Structural Basis of a Rationally Rewired Protein-Protein Interface Critical to Bacterial Signaling
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Visualizing autophosphorylation in histidine kinasesCrystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coliA Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.An SOS Regulon under Control of a Noncanonical LexA-Binding Motif in the BetaproteobacteriaStructure of the response regulator RPA3017 involved in red-light signaling in Rhodopseudomonas palustris.Putative histidine kinase inhibitors with antibacterial effect against multi-drug resistant clinical isolates identified by in vitro and in silico screens.Regulation of signaling directionality revealed by 3D snapshots of a kinase:regulator complex in action.Stress-induced remodeling of the bacterial proteome.Crystal structure of the inactive state of the receiver domain of Spo0A from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier.Signal transduction in histidine kinases: insights from new structures.Conformational dynamics as a key factor of signaling mediated by the receiver domain of sensor histidine kinase from Arabidopsis thaliana.Cross-talk and specificity in two-component signal transduction pathways.Functional Dissection of the CroRS Two-Component System Required for Resistance to Cell Wall Stressors in Enterococcus faecalis.Asymmetric Structure of the Dimerization Domain of PhoR, a Sensor Kinase Important for the Virulence of Mycobacterium tuberculosis.Two Proteins Form a Heteromeric Bacterial Self-Recognition Complex in Which Variable Subdomains Determine Allele-Restricted BindingSpecificity residues determine binding affinity for two-component signal transduction systemsAllosteric activation of bacterial response regulators: the role of the cognate histidine kinase beyond phosphorylation.A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases.Sensory deprivation in Staphylococcus aureus.Structural characterization of the heme-based oxygen sensor, AfGcHK, its interactions with the cognate response regulator, and their combined mechanism of action in a bacterial two-component signaling system.Modification in hydrophobic packing of HAMP domain induces a destabilization of the auto-phosphorylation site in the histidine kinase CpxA.A Single-Domain Response Regulator Functions as an Integrating Hub To Coordinate General Stress Response and Development in Alphaproteobacteria.The Staphylococcus aureus Two-Component System AgrAC Displays Four Distinct Genomic Arrangements That Delineate Genomic Virulence Factor Signatures.
P2860
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P2860
Structural Basis of a Rationally Rewired Protein-Protein Interface Critical to Bacterial Signaling
description
2013 nî lūn-bûn
@nan
2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Structural Basis of a Rational ...... ritical to Bacterial Signaling
@ast
Structural Basis of a Rational ...... ritical to Bacterial Signaling
@en
Structural Basis of a Rational ...... ritical to Bacterial Signaling
@nl
type
label
Structural Basis of a Rational ...... ritical to Bacterial Signaling
@ast
Structural Basis of a Rational ...... ritical to Bacterial Signaling
@en
Structural Basis of a Rational ...... ritical to Bacterial Signaling
@nl
prefLabel
Structural Basis of a Rational ...... ritical to Bacterial Signaling
@ast
Structural Basis of a Rational ...... ritical to Bacterial Signaling
@en
Structural Basis of a Rational ...... ritical to Bacterial Signaling
@nl
P2860
P50
P3181
P1433
P1476
Structural basis of a rational ...... ritical to bacterial signaling
@en
P2093
Anna I Podgornaia
P2860
P304
P3181
P356
10.1016/J.STR.2013.07.005
P577
2013-08-15T00:00:00Z