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Aminoglycoside 2′′-Phosphotransferase IIIa (APH(2′′)-IIIa) Prefers GTP over ATPFancy meeting you here! A fresh look at "prokaryotic" protein phosphorylationExpression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknBNew protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression.Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family.Cells of Escherichia coli contain a protein-tyrosine kinase, Wzc, and a phosphotyrosine-protein phosphatase, WzbThe eukaryotic-type serine/threonine protein kinase Stk is required for biofilm formation and virulence in Staphylococcus epidermidisThe predicted amino acid sequence of the Salmonella typhimurium virulence gene mviAA(+) strongly indicates that MviA is a regulator protein of a previously unknown S. typhimurium response regulator family.Phosphorylation of Mycoplasma pneumoniae cytadherence-accessory proteins in cell extractsTyrosine phosphorylation in Myxococcus xanthus, a multicellular prokaryote.Identification of two eukaryote-like serine/threonine kinases encoded by Chlamydia trachomatis serovar L2 and characterization of interacting partners of Pkn1Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens.A novel bacterial tyrosine kinase essential for cell division and differentiationLegionella pneumophila invasion of MRC-5 cells induces tyrosine protein phosphorylation.Molecular cloning and functional expression of a protein-serine/threonine phosphatase from the hyperthermophilic archaeon Pyrodictium abyssi TAG11.Staphylococcus aureus contains two low-molecular-mass phosphotyrosine protein phosphatases.In vivo and in vitro phosphorylation of rotavirus NSP5 correlates with its localization in viroplasms.Tyrosine phosphorylation of protein kinase Wzc from Escherichia coli K12 occurs through a two-step process.A novel protein kinase that controls carbon catabolite repression in bacteria.The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host cell protein kinases but is not itself a protein kinase.On the binding of ATP to the autophosphorylating protein, Ptk, of the bacterium Acinetobacter johnsonii
P2860
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P2860
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
ATP-dependent protein kinases in bacteria.
@en
type
label
ATP-dependent protein kinases in bacteria.
@en
prefLabel
ATP-dependent protein kinases in bacteria.
@en
P356
P1476
ATP-dependent protein kinases in bacteria.
@en
P2093
A J Cozzone
P356
10.1002/JCB.240510103
P577
1993-01-01T00:00:00Z