Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis.
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Pulsed feedback defers cellular differentiationThe ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite.Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretomeStimulus perception in bacterial signal-transducing histidine kinasesA glutamine-amidotransferase-like protein modulates FixT anti-kinase activity in Sinorhizobium melilotiConformational change-induced repeat domain expansion regulates Rap phosphatase quorum-sensing signal receptorsIdentical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrateStructural Basis of Response Regulator Dephosphorylation by Rap PhosphatasesStructural Basis of Response Regulator Inhibition by a Bacterial Anti-Activator ProteinStructural Basis of Rap Phosphatase Inhibition by Phr PeptidesModulation of Mycobacterium tuberculosis proliferation by MtrA, an essential two-component response regulatorTracing the domestication of a biofilm-forming bacteriumThe membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulatorIdentification of a membrane protein involved in activation of the KinB pathway to sporulation in Bacillus subtilisBacillus subtilis hydrolyzes CheY-P at the location of its action, the flagellar switchScoC regulates peptide transport and sporulation initiation in Bacillus subtilisRegulation of a Bacillus subtilis mobile genetic element by intercellular signaling and the global DNA damage responseRecent advances in the social and developmental biology of the myxobacteriaPAS domains: internal sensors of oxygen, redox potential, and lightRgg protein structure-function and inhibition by cyclic peptide compounds.Effects of phosphorelay perturbations on architecture, sporulation, and spore resistance in biofilms of Bacillus subtilis.Complexity in bacterial cell-cell communication: quorum signal integration and subpopulation signaling in the Bacillus subtilis phosphorelay.A new family of aspartyl phosphate phosphatases targeting the sporulation transcription factor Spo0A of Bacillus subtilis.The Bacillus subtilis SinR and RapA developmental regulators are responsible for inhibition of spore development by alcohol.Extracellular signals that define distinct and coexisting cell fates in Bacillus subtilis.Isolation and characterization of nonchemotactic CheZ mutants of Escherichia coliModeling chemotaxis reveals the role of reversed phosphotransfer and a bi-functional kinase-phosphatase.Two-component signal transduction as a target for microbial anti-infective therapy.Altered srf expression in Bacillus subtilis resulting from changes in culture pH is dependent on the Spo0K oligopeptide permease and the ComQX system of extracellular control.Characterization of a novel member of the DegS-DegU regulon affected by salt stress in Bacillus subtilisSpore formation in Bacillus subtilisSynergistic regulation of competence development in Bacillus subtilis by two Rap-Phr systems.Broadly heterogeneous activation of the master regulator for sporulation in Bacillus subtilis.PAS-A domain of phosphorelay sensor kinase A: a catalytic ATP-binding domain involved in the initiation of development in Bacillus subtilis.Regulation of synthesis of the Bacillus subtilis transition-phase, spore-associated antibacterial protein TasA.Differential processing of propeptide inhibitors of Rap phosphatases in Bacillus subtilis.Control of a family of phosphatase regulatory genes (phr) by the alternate sigma factor sigma-H of Bacillus subtilis.Dynamical consequences of bandpass feedback loops in a bacterial phosphorelayMathematical modelling of the sporulation-initiation network in Bacillus subtilis revealing the dual role of the putative quorum-sensing signal molecule PhrA.Conserved oligopeptide permeases modulate sporulation initiation in Clostridium difficile.
P2860
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P2860
Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh-hant
name
Multiple protein-aspartate pho ...... of development in B. subtilis.
@en
Multiple protein-aspartate pho ...... of development in B. subtilis.
@nl
type
label
Multiple protein-aspartate pho ...... of development in B. subtilis.
@en
Multiple protein-aspartate pho ...... of development in B. subtilis.
@nl
prefLabel
Multiple protein-aspartate pho ...... of development in B. subtilis.
@en
Multiple protein-aspartate pho ...... of development in B. subtilis.
@nl
P2093
P1433
P1476
Multiple protein-aspartate pho ...... of development in B. subtilis.
@en
P2093
P304
P356
10.1016/0092-8674(94)90035-3
P407
P577
1994-12-01T00:00:00Z