Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
about
Functional analysis of Tpr: identification of nuclear pore complex association and nuclear localization domains and a role in mRNA exportA visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane proteinExportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins.Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein exportIdentification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62Sequence and characterization of cytoplasmic nuclear protein import factor p97Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complexThe human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasmResponsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentrationMonoclonal antibodies to NTF2 inhibit nuclear protein import by preventing nuclear translocation of the GTPase RanIdentification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assayNup50, a nucleoplasmically oriented nucleoporin with a role in nuclear protein exportIdentification of an NTF2-related factor that binds Ran-GTP and regulates nuclear protein export.Vaccinia virus DNA replication occurs in endoplasmic reticulum-enclosed cytoplasmic mini-nucleiA major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tailNuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathwayA complex of nuclear pore proteins required for pore functionVaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetryRanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complexIsolation of the yeast nuclear pore complexGradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear importMolecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteinsMacromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: binding of nucleoporin p54 to the rod domain of p62An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like regionNXT1 is necessary for the terminal step of Crm1-mediated nuclear export.Primary sequence and heterologous expression of nuclear pore glycoprotein p62Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear laminaNup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complexA role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear exportTransport of incoming influenza virus nucleocapsids into the nucleusPleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85pExtragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae.A new family of yeast nuclear pore complex proteinsFunctional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p.A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexesThe product of the Saccharomyces cerevisiae RSS1 gene, identified as a high-copy suppressor of the rat7-1 temperature-sensitive allele of the RAT7/NUP159 nucleoporin, is required for efficient mRNA export.nup1 mutants exhibit pleiotropic defects in nuclear pore complex function.C-terminal truncations of the yeast nucleoporin Nup145p produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure.Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96Nuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120 gene.
P2860
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P2860
Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
@ast
Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
@en
type
label
Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
@ast
Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
@en
prefLabel
Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
@ast
Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
@en
P2093
P2860
P356
P1476
Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
@en
P2093
P2860
P304
P356
10.1083/JCB.104.5.1143
P407
P577
1987-05-01T00:00:00Z