(Q27766893)

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L A Alex

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B R Crane

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M I Simon

Protein histidine kinases and signal transduction in prokaryotes and eukaryotes

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language of work or name

English

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publication date

8 January 1999

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131-41

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cites work

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Signal transduction via the multi-step phosphorelay: not necessarily a road less traveled

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DNA topology: topoisomerases keep it simple

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The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW.

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Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay

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Energetics of the structure of the four-alpha-helix bundle in proteins

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Determining phases and anomalous-scattering models from the multiwavelength anomalous diffraction of native protein metal clusters. improved MAD phase error estimates and anomalous-scatterer positions

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Protein structure prediction: recognition of primary, secondary, and tertiary structural features from amino acid sequence.

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Dual chemotaxis signaling pathways in Bacillus subtilis: a sigma D-dependent gene encodes a novel protein with both CheW and CheY homologous domains

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Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA

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Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis

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The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: a thermodynamic and crystallographic study

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Protein structure comparison by alignment of distance matrices

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Identifying the catalytic residue of the ATPase reaction of DNA gyrase

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Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB

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The SH3 domain of Eps8 exists as a novel intertwined dimer

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Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway

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A fragment liberated from the Escherichia coli CheA kinase that blocks stimulatory, but not inhibitory, chemoreceptor signaling

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Mutants defective in bacterial chemotaxis show modified protein phosphorylation

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CATH--a hierarchic classification of protein domain structures

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Processing of X-ray diffraction data collected in oscillation mode

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Two-domain reconstitution of a functional protein histidine kinase

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Communication modules in bacterial signaling proteins

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Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

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Improved Fourier coefficients for maps using phases from partial structures with errors

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Intermolecular complementation of the kinase activity of CheA.

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Expression of CheA fragments which define domains encoding kinase, phosphotransfer, and CheY binding activities

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Histidine and aspartate phosphorylation: two-component systems and the limits of homology

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Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima

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Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase

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Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY

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Crystal structure of an N-terminal fragment of the DNA gyrase B protein.

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Three-dimensional structure of the tyrosine kinase c-Src

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Intermolecular complementation between two defective mutant signal-transducing receptors of Escherichia coli

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Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.

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NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

9989504

1 reference

Consolidated OpenCitations Corpus – April 2017