Distinct specificities of Mycobacterium tuberculosis and mammalian proteasomes for N-acetyl tripeptide substrates.
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Inhibitors selective for mycobacterial versus human proteasomesStructural Insights on the Mycobacterium tuberculosis Proteasomal ATPase MpaFellutamide B is a potent inhibitor of the Mycobacterium tuberculosis proteasomeCharacterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S β5-subunitProteasomal protein degradation in Mycobacteria is dependent upon a prokaryotic ubiquitin-like proteinBortezomib Warhead-Switch Confers Dual Activity against Mycobacterial Caseinolytic Protease and Proteasome and Selectivity against Human Proteasome.Rational Design of Selective and Bioactive Inhibitors of the Mycobacterium tuberculosis Proteasome.Pentapeptide boronic acid inhibitors of Mycobacterium tuberculosis MycP1 protease.PSMB9 codon 60 polymorphisms have no impact on the activity of the immunoproteasome catalytic subunit B1i expressed in multiple types of solid cancerCleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity.Target mechanism-based whole-cell screening identifies bortezomib as an inhibitor of caseinolytic protease in mycobacteriaDiscovery of new [Formula: see text] proteasome inhibitors using a knowledge-based computational screening approach.Optimization and Evaluation of 5-Styryl-Oxathiazol-2-one Mycobacterium tuberculosis Proteasome Inhibitors as Potential Antitubercular Agents.Inhibitors for the immuno- and constitutive proteasome: current and future trends in drug development.Bacterial proteases, untapped antimicrobial drug targets.Targeting proteasomes in infectious organisms to combat disease.Mycobacterium tuberculosis proteasomal ATPase Mpa has a β-grasp domain that hinders docking with the proteasome core protease.Oxathiazolones Selectively Inhibit the Human Immunoproteasome over the Constitutive Proteasome.A luminescence assay for natural product inhibitors of the Mycobacterium tuberculosis proteasome.N,C-Capped dipeptides with selectivity for mycobacterial proteasome over human proteasomes: role of S3 and S1 binding pockets.Structural Basis for the Species-Selective Binding of N,C-Capped Dipeptides to the Mycobacterium tuberculosis Proteasome.Structure of human immunoproteasome with a reversible and noncompetitive inhibitor that selectively inhibits activated lymphocytes.Targeting the Proteostasis Network for Mycobacterial Drug Discovery.
P2860
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P2860
Distinct specificities of Mycobacterium tuberculosis and mammalian proteasomes for N-acetyl tripeptide substrates.
description
2008 nî lūn-bûn
@nan
2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Distinct specificities of Myco ...... -acetyl tripeptide substrates.
@ast
Distinct specificities of Myco ...... -acetyl tripeptide substrates.
@en
type
label
Distinct specificities of Myco ...... -acetyl tripeptide substrates.
@ast
Distinct specificities of Myco ...... -acetyl tripeptide substrates.
@en
prefLabel
Distinct specificities of Myco ...... -acetyl tripeptide substrates.
@ast
Distinct specificities of Myco ...... -acetyl tripeptide substrates.
@en
P2093
P2860
P356
P1476
Distinct specificities of Myco ...... -acetyl tripeptide substrates.
@en
P2093
Carl Nathan
Christopher Tsu
Lawrence Dick
P2860
P304
34423-34431
P356
10.1074/JBC.M805324200
P407
P577
2008-10-01T00:00:00Z