RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex
about
RanBP2 modulates Cox11 and hexokinase I activities and haploinsufficiency of RanBP2 causes deficits in glucose metabolismIn vitro nuclear interactome of the HIV-1 Tat proteinTpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein exportNup153 is an M9-containing mobile nucleoporin with a novel Ran-binding domainNup50, a nucleoplasmically oriented nucleoporin with a role in nuclear protein exportGradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear importNXT1 is necessary for the terminal step of Crm1-mediated nuclear export.Nup358 integrates nuclear envelope breakdown with kinetochore assemblyThe yeast nuclear pore complex: composition, architecture, and transport mechanismA role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear exportMajor binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein TprStructure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transportStructural basis of high-affinity nuclear localization signal interactions with importin-αMolecular basis for the functional interaction of dynein light chain with the nuclear-pore complex.Importin-beta is a GDP-to-GTP exchange factor of Ran: implications for the mechanism of nuclear importProteomic analysis of nucleoporin interacting proteins.Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex.The nucleoporin Nup98 is a site for GDP/GTP exchange on ran and termination of karyopherin beta 2-mediated nuclear importPhosphorylation of the nuclear transport machinery down-regulates nuclear protein import in vitroGTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358Structural Details of Ufd1 Binding to p97 and Their Functional Implications in ER-Associated DegradationThe RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependent nuclear export complexesMolecular Characterization and Functional Analysis of Annulate Lamellae Pore Complexes in Nuclear Transport in Mammalian Cells.Neuroprotection resulting from insufficiency of RANBP2 is associated with the modulation of protein and lipid homeostasis of functionally diverse but linked pathways in response to oxidative stress.The interaction of Epac1 and Ran promotes Rap1 activation at the nuclear envelope.Herpes simplex virus replication: roles of viral proteins and nucleoporins in capsid-nucleus attachmentSimulations of nuclear pore transport yield mechanistic insights and quantitative predictionsAnalysis of the antibody repertoire of astrocytoma patients against antigens expressed by gliomas.Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358.Loss of Ranbp2 in motoneurons causes disruption of nucleocytoplasmic and chemokine signaling, proteostasis of hnRNPH3 and Mmp28, and development of amyotrophic lateral sclerosis-like syndromesSelective impairment of a subset of Ran-GTP-binding domains of ran-binding protein 2 (Ranbp2) suffices to recapitulate the degeneration of the retinal pigment epithelium (RPE) triggered by Ranbp2 ablation.The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis.Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold.The nucleoporin RanBP2 tethers the cAMP effector Epac1 and inhibits its catalytic activity.Nucleocytoplasmic transport: navigating the channel.Importin 7 and Nup358 promote nuclear import of the protein component of human telomerase.Ran-dependent docking of importin-beta to RanBP2/Nup358 filaments is essential for protein import and cell viabilityThe nuclear pore complex: nucleocytoplasmic transport and beyond.Targeting the cyclophilin domain of Ran-binding protein 2 (Ranbp2) with novel small molecules to control the proteostasis of STAT3, hnRNPA2B1 and M-opsin.Ranbp2 haploinsufficiency mediates distinct cellular and biochemical phenotypes in brain and retinal dopaminergic and glia cells elicited by the Parkinsonian neurotoxin, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP).
P2860
Q21145250-6C612A2B-024F-41A2-B958-8775C2A07820Q21245051-B9680C5E-D853-4D3C-A673-ED1F291DF21CQ24292285-5841ED70-27A9-4AA0-9F18-224D0A56F2D4Q24534076-60A575F7-71BD-4BE5-8F96-FE93C6F831B8Q24552769-A719F88D-71C8-4C71-AE74-18F9D18FBF18Q24652021-E1F7E074-59B0-44E1-8173-EBAA80E211E5Q24674855-F4B73B9F-3ED5-4196-98DD-5B96653999FFQ24675421-DE09F00A-CBEA-49A3-A1FC-74314FBBF0D1Q24680784-0B343F94-C5C6-4951-B593-01B5213F0F82Q24682010-39E05012-6A9A-4B48-BCA4-AA09867876DCQ24683280-F12522E6-5F72-4C43-8DD8-903FFDB45608Q27617536-E067FD5F-A5D1-4C8C-AC96-53EF553EF7A8Q27676772-8D97A51D-68A1-426D-BCB6-2AC6235EC99FQ27931773-20EBA7F6-D727-49FF-A28D-58E5CFC72933Q27934302-AF8B59E1-C24F-486D-968A-1C17FE234712Q27934684-220BB730-914A-4E2F-A91C-DD3A95513C6CQ27939615-50C2DA31-F54A-4D22-8929-B474F27DEBD8Q28139684-F6FF8CB1-E114-45D3-9136-7E3A0EA57EF3Q28140841-86235145-25BC-42D8-A84E-DE5B9EEDFD07Q28143781-332B22D9-47F0-49F0-8CAF-8E2F492025BEQ28554390-5D438A28-8728-4D3E-B563-04E1CFE5810CQ28602843-8CE70C7C-0833-4ADE-AC43-D3D1C943BD60Q30362076-C863D0D8-3DDE-4628-AB02-29F699F5E5C1Q30430840-2F08044F-77C0-4EBD-A99A-070DAD52C1F0Q30433366-95B8FA63-7D1D-4891-AE7A-BD15E4A47E96Q30439071-AF2DEDB4-CA56-41D4-B196-9DD098C37A42Q30503289-D036300A-A26B-4033-9198-7977E36B19C3Q30816567-74F02931-3FFF-4D12-B947-9CF76AEAE1AAQ33206242-3E381AEC-20FC-4531-BCD1-E3DAF944E725Q33746245-8DCC5F50-0D7F-427A-8344-8E077CFBA45BQ34396844-F951E0B5-909C-4501-A380-A237720B09E2Q34696926-960CB2A8-6C59-45FE-A1C1-E55F61B59E1CQ35042858-3859C08E-ECA8-4EB4-829B-278762918166Q35047496-A8610192-8773-4B68-A45D-AE781A7CFF36Q35092062-38221EFC-C865-464E-892A-51C192FCF7BEQ35106398-678EC907-0F35-42EE-8D4A-2B266A7BA5C8Q35178128-64B295BD-88AE-4732-8D9C-69C825B4FC64Q35564601-A87C3C85-9B24-480C-976C-E1DD9718E821Q36016095-0B34026F-EAC1-488D-BB91-4F81A1A9DF50Q36243860-B914DE69-D51E-489C-9745-1D8E11833F82
P2860
RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex
description
1997 nî lūn-bûn
@nan
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
RanGTP targets p97 to RanBP2, ...... ry of the nuclear pore complex
@ast
RanGTP targets p97 to RanBP2, ...... ry of the nuclear pore complex
@en
RanGTP targets p97 to RanBP2, ...... ry of the nuclear pore complex
@nl
type
label
RanGTP targets p97 to RanBP2, ...... ry of the nuclear pore complex
@ast
RanGTP targets p97 to RanBP2, ...... ry of the nuclear pore complex
@en
RanGTP targets p97 to RanBP2, ...... ry of the nuclear pore complex
@nl
prefLabel
RanGTP targets p97 to RanBP2, ...... ry of the nuclear pore complex
@ast
RanGTP targets p97 to RanBP2, ...... ry of the nuclear pore complex
@en
RanGTP targets p97 to RanBP2, ...... ry of the nuclear pore complex
@nl
P2093
P2860
P3181
P356
P1476
RanGTP targets p97 to RanBP2, ...... ry of the nuclear pore complex
@en
P2093
P2860
P304
P3181
P356
10.1091/MBC.8.12.2379
P407
P577
1997-12-01T00:00:00Z