Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded - Wikidata - awgldk - TriplyDB

Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded

Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded

http://www.wikidata.org/entity/Q24554044

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Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket Facilitated aggregation of FG nucleoporins under molecular crowding conditions Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion Flexible peptides and cytoplasmic gels.Components of coated vesicles and nuclear pore complexes share a common molecular architecture Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins.Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Role of molecular charge in nucleocytoplasmic transport Assembly of Nsp1 nucleoporins provides insight into nuclear pore complex gating Rapid Brownian Motion Primes Ultrafast Reconstruction of Intrinsically Disordered Phe-Gly Repeats Inside the Nuclear Pore Complex.Brownian dynamics simulation of nucleocytoplasmic transport: a coarse-grained model for the functional state of the nuclear pore complex Nucleoporin's Like Charge Regions Are Major Regulators of FG Coverage and Dynamics Inside the Nuclear Pore Complex Crystallographic and Biochemical Analysis of the Ran-binding Zinc Finger Domain Cryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to the 60S ribosomal subunit Artificial nanopores that mimic the transport selectivity of the nuclear pore complex.Minimal nuclear pore complexes define FG repeat domains essential for transport.Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex.Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex.The yeast integral membrane protein Apq12 potentially links membrane dynamics to assembly of nuclear pore complexes Facilitated transport and diffusion take distinct spatial routes through the nuclear pore complex.Arx1 is a nuclear export receptor for the 60S ribosomal subunit in yeast.FG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties.A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex.Cdk phosphorylation of a nucleoporin controls localization of active genes through the cell cycle.Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium.Deciphering networks of protein interactions at the nuclear pore complex Nup214-Nup88 nucleoporin subcomplex is required for CRM1-mediated 60 S preribosomal nuclear export Cooperative Interactions between Different Classes of Disordered Proteins Play a Functional Role in the Nuclear Pore Complex of Baker's Yeast Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin beta Disordered proteinaceous machines The nuclear pore complex and nuclear transport A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies.Reversibility in nucleocytoplasmic transport Nuclear import time and transport efficiency depend on importin beta concentration.Single-molecule measurements of importin alpha/cargo complex dissociation at the nuclear pore.Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study.Transport-related structures and processes of the nuclear pore complex studied through molecular dynamics Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshots.A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins.Single molecule studies of nucleocytoplasmic transport

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P2860

Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded

http://www.wikidata.org/entity/Q24554044

description

2003 nî lūn-bûn

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2003 թուականի Մարտին հրատարակուած գիտական յօդուած

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2003 թվականի մարտին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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name

Disorder in the nuclear pore c ...... eoporins are natively unfolded

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Disorder in the nuclear pore c ...... eoporins are natively unfolded

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Disorder in the nuclear pore c ...... eoporins are natively unfolded

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type

label

Disorder in the nuclear pore c ...... eoporins are natively unfolded

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Disorder in the nuclear pore c ...... eoporins are natively unfolded

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Disorder in the nuclear pore c ...... eoporins are natively unfolded

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prefLabel

Disorder in the nuclear pore c ...... eoporins are natively unfolded

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Disorder in the nuclear pore c ...... eoporins are natively unfolded

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Disorder in the nuclear pore c ...... eoporins are natively unfolded

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PNAS.0437902100

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Proceedings of the National Academy of Sciences of the United States of America

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Disorder in the nuclear pore c ...... eoporins are natively unfolded

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P2093

Anthony L Fink

http://www.w3.org/2001/XMLSchema#string

Daniel P Denning

http://www.w3.org/2001/XMLSchema#string

Michael Rexach

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Samir S Patel

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Vladimir Uversky

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P2860

T RANSPORT B ETWEEN THE C ELL N UCLEUS AND THE C YTOPLASM

Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex

The yeast nuclear pore complex: composition, architecture, and transport mechanism

Structure of importin-beta bound to the IBB domain of importin-alpha

Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking

Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha

Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin alpha.

The identification of protein-protein interactions of the nuclear pore complex of Saccharomyces cerevisiae using high throughput matrix-assisted laser desorption ionization time-of-flight tandem mass spectrometry.

A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export.

Proteomic analysis of nucleoporin interacting proteins.

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1480371

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10.1073/PNAS.0437902100

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100

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10884041

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12604785

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151361

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