Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator
about
Prokaryotic 2-component systems and the OmpR/PhoB superfamilyThe Pho regulon: a huge regulatory network in bacteriaStructure and dynamics of polymyxin-resistance-associated response regulator PmrA in complex with promoter DNAThe crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interfaceThe X-ray Crystal Structures of Two Constitutively Active Mutants of the Escherichia coli PhoB Receiver Domain Give Insights into ActivationStructural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB SubfamilyThree-dimensional structure of MecI. Molecular basis for transcriptional regulation of staphylococcal methicillin resistanceSolution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificityStructure of the response regulator VicR DNA-binding domainStructure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanismDomain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated stateStructure of the DNA-Binding Domain of the Response Regulator PhoP from Mycobacterium tuberculosis † , ‡Response regulator YycF essential for bacterial growth: X-ray crystal structure of the DNA-binding domain and its PhoB-like DNA recognition motifStructure of the Response Regulator PhoP from Mycobacterium tuberculosis Reveals a Dimer through the Receiver DomainThe structure of a transcription activation subcomplex reveals how σ70is recruited to PhoB promotersStructure-Function Studies of DNA Binding Domain of Response Regulator KdpE Reveals Equal Affinity Interactions at DNA Half-SitesThe dimeric form of the unphosphorylated response regulator BaeRSolution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniaeAtypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA BindingSolution Structure and DNA-binding Properties of the Winged Helix Domain of the Meiotic Recombination HOP2 ProteinStructural dynamics of the two-component response regulator RstA in recognition of promoter DNA elementHemR is an OmpR/PhoB-like response regulator from Leptospira, which simultaneously effects transcriptional activation and repression of key haem metabolism genesStructure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureusThe phosphate regulon and bacterial virulence: a regulatory network connecting phosphate homeostasis and pathogenesisThe atypical OmpR/PhoB response regulator ChxR from Chlamydia trachomatis forms homodimers in vivo and binds a direct repeat of nucleotide sequencesThe two faces of ToxR: activator of ompU, co-regulator of toxT in Vibrio choleraeTranscription of the pst operon of Clostridium acetobutylicum is dependent on phosphate concentration and pHThe structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosisPhosphorylation of PhoP protein plays direct regulatory role in lipid biosynthesis of Mycobacterium tuberculosisPhoB activates Escherichia coli O157:H7 virulence factors in response to inorganic phosphate limitationA biochemical characterization of the DNA binding activity of the response regulator VicR from Streptococcus mutansPhosphorylation-dependent derepression by the response regulator HnoC in the Shewanella oneidensis nitric oxide signaling networkGenes regulated by TorR, the trimethylamine oxide response regulator of Shewanella oneidensis.Defining the plasticity of transcription factor binding sites by Deconstructing DNA consensus sequences: the PhoP-binding sites among gamma/enterobacteria.Fine-tuning of galactoglucan biosynthesis in Sinorhizobium meliloti by differential WggR (ExpG)-, PhoB-, and MucR-dependent regulation of two promotersCompetitive and cooperative effects in quorum-sensing-regulated galactoglucan biosynthesis in Sinorhizobium meliloti.A threading-based method for the prediction of DNA-binding proteins with application to the human genome.Distinct single amino acid replacements in the control of virulence regulator protein differentially impact streptococcal pathogenesisA structural model of the E. coli PhoB dimer in the transcription initiation complex.
P2860
Q26783533-2DB2AE2A-7F8A-40A5-956C-67360918E3BAQ26866942-97D0063A-285A-4EF9-B3FC-3CC21737F97EQ27318559-9D5F6CCB-726E-41C8-9147-7934EA803039Q27640175-332BAA4E-C814-472E-9BEB-D1A439654ACFQ27640869-1B35B7C4-3CA0-4772-B485-787443C30181Q27641594-308C2CAD-F5ED-4221-B0D5-AD247F443421Q27641736-DB81C965-9514-4ACA-AB23-A7FD306C0359Q27642600-4A49ADE8-9105-41D1-B7A4-1A8126E1EC58Q27643628-9908E195-745D-4640-98B6-6412FA91ACDDQ27644734-84721A81-F00E-4F39-9F8A-64C1398D1BA9Q27644822-CF340810-3802-42AF-85EB-7930087C1F97Q27648812-1BDCA959-8381-43B8-8DD2-D6FCEE0B4CCFQ27649175-95D82D9D-2D70-4CCE-9BFC-F9CC345105C7Q27652137-88B0FF5D-F266-4DEB-85A5-595FA67BCAA3Q27668141-DB3D70BA-145D-412E-814E-5F3719BB219BQ27671645-79B4282E-6F27-494A-8C9E-8BE515B3B53BQ27676961-C646BCA5-88D8-4602-8DD0-34194320F8A3Q27679136-0991F787-9B19-460F-88ED-B846B6653CA8Q27681103-254F6373-32CA-4D1E-8719-8B11E32D7D50Q27682297-CA894D42-93F2-41FF-8D5D-1A51086C1C99Q27683102-5410A0A8-025C-4B63-94BD-8C4BD9875F77Q27684524-21E8183B-88B0-40B6-82DA-1C87E52069BBQ27694804-BA9EA1A3-0720-4C51-BCEB-02C795A7A2F1Q27701754-235E8063-EFCE-40FE-AE78-025125A0A2DBQ28267290-19A1EA86-4439-4D9E-B535-E160E3E17CCFQ28484740-AF3D90FC-1B2F-4712-96DC-91A8F11435BBQ28485729-7CFA83CA-1275-4C37-9A92-5F9EC34FECA5Q28485889-FD4953A4-E37C-4E6E-B4DB-28D291B35DA0Q28487093-1FC56BCA-70BF-45E1-B21A-606328EB15A1Q28487131-D2779D6A-DD1D-4D31-A5B3-D1FAADBA30BAQ28542075-718254B7-7802-4963-B852-3A8D2836C854Q28543046-11A4755F-4363-4B77-817B-95A1816F3697Q29346661-A582E5C0-8930-42C7-A658-B224183AE3C2Q29346666-3F1F053A-776B-4121-8C69-FC676D264D5CQ29346719-8C786119-B6CE-4EBF-A18A-1ED348F4A223Q29346921-4C7C3F39-194F-404D-93F8-571AC6590742Q29346929-18A3B949-9C10-46BD-94A7-F47CE66E3465Q30382494-6EFA9D9B-D390-4632-A78A-8ED2A98F4EC7Q30408643-9AE24510-1F00-4E23-81A7-D35A69D71F7BQ30513996-8196CAE2-0B3D-477F-80BF-0BFCC6F4E294
P2860
Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Tandem DNA recognition by PhoB ...... tion transcriptional activator
@ast
Tandem DNA recognition by PhoB ...... tion transcriptional activator
@en
Tandem DNA recognition by PhoB ...... tion transcriptional activator
@nl
type
label
Tandem DNA recognition by PhoB ...... tion transcriptional activator
@ast
Tandem DNA recognition by PhoB ...... tion transcriptional activator
@en
Tandem DNA recognition by PhoB ...... tion transcriptional activator
@nl
prefLabel
Tandem DNA recognition by PhoB ...... tion transcriptional activator
@ast
Tandem DNA recognition by PhoB ...... tion transcriptional activator
@en
Tandem DNA recognition by PhoB ...... tion transcriptional activator
@nl
P50
P3181
P1433
P1476
Tandem DNA recognition by PhoB ...... tion transcriptional activator
@en
P2093
Alexandre G Blanco
P304
P3181
P356
10.1016/S0969-2126(02)00761-X
P577
2002-05-01T00:00:00Z