The mechanism of caseinolytic protease (ClpP) inhibition.
about
Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triadReversible Inhibitors Arrest ClpP in a Defined Conformational State that Can Be Revoked by ClpX AssociationExploring anti-bacterial compounds against intracellular LegionellaAAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.Target mechanism-based whole-cell screening identifies bortezomib as an inhibitor of caseinolytic protease in mycobacteriaThe development of small-molecule modulators for ClpP protease activity.Antibacterial activity of and resistance to small molecule inhibitors of the ClpP peptidaseSubstrate delivery by the AAA+ ClpX and ClpC1 unfoldases activates the mycobacterial ClpP1P2 peptidaseMechanistic analysis of aliphatic β-lactones in Vibrio harveyi reveals a quorum sensing independent mode of action.Activity-Based Proteome Profiling Probes Based on Woodward's Reagent K with Distinct Target Selectivity.
P2860
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P2860
The mechanism of caseinolytic protease (ClpP) inhibition.
description
2013 nî lūn-bûn
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2013年学术文章
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name
The mechanism of caseinolytic protease (ClpP) inhibition.
@en
The mechanism of caseinolytic protease
@nl
type
label
The mechanism of caseinolytic protease (ClpP) inhibition.
@en
The mechanism of caseinolytic protease
@nl
prefLabel
The mechanism of caseinolytic protease (ClpP) inhibition.
@en
The mechanism of caseinolytic protease
@nl
P2093
P2860
P356
P1476
The mechanism of caseinolytic protease (ClpP) inhibition.
@en
P2093
Christian Hedberg
Gerhard Klebe
Johannes Lehmann
Malte Gersch
Marion Rusch
Stephan A Sieber
Thomas Böttcher
Vadim S Korotkov
P2860
P304
P356
10.1002/ANIE.201204690
P407
P577
2013-01-30T00:00:00Z