A novel mode of regulation of the Staphylococcus aureus catabolite control protein A (CcpA) mediated by Stk1 protein phosphorylation - Wikidata - wikimedia - TriplyDB

A novel mode of regulation of the Staphylococcus aureus catabolite control protein A (CcpA) mediated by Stk1 protein phosphorylation

A novel mode of regulation of the Staphylococcus aureus catabolite control protein A (CcpA) mediated by Stk1 protein phosphorylation

http://www.wikidata.org/entity/Q36481806

about

Regulating the Intersection of Metabolism and Pathogenesis in Gram-positive Bacteria Ser/Thr phosphorylation as a regulatory mechanism in bacteria Molecular Events for Promotion of Vancomycin Resistance in Vancomycin Intermediate Staphylococcus aureus Protein kinase B (PknB) of Mycobacterium tuberculosis is essential for growth of the pathogen in vitro as well as for survival within the host.CcpA Affects Infectivity of Staphylococcus aureus in a Hyperglycemic Environment A novel STK1-targeted small-molecule as an "antibiotic resistance breaker" against multidrug-resistant Staphylococcus aureus.Catabolite control protein A is an important regulator of metabolism in Streptococcus suis type 2.The catabolite control protein E (CcpE) affects virulence determinant production and pathogenesis of Staphylococcus aureus Phosphorylation of Mycobacterium tuberculosis ParB participates in regulating the ParABS chromosome segregation system Impact of the Regulators SigB, Rot, SarA and sarS on the Toxic Shock Tst Promoter and TSST-1 Expression in Staphylococcus aureus Carbon Catabolite Repression and the Related Genes of ccpA, ptsH and hprK in Thermoanaerobacterium aotearoense.Regulatory Requirements for Staphylococcus aureus Nitric Oxide Resistance Protein-serine/threonine/tyrosine kinases in bacterial signaling and regulation.Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens.A screen for kinase inhibitors identifies antimicrobial imidazopyridine aminofurazans as specific inhibitors of the Listeria monocytogenes PASTA kinase PrkA.Do Shoot the Messenger: PASTA Kinases as Virulence Determinants and Antibiotic Targets.Ser/Thr protein kinase PrkC-mediated regulation of GroEL is critical for biofilm formation in Bacillus anthracis.Identification of catabolite control protein A from Staphylococcus aureus as a target of silver ions.Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments

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A novel mode of regulation of the Staphylococcus aureus catabolite control protein A (CcpA) mediated by Stk1 protein phosphorylation

http://www.wikidata.org/entity/Q36481806

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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2012年學術文章

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JBC.M112.418913

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Journal of Biological Chemistry

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Frédéric Delolme

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Jade Leiba

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Marie-Eve Cluzel

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Martin Cohen-Gonsaud

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Torsten Hartmann

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P2860

Regulation of hemolysin expression and virulence of Staphylococcus aureus by a serine/threonine kinase and phosphatase

The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue

Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism

Phosphorylation of InhA inhibits mycolic acid biosynthesis and growth of Mycobacterium tuberculosis

Protein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance

Staphylococcus aureus infections

Phosphorylation of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis

An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis

Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria

An improved method to unravel phosphoacceptors in Ser/Thr protein kinase-phosphorylated substrates

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43607-43619

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10.1074/JBC.M112.418913

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52

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287

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Markus Bischoff

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2012-11-06T00:00:00Z

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23132867

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phosphorylation

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3527947

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