Domain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡ - sprookjes - yvandenbroek - TriplyDB

Domain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡

Domain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡

http://www.wikidata.org/entity/Q27644822

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Prokaryotic 2-component systems and the OmpR/PhoB superfamily Structure and dynamics of polymyxin-resistance-associated response regulator PmrA in complex with promoter DNA Crystal Structures of the Receiver Domain of the Response Regulator PhoP from Escherichia coli in the Absence and Presence of the Phosphoryl Analog Beryllofluoride The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state Regulation of Response Regulator Autophosphorylation through Interdomain Contacts Structure of the Response Regulator PhoP from Mycobacterium tuberculosis Reveals a Dimer through the Receiver Domain Structure-Function Studies of DNA Binding Domain of Response Regulator KdpE Reveals Equal Affinity Interactions at DNA Half-Sites The dimeric form of the unphosphorylated response regulator BaeR Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae Structural insights into the dimerization of the response regulator ComE from Streptococcus pneumoniae An asymmetric heterodomain interface stabilizes a response regulator–DNA complex Atypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA Binding Atypical OmpR/PhoB Subfamily Response Regulator GlnR of Actinomycetes Functions as a Homodimer, Stabilized by the Unphosphorylated Conserved Asp-focused Charge Interactions Structure of the DNA-binding domain of the response regulator SaeR from Staphylococcus aureus The atypical OmpR/PhoB response regulator ChxR from Chlamydia trachomatis forms homodimers in vivo and binds a direct repeat of nucleotide sequences Systems perspectives on erythromycin biosynthesis by comparative genomic and transcriptomic analyses of S. erythraea E3 and NRRL23338 strains.Proteome scale comparative modeling for conserved drug and vaccine targets identification in Corynebacterium pseudotuberculosis Adaptation to environmental stimuli within the host: two-component signal transduction systems of Mycobacterium tuberculosis.The prrAB two-component system is essential for Mycobacterium tuberculosis viability and is induced under nitrogen-limiting conditions Conformational Dynamics of Response Regulator RegX3 from Mycobacterium tuberculosis.Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.Septal localization of the Mycobacterium tuberculosis MtrB sensor kinase promotes MtrA regulon expression.Universally applicable methods for monitoring response regulator aspartate phosphorylation both in vitro and in vivo using Phos-tag-based reagents System-level mapping of Escherichia coli response regulator dimerization with FRET hybrids.Probing the roles of the two different dimers mediated by the receiver domain of the response regulator PhoB.Biological insights from structures of two-component proteins.To ∼P or Not to ∼P? Non-canonical activation by two-component response regulators.Molecular strategies for phosphorylation-mediated regulation of response regulator activity.Advances In Mycobacterium Tuberculosis Therapeutics Discovery Utlizing Structural Biology.The Conserved Actinobacterial Two-Component System MtrAB Coordinates Chloramphenicol Production with Sporulation in Streptomyces venezuelae NRRL B-65442.The α10 helix of DevR, the Mycobacterium tuberculosis dormancy response regulator, regulates its DNA binding and activity.Targeting multiple response regulators of Mycobacterium tuberculosis augments the host immune response to infection.Mycobacterium tuberculosis oriC sequestration by MtrA response regulator.Mycobacterium tuberculosis mtrA merodiploid strains with point mutations in the signal-receiving domain of MtrA exhibit growth defects in nutrient broth Target genes, consensus binding site, and role of phosphorylation for the response regulator MtrA of Corynebacterium glutamicum.Evolutionary analysis and lateral gene transfer of two-component regulatory systems associated with heavy-metal tolerance in bacteria.Dual phosphorylation in response regulator protein PrrA is crucial for intracellular survival of mycobacteria consequent upon transcriptional activation.Multisystem Analysis of Mycobacterium tuberculosis Reveals Kinase-Dependent Remodeling of the Pathogen-Environment Interface.RitR is an archetype for a novel family of redox sensors in the streptococci that has evolved from two-component response regulators and is required for pneumococcal colonization.

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P2860

Domain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡

http://www.wikidata.org/entity/Q27644822

description

2007 nî lūn-bûn

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2007 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2007 թվականի հունիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Domain Orientation in the Inac ...... a Barrier to Activation † , ‡

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Domain Orientation in the Inac ...... a Barrier to Activation † , ‡

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Domain Orientation in the Inac ...... a Barrier to Activation † , ‡

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Domain Orientation in the Inac ...... a Barrier to Activation † , ‡

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Domain Orientation in the Inac ...... a Barrier to Activation † , ‡

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Domain Orientation in the Inac ...... a Barrier to Activation † , ‡

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Domain Orientation in the Inac ...... a Barrier to Activation † , ‡

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P2093

Geoffrey S Waldo

http://www.w3.org/2001/XMLSchema#string

Minmin Yu

http://www.w3.org/2001/XMLSchema#string

Natalia Friedland

http://www.w3.org/2001/XMLSchema#string

Timothy R Mack

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P2860

Quorum Sensing in Bacteria

Protein phosphorylation and regulation of adaptive responses in bacteria

Phosphorylated aspartate in the structure of a response regulator protein

Structure of a transiently phosphorylated switch in bacterial signal transduction

Conformational changes induced by phosphorylation of the FixJ receiver domain

The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY

Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima

Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator

The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface

Structural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB Subfamily

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6733-43

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scholarly article

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1625039

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10.1021/BI602546Q

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23

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46

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Thomas C. Terwilliger

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2007-06-12T00:00:00Z

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6321964

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17511470

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Mycobacterium tuberculosis

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2528954

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