p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins
about
The p56(lck)-interacting protein p62 stimulates transcription via the SV40 enhancerp62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibitionStructure and functional properties of the ubiquitin binding protein p62Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathwaySequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradationStructure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of bonep62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcriptionHistone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymesThe adapter protein ZIP binds Grb14 and regulates its inhibitory action on insulin signaling by recruiting protein kinase CzetaIdentification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathwaysSMART, a simple modular architecture research tool: identification of signaling domainsC9ORF72, the new gene on the block, causes C9FTD/ALS: new insights provided by neuropathologyAutophagy, mitochondria and oxidative stress: cross-talk and redox signallingThe ubiquitin-associated domain of hPLIC-2 interacts with the proteasomeAnalysis of intracytoplasmic hyaline bodies in a hepatocellular carcinoma. Demonstration of p62 as major constituentIdentification and confirmation of a module of coexpressed genesA method to identify p62’s UBA domain interacting proteinsThe life cycle of the 26S proteasome: from birth, through regulation and function, and onto its deathThe different roles of selective autophagic protein degradation in mammalian cellsModulation of translation and induction of autophagy by bacterial exoproductsUbiquitin recognition by the ubiquitin-associated domain of p62 involves a novel conformational switchStructural basis of target recognition by Atg8/LC3 during selective autophagySelective Transport of -Mannosidase by Autophagic Pathways: STRUCTURAL BASIS FOR CARGO RECOGNITION BY Atg19 AND Atg34The GATOR2 Component Wdr24 Regulates TORC1 Activity and Lysosome FunctionStarch-binding domain-containing protein 1 (Stbd1) and glycogen metabolism: Identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteinsArgyrophilic grain diseaseGenomic structure and promoter analysis of the p62 gene encoding a non-proteasomal multiubiquitin chain binding proteinSelective autophagy mediated by autophagic adapter proteinsOxidative stress and autophagy: the clash between damage and metabolic needsCloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cellsUBXD4, a UBX-containing protein, regulates the cell surface number and stability of alpha3-containing nicotinic acetylcholine receptorsRaft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE-triggered cell signalingD2 dopamine receptor expression and trafficking is regulated through direct interactions with ZIPCoupling of HIV-1 Antigen to the Selective Autophagy Receptor SQSTM1/p62 Promotes T-Cell-Mediated Immunityp62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell deathUbiquitin signalling in the NF-kappaB pathwayUbiquitin-binding domainsPhosphotyrosine (p-Tyr)-dependent and -independent mechanisms of p190 RhoGAP-p120 RasGAP interaction: Tyr 1105 of p190, a substrate for c-Src, is the sole p-Tyr mediator of complex formationPhosphotyrosine phosphatase activity associated with c-Src in large multimeric complexes isolated from adrenal medullary chromaffin cells.
P2860
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P2860
p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins
description
1996 nî lūn-bûn
@nan
1996 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@ast
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@en
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@en-gb
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@nl
type
label
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@ast
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@en
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@en-gb
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@nl
prefLabel
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@ast
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@en
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@en-gb
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@nl
P2093
P2860
P921
P3181
P356
P1476
p62, a phosphotyrosine-indepen ...... of ubiquitin-binding proteins
@en
P2093
P2860
P304
P3181
P356
10.1074/JBC.271.34.20235
P407
P577
1996-08-23T00:00:00Z