edition, vol. 48, no. 49. Wiley, pp. 9322–9325,
2009.
ista: Schanda P, Huber M, Verel R, Ernst M, Meier B. 2009. Direct detection of 3hJN’
hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy. Angewandte
Chemie International Edition. 48(49), 9322–9325.
mla: Schanda, Paul, et al. “Direct Detection of 3hJN’ Hydrogen-Bond Scalar Couplings
in Proteins by Solid-State NMR Spectroscopy.” Angewandte Chemie International
Edition, vol. 48, no. 49, Wiley, 2009, pp. 9322–25, doi:10.1002/anie.200904411.
short: P. Schanda, M. Huber, R. Verel, M. Ernst, B. Meier, Angewandte Chemie International
Edition 48 (2009) 9322–9325.
date_created: 2020-09-18T10:11:33Z
date_published: 2009-11-17T00:00:00Z
date_updated: 2021-01-12T08:19:31Z
day: '17'
doi: 10.1002/anie.200904411
extern: '1'
intvolume: ' 48'
issue: '49'
keyword:
- General Chemistry
- Catalysis
language:
- iso: eng
month: '11'
oa_version: None
page: 9322-9325
publication: Angewandte Chemie International Edition
publication_identifier:
issn:
- 1433-7851
- 1521-3773
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Direct detection of 3hJN' hydrogen-bond scalar couplings in proteins by solid-state
NMR spectroscopy
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 48
year: '2009'
...
---
_id: '8475'
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Schanda P. Fast-pulsing longitudinal relaxation optimized techniques: Enriching
the toolbox of fast biomolecular NMR spectroscopy. Progress in Nuclear Magnetic
Resonance Spectroscopy. 2009;55(3):238-265. doi:10.1016/j.pnmrs.2009.05.002'
apa: 'Schanda, P. (2009). Fast-pulsing longitudinal relaxation optimized techniques:
Enriching the toolbox of fast biomolecular NMR spectroscopy. Progress in Nuclear
Magnetic Resonance Spectroscopy. Elsevier. https://doi.org/10.1016/j.pnmrs.2009.05.002'
chicago: 'Schanda, Paul. “Fast-Pulsing Longitudinal Relaxation Optimized Techniques:
Enriching the Toolbox of Fast Biomolecular NMR Spectroscopy.” Progress in Nuclear
Magnetic Resonance Spectroscopy. Elsevier, 2009. https://doi.org/10.1016/j.pnmrs.2009.05.002.'
ieee: 'P. Schanda, “Fast-pulsing longitudinal relaxation optimized techniques: Enriching
the toolbox of fast biomolecular NMR spectroscopy,” Progress in Nuclear Magnetic
Resonance Spectroscopy, vol. 55, no. 3. Elsevier, pp. 238–265, 2009.'
ista: 'Schanda P. 2009. Fast-pulsing longitudinal relaxation optimized techniques:
Enriching the toolbox of fast biomolecular NMR spectroscopy. Progress in Nuclear
Magnetic Resonance Spectroscopy. 55(3), 238–265.'
mla: 'Schanda, Paul. “Fast-Pulsing Longitudinal Relaxation Optimized Techniques:
Enriching the Toolbox of Fast Biomolecular NMR Spectroscopy.” Progress in Nuclear
Magnetic Resonance Spectroscopy, vol. 55, no. 3, Elsevier, 2009, pp. 238–65,
doi:10.1016/j.pnmrs.2009.05.002.'
short: P. Schanda, Progress in Nuclear Magnetic Resonance Spectroscopy 55 (2009)
238–265.
date_created: 2020-09-18T10:11:42Z
date_published: 2009-10-01T00:00:00Z
date_updated: 2021-01-12T08:19:32Z
day: '01'
doi: 10.1016/j.pnmrs.2009.05.002
extern: '1'
intvolume: ' 55'
issue: '3'
language:
- iso: eng
month: '10'
oa_version: None
page: 238-265
publication: Progress in Nuclear Magnetic Resonance Spectroscopy
publication_identifier:
issn:
- 0079-6565
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: 'Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox
of fast biomolecular NMR spectroscopy'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 55
year: '2009'
...
---
_id: '8476'
abstract:
- lang: eng
text: Atomic-resolution information on the structure and dynamics of nucleic acids
is essential for a better understanding of the mechanistic basis of many cellular
processes. NMR spectroscopy is a powerful method for studying the structure and
dynamics of nucleic acids; however, solution NMR studies are currently limited
to relatively small nucleic acids at high concentrations. Thus, technological
and methodological improvements that increase the experimental sensitivity and
spectral resolution of NMR spectroscopy are required for studies of larger nucleic
acids or protein−nucleic acid complexes. Here we introduce a series of imino-proton-detected
NMR experiments that yield an over 2-fold increase in sensitivity compared to
conventional pulse schemes. These methods can be applied to the detection of base
pair interactions, RNA−ligand titration experiments, measurement of residual dipolar
15N−1H couplings, and direct measurements of conformational transitions. These
NMR experiments employ longitudinal spin relaxation enhancement techniques that
have proven useful in protein NMR spectroscopy. The performance of these new experiments
is demonstrated for a 10 kDa TAR-TAR*GA RNA kissing complex and a 26 kDa tRNA.
article_processing_charge: No
article_type: original
author:
- first_name: Jonathan
full_name: Farjon, Jonathan
last_name: Farjon
- first_name: Jérôme
full_name: Boisbouvier, Jérôme
last_name: Boisbouvier
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Arthur
full_name: Pardi, Arthur
last_name: Pardi
- first_name: Jean-Pierre
full_name: Simorre, Jean-Pierre
last_name: Simorre
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre J-P, Brutscher B. Longitudinal-relaxation-enhanced
NMR experiments for the study of nucleic acids in solution. Journal of the
American Chemical Society. 2009;131(24):8571-8577. doi:10.1021/ja901633y
apa: Farjon, J., Boisbouvier, J., Schanda, P., Pardi, A., Simorre, J.-P., &
Brutscher, B. (2009). Longitudinal-relaxation-enhanced NMR experiments for the
study of nucleic acids in solution. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/ja901633y
chicago: Farjon, Jonathan, Jérôme Boisbouvier, Paul Schanda, Arthur Pardi, Jean-Pierre
Simorre, and Bernhard Brutscher. “Longitudinal-Relaxation-Enhanced NMR Experiments
for the Study of Nucleic Acids in Solution.” Journal of the American Chemical
Society. American Chemical Society, 2009. https://doi.org/10.1021/ja901633y.
ieee: J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, and B. Brutscher,
“Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids
in solution,” Journal of the American Chemical Society, vol. 131, no. 24.
American Chemical Society, pp. 8571–8577, 2009.
ista: Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre J-P, Brutscher B. 2009.
Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids
in solution. Journal of the American Chemical Society. 131(24), 8571–8577.
mla: Farjon, Jonathan, et al. “Longitudinal-Relaxation-Enhanced NMR Experiments
for the Study of Nucleic Acids in Solution.” Journal of the American Chemical
Society, vol. 131, no. 24, American Chemical Society, 2009, pp. 8571–77, doi:10.1021/ja901633y.
short: J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, B. Brutscher,
Journal of the American Chemical Society 131 (2009) 8571–8577.
date_created: 2020-09-18T10:11:49Z
date_published: 2009-06-01T00:00:00Z
date_updated: 2021-01-12T08:19:32Z
day: '01'
doi: 10.1021/ja901633y
extern: '1'
intvolume: ' 131'
issue: '24'
language:
- iso: eng
month: '06'
oa_version: None
page: 8571-8577
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids
in solution
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 131
year: '2009'
...
---
_id: '8477'
abstract:
- lang: eng
text: An optimized NMR experiment that combines the advantages of methyl-TROSY and
SOFAST-HMQC has been developed. It allows the recording of high quality methyl
1H−13C correlation spectra of protein assemblies of several hundreds of kDa in
a few seconds. The SOFAST-methyl-TROSY-based experiment offers completely new
opportunities for the study of structural and dynamic changes occurring in molecular
nanomachines while they perform their biological function in vitro.
article_processing_charge: No
article_type: original
author:
- first_name: Carlos
full_name: Amero, Carlos
last_name: Amero
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: M. Asunción
full_name: Durá, M. Asunción
last_name: Durá
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Dominique
full_name: Marion, Dominique
last_name: Marion
- first_name: Bruno
full_name: Franzetti, Bruno
last_name: Franzetti
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Jérôme
full_name: Boisbouvier, Jérôme
last_name: Boisbouvier
citation:
ama: Amero C, Schanda P, Durá MA, et al. Fast two-dimensional NMR spectroscopy
of high molecular weight protein assemblies. Journal of the American Chemical
Society. 2009;131(10):3448-3449. doi:10.1021/ja809880p
apa: Amero, C., Schanda, P., Durá, M. A., Ayala, I., Marion, D., Franzetti, B.,
… Boisbouvier, J. (2009). Fast two-dimensional NMR spectroscopy of high molecular
weight protein assemblies. Journal of the American Chemical Society. American
Chemical Society. https://doi.org/10.1021/ja809880p
chicago: Amero, Carlos, Paul Schanda, M. Asunción Durá, Isabel Ayala, Dominique
Marion, Bruno Franzetti, Bernhard Brutscher, and Jérôme Boisbouvier. “Fast Two-Dimensional
NMR Spectroscopy of High Molecular Weight Protein Assemblies.” Journal of the
American Chemical Society. American Chemical Society, 2009. https://doi.org/10.1021/ja809880p.
ieee: C. Amero et al., “Fast two-dimensional NMR spectroscopy of high molecular
weight protein assemblies,” Journal of the American Chemical Society, vol.
131, no. 10. American Chemical Society, pp. 3448–3449, 2009.
ista: Amero C, Schanda P, Durá MA, Ayala I, Marion D, Franzetti B, Brutscher B,
Boisbouvier J. 2009. Fast two-dimensional NMR spectroscopy of high molecular weight
protein assemblies. Journal of the American Chemical Society. 131(10), 3448–3449.
mla: Amero, Carlos, et al. “Fast Two-Dimensional NMR Spectroscopy of High Molecular
Weight Protein Assemblies.” Journal of the American Chemical Society, vol.
131, no. 10, American Chemical Society, 2009, pp. 3448–49, doi:10.1021/ja809880p.
short: C. Amero, P. Schanda, M.A. Durá, I. Ayala, D. Marion, B. Franzetti, B. Brutscher,
J. Boisbouvier, Journal of the American Chemical Society 131 (2009) 3448–3449.
date_created: 2020-09-18T10:12:01Z
date_published: 2009-02-25T00:00:00Z
date_updated: 2021-01-12T08:19:32Z
day: '25'
doi: 10.1021/ja809880p
extern: '1'
intvolume: ' 131'
issue: '10'
language:
- iso: eng
month: '02'
oa_version: None
page: 3448-3449
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 131
year: '2009'
...
---
_id: '8478'
abstract:
- lang: eng
text: Allosteric regulation is an effective mechanism of control in biological processes.
In allosteric proteins a signal originating at one site in the molecule is communicated
through the protein structure to trigger a specific response at a remote site.
Using NMR relaxation dispersion techniques we directly observe the dynamic process
through which the KIX domain of CREB binding protein communicates allosteric information
between binding sites. KIX mediates cooperativity between pairs of transcription
factors through binding to two distinct interaction surfaces in an allosteric
manner. We show that binding the activation domain of the mixed lineage leukemia
(MLL) transcription factor to KIX induces a redistribution of the relative populations
of KIX conformations toward a high-energy state in which the allosterically activated
second binding site is already preformed, consistent with the Monod−Wyman−Changeux
(WMC) model of allostery. The structural rearrangement process that links the
two conformers and by which allosteric information is communicated occurs with
a time constant of 3 ms at 27 °C. Our dynamic NMR data reveal that an evolutionarily
conserved network of hydrophobic amino acids constitutes the pathway through which
information is transmitted.
article_processing_charge: No
article_type: original
author:
- first_name: Sven
full_name: Brüschweiler, Sven
last_name: Brüschweiler
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Karin
full_name: Kloiber, Karin
last_name: Kloiber
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Georg
full_name: Kontaxis, Georg
last_name: Kontaxis
- first_name: Robert
full_name: Konrat, Robert
last_name: Konrat
- first_name: Martin
full_name: Tollinger, Martin
last_name: Tollinger
citation:
ama: Brüschweiler S, Schanda P, Kloiber K, et al. Direct observation of the dynamic
process underlying allosteric signal transmission. Journal of the American
Chemical Society. 2009;131(8):3063-3068. doi:10.1021/ja809947w
apa: Brüschweiler, S., Schanda, P., Kloiber, K., Brutscher, B., Kontaxis, G., Konrat,
R., & Tollinger, M. (2009). Direct observation of the dynamic process underlying
allosteric signal transmission. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/ja809947w
chicago: Brüschweiler, Sven, Paul Schanda, Karin Kloiber, Bernhard Brutscher, Georg
Kontaxis, Robert Konrat, and Martin Tollinger. “Direct Observation of the Dynamic
Process Underlying Allosteric Signal Transmission.” Journal of the American
Chemical Society. American Chemical Society, 2009. https://doi.org/10.1021/ja809947w.
ieee: S. Brüschweiler et al., “Direct observation of the dynamic process
underlying allosteric signal transmission,” Journal of the American Chemical
Society, vol. 131, no. 8. American Chemical Society, pp. 3063–3068, 2009.
ista: Brüschweiler S, Schanda P, Kloiber K, Brutscher B, Kontaxis G, Konrat R,
Tollinger M. 2009. Direct observation of the dynamic process underlying allosteric
signal transmission. Journal of the American Chemical Society. 131(8), 3063–3068.
mla: Brüschweiler, Sven, et al. “Direct Observation of the Dynamic Process Underlying
Allosteric Signal Transmission.” Journal of the American Chemical Society,
vol. 131, no. 8, American Chemical Society, 2009, pp. 3063–68, doi:10.1021/ja809947w.
short: S. Brüschweiler, P. Schanda, K. Kloiber, B. Brutscher, G. Kontaxis, R. Konrat,
M. Tollinger, Journal of the American Chemical Society 131 (2009) 3063–3068.
date_created: 2020-09-18T10:12:14Z
date_published: 2009-02-09T00:00:00Z
date_updated: 2021-01-12T08:19:33Z
day: '09'
doi: 10.1021/ja809947w
extern: '1'
intvolume: ' 131'
issue: '8'
language:
- iso: eng
month: '02'
oa_version: None
page: 3063-3068
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Direct observation of the dynamic process underlying allosteric signal transmission
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 131
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: '8508'
abstract:
- lang: eng
text: We study generic unfoldings of homoclinic tangencies of two-dimensional area-preserving
diffeomorphisms (conservative New house phenomena) and show that they give rise
to invariant hyperbolic sets of arbitrarily large Hausdorff dimension. As applications,
we discuss the size of the stochastic layer of a standard map and the Hausdorff
dimension of invariant hyperbolic sets for certain restricted three-body problems.
We avoid involved technical details and only concentrate on the ideas of the proof
of the presented results.
article_processing_charge: No
article_type: original
author:
- first_name: Anton
full_name: Gorodetski, Anton
last_name: Gorodetski
- first_name: Vadim
full_name: Kaloshin, Vadim
id: FE553552-CDE8-11E9-B324-C0EBE5697425
last_name: Kaloshin
orcid: 0000-0002-6051-2628
citation:
ama: Gorodetski A, Kaloshin V. Conservative homoclinic bifurcations and some applications.
Proceedings of the Steklov Institute of Mathematics. 2009;267(1):76-90.
doi:10.1134/s0081543809040063
apa: Gorodetski, A., & Kaloshin, V. (2009). Conservative homoclinic bifurcations
and some applications. Proceedings of the Steklov Institute of Mathematics.
Springer Nature. https://doi.org/10.1134/s0081543809040063
chicago: Gorodetski, Anton, and Vadim Kaloshin. “Conservative Homoclinic Bifurcations
and Some Applications.” Proceedings of the Steklov Institute of Mathematics.
Springer Nature, 2009. https://doi.org/10.1134/s0081543809040063.
ieee: A. Gorodetski and V. Kaloshin, “Conservative homoclinic bifurcations and some
applications,” Proceedings of the Steklov Institute of Mathematics, vol.
267, no. 1. Springer Nature, pp. 76–90, 2009.
ista: Gorodetski A, Kaloshin V. 2009. Conservative homoclinic bifurcations and some
applications. Proceedings of the Steklov Institute of Mathematics. 267(1), 76–90.
mla: Gorodetski, Anton, and Vadim Kaloshin. “Conservative Homoclinic Bifurcations
and Some Applications.” Proceedings of the Steklov Institute of Mathematics,
vol. 267, no. 1, Springer Nature, 2009, pp. 76–90, doi:10.1134/s0081543809040063.
short: A. Gorodetski, V. Kaloshin, Proceedings of the Steklov Institute of Mathematics
267 (2009) 76–90.
date_created: 2020-09-18T10:48:03Z
date_published: 2009-12-01T00:00:00Z
date_updated: 2021-01-12T08:19:46Z
day: '01'
doi: 10.1134/s0081543809040063
extern: '1'
intvolume: ' 267'
issue: '1'
keyword:
- Mathematics (miscellaneous)
language:
- iso: eng
month: '12'
oa_version: None
page: 76-90
publication: Proceedings of the Steklov Institute of Mathematics
publication_identifier:
issn:
- 0081-5438
- 1531-8605
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Conservative homoclinic bifurcations and some applications
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 267
year: '2009'
...
---
_id: '88'
abstract:
- lang: eng
text: 'We have developed a tunable source of Mie scale microdroplet aerosols that
can be used for the generation of energetic ions. To demonstrate this potential,
a terawatt Ti: Al2 O3 laser focused to 2×10 19 W/cm2 was used to irradiate heavy
water (D2 O) aerosols composed of micron-scale droplets. Energetic deuterium ions,
which were generated in the laser-droplet interaction, produced deuterium-deuterium
fusion with approximately 2×10^3 fusion neutrons measured per joule of incident
laser energy. '
acknowledgement: This work was supported by the National Science Foundation under
Grant Nos. PHY-0456898, PHY-0757989, and PHY-0456870 and the National Nuclear Security
Administration under Cooperative Agreement No. DE-FC52-03NA00156. Acknowledgment
is made to the Donors of the Petroleum Research Fund administered by the American
Chemical Society for partial support of this research.
article_number: '063503'
author:
- first_name: Andrew P
full_name: Higginbotham, Andrew P
id: 4AD6785A-F248-11E8-B48F-1D18A9856A87
last_name: Higginbotham
orcid: 0000-0003-2607-2363
- first_name: Octavi
full_name: Semonin, Octavi
last_name: Semonin
- first_name: S
full_name: Bruce, S
last_name: Bruce
- first_name: C
full_name: Chan, C
last_name: Chan
- first_name: M
full_name: Maindi, M
last_name: Maindi
- first_name: Tom
full_name: Donnelly, Tom
last_name: Donnelly
- first_name: M
full_name: Maurer, M
last_name: Maurer
- first_name: Woosuk
full_name: Bang, Woosuk
last_name: Bang
- first_name: I.V
full_name: Churina, I.V
last_name: Churina
- first_name: Jens
full_name: Osterholz, Jens
last_name: Osterholz
- first_name: I
full_name: Kim, I
last_name: Kim
- first_name: Aaron
full_name: Bernstein, Aaron
last_name: Bernstein
- first_name: Todd
full_name: Ditmire, Todd
last_name: Ditmire
citation:
ama: Higginbotham AP, Semonin O, Bruce S, et al. Generation of Mie size microdroplet
aerosols with applications in laser-driven fusion experiments. Review of Scientific
Instruments. 2009;80(6). doi:10.1063/1.3155302
apa: Higginbotham, A. P., Semonin, O., Bruce, S., Chan, C., Maindi, M., Donnelly,
T., … Ditmire, T. (2009). Generation of Mie size microdroplet aerosols with applications
in laser-driven fusion experiments. Review of Scientific Instruments. American
Institute of Physics. https://doi.org/10.1063/1.3155302
chicago: Higginbotham, Andrew P, Octavi Semonin, S Bruce, C Chan, M Maindi, Tom
Donnelly, M Maurer, et al. “Generation of Mie Size Microdroplet Aerosols with
Applications in Laser-Driven Fusion Experiments.” Review of Scientific Instruments.
American Institute of Physics, 2009. https://doi.org/10.1063/1.3155302.
ieee: A. P. Higginbotham et al., “Generation of Mie size microdroplet aerosols
with applications in laser-driven fusion experiments,” Review of Scientific
Instruments, vol. 80, no. 6. American Institute of Physics, 2009.
ista: Higginbotham AP, Semonin O, Bruce S, Chan C, Maindi M, Donnelly T, Maurer
M, Bang W, Churina I., Osterholz J, Kim I, Bernstein A, Ditmire T. 2009. Generation
of Mie size microdroplet aerosols with applications in laser-driven fusion experiments.
Review of Scientific Instruments. 80(6), 063503.
mla: Higginbotham, Andrew P., et al. “Generation of Mie Size Microdroplet Aerosols
with Applications in Laser-Driven Fusion Experiments.” Review of Scientific
Instruments, vol. 80, no. 6, 063503, American Institute of Physics, 2009,
doi:10.1063/1.3155302.
short: A.P. Higginbotham, O. Semonin, S. Bruce, C. Chan, M. Maindi, T. Donnelly,
M. Maurer, W. Bang, I.. Churina, J. Osterholz, I. Kim, A. Bernstein, T. Ditmire,
Review of Scientific Instruments 80 (2009).
date_created: 2018-12-11T11:44:34Z
date_published: 2009-06-25T00:00:00Z
date_updated: 2021-01-12T08:21:06Z
day: '25'
doi: 10.1063/1.3155302
extern: '1'
external_id:
pmid:
- ' 19566203'
intvolume: ' 80'
issue: '6'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.osti.gov/biblio/22053583
month: '06'
oa: 1
oa_version: Submitted Version
pmid: 1
publication: Review of Scientific Instruments
publication_status: published
publisher: American Institute of Physics
publist_id: '7966'
quality_controlled: '1'
status: public
title: Generation of Mie size microdroplet aerosols with applications in laser-driven
fusion experiments
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 80
year: '2009'
...
---
_id: '164'
abstract:
- lang: eng
text: Let g be a cubic polynomial with integer coefficients and n>9 variables,
and assume that the congruence g=0 modulo p^k is soluble for all prime powers
p^k. We show that the equation g=0 has infinitely many integer solutions when
the cubic part of g defines a projective hypersurface with singular locus of dimension
<n-10. The proof is based on the Hardy-Littlewood circle method.
article_processing_charge: No
arxiv: 1
author:
- first_name: Timothy D
full_name: Browning, Timothy D
id: 35827D50-F248-11E8-B48F-1D18A9856A87
last_name: Browning
orcid: 0000-0002-8314-0177
- first_name: Roger
full_name: Heath Brown, Roger
last_name: Heath Brown
citation:
ama: 'Browning TD, Heath Brown R. Integral points on cubic hypersurfaces. In: Analytic
Number Theory: Essays in Honour of Klaus Roth. Cambridge University Press;
2009:75-90.'
apa: 'Browning, T. D., & Heath Brown, R. (2009). Integral points on cubic hypersurfaces.
In Analytic Number Theory: Essays in honour of Klaus Roth (pp. 75–90).
Cambridge University Press.'
chicago: 'Browning, Timothy D, and Roger Heath Brown. “Integral Points on Cubic
Hypersurfaces.” In Analytic Number Theory: Essays in Honour of Klaus Roth,
75–90. Cambridge University Press, 2009.'
ieee: 'T. D. Browning and R. Heath Brown, “Integral points on cubic hypersurfaces,”
in Analytic Number Theory: Essays in honour of Klaus Roth, Cambridge University
Press, 2009, pp. 75–90.'
ista: 'Browning TD, Heath Brown R. 2009.Integral points on cubic hypersurfaces.
In: Analytic Number Theory: Essays in honour of Klaus Roth. , 75–90.'
mla: 'Browning, Timothy D., and Roger Heath Brown. “Integral Points on Cubic Hypersurfaces.”
Analytic Number Theory: Essays in Honour of Klaus Roth, Cambridge University
Press, 2009, pp. 75–90.'
short: 'T.D. Browning, R. Heath Brown, in:, Analytic Number Theory: Essays in Honour
of Klaus Roth, Cambridge University Press, 2009, pp. 75–90.'
date_created: 2018-12-11T11:44:58Z
date_published: 2009-01-31T00:00:00Z
date_updated: 2021-01-12T06:52:11Z
day: '31'
extern: '1'
external_id:
arxiv:
- '0611086'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/math/0611086
month: '01'
oa: 1
oa_version: Preprint
page: 75 - 90
publication: 'Analytic Number Theory: Essays in honour of Klaus Roth'
publication_status: published
publisher: Cambridge University Press
publist_id: '7757'
quality_controlled: '1'
status: public
title: Integral points on cubic hypersurfaces
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2009'
...
---
_id: '165'
abstract:
- lang: eng
text: We survey the state of affairs for the distribution of ℚ-rational points on
non-singular del Pezzo surfaces of low degree, highlighting the recent resolution
of Manin's conjecture for a non-singular del Pezzo surface of degree 4 by la Bretèche
and Browning.
acknowledgement: Proceedings of the 5th China-Japan Seminar
alternative_title:
- Series on number theory and its application
author:
- first_name: Timothy D
full_name: Timothy Browning
id: 35827D50-F248-11E8-B48F-1D18A9856A87
last_name: Browning
orcid: 0000-0002-8314-0177
citation:
ama: 'Browning TD. Resent progress on the quantitative arithmetic of del Pezzo surfaces.
In: Aoki T, Kanemitsu S, Liu J, eds. Vol 6. World Scientific Publishing; 2009:1-18.
doi:https://doi.org/10.1142/9789814289924_0001'
apa: 'Browning, T. D. (2009). Resent progress on the quantitative arithmetic of
del Pezzo surfaces. In T. Aoki, S. Kanemitsu, & J. Liu (Eds.) (Vol. 6, pp.
1–18). Presented at the Number Theory: Dreaming in dreams, World Scientific Publishing.
https://doi.org/10.1142/9789814289924_0001'
chicago: Browning, Timothy D. “Resent Progress on the Quantitative Arithmetic of
Del Pezzo Surfaces.” edited by Takashi Aoki, Shigeru Kanemitsu, and Jianya Liu,
6:1–18. World Scientific Publishing, 2009. https://doi.org/10.1142/9789814289924_0001.
ieee: 'T. D. Browning, “Resent progress on the quantitative arithmetic of del Pezzo
surfaces,” presented at the Number Theory: Dreaming in dreams, 2009, vol. 6, pp.
1–18.'
ista: 'Browning TD. 2009. Resent progress on the quantitative arithmetic of del
Pezzo surfaces. Number Theory: Dreaming in dreams, Series on number theory and
its application, vol. 6, 1–18.'
mla: Browning, Timothy D. Resent Progress on the Quantitative Arithmetic of Del
Pezzo Surfaces. Edited by Takashi Aoki et al., vol. 6, World Scientific Publishing,
2009, pp. 1–18, doi:https://doi.org/10.1142/9789814289924_0001.
short: T.D. Browning, in:, T. Aoki, S. Kanemitsu, J. Liu (Eds.), World Scientific
Publishing, 2009, pp. 1–18.
conference:
name: 'Number Theory: Dreaming in dreams'
date_created: 2018-12-11T11:44:58Z
date_published: 2009-08-24T00:00:00Z
date_updated: 2021-01-12T06:52:15Z
day: '24'
doi: https://doi.org/10.1142/9789814289924_0001
editor:
- first_name: Takashi
full_name: Aoki, Takashi
last_name: Aoki
- first_name: Shigeru
full_name: Kanemitsu, Shigeru
last_name: Kanemitsu
- first_name: Jianya
full_name: Liu, Jianya
last_name: Liu
extern: 1
intvolume: ' 6'
month: '08'
page: 1 - 18
publication_status: published
publisher: World Scientific Publishing
publist_id: '7756'
quality_controlled: 0
status: public
title: Resent progress on the quantitative arithmetic of del Pezzo surfaces
type: conference
volume: 6
year: '2009'
...
---
_id: '168'
abstract:
- lang: eng
text: The arithmetic of ternary diagonal equation is considered for degree d >1,
with the outcome that the set of coefficients for which the equation admits a
non-zero integer solution is shown to have density zero.
alternative_title:
- Contemporary Mathematics
author:
- first_name: Timothy D
full_name: Timothy Browning
id: 35827D50-F248-11E8-B48F-1D18A9856A87
last_name: Browning
orcid: 0000-0002-8314-0177
- first_name: Rainer
full_name: Dietmann, Rainer
last_name: Dietmann
citation:
ama: 'Browning TD, Dietmann R. Solubility of Fermat equations. In: Quadratic
Forms - Algebra, Arithmetic and Geometry. Vol 493. American Mathematical Society;
2009:99-106. doi:http://dx.doi.org/10.1090/conm/493'
apa: Browning, T. D., & Dietmann, R. (2009). Solubility of Fermat equations.
In Quadratic Forms - algebra, arithmetic and geometry (Vol. 493, pp. 99–106).
American Mathematical Society. http://dx.doi.org/10.1090/conm/493
chicago: Browning, Timothy D, and Rainer Dietmann. “Solubility of Fermat Equations.”
In Quadratic Forms - Algebra, Arithmetic and Geometry, 493:99–106. American
Mathematical Society, 2009. http://dx.doi.org/10.1090/conm/493.
ieee: T. D. Browning and R. Dietmann, “Solubility of Fermat equations,” in Quadratic
Forms - algebra, arithmetic and geometry, vol. 493, American Mathematical
Society, 2009, pp. 99–106.
ista: 'Browning TD, Dietmann R. 2009.Solubility of Fermat equations. In: Quadratic
Forms - algebra, arithmetic and geometry. Contemporary Mathematics, vol. 493,
99–106.'
mla: Browning, Timothy D., and Rainer Dietmann. “Solubility of Fermat Equations.”
Quadratic Forms - Algebra, Arithmetic and Geometry, vol. 493, American
Mathematical Society, 2009, pp. 99–106, doi:http://dx.doi.org/10.1090/conm/493.
short: T.D. Browning, R. Dietmann, in:, Quadratic Forms - Algebra, Arithmetic and
Geometry, American Mathematical Society, 2009, pp. 99–106.
date_created: 2018-12-11T11:44:59Z
date_published: 2009-01-01T00:00:00Z
date_updated: 2021-01-12T06:52:29Z
day: '01'
doi: http://dx.doi.org/10.1090/conm/493
extern: 1
intvolume: ' 493'
main_file_link:
- open_access: '0'
url: https://arxiv.org/abs/0805.3354
month: '01'
page: 99 - 106
publication: Quadratic Forms - algebra, arithmetic and geometry
publication_status: published
publisher: American Mathematical Society
publist_id: '7753'
quality_controlled: 0
status: public
title: Solubility of Fermat equations
type: book_chapter
volume: 493
year: '2009'
...
---
_id: '1718'
abstract:
- lang: eng
text: Morphogens act as graded positional cues to control cell fate specification
in many developing tissues. This concept, in which a signaling gradient regulates
differential gene expression in a concentration-dependent manner, has received
considerable experimental support. Nevertheless, several recent studies have challenged
the straightforward model of morphogen activity. In particular, the observation
that pattern formation is a dynamic process has raised questions about the influence
of time on morphogen activity. Here we propose that the spatiotemporal dynamics
of the cellular response to a morphogen gradient depend on a combination of temporal
alterations to the morphogen gradient itself, the dynamics of its signal transduction
and downstream interactions between target genes.
acknowledgement: EK is supported by an EMBO LTF, AK by a FEBS fellowship, and JB by
MRC (UK) and the Wellcome Trust
author:
- first_name: Eva
full_name: Kutějová, Eva
last_name: Kutějová
- first_name: James
full_name: Briscoe, James
last_name: Briscoe
- first_name: Anna
full_name: Anna Kicheva
id: 3959A2A0-F248-11E8-B48F-1D18A9856A87
last_name: Kicheva
orcid: 0000-0003-4509-4998
citation:
ama: Kutějová E, Briscoe J, Kicheva A. Temporal dynamics of patterning by morphogen
gradients. Current Opinion in Genetics & Development. 2009;19(4):315-322.
doi:10.1016/j.gde.2009.05.004
apa: Kutějová, E., Briscoe, J., & Kicheva, A. (2009). Temporal dynamics of patterning
by morphogen gradients. Current Opinion in Genetics & Development.
Elsevier. https://doi.org/10.1016/j.gde.2009.05.004
chicago: Kutějová, Eva, James Briscoe, and Anna Kicheva. “Temporal Dynamics of Patterning
by Morphogen Gradients.” Current Opinion in Genetics & Development.
Elsevier, 2009. https://doi.org/10.1016/j.gde.2009.05.004.
ieee: E. Kutějová, J. Briscoe, and A. Kicheva, “Temporal dynamics of patterning
by morphogen gradients,” Current Opinion in Genetics & Development,
vol. 19, no. 4. Elsevier, pp. 315–322, 2009.
ista: Kutějová E, Briscoe J, Kicheva A. 2009. Temporal dynamics of patterning by
morphogen gradients. Current Opinion in Genetics & Development. 19(4), 315–322.
mla: Kutějová, Eva, et al. “Temporal Dynamics of Patterning by Morphogen Gradients.”
Current Opinion in Genetics & Development, vol. 19, no. 4, Elsevier,
2009, pp. 315–22, doi:10.1016/j.gde.2009.05.004.
short: E. Kutějová, J. Briscoe, A. Kicheva, Current Opinion in Genetics & Development
19 (2009) 315–322.
date_created: 2018-12-11T11:53:38Z
date_published: 2009-08-01T00:00:00Z
date_updated: 2021-01-12T06:52:44Z
day: '01'
doi: 10.1016/j.gde.2009.05.004
extern: 1
intvolume: ' 19'
issue: '4'
month: '08'
page: 315 - 322
publication: Current Opinion in Genetics & Development
publication_status: published
publisher: Elsevier
publist_id: '5410'
quality_controlled: 0
status: public
title: Temporal dynamics of patterning by morphogen gradients
type: journal_article
volume: 19
year: '2009'
...
---
_id: '1720'
abstract:
- lang: eng
text: How morphogen gradients are formed in target tissues is a key question for
understanding the mechanisms of morphological patterning. Here, we review different
mechanisms of morphogen gradient formation from theoretical and experimental points
of view. First, a simple, comprehensive overview of the underlying biophysical
principles of several mechanisms of gradient formation is provided. We then discuss
the advantages and limitations of different experimental approaches to gradient
formation analysis.
author:
- first_name: Ortrud
full_name: Wartlick, Ortrud
last_name: Wartlick
- first_name: Anna
full_name: Anna Kicheva
id: 3959A2A0-F248-11E8-B48F-1D18A9856A87
last_name: Kicheva
orcid: 0000-0003-4509-4998
- first_name: Marcos
full_name: González-Gaitán, Marcos A
last_name: González Gaitán
citation:
ama: Wartlick O, Kicheva A, González Gaitán M. Morphogen gradient formation . Cold
Spring Harbor perspectives in biology. 2009;1(3). doi:10.1101/cshperspect.a001255
apa: Wartlick, O., Kicheva, A., & González Gaitán, M. (2009). Morphogen gradient
formation . Cold Spring Harbor Perspectives in Biology. Cold Spring Harbor
Laboratory Press. https://doi.org/10.1101/cshperspect.a001255
chicago: Wartlick, Ortrud, Anna Kicheva, and Marcos González Gaitán. “Morphogen
Gradient Formation .” Cold Spring Harbor Perspectives in Biology. Cold
Spring Harbor Laboratory Press, 2009. https://doi.org/10.1101/cshperspect.a001255.
ieee: O. Wartlick, A. Kicheva, and M. González Gaitán, “Morphogen gradient formation
,” Cold Spring Harbor perspectives in biology, vol. 1, no. 3. Cold Spring
Harbor Laboratory Press, 2009.
ista: Wartlick O, Kicheva A, González Gaitán M. 2009. Morphogen gradient formation
. Cold Spring Harbor perspectives in biology. 1(3).
mla: Wartlick, Ortrud, et al. “Morphogen Gradient Formation .” Cold Spring Harbor
Perspectives in Biology, vol. 1, no. 3, Cold Spring Harbor Laboratory Press,
2009, doi:10.1101/cshperspect.a001255.
short: O. Wartlick, A. Kicheva, M. González Gaitán, Cold Spring Harbor Perspectives
in Biology 1 (2009).
date_created: 2018-12-11T11:53:39Z
date_published: 2009-09-01T00:00:00Z
date_updated: 2021-01-12T06:52:45Z
day: '01'
doi: 10.1101/cshperspect.a001255
extern: 1
intvolume: ' 1'
issue: '3'
month: '09'
publication: Cold Spring Harbor perspectives in biology
publication_status: published
publisher: Cold Spring Harbor Laboratory Press
publist_id: '5409'
quality_controlled: 0
status: public
title: 'Morphogen gradient formation '
type: journal_article
volume: 1
year: '2009'
...