The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring.
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An essential nonredundant role for mycobacterial DnaK in native protein foldingMycobacterium tuberculosis RsdA provides a conformational rationale for selective regulation of -factor activity by proteolysisStructural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triadStructural Basis of Mycobacterial Inhibition by Cyclomarin ALassomycin, a Ribosomally Synthesized Cyclic Peptide, Kills Mycobacterium tuberculosis by Targeting the ATP-Dependent Protease ClpC1P1P2Towards Selective Mycobacterial ClpP1P2 Inhibitors with Reduced Activity against the Human Proteasome.Bortezomib Warhead-Switch Confers Dual Activity against Mycobacterial Caseinolytic Protease and Proteasome and Selectivity against Human Proteasome.In Vivo-Selected Pyrazinoic Acid-Resistant Mycobacterium tuberculosis Strains Harbor Missense Mutations in the Aspartate Decarboxylase PanD and the Unfoldase ClpC1.Cloning and characterization of Clp protease proteolytic subunit 2 and its implication in clinical diagnosis of tuberculosisStructure and activation of a heteromeric protease complex.Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery.The C-terminus of ClpC1 of Mycobacterium tuberculosis is crucial for its oligomerization and functionMycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.The cyclic peptide ecumicin targeting ClpC1 is active against Mycobacterium tuberculosis in vivo.Post-translational regulation via Clp protease is critical for survival of Mycobacterium tuberculosis.Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity.The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1Target mechanism-based whole-cell screening identifies bortezomib as an inhibitor of caseinolytic protease in mycobacteriaInsights into ClpXP proteolysis: heterooligomerization and partial deactivation enhance chaperone affinity and substrate turnover in Listeria monocytogenes.The purification of the Chlamydomonas reinhardtii chloroplast ClpP complex: additional subunits and structural featuresMycobacterium tuberculosis ESAT-6 exhibits a unique membrane-interacting activity that is not found in its ortholog from non-pathogenic Mycobacterium smegmatis.Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis.Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosisProteases in Mycobacterium tuberculosis pathogenesis: potential as drug targets.Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Acyldepsipeptide antibiotics as a potential therapeutic agent against Clostridium difficile recurrent infections.The development of small-molecule modulators for ClpP protease activity.Two ways to skin a cat: acyldepsipeptides antibiotics can kill bacteria through activation or inhibition of ClpP activityAcyldepsipeptide antibiotics kill mycobacteria by preventing the physiological functions of the ClpP1P2 protease.AAA+ Machines of Protein Destruction in Mycobacteria.Dual stoichiometry and subunit organization in the ClpP1/P2 protease from the cyanobacterium Synechococcus elongatus.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 peptidaseTargeting the Proteostasis Network for Mycobacterial Drug Discovery.The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.Pneumococcal ClpP modulates the maturation and activation of human dendritic cells: implications for pneumococcal infections.Regulation of the clpP1clpP2 operon by the pleiotropic regulator AdpA in Streptomyces lividans.The caseinolytic protease complex component CLPC1 in Arabidopsis maintains proteome and RNA homeostasis in chloroplasts
P2860
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P2860
The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
The active ClpP protease from ...... americ ClpP1 and a ClpP2 ring.
@en
The active ClpP protease from ...... americ ClpP1 and a ClpP2 ring.
@nl
type
label
The active ClpP protease from ...... americ ClpP1 and a ClpP2 ring.
@en
The active ClpP protease from ...... americ ClpP1 and a ClpP2 ring.
@nl
prefLabel
The active ClpP protease from ...... americ ClpP1 and a ClpP2 ring.
@en
The active ClpP protease from ...... americ ClpP1 and a ClpP2 ring.
@nl
P2093
P2860
P356
P1433
P1476
The active ClpP protease from ...... tameric ClpP1 and a ClpP2 ring
@en
P2093
Alfred L Goldberg
Olga Kandror
Ravikiran M Raju
Tatos Akopian
P2860
P304
P356
10.1038/EMBOJ.2012.5
P407
P577
2012-01-27T00:00:00Z