Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
about
The proteasome and the delicate balance between destruction and rescueMPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 functionIdentification of two proteins, S14 and UIP1, that interact with UCH37The de-ubiquitinating enzyme Unp interacts with the retinoblastoma proteinA novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomesRelative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasomeSuppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53Evidence for bidentate substrate binding as the basis for the K48 linkage specificity of otubain 1K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substratesDistinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complexInvolvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalphaA deubiquitinase negatively regulates retro-translocation of nonubiquitinated substratesProteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPasesStructure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14Proteasomal degradation of ubiquitinated Insig proteins is determined by serine residues flanking ubiquitinated lysinesEvidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasomeAn emerging model for BAP1's role in regulating cell cycle progressionUse of RNA interference and complementation to study the function of the Drosophila and human 26S proteasome subunit S13The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its deathUbiquitin C-terminal hydrolase L1 (UCH-L1): structure, distribution and roles in brain function and dysfunctionIntracellular Dynamics of the Ubiquitin-Proteasome-SystemFunctions of the 19S complex in proteasomal degradationProteasome subunit Rpn13 is a novel ubiquitin receptorUbiquitin docking at the proteasome through a novel pleckstrin-homology domain interactionStructure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chainsStructural characterization of human Uch37Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzymeStabilization of an Unusual Salt Bridge in Ubiquitin by the Extra C-Terminal Domain of the Proteasome-Associated Deubiquitinase UCH37 as a Mechanism of Its Exo SpecificityMechanism of the Rpn13-induced activation of Uch37Structure characterization of the 26S proteasome.DOT4 links silencing and cell growth in Saccharomyces cerevisiaeInteraction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome.Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast.MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes.Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasomeTwo-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome.The regulatory particle of the Saccharomyces cerevisiae proteasome.Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome.
P2860
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P2860
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
description
1997 nî lūn-bûn
@nan
1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի փետրվարին 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
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
@ast
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
@en
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
@nl
type
label
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
@ast
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
@en
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
@nl
prefLabel
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
@ast
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
@en
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
@nl
P2093
P3181
P356
P1433
P1476
Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
@en
P2093
P2888
P304
P3181
P356
10.1038/385737A0
P407
P577
1997-02-20T00:00:00Z
P6179
1008495771