Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria.
about
BYKdb: the Bacterial protein tYrosine Kinase databaseProtein phosphorylation and regulation of adaptive responses in bacteriaChemotaxis in Bacillus subtilis requires either of two functionally redundant CheW homologsBacterial chemotaxis: the early years of molecular studiesArchaeal protein kinases and protein phosphatases: insights from genomics and biochemistryChemotaxis of bacteria in glass capillary arrays. Escherichia coli, motility, microchannel plate, and light scatteringA PAS domain binds asparagine in the chemotaxis receptor McpB in Bacillus subtilisA framework for classification of prokaryotic protein kinasesAn Overview of Two-Component Signal Transduction Systems Implicated in Extra-Intestinal Pathogenic E. coli InfectionsCalcium(II) site specificity: effect of size and charge on metal ion binding to an EF-hand-like site19F NMR studies of the D-galactose chemosensory receptor. 1. Sugar binding yields a global structural change.How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.Three strategically placed hydrogen-bonding residues convert a proton pump into a sensory receptorInhibition of Escherichia coli chemotaxis by omega-conotoxin, a calcium ion channel blockerIs cross regulation by phosphorylation of two-component response regulator proteins important in bacteria?Mutational analysis of the regulatory region of the srfA operon in Bacillus subtilis.The Alcaligenes eutrophus H16 hoxX gene participates in hydrogenase regulationSubcellular localization and immunological detection of proteins encoded by the vir locus of Bordetella pertussisTranscription initiation region of the srfA operon, which is controlled by the comP-comA signal transduction system in Bacillus subtilisIdentification and sequence analysis of the hupR1 gene, which encodes a response regulator of the NtrC family required for hydrogenase expression in Rhodobacter capsulatusTranscriptional organization of a cloned chemotaxis locus of Bacillus subtilisThe Cpx proteins of Escherichia coli K-12: evidence that cpxA, ecfB, ssd, and eup mutations all identify the same gene.Identification of phosphate starvation-inducible genes in Escherichia coli K-12 by DNA sequence analysis of psi::lacZ(Mu d1) transcriptional fusions.Analysis of Bordetella pertussis virulence gene regulation by use of transcriptional fusions in Escherichia coliGrowth-phase-dependent expression of the Pseudomonas putida TOL plasmid pWW0 catabolic genes.Effect of outer membrane permeability on chemotaxis in Escherichia coliCritical regions of the Vibrio fischeri luxR protein defined by mutational analysis."Frozen" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors.Organization of the aerotaxis receptor aer in the membrane of Escherichia coliBglG, the response regulator of the Escherichia coli bgl operon, is phosphorylated on a histidine residue.Mutational analysis of the VirG protein, a transcriptional activator of Agrobacterium tumefaciens virulence genes.Identification of cyclic AMP as the response regulator for neurosecretory potentiation: a memory model system.Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY.FlbD of Caulobacter crescentus is a homologue of the NtrC (NRI) protein and activates sigma 54-dependent flagellar gene promoters.Genetic and behavioral analysis of flagellar switch mutants of Salmonella typhimurium.The mammalian mitogen activated protein kinase network.Involvement of Two-Component Signaling on Bacterial Motility and Biofilm Development.
P2860
Q24621380-49A05549-3CE2-4C8A-9577-B1247F854954Q24634755-EAA9F2FC-0672-48B2-A831-C00861D64B2BQ28488864-17AD1B5B-F8CE-4874-A630-0C6E42369460Q28659940-D9F081B4-4BBD-40CF-B58F-31488A5DD317Q28769396-DA71F3F1-70B8-43E8-A655-9C8CA9ACB258Q31054313-5BB67847-32B3-41B4-A05F-A5F474CAF404Q33581948-ECF1F186-53DC-4881-822F-58BB449AFEEBQ33592975-EE34A6A1-A279-4C2E-BF15-0FF0C2D758BEQ33650044-B1E9F256-7C92-48BE-9433-4E93832AA0DDQ33973419-36D1F256-0A66-4A91-A454-FC2756BB1B41Q33997058-9EB34D23-3D71-4DCB-8AC9-DC73928C8041Q34090837-8DDB5D52-6B5B-4CAA-803C-E88819417D3DQ35133704-17204663-AA29-4D04-8C58-C74E39780293Q35911828-D5D5A894-E0F1-4857-8B0F-DC158226D5CBQ35934884-D7A817D8-24E9-4F87-8A83-DD02661B8643Q36100306-AED03350-0471-4DE5-9306-E5D4D63D23A5Q36109156-930FDD5F-C82D-49CD-8E03-23E4C58F55AEQ36149195-06FB58DF-75A2-4ED3-B1E1-94C6786707AFQ36152660-664207B5-AA93-4BEE-AB0E-8C489F993DA7Q36154344-CD715CE4-3700-4FE5-AD5A-41B9BC6FD0E0Q36159903-64E71EAA-DC94-43D3-AC40-F38046AAD450Q36162171-D42574A0-8704-4C5C-BABD-C566FF6A53F6Q36165143-3F7F85F7-F69E-4780-8E52-F6413D200FB2Q36184454-3D4E0A3B-D109-48F4-993E-76769856C8ACQ36190843-C28178E5-ABAC-4827-8D2D-A9C721898D08Q36256755-BAF003AC-5DF7-406F-A67C-57B2969C6924Q36257362-248D24B8-C07D-440A-8F70-42B9D2220E8AQ36278622-EA386A53-1F0F-46DA-8006-F08B54BA199DQ36314219-1549AA00-35A3-4180-A4A7-6A2C29ECA985Q36881268-B4C78778-E6BE-456B-A2A5-E5EEBF596F5DQ37609009-8DF23918-048F-4936-8B55-6E55B3483CD7Q37636335-4CBA421A-4ADE-4B49-8EF4-35738E829D07Q37656265-B2D45CCC-7C07-49F4-97FB-70B5D9ED3CD2Q37724161-36208E1F-2C9A-42BE-9695-AAEAFE8E8F96Q39960523-2B250A19-3FA4-4768-9B3C-1778C810C854Q40849045-B8F13FA7-C48F-4E6D-B7F8-FEA298972184Q50256445-F5A0E0EC-2229-46C8-9C1D-36ED55BA3896
P2860
Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh
1989年學術文章
@zh-hant
name
Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria.
@en
type
label
Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria.
@en
prefLabel
Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria.
@en
P2093
P1476
Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria.
@en
P2093
P304
P407
P577
1989-05-01T00:00:00Z