Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases.
about
Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine.Bacterial tyrosine kinases: evolution, biological function and structural insightsMicrobial protein-tyrosine kinasesAutophosphorylation of the Bacterial Tyrosine-Kinase CpsD Connects Capsule Synthesis with the Cell Cycle in Streptococcus pneumoniaeStructure of Escherichia coli tyrosine kinase Etk reveals a novel activation mechanismStructural Basis for the Regulation Mechanism of the Tyrosine Kinase CapB from Staphylococcus aureusStructure Analysis of the Staphylococcus aureus UDP- N -acetyl-mannosamine Dehydrogenase Cap5O Involved in Capsular Polysaccharide BiosynthesisComparative analysis of the Tyr-kinases CapB1 and CapB2 fused to their cognate modulators CapA1 and CapA2 from Staphylococcus aureusMechanistic Basis of Antimicrobial Actions of Silver NanoparticlesTyrosine phosphorylation of the UDP-glucose dehydrogenase of Escherichia coli is at the crossroads of colanic acid synthesis and polymyxin resistanceCross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residuesProtein-tyrosine phosphorylation interaction network in Bacillus subtilis reveals new substrates, kinase activators and kinase cross-talkBacillus subtilis serine/threonine protein kinase YabT is involved in spore development via phosphorylation of a bacterial recombinaseMcsA and B mediate the delocalization of competence proteins from the cell poles of Bacillus subtilis.In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqECharacterization and site-directed mutagenesis of Wzb, an O-phosphatase from Lactobacillus rhamnosus.Evolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substratesStreptococcus pneumoniae phosphotyrosine phosphatase CpsB and alterations in capsule production resulting from changes in oxygen availability.FlgN is required for flagellum-based motility by Bacillus subtilis.The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain.Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis.Self-regulation of exopolysaccharide production in Bacillus subtilis by a tyrosine kinase.Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpCSolution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilisSer/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established.A Combinatorial Kin Discrimination System in Bacillus subtilisProtein-tyrosine phosphorylation in Bacillus subtilis: a 10-year retrospective.A tyrosine phosphorylation switch controls the interaction between the transmembrane modulator protein Wzd and the tyrosine kinase Wze of Lactobacillus rhamnosusFunctional analysis of Burkholderia cepacia genes bceD and bceF, encoding a phosphotyrosine phosphatase and a tyrosine autokinase, respectively: role in exopolysaccharide biosynthesis and biofilm formation.Control of EpsE, the phosphoglycosyltransferase initiating exopolysaccharide synthesis in Streptococcus thermophilus, by EpsD tyrosine kinaseFunctional genomics of gram-positive microorganismsComparative genomics of enterococci: variation in Enterococcus faecalis, clade structure in E. faecium, and defining characteristics of E. gallinarum and E. casseliflavus.The Bacterial Tyrosine Kinase Activator TkmA Contributes to Biofilm Formation Largely Independently of the Cognate Kinase PtkA in Bacillus subtilis.A new tyrosine phosphorylation mechanism involved in signal transduction in Bacillus subtilis.Protein-tyrosine phosphorylation in Bacillus subtilis.Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens.Tyrosine Phosphorylation and Dephosphorylation in Burkholderia cenocepacia Affect Biofilm Formation, Growth under Nutritional Deprivation, and PathogenicityComparative transcriptomic analysis of the Burkholderia cepacia tyrosine kinase bceF mutant reveals a role in tolerance to stress, biofilm formation, and virulence.Regulatory interactions between a bacterial tyrosine kinase and its cognate phosphatase.
P2860
Q25255885-F9A915DB-EEC3-4EB3-80A7-619291359B6AQ27016005-4E9C4656-46C9-4715-BE5B-B44C1F8BA6DEQ27022003-EDB5E390-8278-4E13-9D79-16B8781BD9DBQ27310278-08AC0FCA-3867-4324-8637-AF11AB897510Q27650660-7CAF46AF-1A36-4381-9081-FD8F04B9B3DCQ27650793-0F8AAC2B-29AE-4CBD-94B8-70609DCE9BBCQ27667366-812A6DCE-98AB-443D-986D-D16827E59606Q27680416-44B3221B-9DF0-4E96-8E9E-5A959B4FF0B3Q28079834-93AAE343-D434-421D-9F57-CA7A3DBAA916Q28473483-A8C71557-784F-46F8-97A6-0A375F1937ACQ29346685-DD63C856-86AB-4EE2-AF0B-2B46940AACF0Q29346708-1D7EC592-DB42-4A7E-846C-3AB1B8FBE8D4Q30541337-2B5EC870-A80C-4C5A-9401-B8B8E752DA9CQ30650314-998E66B2-5A7C-4314-B34A-49E6DDF251FAQ30988742-5112FEE7-C8E1-4EA6-B74E-9867416D13A4Q33326892-487DF2C6-DD95-4F1A-89A7-FD6AF213FD13Q33556655-1B99F75C-2082-4317-BAAE-ABB9C6D87CE8Q33570187-C8493176-E46D-4FD4-B4EA-BF193232ED39Q33743275-78F95DF3-C6B1-470E-B4B6-FAE0128DA03DQ33743505-3BFD0C70-A9C6-44F0-AD44-927E446BB928Q33815417-6A14501C-FA17-47FB-BFEB-F45289027BCAQ33885797-12B76C76-3BD7-4199-97B4-7AF46BEB2AB6Q33984513-0E89BF43-E306-4231-A830-9C8B70DC4F0CQ34018040-75D68BD0-3075-4839-84FE-18E3B93ACCADQ34353771-29D31FE8-1BAB-4279-9799-94D028AEF787Q34484994-3B118EC7-A745-4EFB-8AFA-63ED0F9D22B1Q34516055-97D0163B-801A-44CC-B05C-6D1F8F7F4316Q35005370-6BDFE785-D618-41FB-9856-7388D77C47EEQ35606163-0354107F-5459-4D20-824F-F25110453758Q35633491-523D0937-3C86-4C2C-A40C-121AAEE4D93FQ35634725-1745199C-A9E9-4F5D-8C48-4AE5D44CC920Q35648492-A3506E6B-DC36-4689-97C1-AD9C6D9CE914Q36029203-D8682571-AC26-457F-8825-C6A32265F1C1Q36207973-55F18FD5-A57A-419B-88FC-A93FF66D40B7Q36369658-693AEA77-8229-48F3-8D06-F1BA14AA6175Q36369661-D543EF27-736B-40FC-B8C0-3E67325BEA96Q36369665-EDF4104D-CB7E-4B27-9660-B57DC440F2D5Q36497517-B476494E-C8C0-4DC8-B75F-06434F1A5987Q36757155-5E9DB84C-DFCA-46FC-973C-F9E57B94C2A6Q36873686-54B21AB9-CA06-4FB6-B123-571CB26EB035
P2860
Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
Transmembrane modulator-depend ...... es UDP-glucose dehydrogenases.
@en
Transmembrane modulator-depend ...... es UDP-glucose dehydrogenases.
@nl
type
label
Transmembrane modulator-depend ...... es UDP-glucose dehydrogenases.
@en
Transmembrane modulator-depend ...... es UDP-glucose dehydrogenases.
@nl
prefLabel
Transmembrane modulator-depend ...... es UDP-glucose dehydrogenases.
@en
Transmembrane modulator-depend ...... es UDP-glucose dehydrogenases.
@nl
P2093
P2860
P50
P921
P356
P1433
P1476
Transmembrane modulator-depend ...... es UDP-glucose dehydrogenases.
@en
P2093
Alain Mazé
Emmanuel Jamet
Grégory Boël
Patricia Doublet
Paulette Decottignies
Pierre Le Maréchal
Sandrine Poncet
Sylvie Gillet
P2860
P304
P356
10.1093/EMBOJ/CDG458
P407
P577
2003-09-01T00:00:00Z