Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.
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Chasing Phosphoarginine Proteins: Development of a Selective Enrichment Method Using a Phosphatase TrapCross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residuesProtein-tyrosine phosphorylation interaction network in Bacillus subtilis reveals new substrates, kinase activators and kinase cross-talkCharacterization and site-directed mutagenesis of Wzb, an O-phosphatase from Lactobacillus rhamnosus.Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilisProtein-tyrosine phosphorylation in Bacillus subtilis: a 10-year retrospective.Listeria monocytogenes tyrosine phosphatases affect wall teichoic acid composition and phage resistanceGlobal impact of protein arginine phosphorylation on the physiology of Bacillus subtilisProtein-tyrosine phosphorylation in Bacillus subtilis.Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni.Tyrosine Phosphorylation and Dephosphorylation in Burkholderia cenocepacia Affect Biofilm Formation, Growth under Nutritional Deprivation, and PathogenicityGenome sequencing and analysis of the first complete genome of Lactobacillus kunkeei strain MP2, an Apis mellifera gut isolate.The role of bacterial protein tyrosine phosphatases in the regulation of the biosynthesis of secreted polysaccharides.Activity-Based Profiling Reveals a Regulatory Link between Oxidative Stress and Protein Arginine Phosphorylation.Exploring the diversity of protein modifications: special bacterial phosphorylation systems.The Streptococcus pyogenes orphan protein tyrosine phosphatase, SP-PTP, possesses dual specificity and essential virulence regulatory functions.Characterization and 1.57 Å resolution structure of the key fire blight phosphatase AmsI from Erwinia amylovora.A Porphyromonas gingivalis tyrosine phosphatase is a multifunctional regulator of virulence attributes.Activity control of the ClpC adaptor McsB in Bacillus subtilisQuantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response.Red light activates the sigmaB-mediated general stress response of Bacillus subtilis via the energy branch of the upstream signaling cascade.Molecular characterization of Alr1105 a novel arsenate reductase of the diazotrophic cyanobacterium Anabaena sp. PCC7120 and decoding its role in abiotic stress management in Escherichia coli.Spectral library based analysis of arginine phosphorylations in Staphylococcus aureus.
P2860
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P2860
Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.
@ast
Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.
@en
type
label
Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.
@ast
Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.
@en
prefLabel
Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.
@ast
Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.
@en
P2093
P2860
P1476
Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis
@en
P2093
Andrei Osterman
Cristina Bongiorni
Lucia Musumeci
Lutz Tautz
Marta Perego
Nunzio Bottini
Tomas Mustelin
P2860
P304
P356
10.1128/JB.187.14.4945-4956.2005
P407
P577
2005-07-01T00:00:00Z