ArticleJournal of proteome research2009
Identification of serine/threonine kinase substrates in the human pathogen group B streptococcus.
Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Article
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- Dynamic Protein Phosphorylation inMicroorganisms · 2024Article
- Ligand-Based Design of Novel Quinoline Derivatives as Potential Anticancer Agents: An In-Silico Virtual Screening Approach.Molecules (Basel, Switzerland) · 2024Article
- eCell Technology for Cell-Free Protein Synthesis, Biosensing, and Remediation.Advances in biochemical engineering/biotechnology · 2023Article
- IreK-Mediated, Cell Wall-Protective Phosphorylation inJournal of proteome research · 2021Article
- Tumor reversion: a dream or a reality.Biomarker research · 2021Review
- ¡vIVA la DivIVA!Journal of bacteriology · 2019Review
- Identification of Hanks-Type Kinase PknB-Specific Targets in theFrontiers in microbiology · 2019Article
- Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments.International journal of molecular sciences · 2018Review
- Article
- Structure and Dimerization of IreB, a Negative Regulator of Cephalosporin Resistance in Enterococcus faecalis.Journal of molecular biology · 2017Article
- The Eukaryote-Like Serine/Threonine Kinase STK Regulates the Growth and Metabolism of ZoonoticFrontiers in cellular and infection microbiology · 2017Article
- The sensor histidine kinase RgfC affects group B streptococcal virulence factor expression independent of its response regulator RgfA.Infection and immunity · 2015Article
- Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens.Virulence · 2014Review
- IreB, a Ser/Thr kinase substrate, influences antimicrobial resistance in Enterococcus faecalis.Antimicrobial agents and chemotherapy · 2013Article
- The Abi-domain protein Abx1 interacts with the CovS histidine kinase to control virulence gene expression in group B Streptococcus.PLoS pathogens · 2013Article
- Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Serine/threonine phosphatase Stp1 mediates post-transcriptional regulation of hemolysin, autolysis, and virulence of group B Streptococcus.The Journal of biological chemistry · 2011Article
- Aspects of eukaryotic-like signaling in Gram-positive cocci: a focus on virulence.Future microbiology · 2011Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
All living organisms respond to changes in their internal and external environment for their survival and existence. Signaling is primarily achieved through reversible phosphorylation of proteins in both prokaryotes and eukaryotes. A change in the phosphorylation state of a protein alters its function to enable the control of cellular responses. A number of serine/threonine kinases regulate the cellular responses of eukaryotes. Although common in eukaryotes, serine/threonine kinases have only recently been identified in prokaryotes. We have described that the human pathogen Group B Streptococcus (GBS, Streptococcus agalactiae) encodes a single membrane-associated, serine/threonine kinase (Stk1) that is important for virulence of this bacterium. In this study, we used a combination of phosphopeptide enrichment and mass spectrometry to enrich and identify serine (S) and threonine (T) phosphopeptides of GBS. A comparison of S/T phosphopeptides identified from the Stk1 expressing strains to the isogenic stk1 mutant indicates that 10 proteins are potential substrates of the GBS Stk1 enzyme. Some of these proteins are phosphorylated by Stk1 in vitro and a site-directed substitution of the phosphorylated threonine to an alanine abolished phosphorylation of an Stk1 substrate. Collectively, these studies provide a novel approach to identify serine/threonine kinase substrates for insight into their signaling in human pathogens like GBS.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.