about
GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28The ubiquitin ligase HACE1 regulates Golgi membrane dynamics during the cell cycleIdentification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arraysHuman Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathwayAn arginine/lysine-rich motif is crucial for VCP/p97-mediated modulation of ataxin-3 fibrillogenesis.Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chainsUBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnoverThe tissue-specific Rep8/UBXD6 tethers p97 to the endoplasmic reticulum membrane for degradation of misfolded proteinsDirect binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4.SVIP is a novel VCP/p97-interacting protein whose expression causes cell vacuolation.A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathwaysThe nuclear envelopeVCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivoThe localization and phosphorylation of p47 are important for Golgi disassembly-assembly during the cell cycleTwo dimensional VOPBA reveals laminin receptor (LAMR1) interaction with dengue virus serotypes 1, 2 and 3Targeting p97 to Disrupt Protein Homeostasis in CancerMechanisms and Regulation of the Mitotic Inheritance of the Golgi ComplexFrom neurodevelopment to neurodegeneration: the interaction of neurofibromin and valosin-containing protein/p97 in regulation of dendritic spine formationCrystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion proteinCrystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP proteaseCrystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpAStructure and Ubiquitin Interactions of the Conserved Zinc Finger Domain of Npl4Detailed structural insights into the p97-Npl4-Ufd1 interfaceStudies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradationStructure and Function of the N-terminal Nucleolin Binding Domain of Nuclear Valosin-containing Protein-like 2 (NVL2) Harboring a Nucleolar Localization SignalCrystal structure of FAF1 UBX domain in complex with p97/VCP N domain reveals a conformational change in the conserved FcisP touch-turn motif of UBX domainA ribosome-bound quality control complex triggers degradation of nascent peptides and signals translation stressDoa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domainShp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradationA Cdc48p-associated factor modulates endoplasmic reticulum-associated degradation, cell stress, and ubiquitinated protein homeostasisStructural and enzymatic properties of the AAA protein Drg1p from Saccharomyces cerevisiae. Decoupling of intracellular function from ATPase activity and hexamerization.Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination.The ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48pCdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with ubiquitin-like Atg8The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol.Sel1p/Ubx2p participates in a distinct Cdc48p-dependent endoplasmic reticulum-associated degradation pathway.A conserved protein with AN1 zinc finger and ubiquitin-like domains modulates Cdc48 (p97) function in the ubiquitin-proteasome pathwayAAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation.UBXD Proteins: A Family of Proteins with Diverse Functions in CancerPhosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation
P2860
Q22253422-EDABD8A3-8999-4DA1-A0A6-AAD2819CD49AQ24293051-16D2790A-7DB8-44C6-9CF2-3F4AEB95425DQ24294183-17A4166A-2646-4308-9FFF-134604774F6BQ24297296-7FDB12C2-B993-47C6-9CAF-247F50C178B2Q24307381-8E4412E3-8FA6-47B5-BBFB-25A9FF57F700Q24307429-138182E7-3C9A-4E47-83DA-95919E95E9C7Q24310742-4F8F8239-E5FE-41D0-BF6E-B40458A8BEFAQ24338770-5BEE9244-D5B8-44BE-B665-69B518A4E975Q24539071-FA454D7D-F904-41E2-A42D-2DE8F585F144Q24540390-E9B1BC4F-26D3-452F-9A07-4BBBB31706D5Q24594082-149C31DF-FDA5-40B3-8656-54CB7A10BA16Q24634678-E02E6132-F708-4781-82F4-552B7F47D036Q24673098-6FD564DB-C0AF-4FBB-A98E-F6B871B59BA0Q24674944-FC27BAB9-038F-4272-A6F9-26FA7383F1E0Q24796909-AAFE37D2-28F7-4E5E-968F-BD161B22FEE3Q26740517-4FF31F10-EB87-4740-A4BA-BBD559741FF0Q26770524-776693DB-81A3-420E-8D84-A1BFE29F2A6DQ27015865-DAE0E196-93D4-4545-9B77-D7B068D51999Q27620369-639B90F8-9C91-4FD4-B314-11496EB0CB6CQ27639561-06DCECF7-5A99-454A-8889-424586A480A6Q27639658-1CC76CCB-5120-4BBD-9038-6BC7DDDE3B2BQ27640720-92941E67-FAE7-4890-A0E6-EC3B74F8C2C7Q27644733-AAEC4A9D-9174-40F4-A7C0-0F383A397658Q27644749-4F6C0098-54B3-49D9-8689-6EEB4E98CC32Q27667463-DCFDC859-9BD5-4EE7-A509-62984F61F20EQ27670731-7161DBCF-177F-45EB-95CD-9F9B652DE336Q27929786-50938429-E5E8-4CF8-84B7-7C95C8D8E8F5Q27930054-73DDDBC3-C2CD-47C3-B02E-B670FFAA5A9AQ27931114-E9DEF265-96FE-43C0-8FE4-2D92CF728A13Q27931659-5291CE62-4393-4245-AFD3-12A163BC3F93Q27932034-6F803650-1830-402D-8F08-0F8ED9E9684FQ27932737-3356B459-4E5F-41BC-BC42-C4284CF5EDF9Q27934285-98AEED87-5212-417F-A6EF-281EC41787E0Q27936229-AEC8818C-4F8C-452B-A8A0-74D338780505Q27936514-D8E73249-1C7A-47C5-87C6-36E87D5D797EQ27936694-3388AA23-9294-4289-B7D9-611102E646ECQ27939846-069280E4-8EDE-4B41-A9EC-4AB974779637Q27939982-A9B1854A-A785-46E1-BF99-07062700B350Q28069036-D44F0740-186D-4DE7-A0C9-8B225FB80DC2Q28201277-D5C21A9A-175A-4594-8DEB-7FDE84355897
P2860
description
1997 nî lūn-bûn
@nan
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին 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
p47 is a cofactor for p97-mediated membrane fusion
@ast
p47 is a cofactor for p97-mediated membrane fusion
@en
p47 is a cofactor for p97-mediated membrane fusion
@nl
type
label
p47 is a cofactor for p97-mediated membrane fusion
@ast
p47 is a cofactor for p97-mediated membrane fusion
@en
p47 is a cofactor for p97-mediated membrane fusion
@nl
prefLabel
p47 is a cofactor for p97-mediated membrane fusion
@ast
p47 is a cofactor for p97-mediated membrane fusion
@en
p47 is a cofactor for p97-mediated membrane fusion
@nl
P2093
P2860
P3181
P356
P1433
P1476
p47 is a cofactor for p97-mediated membrane fusion
@en
P2093
P2860
P2888
P3181
P356
10.1038/40411
P407
P577
1997-07-03T00:00:00Z
P5875
P6179
1010703254