Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin
about
Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitinHDAC6 as a target for neurodegenerative diseases: what makes it different from the other HDACs?Structural Basis for Assembly and Activation of the Heterotetrameric SAGA Histone H2B Deubiquitinase ModuleProtein Aggregates Are Recruited to Aggresome by Histone Deacetylase 6 via Unanchored Ubiquitin C TerminiThe crystal structure of S. cerevisiae Sad1, a catalytically inactive deubiquitinase that is broadly required for pre-mRNA splicingThe role of prostate tumor overexpressed 1 in cancer progressionProteasomes activate aggresome disassembly and clearance by producing unanchored ubiquitin chainsHDAC6 and Ubp-M BUZ domains recognize specific C-terminal sequences of proteins.The unusual UBZ domain of Saccharomyces cerevisiae polymerase ηInterferon-stimulated gene 15 (ISG15) and ISG15-linked proteins can associate with members of the selective autophagic process, histone deacetylase 6 (HDAC6) and SQSTM1/p62.Chaperone-mediated 26S proteasome remodeling facilitates free K63 ubiquitin chain production and aggresome clearanceThe HDAC6/APOBEC3G complex regulates HIV-1 infectiveness by inducing Vif autophagic degradation.Synthesis and screening of peptide libraries with free C-termini.A targeted in vivo RNAi screen reveals deubiquitinases as new regulators of Notch signaling.Deciphering histone 2A deubiquitinationRegulation of proteolysis by human deubiquitinating enzymes.Deubiquitylases from genes to organism.DUBs, the regulation of cell identity and disease.Mass spectrometry insights into a tandem ubiquitin-binding domain hybrid engineered for the selective recognition of unanchored polyubiquitin.Molecular dynamics of zinc-finger ubiquitin binding domains: a comparative study of histone deacetylase 6 and ubiquitin-specific protease 5.Central catalytic domain of BRAP (RNF52) recognizes the types of ubiquitin chains and utilizes oligo-ubiquitin for ubiquitylation.
P2860
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P2860
Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin
description
2007 nî lūn-bûn
@nan
2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@ast
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@en
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@en-gb
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@nl
type
label
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@ast
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@en
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@en-gb
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@nl
altLabel
Solution Structure of the Ubp- ...... erminal Tail of Free Ubiquitin
@en
prefLabel
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@ast
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@en
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@en-gb
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@nl
P2093
P2860
P921
P1476
Solution structure of the Ubp- ...... erminal tail of free ubiquitin
@en
P2093
Jeffrey J Kovacs
Mignon A Keaton
Ming-Tao Pai
Shawn S-C Li
Shiou-Ru Tzeng
Tso-Pang Yao
P2860
P304
P356
10.1016/J.JMB.2007.04.015
P407
P50
P577
2007-04-12T00:00:00Z