Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.
about
The Sorcerer II Global Ocean Sampling expedition: expanding the universe of protein familiesIdentification of a novel PP2C-type mitochondrial phosphataseDeterminants for substrate specificity of the bacterial PP2C protein phosphatase tPphA from Thermosynechococcus elongatusTrends in selenium utilization in marine microbial world revealed through the analysis of the global ocean sampling (GOS) projectProtein-tyrosine phosphorylation interaction network in Bacillus subtilis reveals new substrates, kinase activators and kinase cross-talkRegulatory interactions of a virulence-associated serine/threonine phosphatase-kinase pair in Bacillus anthracis.A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803.Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established.The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells.Actin dynamics is controlled by a casein kinase II and phosphatase 2C interplay on Toxoplasma gondii Toxofilin.Aspects of eukaryotic-like signaling in Gram-positive cocci: a focus on virulence.Identification of a glycosylated Ehrlichia canis 19-kilodalton major immunoreactive protein with a species-specific serine-rich glycopeptide epitopeThe GTPase CpgA is implicated in the deposition of the peptidoglycan sacculus in Bacillus subtilis.CTL0511 from Chlamydia trachomatis Is a Type 2C Protein Phosphatase with Broad Substrate SpecificityCharacterization of a serine/threonine kinase involved in virulence of Staphylococcus aureus.Eukaryote-like serine/threonine kinases and phosphatases in bacteria.Phosphorylation of the cell division protein GpsB regulates PrkC kinase activity through a negative feedback loop in Bacillus subtilis.PrkC-mediated phosphorylation of overexpressed YvcK protein regulates PBP1 protein localization in Bacillus subtilis mreB mutant cells.Pph1 from Myxococcus xanthus is a protein phosphatase involved in vegetative growth and development.The unique serine/threonine phosphatase from the minimal bacterium Mycoplasma synoviae: biochemical characterization and metal dependence.Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes.Perturbation of manganese metabolism disrupts cell division in Streptococcus pneumoniae.Suppression and synthetic-lethal genetic relationships of ΔgpsB mutations indicate that GpsB mediates protein phosphorylation and penicillin-binding protein interactions in Streptococcus pneumoniae D39.Characterization of the chaperonin GroEL in Mycoplasma gallisepticum.Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments
P2860
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P2860
Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.
description
2000 nî lūn-bûn
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2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
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2000年論文
@zh-mo
2000年論文
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2000年论文
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name
Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.
@ast
Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.
@en
type
label
Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.
@ast
Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.
@en
prefLabel
Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.
@ast
Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.
@en
P2093
P2860
P1476
Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family
@en
P2093
P2860
P304
P356
10.1128/JB.182.19.5634-5638.2000
P407
P577
2000-10-01T00:00:00Z