Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells - Wikidata - awgldk - TriplyDB

Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells

Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells

http://www.wikidata.org/entity/Q24654097

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An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export.The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket The nuclear pore complex protein ALADIN is mislocalized in triple A syndrome Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins The nuclear pore complex.Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes Sec13 shuttles between the nucleus and the cytoplasm and stably interacts with Nup96 at the nuclear pore complex An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export.The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly HIV-1 capsid: the multifaceted key player in HIV-1 infection Breaching the nuclear envelope in development and disease Dynamics and diverse functions of nuclear pore complex proteins Building a nuclear envelope at the end of mitosis: coordinating membrane reorganization, nuclear pore complex assembly, and chromatin de-condensation Nuclear pore complex protein mediated nuclear localization of dicer protein in human cells Parvoviruses cause nuclear envelope breakdown by activating key enzymes of mitosis The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic interactome including Esc1p and the proteasome.The karyopherin Kap95 regulates nuclear pore complex assembly into intact nuclear envelopes in vivo.A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to cellular structures.Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells Translational mobility of the type 3 inositol 1,4,5-trisphosphate receptor Ca2+ release channel in endoplasmic reticulum membrane Nup98 is a mobile nucleoporin with transcription-dependent dynamics.The functionally conserved nucleoporins Nup124p from fission yeast and the human Nup153 mediate nuclear import and activity of the Tf1 retrotransposon and HIV-1 Vpr.Cdk1 and okadaic acid-sensitive phosphatases control assembly of nuclear pore complexes in Drosophila embryos.Nuclear import time and transport efficiency depend on importin beta concentration.Abnormal expression of TIP30 and arrested nucleocytoplasmic transport within oligodendrocyte precursor cells in multiple sclerosis The nucleoporin Nup153 has separable roles in both early mitotic progression and the resolution of mitosis Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshots.Localization of Pom121 to the inner nuclear membrane is required for an early step of interphase nuclear pore complex assembly Single molecule studies of nucleocytoplasmic transport Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor.Motor-driven motility of fungal nuclear pores organizes chromosomes and fosters nucleocytoplasmic transport.

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Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells

http://www.wikidata.org/entity/Q24654097

description

2001 nî lūn-bûn

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2001 թվականի հուլիսին հրատարակված գիտական հոդված

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2001年の論文

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Journal of Cell Biology

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Nuclear pore complexes form im ...... rnover in live mammalian cells

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G Imreh

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J Beaudouin

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L Hartnell

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N Daigle

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P2860

Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells

Nup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domain

In vitro posttranslational modification of lamin B cloned from a human T-cell line

The nucleoporin nup153 plays a critical role in multiple types of nuclear export

The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope

An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region

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

Nuclear pore complexes in the organization of silent telomeric chromatin.

Review: nuclear lamins--structural proteins with fundamental functions

Sequential recruitment of NPC proteins to the nuclear periphery at the end of mitosis

P304

71-84

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scholarly article

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4627665

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10.1083/JCB.200101089

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1

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154

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Jennifer Lippincott-Schwartz

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2001-07-09T00:00:00Z

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11892607

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11448991

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2196857

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