Use of allostery to identify inhibitors of calmodulin-induced activation of Bacillus anthracis edema factor.
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Bacillus anthracis edema factor substrate specificity: evidence for new modes of actionNovel allosteric sites on Ras for lead generationDesigning Allosteric Control into Enzymes by Chemical Rescue of StructureThe Designability of Protein Switches by Chemical Rescue of Structure: Mechanisms of Inactivation and ReactivationMutation D816V alters the internal structure and dynamics of c-KIT receptor cytoplasmic region: implications for dimerization and activation mechanismsCombined approaches for drug design points the way to novel proline racemase inhibitor candidates to fight Chagas' diseaseLocal Geometry and Evolutionary Conservation of Protein Surfaces Reveal the Multiple Recognition Patches in Protein-Protein InteractionsMolecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors.A tethered bilayer assembled on top of immobilized calmodulin to mimic cellular compartmentalization.New developments in vaccines, inhibitors of anthrax toxins, and antibiotic therapeutics for Bacillus anthracis.Structural basis of anthrax edema factor neutralization by a neutralizing antibodyActivation of the edema factor of Bacillus anthracis by calmodulin: evidence of an interplay between the EF-calmodulin interaction and calcium binding.Designing inhibitors of anthrax toxinStructure-based redesign of an edema toxin inhibitor.AlloPred: prediction of allosteric pockets on proteins using normal mode perturbation analysis.Interactions of Bordetella pertussis adenylyl cyclase toxin CyaA with calmodulin mutants and calmodulin antagonists: comparison with membranous adenylyl cyclase I.Targeting bacterial toxins.An overview of investigational toxin-directed therapies for the adjunctive management of Bacillus anthracis infection and sepsis.Exploiting computationally derived out-of-the-box protein conformations for drug design.JET2 Viewer: a database of predicted multiple, possibly overlapping, protein-protein interaction sites for PDB structures.Molecular Modeling of the Catalytic Domain of CyaA Deepened the Knowledge of Its Functional Dynamics.Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin.Allosteric activation of Bordetella pertussis adenylyl cyclase by calmodulin: molecular dynamics and mutagenesis studiesAb initio sampling of transition paths by conditioned Langevin dynamics.Allosteric sites can be identified based on the residue-residue interaction energy difference.Small molecule inhibitors of anthrax edema factor.Polypharmacology modelling using proteochemometrics (PCM): recent methodological developments, applications to target families, and future prospects
P2860
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P2860
Use of allostery to identify inhibitors of calmodulin-induced activation of Bacillus anthracis edema factor.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Use of allostery to identify i ...... cillus anthracis edema factor.
@ast
Use of allostery to identify i ...... cillus anthracis edema factor.
@en
type
label
Use of allostery to identify i ...... cillus anthracis edema factor.
@ast
Use of allostery to identify i ...... cillus anthracis edema factor.
@en
prefLabel
Use of allostery to identify i ...... cillus anthracis edema factor.
@ast
Use of allostery to identify i ...... cillus anthracis edema factor.
@en
P2093
P2860
P50
P356
P1476
Use of allostery to identify i ...... acillus anthracis edema factor
@en
P2093
Arnaud Blondel
Aurélien Lesnard
Christophe Goncalves
Elodie Laine
Johanna C Karst
Sylvain Rault
P2860
P304
11277-11282
P356
10.1073/PNAS.0914611107
P407
P577
2010-06-07T00:00:00Z