The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ
about
Structure of the cytoplasmic segment of histidine kinase receptor QseC, a key player in bacterial virulenceA high-throughput TNP-ATP displacement assay for screening inhibitors of ATP-binding in bacterial histidine kinasesSite-specific mutation of Staphylococcus aureus VraS reveals a crucial role for the VraR-VraS sensor in the emergence of glycopeptide resistance.Small-molecule inhibition of bacterial two-component systems to combat antibiotic resistance and virulence.Inactivation of multiple bacterial histidine kinases by targeting the ATP-binding domain.Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases.Putative histidine kinase inhibitors with antibacterial effect against multi-drug resistant clinical isolates identified by in vitro and in silico screens.The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts.Analysis of HSP90-related folds with MED-SuMo classification approach.Biological insights from structures of two-component proteins.Crystallization and preliminary X-ray characterization of a catalytic and ATP-binding domain of a putative PhoR histidine kinase from the gamma-radioresistant bacterium Deinococcus radiodurans.The Rational Design, Synthesis, and Antimicrobial Properties of Thiophene Derivatives That Inhibit Bacterial Histidine Kinases.Crystallization and preliminary X-ray analysis of a putative sensor histidine kinase domain: the C-terminal domain of HksP4 from Aquifex aeolicus VF5.Activity-based probe for histidine kinase signaling.2.4 Å resolution crystal structure of human TRAP1NM, the Hsp90 paralog in the mitochondrial matrix.All signals lost.Mechanistic insight into inhibition of two-component system signaling.Ensemble Architecture for Prediction of Enzyme-ligand Binding Residues Using Evolutionary Information.Rational Design of Selective Adenine-Based Scaffolds for Inactivation of Bacterial Histidine Kinases.Angucycline antibiotic waldiomycin recognizes common structural motif conserved in bacterial histidine kinases.Structural ensemble-based docking simulation and biophysical studies discovered new inhibitors of Hsp90 N-terminal domain.
P2860
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P2860
The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին 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
The Hsp90 inhibitor radicicol ...... f bacterial sensor kinase PhoQ
@ast
The Hsp90 inhibitor radicicol ...... f bacterial sensor kinase PhoQ
@en
The Hsp90 inhibitor radicicol ...... f bacterial sensor kinase PhoQ
@nl
type
label
The Hsp90 inhibitor radicicol ...... f bacterial sensor kinase PhoQ
@ast
The Hsp90 inhibitor radicicol ...... f bacterial sensor kinase PhoQ
@en
The Hsp90 inhibitor radicicol ...... f bacterial sensor kinase PhoQ
@nl
prefLabel
The Hsp90 inhibitor radicicol ...... f bacterial sensor kinase PhoQ
@ast
The Hsp90 inhibitor radicicol ...... f bacterial sensor kinase PhoQ
@en
The Hsp90 inhibitor radicicol ...... f bacterial sensor kinase PhoQ
@nl
P2093
P3181
P1476
The Hsp90 inhibitor radicicol ...... f bacterial sensor kinase PhoQ
@en
P2093
Jingping Shen
Lingdi Zhang
Michael T Guarnieri
P3181
P356
10.1016/J.JMB.2008.03.036
P407
P577
2008-05-23T00:00:00Z