Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli.
about
Structural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB SubfamilyStructure of the response regulator VicR DNA-binding domainCrystal Structures of the Receiver Domain of the Response Regulator PhoP from Escherichia coli in the Absence and Presence of the Phosphoryl Analog BeryllofluorideThe structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated stateStructural dynamics of the two-component response regulator RstA in recognition of promoter DNA elementBacterial regulon evolution: distinct responses and roles for the identical OmpR proteins of Salmonella Typhimurium and Escherichia coli in the acid stress responseRemodelling of the Escherichia coli outer membrane by two small regulatory RNAsThe QseC adrenergic signaling cascade in Enterohemorrhagic E. coli (EHEC)The atypical OmpR/PhoB response regulator ChxR from Chlamydia trachomatis forms homodimers in vivo and binds a direct repeat of nucleotide sequencesIdentification and characterization of a regulatory sequence recognized by Mycobacterium tuberculosis persistence regulator MprACell cycle regulator phosphorylation stimulates two distinct modes of binding at a chromosome replication origin.Phosphorylation-dependent derepression by the response regulator HnoC in the Shewanella oneidensis nitric oxide signaling networkMutational scanning and affinity cleavage analysis of UhpA-binding sites in the Escherichia coli uhpT promoter.Protein phosphorylation affects binding of the Escherichia coli transcription activator UhpA to the uhpT promoter.Comprehensive analysis of OmpR phosphorylation, dimerization, and DNA binding supports a canonical model for activation.Determinants outside the DevR C-terminal domain are essential for cooperativity and robust activation of dormancy genes in Mycobacterium tuberculosis.Structure-function analysis of the DNA-binding domain of a transmembrane transcriptional activator.The two-component signal transduction system RR06/HK06 regulates expression of cbpA in Streptococcus pneumoniae.Segmental isotope labeling of proteins for NMR structural study using a protein S tag for higher expression and solubilityMutational analysis of the phoD promoter in Bacillus subtilis: implications for PhoP binding and promoter activation of Pho regulon promotersThe VirR response regulator from Clostridium perfringens binds independently to two imperfect direct repeats located upstream of the pfoA promoterThe TorR high-affinity binding site plays a key role in both torR autoregulation and torCAD operon expression in Escherichia coliPhosphorylated PmrA interacts with the promoter region of ugd in Salmonella enterica serovar typhimurium.Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene.EnvZ-OmpR interaction and osmoregulation in Escherichia coli.ChxR is a transcriptional activator in Chlamydia.Transcriptional activation of the Rhodobacter sphaeroides cytochrome c(2) gene P2 promoter by the response regulator PrrAResidue R113 is essential for PhoP dimerization and function: a residue buried in the asymmetric PhoP dimer interface determined in the PhoPN three-dimensional crystal structureThe critical role of DNA in the equilibrium between OmpR and phosphorylated OmpR mediated by EnvZ in Escherichia coli.DNA consensus sequence motif for binding response regulator PhoP, a virulence regulator of Mycobacterium tuberculosis.Regulation of sialic acid catabolism by the DNA binding protein NanR in Escherichia coli.Negative control of bacterial DNA replication by a cell cycle regulatory protein that binds at the chromosome origin.Differential regulation of two oligogalacturonate outer membrane channels, KdgN and KdgM, of Dickeya dadantii (Erwinia chrysanthemi).Phosphorylation stimulates the cooperative DNA-binding properties of the transcription factor OmpR.A common dimerization interface in bacterial response regulators KdpE and TorR.ChIP-seq and transcriptome analysis of the OmpR regulon of Salmonella enterica serovars Typhi and Typhimurium reveals accessory genes implicated in host colonization.Amino acids important for DNA recognition by the response regulator OmpR.Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face.System-level mapping of Escherichia coli response regulator dimerization with FRET hybrids.OmpR regulation of the uropathogenic Escherichia coli fimB gene in an acidic/high osmolality environment.
P2860
Q27641594-FE2B8880-9BD5-4BD3-8D8E-350A0F1B16D9Q27643628-80676F82-52AA-49AD-BC76-6EFC433403ACQ27645204-57B54EAE-EA50-4D0B-807D-448415184265Q27648812-56A967EC-1FDB-4538-B0DB-694B77F6B411Q27684524-6B9F79E5-0892-4CA6-8B22-5E82634766F2Q28235450-90BE3707-F02F-4BFF-B3F2-8DC7C37AD994Q28287313-4306D46A-BBED-4B19-8ADD-2DD8E4BC77A3Q28475983-6237E528-31B4-4225-AD66-C07E9700F271Q28484740-AC98C31A-08D8-4AB3-86E0-AC85E5DF5468Q28486912-131BFCAA-38FD-4E3E-BD8D-C2C0A1A07E06Q29346647-DC0D83E7-1449-4182-9385-1937727FE91BQ29346661-8F6BEB6B-094F-460A-818D-969F27502903Q30309257-64987046-B449-4DB3-B36D-19D618422A66Q30469920-6760C01C-1E2F-4746-A4FA-B3E307A43A57Q30539617-6C9E1B5E-79B0-4EA1-BC75-9FBC3A3AEC08Q30999231-43943903-2E0E-4320-A006-57AF1E53CC6FQ33683142-4D3EDC18-EF7C-4D5D-A442-16AD01A53A30Q33836238-28D6A679-AEC7-4DC9-9A8D-DDC591A86202Q33981360-835F3041-6CC9-4565-B09C-6CF72098D534Q33991585-67123149-082D-482A-8C4D-7C2A71F76F02Q33993392-DFA3D941-5482-4C3C-B689-61E0E41AA30CQ33993777-1BCF1153-8AA5-4810-9CAE-5C0C61E8BA33Q33994345-204E7D9C-0837-4510-B9BF-2CB2EED3617CQ33997251-19C9481F-2CBA-4B68-8D60-E212D1ED140EQ34125238-81B356A6-6CDF-4D15-9459-02767C341D7FQ34249291-0792A574-CB21-45B6-AD3D-A37EEE468B09Q34435280-A582588F-09AB-4894-876E-C45ED1C4A4EDQ34490818-062CA909-FA8A-4003-8390-357ACEC232E4Q34632070-FA91EF86-5546-4EDF-9AE4-46164CC90051Q34822262-BE6EA778-4014-404E-8968-160B82250905Q35172380-A7C2F6EE-1DBB-4BBE-B88E-F08BE1D0B6FAQ35669148-FB8FE816-1EA5-4791-81D9-6C4ECB709F49Q35949953-829B759A-524B-4BA7-894C-8A4CDCC11299Q36071364-FF91D8B4-AE69-4C0A-B00C-647F1ABD436AQ36476585-7F7043A5-A937-4BDD-BA3E-C2C5046C4EC8Q36651833-939FD87B-7A78-4622-8544-26D46A231DFDQ36704156-7F0A018B-61D6-4AA7-A2B9-03DD18A75FF7Q36949989-094D497B-5FBE-4C45-9326-A9D00D89D860Q36982395-D0428170-15AF-4040-9128-2DCFCB8BD8F8Q37006508-231B3700-ED58-4D76-B076-BB2C9E9C74DF
P2860
Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Tandem binding of six OmpR pro ...... sequence of Escherichia coli.
@en
type
label
Tandem binding of six OmpR pro ...... sequence of Escherichia coli.
@en
prefLabel
Tandem binding of six OmpR pro ...... sequence of Escherichia coli.
@en
P2093
P2860
P356
P1476
Tandem binding of six OmpR pro ...... sequence of Escherichia coli.
@en
P2093
Bergstrom L
Harlocker SL
P2860
P304
26849-26856
P356
10.1074/JBC.270.45.26849
P407
P577
1995-11-01T00:00:00Z