Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
about
cDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antiseraIsolation of a cDNA clone of the 14-kDa subunit of the signal recognition particle by cross-hybridization of differently primed polymerase chain reactionsIdentification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filamentsVertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complexA major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tailThe 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 functionIsolation of the yeast nuclear pore complexGERp95, a membrane-associated protein that belongs to a family of proteins involved in stem cell differentiationMacromolecular 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 regionAutoantibodies 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 cirrhosisIntegral 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 GP210POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope.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.The 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.Topology and functional domains of the yeast pore membrane protein Pom152p.Nuclear pore complex function in Saccharomyces cerevisiae is influenced by glycosylation of the transmembrane nucleoporin Pom152p.Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96The integral membrane protein Pom34p functionally links nucleoporin subcomplexesThe integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function.Inner/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 trafficPrimary biliary cirrhosis and the nuclear pore complex.Function and assembly of nuclear pore complex proteins.Meta-analysis assessment of GP210 and SP100 for the diagnosis of primary biliary cirrhosis.The lamin B receptor of the nuclear envelope inner membrane: a polytopic protein with eight potential transmembrane domainsThe 210-kD nuclear envelope polypeptide recognized by human autoantibodies in primary biliary cirrhosis is the major glycoprotein of the nuclear pore.Dynamic properties of nuclear pore complex proteins in gp210 deficient cells.Pom121 links two essential subcomplexes of the nuclear pore complex core to the membrane.Caspases target only two architectural components within the core structure of the nuclear pore complex.The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasisYeast nuclear envelope proteins cross react with an antibody against mammalian pore complex proteins.Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy.
P2860
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P2860
Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
@ast
Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
@en
type
label
Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
@ast
Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
@en
prefLabel
Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
@ast
Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
@en
P2860
P356
P1476
Primary structure analysis of an integral membrane glycoprotein of the nuclear pore.
@en
P2093
Wozniak RW
P2860
P304
P356
10.1083/JCB.108.6.2083
P407
P577
1989-06-01T00:00:00Z