AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.
about
Reversible Inhibitors Arrest ClpP in a Defined Conformational State that Can Be Revoked by ClpX AssociationThe N-terminal Region of the Ubiquitin Regulatory X (UBX) Domain-containing Protein 1 (UBXD1) Modulates Interdomain Communication within the Valosin-containing Protein p97.The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease.Insights into ClpXP proteolysis: heterooligomerization and partial deactivation enhance chaperone affinity and substrate turnover in Listeria monocytogenes.Sclerotiamide: The First Non-Peptide-Based Natural Product Activator of Bacterial Caseinolytic Protease P.Salmonella enterica serovar Typhimurium utilizes the ClpPX and Lon proteases for optimal fitness in the ceca of chickens.Examination of a Structural Model of Peptidomimicry by Cyclic Acyldepsipeptide Antibiotics in Their Interaction with the ClpP PeptidaseUncoupling conformational states from activity in an allosteric enzyme.Determining Atomistic SAXS Models of Tri-Ubiquitin Chains from Bayesian Analysis of Accelerated Molecular Dynamics Simulations.The development of small-molecule modulators for ClpP protease activity.Bacterial proteases, untapped antimicrobial drug targets.Small molecule inhibition of apicomplexan FtsH1 disrupts plastid biogenesis in human pathogens.Antibiotics: Precious Goods in Changing Times.Two ways to skin a cat: acyldepsipeptides antibiotics can kill bacteria through activation or inhibition of ClpP activityPfClpC Is an Essential Clp Chaperone Required for Plastid Integrity and Clp Protease Stability in Plasmodium falciparum.In vivo and in vitro effects of a ClpP activating antibiotic against vancomycin resistant enterococci.Reversible inhibition of the ClpP protease via an N-terminal conformational switch
P2860
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P2860
AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.
description
2015 nî lūn-bûn
@nan
2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
AAA+ chaperones and acyldepsip ...... se via conformational control.
@ast
AAA+ chaperones and acyldepsip ...... se via conformational control.
@en
AAA+ chaperones and acyldepsip ...... se via conformational control.
@nl
type
label
AAA+ chaperones and acyldepsip ...... se via conformational control.
@ast
AAA+ chaperones and acyldepsip ...... se via conformational control.
@en
AAA+ chaperones and acyldepsip ...... se via conformational control.
@nl
prefLabel
AAA+ chaperones and acyldepsip ...... se via conformational control.
@ast
AAA+ chaperones and acyldepsip ...... se via conformational control.
@en
AAA+ chaperones and acyldepsip ...... se via conformational control.
@nl
P2093
P2860
P50
P356
P1476
AAA+ chaperones and acyldepsip ...... se via conformational control.
@en
P2093
Heike Brötz-Oesterhelt
Helga Rübsamen-Schaeff
Imran Malik
Kirsten Famulla
Malte Gersch
Maria Dahmen
Stephan A Sieber
Vadim S Korotkov
P2860
P2888
P356
10.1038/NCOMMS7320
P407
P577
2015-02-19T00:00:00Z
P5875
P6179
1037196231