Structure and interactions of the helical and U-box domains of CHIP, the C terminus of HSP70 interacting protein.
about
Structural and functional characterization of the monomeric U-box domain from E4BDocking-dependent ubiquitination of the interferon regulatory factor-1 tumor suppressor protein by the ubiquitin ligase CHIPInteractions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymesE2 interaction and dimerization in the crystal structure of TRAF6Structural and Functional Insights into the Roles of the Mms21 Subunit of the Smc5/6 ComplexMolecular Basis for the Association of Human E4B U Box Ubiquitin Ligase with E2-Conjugating Enzymes UbcH5c and Ubc4Solution Structure of RING Finger-like Domain of Retinoblastoma-binding Protein-6 (RBBP6) Suggests It Functions as a U-boxSymmetry breaking during homodimeric assembly activates an E3 ubiquitin ligaseChanges in PUB22 Ubiquitination Modes Triggered by MITOGEN-ACTIVATED PROTEIN KINASE3 Dampen the Immune Response.Chaperone functions of the E3 ubiquitin ligase CHIP.Engineering a ubiquitin ligase reveals conformational flexibility required for ubiquitin transferNovel role of C terminus of Hsc70-interacting protein (CHIP) ubiquitin ligase on inhibiting cardiac apoptosis and dysfunction via regulating ERK5-mediated degradation of inducible cAMP early repressor.Quality control for unfolded proteins at the plasma membrane.Intrinsic disorder drives N-terminal ubiquitination by Ube2wE2 conjugating enzyme selectivity and requirements for function of the E3 ubiquitin ligase CHIP.Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP.A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteinsAct1, a U-box E3 ubiquitin ligase for IL-17 signaling.Stress-dependent Daxx-CHIP interaction suppresses the p53 apoptotic program.Ubiquibodies, synthetic E3 ubiquitin ligases endowed with unnatural substrate specificity for targeted protein silencingTRAF-mediated regulation of immune and inflammatory responses.Ca2+/S100 proteins act as upstream regulators of the chaperone-associated ubiquitin ligase CHIP (C terminus of Hsc70-interacting protein)Hetero-oligomerization with MdmX rescues the ubiquitin/Nedd8 ligase activity of RING finger mutants of Mdm2.
P2860
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P2860
Structure and interactions of the helical and U-box domains of CHIP, the C terminus of HSP70 interacting protein.
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
@wuu
2006年学术文章
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2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Structure and interactions of ...... of HSP70 interacting protein.
@en
Structure and interactions of ...... of HSP70 interacting protein.
@nl
type
label
Structure and interactions of ...... of HSP70 interacting protein.
@en
Structure and interactions of ...... of HSP70 interacting protein.
@nl
prefLabel
Structure and interactions of ...... of HSP70 interacting protein.
@en
Structure and interactions of ...... of HSP70 interacting protein.
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P2093
P356
P1433
P1476
Structure and interactions of ...... s of HSP70 interacting protein
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P2093
Karl I Devlin
Michael G Ford
P304
P356
10.1021/BI0601508
P407
P50
P577
2006-04-01T00:00:00Z