About: The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein

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rdf:type	Item
description	artículu científicu espublizáu en 2002 (ast) 2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована у вересні 2002 (uk) 2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած (hyw) wetenschappelijk artikel (gepubliceerd op 2002/09/06) (nl) مقالة علمية (نشرت في 6-9-2002) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im September 2002 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28909274-1EF8719A-EBD6-4F18-836B-4F97560F8B6C
publication date	2002-09-06 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28909274-94D7BEC1-04F3-4754-B9BD-B9059AA5875E
language of work or name	English
author name string	wds:Q28909274-37EAACEE-A8AC-4CE3-A84D-C5BFF7EB5C8C wds:Q28909274-5C4F6432-BFB8-4C35-AC67-4621744F5748 wds:Q28909274-8C57ED9E-44B1-4563-AB13-89FF58086192 wds:Q28909274-9F350464-BC15-4F79-9E16-9394A785E405
OpenCitations bibliographic resource ID	wds:Q28909274-97F44087-2612-45AA-B781-815F56B5175C
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/2415737
author name string	Michael Rexach Anthony L. Fink Daniel P. Denning Samir S. Patel
OpenCitations bibliographic resource ID	2415737
rdfs:label	The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein (en) The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein (ast)
skos:prefLabel	The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein (en) The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein (ast)
name	The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein (en) The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein (ast)
author	wds:Q28909274-31A1B94A-ADC6-458F-85FD-25D07C6CA6AE
author	Vladimir N. Uversky
title	wds:Q28909274-AB7259F8-BCDD-4631-BAFB-601B384D31B0
title	The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein (en)
page(s)	wds:Q28909274-59B0A6E5-5132-4B9F-9284-D7BE84F1AEB6
page(s)	33447–33455
instance of	wds:Q28909274-30E1FADB-0623-4B2D-A790-E83145296417
instance of	scholarly article
main subject	wds:Q28909274-733D831B-72EE-4DC1-8277-19DA5671C6F9 wds:Q28909274-94C5EA5D-0186-4082-8544-B8ECACB26304 wds:Q28909274-B99B4AC5-DB8B-495F-821D-45F5AD02CF0C wds:Q28909274-C685D980-1FB5-4407-A0E3-5D55CFB99DBE
main subject	Saccharomyces cerevisiae Karyopherin alpha YNL189W Karyopherin beta YLR347C Nucleoporin NUP2 YLR335W
PubMed ID	wds:Q28909274-D972611A-C817-46C2-B0C3-82AAC6210F18
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12065587
PubMed ID	12065587
published in	wds:Q28909274-76D086D7-A980-4FC6-910E-CA635593B452
published in	Journal of Biological Chemistry
issue	wds:Q28909274-EDCB5F5C-1EB1-4C33-B063-41E73DE7B569
volume	wds:Q28909274-C64797C8-750A-4E71-84EB-DFFBCFF43F8E
issue	36
volume	277
DOI	wds:Q28909274-AB51931D-AE11-40E5-B4B1-1219EDBE5C55
DOI	http://dx.doi.org/10.1074/JBC.M203499200
DOI	10.1074/JBC.M203499200
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28909274
is cites work of	Charge as a selection criterion for translocation through the nuclear pore complex Towards reconciling structure and function in the nuclear pore complex Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins Functionalization of a nanopore: the nuclear pore complex paradigm Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport Complex formation among the RNA export proteins Nup98, Rae1/Gle2, and TAP Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import Nuclear transport is becoming crystal clear Prokaryotic ubiquitin-like protein pup is intrinsically disordered 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 nuclear pore complex: nucleocytoplasmic transport and beyond Characterization of molecular recognition features, MoRFs, and their binding partners Deciphering networks of protein interactions at the nuclear pore complex Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transport Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology Molecular mechanism of the nuclear protein import cycle Mutagenesis reveals a specific role for Cox17p in copper transport to cytochrome oxidase. Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. Systematic deletion and mitotic localization of the nuclear pore complex proteins of Aspergillus nidulans. Probing a structural model of the nuclear pore complex channel through molecular dynamics A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies Rapid evolution exposes the boundaries of domain structure and function in natively unfolded FG nucleoporins Nucleocytoplasmic transport: navigating the channel From the trap to the basket: getting to the bottom of the nuclear pore complex The selective permeability barrier in the nuclear pore complex Disordered proteinaceous machines Mycobacterium tuberculosis copper-regulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayer Compartmentalization and Functionality of Nuclear Disorder: Intrinsic Disorder and Protein-Protein Interactions in Intra-Nuclear Compartments Structural flexibility of multifunctional HABP1 may be important for regulating its binding to different ligands Intrinsically disordered proteins in the nucleus of human cells. Biophysical characterization of the enzyme I of the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system Assembly and function of the photosystem II manganese stabilizing protein: lessons from its natively unfolded behavior. Spectroscopic approaches to the conformation of tau protein in solution and in paired helical filaments Nup2 requires a highly divergent partner, NupA, to fulfill functions at nuclear pore complexes and the mitotic chromatin region Hug1 is an intrinsically disordered protein that inhibits ribonucleotide reductase activity by directly binding Rnr2 subunit. The inactivating factor of glutamine synthetase, IF7, is a "natively unfolded" protein

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