Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Mary Marfori"'
Autor:
László Buday, Anna Erdei, Bostjan Kobe, Fruzsina Babos, Mary Marfori, Anna Magyar, Beáta G. Vértessy, Máté Borsos, Enikő Takács, Ildikó Scheer, Judit Tóth, Zoltán Bozóky, Gergely Róna
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 69:2495-2505
Phosphorylation adjacent to nuclear localization signals (NLSs) is involved in the regulation of nucleocytoplasmic transport. The nuclear isoform of human dUTPase, an enzyme that is essential for genomic integrity, has been shown to be phosphorylated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c1b1f9a2c2e582e7c0f5dabd0dd69b06
https://doi.org/10.1107/s0907444913023354
https://doi.org/10.1107/s0907444913023354
Publikováno v:
Traffic. 13:532-548
Classical nuclear localization signals (cNLSs), comprising one (monopartite cNLSs) or two clusters of basic residues connected by a 10–12 residue linker (bipartite cNLSs), are recognized by the nuclear import factor importin-α. The cNLSs bind alon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::620cad0794cf18eb4ced945c75798d56
https://doi.org/10.1111/j.1600-0854.2012.01329.x
https://doi.org/10.1111/j.1600-0854.2012.01329.x
Autor:
Mary Marfori, Bernard J. Carroll, Bostjan Kobe, Thierry G. A. Lonhienne, Jade K. Forwood, Gautier Robin
Publikováno v:
Journal of Biological Chemistry. 284:22549-22558
Ran-GTP interacts strongly with importin-β, and this interaction promotes the release of the importin-α-nuclear localization signal cargo from importin-β. Ran-GDP also interacts with importin-β, but this interaction is 4 orders of magnitude weake
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9935f09ca089702d18d1494287dca041
https://doi.org/10.1074/jbc.m109.019935
https://doi.org/10.1074/jbc.m109.019935
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:625-628
The transport of macromolecules across the nuclear envelope is an essential eukaryotic process that enables proteins such as transcription factors, polymerases and histones to gain access to the genetic material contained within the nucleus. Importin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::696c4deeab6b764d691b48d9e38bb709
https://doi.org/10.1107/s1744309109016820
https://doi.org/10.1107/s1744309109016820
Autor:
Gautier Robin, Bernard J. Carroll, Murray Stewart, Bostjan Kobe, Sai Man Liu, Thierry G. A. Lonhienne, Mary Marfori, Jade K. Forwood, Weining Meng, Gregor Gunčar
Publikováno v:
Journal of Molecular Biology. 383:772-782
The asymmetric distribution of the nucleotide-bound state of Ran across the nuclear envelope is crucial for determining the directionality of nuclear transport. In the nucleus, Ran is primarily in the guanosine 5'-triphosphate (GTP)-bound state, wher
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e1066fbac71d396ad61ab9e2ad1f9d5
https://doi.org/10.1016/j.jmb.2008.07.090
https://doi.org/10.1016/j.jmb.2008.07.090
Acyl-coenzyme A (acyl-CoA) thioesterases play a crucial role in the metabolism of activated fatty acids, coenzyme A, and other metabolic precursor molecules including arachidonic acid and palmitic acid. These enzymes hydrolyze coenzyme A from acyl-Co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28cca865be481a2d7ca3f6ee299bc9ac
https://europepmc.org/articles/PMC3195577/
https://europepmc.org/articles/PMC3195577/
Publikováno v:
Traffic (Copenhagen, Denmark). 13(4)
Classical nuclear localization signals (cNLSs), comprising one (monopartite cNLSs) or two clusters of basic residues connected by a 10-12 residue linker (bipartite cNLSs), are recognized by the nuclear import factor importin-α. The cNLSs bind along
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::beca1053cc2a9eb54db8e19153a819a3
https://pubmed.ncbi.nlm.nih.gov/22248489
https://pubmed.ncbi.nlm.nih.gov/22248489
Quantitative structural analysis of importin-β flexibility: Paradigm for solenoid protein structures
Autor:
Anita H. Corbett, Allison Lange, Jade K. Forwood, Callie Preast, Murray Stewart, Mary Marfori, Helmut Grubmüller, Bostjan Kobe, Ulrich Zachariae
Publikováno v:
Structure
SummaryThe structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-β, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b49e0368c6ec9ce85b8491061bb43c31
https://hdl.handle.net/11858/00-001M-0000-0027-C07B-111858/00-001M-0000-0027-C07F-A11858/00-001M-0000-0027-C07E-C
https://hdl.handle.net/11858/00-001M-0000-0027-C07B-111858/00-001M-0000-0027-C07F-A11858/00-001M-0000-0027-C07E-C
Autor:
Jonathan Ellis, Ahmed M. Mehdi, Paul M. G. Curmi, Bostjan Kobe, Jade K. Forwood, Mikael Bodén, Andrew V. Mynott, Neil F. W. Saunders, Mary Marfori
Publikováno v:
Biochimica et biophysica acta. 1813(9)
Although proteins are translated on cytoplasmic ribosomes, many of these proteins play essential roles in the nucleus, mediating key cellular processes including but not limited to DNA replication and repair as well as transcription and RNA processin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4374af4bb37d7cdbe6489e4534ed6bc1
https://pubmed.ncbi.nlm.nih.gov/20977914
https://pubmed.ncbi.nlm.nih.gov/20977914
Autor:
Thierry G, Lonhienne, Jade K, Forwood, Mary, Marfori, Gautier, Robin, Bostjan, Kobe, Bernard J, Carroll
Publikováno v:
The Journal of biological chemistry. 284(34)
Ran-GTP interacts strongly with importin-beta, and this interaction promotes the release of the importin-alpha-nuclear localization signal cargo from importin-beta. Ran-GDP also interacts with importin-beta, but this interaction is 4 orders of magnit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1fbe3e69644097afa462e37981411141
https://pubmed.ncbi.nlm.nih.gov/19549784
https://pubmed.ncbi.nlm.nih.gov/19549784