scholarly article | Q13442814 |
P2093 | author name string | K Volz | |
X Zhu | |||
P Matsumura | |||
J Rebello | |||
P2860 | cites work | Assembly of an MCP receptor, CheW, and kinase CheA complex in the bacterial chemotaxis signal transduction pathway | Q42016227 |
Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis | Q46219823 | ||
Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate. | Q52889446 | ||
Mutations leading to altered CheA binding cluster on a face of CheY. | Q54601722 | ||
Crystallographic refinement by simulated annealing. Application to a 2.8 A resolution structure of aspartate aminotransferase. | Q54740459 | ||
Ribonuclease T1 with free recognition and catalytic site: crystal structure analysis at 1.5 A resolution | Q27656483 | ||
Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis | Q27702270 | ||
Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.1-A structure of a threonine to isoleucine mutant at position 87 of CheY | Q27729774 | ||
Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface | Q27731310 | ||
Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis | Q27731489 | ||
Communication modules in bacterial signaling proteins | Q28243451 | ||
Protein phosphorylation is involved in bacterial chemotaxis | Q30450891 | ||
Structure, function and properties of antibody binding sites | Q35011078 | ||
The smaller of two overlapping cheA gene products is not essential for chemotaxis in Escherichia coli | Q35585534 | ||
Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli | Q35609743 | ||
The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW. | Q36094633 | ||
Exchange of chromosomal and plasmid alleles in Escherichia coli by selection for loss of a dominant antibiotic sensitivity marker | Q36177096 | ||
Multiple kinetic states for the flagellar motor switch | Q36184431 | ||
Roles of cheY and cheZ gene products in controlling flagellar rotation in bacterial chemotaxis of Escherichia coli | Q36231721 | ||
Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY. | Q37656265 | ||
Multiple factors underlying the maximum motility of Escherichia coli as cultures enter post-exponential growth | Q39937159 | ||
A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations | Q39940781 | ||
Structural conservation in the CheY superfamily | Q40770453 | ||
P433 | issue | 8 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | crystal structure | Q895901 |
P304 | page(s) | 5000-6 | |
P577 | publication date | 1997-02-21 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106 | |
P478 | volume | 272 |
Q27632631 | A distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheY |
Q30375642 | A network of molecular switches controls the activation of the two-component response regulator NtrC. |
Q39110484 | A new perspective on response regulator activation |
Q36059913 | Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY. |
Q36922432 | Activation mechanism of a signaling protein at atomic resolution from advanced computations |
Q78016801 | Alanine mutants of the Spo0F response regulator modifying specificity for sensor kinases in sporulation initiation |
Q27681718 | An asymmetric heterodomain interface stabilizes a response regulator–DNA complex |
Q47890080 | Bacterial chemotaxis: unsolved mystery of the flagellar switch |
Q41073425 | Biochemical study of multiple CheY response regulators of the chemotactic pathway of Rhodobacter sphaeroides. |
Q27680054 | Conformational barrier of CheY3 and inability of CheY4 to bind FliM control the flagellar motor action in Vibrio cholerae |
Q27621048 | Conformational changes induced by phosphorylation of the FixJ receiver domain |
Q34230990 | Conformational changes of Spo0F along the phosphotransfer pathway |
Q27622080 | Correlated switch binding and signaling in bacterial chemotaxis |
Q27649301 | Crystal Structure of a Complex between the Phosphorelay Protein YPD1 and the Response Regulator Domain of SLN1 Bound to a Phosphoryl Analog |
Q27637834 | Crystal structure of a cyanobacterial phytochrome response regulator |
Q27630942 | Crystal structure of activated CheY. Comparison with other activated receiver domains |
Q36883672 | Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation |
Q27639502 | Crystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentus |
Q34349346 | Diversity in chemotaxis mechanisms among the bacteria and archaea. |
Q43215301 | Evidence against the "Y-T coupling" mechanism of activation in the response regulator NtrC. |
Q37791003 | Focus on phosphoaspartate and phosphoglutamate. |
Q36639563 | Genetic analysis of response regulator activation in bacterial chemotaxis suggests an intermolecular mechanism |
Q34090837 | How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation |
Q41738097 | Identification of communication networks in Spo0F: a model for phosphorylation-induced conformational change and implications for activation of multiple domain bacterial response regulators |
Q42826580 | Insights into correlated motions and long-range interactions in CheY derived from molecular dynamics simulations |
Q59086641 | Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F |
Q38270504 | Molecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101. |
Q35892726 | Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases |
Q33733421 | Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet |
Q33538598 | Signal transduction in bacteria: molecular mechanisms of stimulus-response coupling |
Q33932897 | Signal transduction: response regulators on and off. |
Q27748852 | Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain |
Q27748790 | Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY |
Q35940689 | Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance |
Q43175612 | Subdomain competition, cooperativity, and topological frustration in the folding of CheY. |
Q27641713 | The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system |
Q27640869 | The X-ray Crystal Structures of Two Constitutively Active Mutants of the Escherichia coli PhoB Receiver Domain Give Insights into Activation |
Q28487093 | The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis |
Q27652225 | The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptides |
Q40293155 | Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins. |
Q33362188 | Transcriptome analysis reveals response regulator SO2426-mediated gene expression in Shewanella oneidensis MR-1 under chromate challenge |
Q27759197 | Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway |
Q27736290 | Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheY |
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