The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
about
Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfoldedStructural basis for Nup2p function in cargo release and karyopherin recycling in nuclear importBinding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gatingHug1 is an intrinsically disordered protein that inhibits ribonucleotide reductase activity by directly binding Rnr2 subunit.Deciphering networks of protein interactions at the nuclear pore complexProkaryotic ubiquitin-like protein pup is intrinsically disorderedDisordered proteinaceous machinesA physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies.Systematic deletion and mitotic localization of the nuclear pore complex proteins of Aspergillus nidulans.A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins.Charge as a selection criterion for translocation through the nuclear pore complex.Probing a structural model of the nuclear pore complex channel through molecular dynamics.Nup2 requires a highly divergent partner, NupA, to fulfill functions at nuclear pore complexes and the mitotic chromatin region.Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathologyNucleocytoplasmic transport: navigating the channel.The nuclear pore complex: nucleocytoplasmic transport and beyond.Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transportMycobacterium tuberculosis copper-regulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayerSpectroscopic approaches to the conformation of tau protein in solution and in paired helical filaments.Characterization of molecular recognition features, MoRFs, and their binding partnersTowards reconciling structure and function in the nuclear pore complex.Functionalization of a nanopore: the nuclear pore complex paradigm.Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport.The selective permeability barrier in the nuclear pore complexCompartmentalization and Functionality of Nuclear Disorder: Intrinsic Disorder and Protein-Protein Interactions in Intra-Nuclear Compartments.Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes.Biophysical characterization of the enzyme I of the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system.Multiple conserved domains of the nucleoporin Nup124p and its orthologs Nup1p and Nup153 are critical for nuclear import and activity of the fission yeast Tf1 retrotransposon.The inactivating factor of glutamine synthetase, IF7, is a "natively unfolded" protein.Structural flexibility of multifunctional HABP1 may be important for regulating its binding to different ligands.Rapid evolution exposes the boundaries of domain structure and function in natively unfolded FG nucleoporins.Stories of Cells: The American Society for Cell Biology San Francisco, CA December 14–18, 2002.Intrinsically disordered proteins in the nucleus of human cells.Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences.Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein.Mutagenesis reveals a specific role for Cox17p in copper transport to cytochrome oxidase.Purification of Intrinsically Disordered ProteinsNucleoporin Gene Fusions and Hematopoietic Malignancies
P2860
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P248
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P2860
The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
description
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2002
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im September 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
wetenschappelijk artikel (gepubliceerd op 2002/09/06)
@nl
наукова стаття, опублікована у вересні 2002
@uk
مقالة علمية (نشرت في 6-9-2002)
@ar
name
The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
@ast
The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
@en
type
label
The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
@ast
The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
@en
prefLabel
The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
@ast
The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
@en
P2093
P3181
P356
P1476
The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
@en
P2093
Anthony L. Fink
Daniel P. Denning
Michael Rexach
Samir S. Patel
Vladimir Uversky
P304
33447–33455
P3181
P356
10.1074/JBC.M203499200
P407
P577
2002-09-06T00:00:00Z