Identification of a major polypeptide of the nuclear pore complex
about
A visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane proteinHerpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathwaysIdentification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filamentsStructural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complexA major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tailAn endoplasmic reticulum-specific cyclophilinThe single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelopeA complex of nuclear pore proteins required for pore functionVaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetryIsolation of the yeast nuclear pore complexSignals and structural features involved in integral membrane protein targeting to the inner nuclear membraneThe amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signalAn integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like regionIntegral membrane proteins specific to the inner nuclear membrane and associated with the nuclear laminaAutoantibodies from patients with primary biliary cirrhosis recognize a restricted region within the cytoplasmic tail of nuclear pore membrane glycoprotein Gp210Identification and characterization of autoantibodies against the nuclear envelope lamin B receptor from patients with primary biliary cirrhosisNDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore complexesIntegral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosisDespite WT1 binding sites in the promoter region of human and mouse nucleoporin glycoprotein 210, WT1 does not influence expression of GP210The nuclear envelope: an intriguing focal point for neurogenetic diseaseExpression of constitutively active CDK1 stabilizes APC-Cdh1 substrates and potentiates premature spindle assembly and checkpoint function in G1 cellsPOM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope.Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae.Nup120p: a yeast nucleoporin required for NPC distribution and mRNA transportA novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly.Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p.Topology and functional domains of the yeast pore membrane protein Pom152p.Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporinsPurification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function.Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complexInner/Outer nuclear membrane fusion in nuclear pore assembly: biochemical demonstration and molecular analysisBiochemical characterization of nuclear pore complex protein gp210 oligomersNup155 is a novel nuclear pore complex protein that contains neither repetitive sequence motifs nor reacts with WGAA temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic trafficNuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factorsDissociation of newly synthesized Sendai viral proteins from the cytoplasmic surface of isolated plasma membranes of infected cells.The three fungal transmembrane nuclear pore complex proteins of Aspergillus nidulans are dispensable in the presence of an intact An-Nup84-120 complex.High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores.Function and assembly of nuclear pore complex proteins.
P2860
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P2860
Identification of a major polypeptide of the nuclear pore complex
description
1982 nî lūn-bûn
@nan
1982年の論文
@ja
1982年論文
@yue
1982年論文
@zh-hant
1982年論文
@zh-hk
1982年論文
@zh-mo
1982年論文
@zh-tw
1982年论文
@wuu
1982年论文
@zh
1982年论文
@zh-cn
name
Identification of a major polypeptide of the nuclear pore complex
@ast
Identification of a major polypeptide of the nuclear pore complex
@en
type
label
Identification of a major polypeptide of the nuclear pore complex
@ast
Identification of a major polypeptide of the nuclear pore complex
@en
prefLabel
Identification of a major polypeptide of the nuclear pore complex
@ast
Identification of a major polypeptide of the nuclear pore complex
@en
P2093
P2860
P356
P1476
Identification of a major polypeptide of the nuclear pore complex
@en
P2093
C Kondor-Koch
Y Ottaviano
P2860
P304
P356
10.1083/JCB.95.3.826
P407
P577
1982-12-01T00:00:00Z