Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome.
about
Variably modulated gating of the 26S proteasome by ATP and polyubiquitinInteractions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome–ATPase interactionsThe predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradationModelling proteasome and proteasome regulator activities.Assembly, structure, and function of the 26S proteasome.Ubiquitin/proteasome pathway impairment in neurodegeneration: therapeutic implicationsDriving forces of proteasome-catalyzed peptide splicing in yeast and humans.Paradigms of protein degradation by the proteasome.Poly-Ub-substrate-degradative activity of 26S proteasome is not impaired in the aging rat brain.Misfolded PrP impairs the UPS by interaction with the 20S proteasome and inhibition of substrate entryRegulated protein turnover: snapshots of the proteasome in action.Substrate degradation by the proteasome: a single-molecule kinetic analysis.Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.ATP binding by proteasomal ATPases regulates cellular assembly and substrate-induced functions of the 26 S proteasome.High glucose and diabetes modulate cellular proteasome function: Implications in the pathogenesis of diabetes complications.Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs.The role of allostery in the ubiquitin-proteasome systemThe ATP costs and time required to degrade ubiquitinated proteins by the 26 S proteasome.Negatively charged metal oxide nanoparticles interact with the 20S proteasome and differentially modulate its biologic functional effects.Proteasome activators.Stalled proteasomes are directly relieved by P97 recruitment.Proteasome dynamics between proliferation and quiescence stages of Saccharomyces cerevisiae.High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx.AAA-ATPases in Protein Degradation.Role of the Ubiquitin-Proteasome Systems in the Biology and Virulence of Protozoan ParasitesUbiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening.ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation.Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.Ramping up degradation for proliferation.
P2860
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P2860
Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome.
description
2009 nî lūn-bûn
@nan
2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
@zh-hans
2009年学术文章
@zh-my
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2009年學術文章
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name
Polyubiquitin substrates allos ...... adation by the 26S proteasome.
@en
Polyubiquitin substrates allos ...... adation by the 26S proteasome.
@nl
type
label
Polyubiquitin substrates allos ...... adation by the 26S proteasome.
@en
Polyubiquitin substrates allos ...... adation by the 26S proteasome.
@nl
prefLabel
Polyubiquitin substrates allos ...... adation by the 26S proteasome.
@en
Polyubiquitin substrates allos ...... adation by the 26S proteasome.
@nl
P2093
P356
P1476
Polyubiquitin substrates allos ...... adation by the 26S proteasome.
@en
P2093
Annett Helfrich
Burkhardt Dahlmann
Cordula Enenkel
Dawadschargal Bech-Otschir
Gesa Consiglieri
Michael Seeger
Peter-Michael Kloetzel
P2888
P304
P356
10.1038/NSMB.1547
P577
2009-01-25T00:00:00Z