Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability - Wikidata - awgldk - TriplyDB

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

http://www.wikidata.org/entity/Q22066164

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Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex Nuclear distribution and chromatin association of DNA polymerase alpha-primase is affected by TEV protease cleavage of Cdc23 (Mcm10) in fission yeast.Brownian dynamics simulation of nucleocytoplasmic transport: a coarse-grained model for the functional state of the nuclear pore complex Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element.Structure, Dynamics, Evolution, and Function of a Major Scaffold Component in the Nuclear Pore Complex The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly Zinc and the Msc2 zinc transporter protein are required for endoplasmic reticulum function.The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function Minimal nuclear pore complexes define FG repeat domains essential for transport.A versatile interaction platform on the Mex67-Mtr2 receptor creates an overlap between mRNA and ribosome export.Two structurally distinct domains of the nucleoporin Nup170 cooperate to tether a subset of nucleoporins to nuclear pores.Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex.Novel role for a Saccharomyces cerevisiae nucleoporin, Nup170p, in chromosome segregation.A novel mechanism for SUMO system control: regulated Ulp1 nucleolar sequestration Facilitated transport and diffusion take distinct spatial routes through the nuclear pore complex.Nuclear export modulates the cytoplasmic Sir2 homologue Hst2.Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating ER membrane-bending proteins are necessary for de novo nuclear pore formation Nuclear pore complex function in Saccharomyces cerevisiae is influenced by glycosylation of the transmembrane nucleoporin Pom152p.A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex.A role for the nucleoporin Nup170p in chromatin structure and gene silencing.The integral membrane protein Pom34p functionally links nucleoporin subcomplexes The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint 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.The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex.Regulation of tRNA bidirectional nuclear-cytoplasmic trafficking in Saccharomyces cerevisiae.The nuclear pore complex and nuclear transport Nuclear import time and transport efficiency depend on importin beta concentration.Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit of nuclear pore complex size exclusion in vivo.Global motions of the nuclear pore complex: insights from elastic network models.The nuclear pore complex as a transport machine.Nucleoporins NPP-1, NPP-3, NPP-4, NPP-11 and NPP-13 are required for proper spindle orientation in C. elegans Regulated inactivation of the spindle assembly checkpoint without functional mitotic spindles.Altering nuclear pore complex function impacts longevity and mitochondrial function in S. cerevisiae New ways to skin a kap: mechanisms for controlling nuclear transport.Simple kinetic relationships and nonspecific competition govern nuclear import rates in vivo.Caspases disrupt the nuclear-cytoplasmic barrier.Cellular dynamics of small RNAs.Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility.Nuclear pore complexes: guardians of the nuclear genome.

P2860

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P2860

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

http://www.wikidata.org/entity/Q22066164

description

2000 nî lūn-bûn

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2000 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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name

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

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Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

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Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

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Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

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type

label

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

@ast

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

@en

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

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Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

@nl

altLabel

Yeast nucleoporins involved in passive nuclear envelope permeability

@en

prefLabel

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

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Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

@en

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

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Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

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P1433

Journal of Cell Biology

P1476

Yeast Nucleoporins Involved in Passive Nuclear Envelope Permeability

@en

P2093

D S Goldfarb

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

N Mosammaparast

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

N Shulga

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

R Wozniak

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

P2860

Functional analysis of Tpr: identification of nuclear pore complex association and nuclear localization domains and a role in mRNA export

Nuclear envelope permeability

The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex

Permeability of single nuclear pores.

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

A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export

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

A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores.

POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope.

Nuclear export of the small ribosomal subunit requires the ran-GTPase cycle and certain nucleoporins.

P304

1027-1038

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scholarly article

P356

10.1083/JCB.149.5.1027

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P407

P433

5

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P478

149

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P577

2000-05-29T00:00:00Z

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277542748

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10831607

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P932

2174828

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