Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis - Wikidata - wikimedia - TriplyDB

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

http://www.wikidata.org/entity/Q35982784

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The genome of the obligate intracellular parasite Trachipleistophora hominis: new insights into microsporidian genome dynamics and reductive evolution Impact of Serine/Threonine Protein Kinases on the Regulation of Sporulation in Bacillus subtilis Role of Protein Phosphorylation in the Regulation of Cell Cycle and DNA-Related Processes in Bacteria The cell pole: the site of cross talk between the DNA uptake and genetic recombination machinery The aspartate-less receiver (ALR) domains: distribution, structure and function Chasing Phosphoarginine Proteins: Development of a Selective Enrichment Method Using a Phosphatase Trap Arginine phosphorylation marks proteins for degradation by a Clp protease Protein phosphorylation and its role in archaeal signal transduction Chemoselective synthesis and analysis of naturally occurring phosphorylated cysteine peptides Protein-tyrosine phosphorylation interaction network in Bacillus subtilis reveals new substrates, kinase activators and kinase cross-talk Bacillus subtilis serine/threonine protein kinase YabT is involved in spore development via phosphorylation of a bacterial recombinase Meta-Analysis of Arabidopsis thaliana Phospho-Proteomics Data Reveals Compartmentalization of Phosphorylation Motifs.Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance.FlgN is required for flagellum-based motility by Bacillus subtilis.clpC operon regulates cell architecture and sporulation in Bacillus anthracis.dbPSP: a curated database for protein phosphorylation sites in prokaryotes.Chemical biology of protein arginine modifications in epigenetic regulation Phosphoproteome dynamics mediate revival of bacterial spores Interactive regulation by the Bacillus subtilis global regulators CodY and ScoC.Roles of adaptor proteins in regulation of bacterial proteolysis Technologies and challenges in large-scale phosphoproteomics.Orphan PTMs: Rare, yet functionally important modifications of cysteine.Protein-serine/threonine/tyrosine kinases in bacterial signaling and regulation.From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division?Biofilm formation by Bacillus subtilis: new insights into regulatory strategies and assembly mechanisms.Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens.Activity-Based Profiling Reveals a Regulatory Link between Oxidative Stress and Protein Arginine Phosphorylation.Synthesis and Use of a Phosphonate Amidine to Generate an Anti-Phosphoarginine-Specific Antibody Role of eukaryotic-like serine/threonine kinases in bacterial cell division and morphogenesis.Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis.Exploring the diversity of protein modifications: special bacterial phosphorylation systems.Chemical Approaches to Studying Labile Amino Acid Phosphorylation.Selective adaptor dependent protein degradation in bacteria.Factors that mediate and prevent degradation of the inactive and unstable GudB protein in Bacillus subtilis.Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response.Protein-protein interaction domains of Bacillus subtilis DivIVA.The role of thiol oxidative stress response in heat-induced protein aggregate formation during thermotolerance in Bacillus subtilis.Spectral library based analysis of arginine phosphorylations in Staphylococcus aureus.Recent advances in phosphoproteomics and application to neurological diseases.Development of a stable phosphoarginine analog for producing phosphoarginine antibodies.

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P2860

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

http://www.wikidata.org/entity/Q35982784

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name

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

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Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

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Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

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Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

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prefLabel

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

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Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

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PNAS.1117483109

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

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P2093

Alexander K W Elsholz

http://www.w3.org/2001/XMLSchema#string

Bernd Hessling

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Dan Oertel

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Dörte Becher

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Jörg Bernhardt

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Katrin Gronau

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Kürsad Turgay

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Michael Hecker

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Ulf Gerth

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Ulrike Mäder

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P2860

Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor.

McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR

Adaptor protein controlled oligomerization activates the AAA+ protein ClpC

McsA and B mediate the delocalization of competence proteins from the cell poles of Bacillus subtilis.

Two-component and phosphorelay signal transduction.

Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.

Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established.

MecA, an adaptor protein necessary for ClpC chaperone activity.

Localization of general and regulatory proteolysis in Bacillus subtilis cells.

Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases.

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10.1073/PNAS.1117483109

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19

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109

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Stephan Michalik

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2012-04-19T00:00:00Z

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224770152

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22517742

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protein arginine kinase activity

phosphorylation

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3358850

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