Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins - Wikidata - awgldk - TriplyDB

Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins

Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins

http://www.wikidata.org/entity/Q24671748

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Functional analysis of Tpr: identification of nuclear pore complex association and nuclear localization domains and a role in mRNA export A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96 IkappaBalpha and IkappaBalpha /NF-kappa B complexes are retained in the cytoplasm through interaction with a novel partner, RasGAP SH3-binding protein 2 Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly Viral protein R regulates nuclear import of the HIV-1 pre-integration complex Nup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domain Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes Nup50, a nucleoplasmically oriented nucleoporin with a role in nuclear protein export Identification of an NTF2-related factor that binds Ran-GTP and regulates nuclear protein export.Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complex A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export Structure Determination of the Nuclear Pore Complex with Three-Dimensional Cryo electron Microscopy NMR structure of the (1-51) N-terminal domain of the HIV-1 regulatory protein Vpr Molecular Architecture of the Transport Channel of the Nuclear Pore Complex Ring cycle for dilating and constricting the nuclear pore The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution.Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p.Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p.Molecular architecture of the yeast nuclear pore complex: localization of Nsp1p subcomplexes The nucleoporin Nup98 is a site for GDP/GTP exchange on ran and termination of karyopherin beta 2-mediated nuclear import Phosphorylation of the nuclear transport machinery down-regulates nuclear protein import in vitro GTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358 Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex Protein homeostasis: live long, won't prosper Different binding domains for Ran-GTP and Ran-GDP/RanBP1 on nuclear import factor p97 RNA export mediated by tap involves NXT1-dependent interactions with the nuclear pore complex Nucleoporin Nup62 maintains centrosome homeostasis Mutations in tap uncouple RNA export activity from translocation through the nuclear pore complex.Nuclear hourglass technique: an approach that detects electrically open nuclear pores in Xenopus laevis oocyte The importin beta binding domain modulates the avidity of importin beta for the nuclear pore complex Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p.The importin β binding domain as a master regulator of nucleocytoplasmic transport Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.Nuclear distributions of NUP62 and NUP214 suggest architectural diversity and spatial patterning among nuclear pore complexes.Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus.Nucleoporins NPP-1, NPP-3, NPP-4, NPP-11 and NPP-13 are required for proper spindle orientation in C. elegans Developmental genetics of the essential Drosophila nucleoporin nup154: allelic differences due to an outward-directed promoter in the P-element 3' end.

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P2860

Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins

http://www.wikidata.org/entity/Q24671748

description

1996 nî lūn-bûn

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1996 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի օգոստոսին հրատարակված գիտական հոդված

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1996年の論文

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年學術文章

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name

Molecular and functional chara ...... ear pore complex glycoproteins

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Molecular and functional chara ...... ear pore complex glycoproteins

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Molecular and functional chara ...... ear pore complex glycoproteins

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Molecular and functional chara ...... ear pore complex glycoproteins

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Molecular and functional chara ...... ear pore complex glycoproteins

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Molecular and functional chara ...... ear pore complex glycoproteins

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Molecular and functional chara ...... ear pore complex glycoproteins

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Molecular and functional chara ...... ear pore complex glycoproteins

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Journal of Cell Biology

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Molecular and functional chara ...... ear pore complex glycoproteins

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L Gerace

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T Guan

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P2860

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

Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62

Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences

Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization

Sequence and characterization of cytoplasmic nuclear protein import factor p97

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

Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope

The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm

Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins

Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes

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scholarly article

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10.1083/JCB.134.3.589

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3

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134

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2120945

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