In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
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sameAs
Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathwaysInteraction between the shuttling mRNA export factor Gle1 and the nucleoporin hCG1: a conserved mechanism in the export of Hsp70 mRNA.ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway.Karyopherin beta 2B participates in mRNA export from the nucleus.Mutations in tap uncouple RNA export activity from translocation through the nuclear pore complex.NXF2 is involved in cytoplasmic mRNA dynamics through interactions with motor proteins.Complex formation between Tap and p15 affects binding to FG-repeat nucleoporins and nucleocytoplasmic shuttling.Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore.Formation of a Tap/NXF1 homotypic complex is mediated through the amino-terminal domain of Tap and enhances interaction with nucleoporins.Characterizing the normal proteome of human ciliary body.Nanomaterials in complex biological systems: insights from Raman spectroscopy.Sequence preference in RNA recognition by the nucleoporin Nup153.SDE5, a putative RNA export protein, participates in plant innate immunity through a flagellin-dependent signaling pathway in ArabidopsisCharacterization of a novel transferable CRM-1-independent nuclear export signal in a herpesvirus tegument protein that shuttles between the nucleus and cytoplasm.Nuclear import of adenovirus DNA involves direct interaction of hexon with an N-terminal domain of the nucleoporin Nup214.In vitro analysis of nuclear mRNA export using molecular beacons for target detection.RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the nuclear pore complex and functions in nuclear mRNA export.The evolutionarily conserved Kaposi's sarcoma-associated herpesvirus ORF57 protein interacts with REF protein and acts as an RNA export factor.Viral regulation of mRNA export.
P2860
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P2860
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
@ast
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
@en
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
@nl
type
label
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
@ast
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
@en
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
@nl
prefLabel
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
@ast
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
@en
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
@nl
P2860
P356
P1476
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of Tap
@en
P2093
P2860
P304
P356
10.1074/JBC.M103916200
P407
P577
2001-11-09T00:00:00Z