How to Switch Off a Histidine Kinase: Crystal Structure of Geobacillus stearothermophilus KinB with the inhibitor Sda
about
Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution stateStructural Insights into High Density Lipoprotein: Old Models and New FactsCell fate regulation governed by a repurposed bacterial histidine kinaseStructural plasticity and catalysis regulation of a thermosensor histidine kinaseStructure of the cytoplasmic segment of histidine kinase receptor QseC, a key player in bacterial virulenceStructural insights into ChpT, an essential dimeric histidine phosphotransferase regulating the cell cycle inCaulobacter crescentusInsight into the sporulation phosphorelay: Crystal structure of the sensor domain ofBacillus subtilishistidine kinase, KinDBranched Signal Wiring of an Essential Bacterial Cell-Cycle Phosphotransfer ProteinSegmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylationVisualizing autophosphorylation in histidine kinasesIn vivo domain-based functional analysis of the major sporulation sensor kinase, KinA, in Bacillus subtilisSinorhizobium meliloti CheA complexed with CheS exhibits enhanced binding to CheY1, resulting in accelerated CheY1 dephosphorylationThe regulatory factor SipA is a highly stable beta-II class protein with a SH3 fold.Small-angle scattering for structural biology--expanding the frontier while avoiding the pitfalls.The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12.Protein histidine kinases: assembly of active sites and their regulation in signaling pathways.An expanding universe of small proteins.Dynamical consequences of bandpass feedback loops in a bacterial phosphorelaySmall proteins can no longer be ignoredDeterminants of homodimerization specificity in histidine kinases.Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesisHelix bundle loops determine whether histidine kinases autophosphorylate in cis or in trans.Putative histidine kinase inhibitors with antibacterial effect against multi-drug resistant clinical isolates identified by in vitro and in silico screens.Biological insights from structures of two-component proteins.Recent progress in Bacillus subtilis sporulation.Control of Initiation of DNA Replication in Bacillus subtilis and Escherichia coli.Phosphorylation of Spo0A by the histidine kinase KinD requires the lipoprotein med in Bacillus subtilis.Crystallization and preliminary X-ray analysis of a putative sensor histidine kinase domain: the C-terminal domain of HksP4 from Aquifex aeolicus VF5.Oligomeric sensor kinase DcuS in the membrane of Escherichia coli and in proteoliposomes: chemical cross-linking and FRET spectroscopy.Mechanistic insight into inhibition of two-component system signaling.Sensor kinase KinB and its pathway-associated key factors sense the signal of nutrition starvation in sporulation of Bacillus subtilis.Small-Angle Scattering of Neutrons and X-RaysFlexibility and constraint: Evolutionary remodeling of the sporulation initiation pathway in Firmicutes
P2860
Q24652923-B0A8BE34-A80B-427F-AA3A-A87DCE4E04F4Q26770434-6B11769B-5CB5-4452-80E1-553604E774FFQ27313783-977FD32C-29CE-4494-BA37-3F9EAA859D46Q27657688-20E8142F-D7EB-4D51-A381-620607C9DC1DQ27662940-456FF9E6-F947-4C02-98FD-FDDD0CC5E6D7Q27672069-4919E0B7-9C3E-4600-BF7D-C6EE061A4051Q27676622-0C6CA847-BCC5-4FDC-84C1-570653406C68Q27679497-9C826197-269D-4559-BB22-DBA262E9B19DQ27681573-EFCFC4CD-7661-4F4B-94FF-618F113D1633Q27689044-DC2998E3-8869-45B8-8391-C98DEB47EFDDQ28489004-4795B4C8-8ACF-42F1-A68D-6EAA0E12770CQ28500964-6D0E4324-64DB-4CC0-8E89-F581C869D9E9Q30156982-FB02189C-6846-4E12-BA2B-291413EF15FBQ30385150-72F892B7-1FC5-4398-81F9-3A8B44D4C143Q33614907-C95DBBD3-E173-4599-8353-DA5DE217F804Q33762077-79A3077E-E36A-4E21-8145-BF418DDF75B2Q33827150-21CDF090-2A5C-40C1-9B15-EB435A1D37D6Q34042933-AEBB542B-015B-4E9F-9D62-5B0090FA7AB0Q34200467-96CC2F48-7F50-4D7B-805A-2DD5F57A8515Q35534569-2789DAC3-B1D7-48BB-8848-92BF2F27AE9DQ36068846-0BA2AFE1-2825-494D-92AD-B3FC4723C570Q36796485-A70C427F-513B-4B61-909B-07C0608D00D2Q36898003-5E810251-71AC-45E7-9575-070B868C027BQ37539921-8F06E0BD-F7E3-4878-84B8-08C6A3C16F57Q37957161-A6D94221-14E4-44A5-A246-8CA36570582FQ39079493-2C75201F-B909-4D85-8690-C9D8E1F57698Q41899167-BC0EA1D5-8A5B-4477-867A-2FEAD8427968Q42000249-F3219C53-8A91-44C7-ACD0-1275CC9E5206Q42737997-E4F62066-4422-409E-9F66-3F47F4F41EA1Q42748326-27899C1D-EB22-47BD-BBFC-6DF7CC5995FFQ47218770-FCC72EEB-8E33-490B-8DF9-71476378CD28Q57979753-87ACFC87-4B7D-4FD7-BFD4-B6684B9B4BE1Q58744478-8129088B-7239-4D6B-B0F4-DE779522B9BB
P2860
How to Switch Off a Histidine Kinase: Crystal Structure of Geobacillus stearothermophilus KinB with the inhibitor Sda
description
2009 nî lūn-bûn
@nan
2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
How to Switch Off a Histidine ...... us KinB with the inhibitor Sda
@ast
How to Switch Off a Histidine ...... us KinB with the inhibitor Sda
@en
How to Switch Off a Histidine ...... us KinB with the inhibitor Sda
@nl
type
label
How to Switch Off a Histidine ...... us KinB with the inhibitor Sda
@ast
How to Switch Off a Histidine ...... us KinB with the inhibitor Sda
@en
How to Switch Off a Histidine ...... us KinB with the inhibitor Sda
@nl
prefLabel
How to Switch Off a Histidine ...... us KinB with the inhibitor Sda
@ast
How to Switch Off a Histidine ...... us KinB with the inhibitor Sda
@en
How to Switch Off a Histidine ...... us KinB with the inhibitor Sda
@nl
P2093
P2860
P50
P3181
P1476
How to Switch Off a Histidine ...... us KinB with the inhibitor Sda
@en
P2093
Kanagalaghatta R Rajashankar
Seth A Darst
Yuliya Gordiyenko
P2860
P304
P3181
P356
10.1016/J.JMB.2008.12.006
P407
P577
2009-02-13T00:00:00Z