Phosphoproteomics in bacteria: towards a systemic understanding of bacterial phosphorylation networks
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Summary
This research avenue will enable the study of bacterial pathogens to dissect phosphorylation-related events during different stages of infection and stimulate the efforts to find inhibitors for key kinases and phosphatases implicated therein.
- Type
- review
- Published
- 2008-08-01
- Cited by
- 66
- References
- 94
- OpenAlex
- https://openalex.org/W2104107382
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:19664973
Keywords
Phosphoproteomics, Phosphorylation, Protein phosphorylation, Biology, Kinase
References
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- Functional and quantitative proteomics using SILAC in cancer research
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- Enteropathogenic Escherichia coli Tir is an SH2/3 ligand that recruits and activates tyrosine kinases required for pedestal formation
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- Histidine kinase-mediated signal transduction systems of pathogenic microorganisms as targets for therapeutic intervention.
- The 3D structure of a periplasm-spanning platform required for assembly of group 1 capsular polysaccharides in Escherichia coli
- Yersinia Protein Kinase YopO Is Activated by A Novel G-actin Binding Process*
- A Eukaryotic Type Serine/Threonine Kinase and Phosphatase inStreptococcus agalactiae Reversibly Phosphorylate an Inorganic Pyrophosphatase and Affect Growth, Cell Segregation, and Virulence*
- Autophosphorylation of the Escherichia coli Protein Kinase Wzc Regulates Tyrosine Phosphorylation of Ugd, a UDP-glucose Dehydrogenase*
- Yersinia YopJ Acetylates and Inhibits Kinase Activation by Blocking Phosphorylation
- Mass spectrometry–based proteomics turns quantitative
- Tyrosine-phosphorylated bacterial effector proteins: the enemies within.
- WaaP of Pseudomonas aeruginosa Is a Novel Eukaryotic Type Protein-tyrosine Kinase as Well as a Sugar Kinase Essential for the Biosynthesis of Core Lipopolysaccharide*
- Role of the cell envelope in bacterial adaptation to growth in vivo in infections.
- UDP-Acetyl-Mannosamine Dehydrogenase Is an Endogenous Protein Substrate of Staphylococcus aureus Protein-Tyrosine Kinase Activity
- A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
- The Condensing Activities of the Mycobacterium tuberculosis Type II Fatty Acid Synthase Are Differentially Regulated by Phosphorylation*
- SigmaB contributes to Listeria monocytogenes invasion by controlling expression of inlA and inlB.
Cited by
- Phosphoproteomic analysis of Rhodopseudomonas palustris reveals the role of pyruvate phosphate dikinase phosphorylation in lipid production.
- Shotgun proteomics of bacterial pathogens: advances, challenges and clinical implications
- Découverte d'une nouvelle famille de protéine kinases bactériennes : mécanismes de fonctionnement et rôle cellulaire de YdiB, un archétype chez Baccillus subtilis
- Global dynamics of Escherichia coli phosphoproteome in central carbon metabolism under changing culture conditions.
- Proteomic analysis of post translational modifications in cyanobacteria.
- Automated immobilized metal affinity chromatography system for enrichment of Escherichia coli phosphoproteome
- Molecular analysis of candidate probiotic effector molecules of Lactobacillus plantarum
- Mutational dissection of the S/T‐kinase StkP reveals crucial roles in cell division of Streptococcus pneumoniae
- Mycobacterial proteomics: analysis of expressed proteomes and post-translational modifications to identify candidate virulence factors
- Regulatory Interactions between a Bacterial Tyrosine Kinase and Its Cognate Phosphatase*
- Phosphoproteomics of Klebsiella pneumoniae NTUH-K2044 Reveals a Tight Link between Tyrosine Phosphorylation and Virulence*
- Bacterial Phosphoproteomic Analysis Reveals the Correlation Between Protein Phosphorylation and Bacterial Pathogenicity
- Phosphoproteome of the cyanobacterium Synechocystis sp. PCC 6803 and its dynamics during nitrogen starvation
- Molecular mechanisms of probiotic action: a proteomic perspective.
- Analysis of the phosphoproteome of the multicellular bacterium Streptomyces coelicolor A3(2) by protein/peptide fractionation, phosphopeptide enrichment and high‐accuracy mass spectrometry
- Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae.
- Analysis of the serine/threonine/tyrosine phosphoproteome of the pathogenic bacterium Listeria monocytogenes reveals phosphorylated proteins related to virulence
- Protein phosphorylation from the perspective of systems biology.
- Characterization of Riemerella anatipestifer CH-1 gldJ gene and GldJ protein.
- Quantitative analysis of phosphorylation-based protein signaling networks in the immune system by mass spectrometry
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