A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
about
Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assemblyThe human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88Npp106p, a Schizosaccharomyces pombe nucleoporin similar to Saccharomyces cerevisiae Nic96p, functionally interacts with Rae1p in mRNA exportThe yeast nuclear pore complex: composition, architecture, and transport mechanismNup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complexArchitectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element.Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complexMolecular Basis for the Anchoring of Proto-Oncoprotein Nup98 to the Cytoplasmic Face of the Nuclear Pore ComplexPleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85pBinding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export.Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex.The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution.Nuclear export of the small ribosomal subunit requires the ran-GTPase cycle and certain nucleoporins.Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export.Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p.A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly.Molecular architecture of the yeast nuclear pore complex: localization of Nsp1p subcomplexesThe yeast nucleoporin rip1p contributes to multiple export pathways with no essential role for its FG-repeat region.Partners of Rpb8p, a small subunit shared by yeast RNA polymerases I, II and IIIC-terminal truncations of the yeast nucleoporin Nup145p produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure.Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNAUltrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex.Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase Acc1p.Proteins connecting the nuclear pore complex with the nuclear interiorNuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120 gene.Systematic Protein-Protein Interaction Analysis Reveals Intersubcomplex Contacts in the Nuclear Pore Complex.Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p.The integral membrane protein Pom34p functionally links nucleoporin subcomplexesNuclear pore proteins are involved in the biogenesis of functional tRNATwo yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex.The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function.Nup214-Nup88 nucleoporin subcomplex is required for CRM1-mediated 60 S preribosomal nuclear exportThe transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1Nuclear RNA export in yeast.Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p.Multiple mechanisms of suppression circumvent transcription defects in an RNA polymerase mutant.In situ analysis of spatial relationships between proteins of the nuclear pore complexRegulation of mRNA trafficking by nuclear pore complexes.Pom121 links two essential subcomplexes of the nuclear pore complex core to the membrane.Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold.
P2860
Q24322104-8D61E47B-EA58-4CF8-9838-8997C28E3854Q24322912-C2E82C78-5244-4E63-9947-8E863EF729C4Q24644057-77719143-67C4-44F0-972E-D56C4F0B7129Q24680784-52B97D97-CD2F-4486-9B24-792F38C0AD6EQ24680805-41B3CCA4-163A-4249-8E12-927B894BEBADQ27656977-4AB3DA11-BABE-4A19-B8CA-4DC0EB69820EQ27674220-897EB957-A0DC-44F3-B78F-DE59AC3069AAQ27678343-32D9CDC0-E296-4450-9099-8520DC7852C1Q27929971-12E9D8D2-CDDD-4E21-8892-26E112043A78Q27931219-9FD05CEE-F62A-4F61-A5FE-FFD1D288C0B7Q27931773-0BDAB33C-9E0E-4A7B-A9C3-E2714F080B94Q27931878-0EB0265A-2C61-4581-994F-6334A6E2AE02Q27931933-4B05C7B7-5AA4-40EF-8057-5DDE2E2FEC42Q27932060-C1E463C8-1C18-48AE-84E4-F3F05D20E6E1Q27933063-934A9BAF-A1C1-4766-B38E-FAD3F483464AQ27933301-762BBD45-72F0-4B83-B1D5-212FBC58A66EQ27933725-F651C730-2A79-4E2A-8B66-29D6DA77B2FDQ27934181-BDCE1863-C346-47CB-A854-BE4CBB5D6581Q27935755-3D73531A-AFD6-4E63-88D2-8C6423779D59Q27936268-08A24F79-AA9C-4691-B9AF-B4D923D4743EQ27937371-1BE643F7-6529-44EB-A8CE-A300DBF65B5BQ27937486-D44801CA-6AAB-4ECE-8174-B24ABF6DDDB0Q27937534-5CE08328-0AA7-4E59-895D-966CD9A213A9Q27937540-D6B2FF1A-8321-4B66-9C66-7D69294CD70BQ27937777-9CBF399F-B77E-48D1-AC14-7D0F06228FC2Q27937803-BF95E5F3-1331-41AC-BEDD-2114FBF27CD6Q27938007-F4AA9154-515A-4907-836B-3719A67750A7Q27938646-2E593D8F-49B7-4AE0-85FB-2201DD20D74CQ27939266-76F30FBC-9F9B-4CC4-BB11-E9E478CC39FFQ27939615-22CB5EF0-328B-4759-AB58-DC5E9754A0B5Q27939968-F786AB27-05F5-46AA-B5CD-A9E7AD3DCFB7Q28238313-E8766CC3-E1BA-4CFC-8937-2F5A64BE5709Q30555736-1AEBD0F9-F223-42E7-9992-269F6501FE9AQ33665629-5F052736-C12E-40BB-AB58-9A15A744CF4DQ33964950-DC65BBF7-6C46-4C1F-A9E3-9722F6D4F24FQ33966226-93B20A53-A0D5-4D34-9E16-AAB86F976A3FQ34179572-CE8217E6-37A2-4496-A31C-53457F63CB4FQ34347710-8B5B5EF5-49D0-4E18-901E-63284A6E2149Q34412386-F70FD590-25CD-4017-B102-44320088996EQ35042858-C02288B2-2147-4E15-99D7-0EAA80EE3AF4
P2860
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
description
1995 nî lūn-bûn
@nan
1995 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
@ast
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
@en
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
@nl
type
label
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
@ast
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
@en
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
@nl
prefLabel
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
@ast
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
@en
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
@nl
P2093
P2860
P356
P1476
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
@en
P2093
P2860
P304
P356
10.1083/JCB.130.6.1263
P407
P577
1995-09-01T00:00:00Z