The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins.
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Mass Spectrometry-Based Bacterial Proteomics: Focus on Dermatologic Microbial PathogensRole of Protein Phosphorylation in the Regulation of Cell Cycle and DNA-Related Processes in BacteriaTyrosine phosphorylation and bacterial virulenceBacterial tyrosine kinases: evolution, biological function and structural insightsBacterial phosphoproteomic analysis reveals the correlation between protein phosphorylation and bacterial pathogenicityFlagellin FliC Phosphorylation Affects Type 2 Protease Secretion and Biofilm Dispersal in Pseudomonas aeruginosa PAO1A novel signaling network essential for regulating Pseudomonas aeruginosa biofilm developmentThe Escherichia coli phosphotyrosine proteome relates to core pathways and virulenceSer/Thr/Tyr protein phosphorylation in the archaeon Halobacterium salinarum--a representative of the third domain of life.Transcriptional activator YesS is stimulated by histidine-phosphorylated HPr of the Bacillus subtilis phosphotransferase system.Integration of 'omics' data: does it lead to new insights into host-microbe interactions?Phosphoproteomics of Klebsiella pneumoniae NTUH-K2044 reveals a tight link between tyrosine phosphorylation and virulenceThe bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.Identification of serine/threonine kinase substrates in the human pathogen group B streptococcusMapping phosphoproteins in Neisseria meningitidis serogroup A.Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinasesQuantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpCEvolutionary constraints of phosphorylation in eukaryotes, prokaryotes, and mitochondria.Phosphoproteomics analysis of a clinical Mycobacterium tuberculosis Beijing isolate: expanding the mycobacterial phosphoproteome catalog.Site-Specific Ser/Thr/Tyr Phosphoproteome of Sinorhizobium meliloti at Stationary Phase.Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.Mass Spectrometry Targeted Assays as a Tool to Improve Our Understanding of Post-translational Modifications in Pathogenic Bacteria.Phosphoproteomic analysis reveals the effects of PilF phosphorylation on type IV pilus and biofilm formation in Thermus thermophilus HB27Campylobacter proteomics: guidelines, challenges and future perspectives.Activation of SsoPK4, an Archaeal eIF2α Kinase Homolog, by Oxidized CoA.Systems-wide proteomic characterization of combinatorial post-translational modification patterns.Eukaryote-like serine/threonine kinases and phosphatases in bacteria.Site-specific analysis of bacterial phosphoproteomes.The current state of microbial proteomics: where we are and where we want to go.Protein-serine/threonine/tyrosine kinases in bacterial signaling and regulation.Exploitation of physiology and metabolomics to identify pneumococcal vaccine candidates.Protein lysine acetylation in bacteria: Current state of the art.Separation of novel phosphoproteins of Porphyromonas gingivalis using phosphate-affinity chromatography.Exploring the diversity of protein modifications: special bacterial phosphorylation systems.Systematic profiling of the bacterial phosphoproteome reveals bacterium-specific features of phosphorylation.Temporal dynamics of the Saccharopolyspora erythraea phosphoproteome.The Streptococcus mutans serine/threonine kinase, PknB, regulates competence development, bacteriocin production, and cell wall metabolism.The phosphoproteome of the minimal bacterium Mycoplasma pneumoniae: analysis of the complete known Ser/Thr kinome suggests the existence of novel kinases.Protein costs do not explain evolution of metabolic strategies and regulation of ribosomal content: does protein investment explain an anaerobic bacterial Crabtree effect?
P2860
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P2860
The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh-hant
name
The Ser/Thr/Tyr phosphoproteom ...... tiply phosphorylated proteins.
@en
The Ser/Thr/Tyr phosphoproteom ...... tiply phosphorylated proteins.
@nl
type
label
The Ser/Thr/Tyr phosphoproteom ...... tiply phosphorylated proteins.
@en
The Ser/Thr/Tyr phosphoproteom ...... tiply phosphorylated proteins.
@nl
prefLabel
The Ser/Thr/Tyr phosphoproteom ...... tiply phosphorylated proteins.
@en
The Ser/Thr/Tyr phosphoproteom ...... tiply phosphorylated proteins.
@nl
P50
P356
P1433
P1476
The Ser/Thr/Tyr phosphoproteom ...... tiply phosphorylated proteins.
@en
P2093
Boumediene Soufi
Matthias Mann
P304
P356
10.1002/PMIC.200800069
P577
2008-09-01T00:00:00Z