Organization of the Receptor-Kinase Signaling Array That Regulates Escherichia coli Chemotaxis
Open Access
- 1 September 2002
- journal article
- Published by Elsevier
- Vol. 277 (39) , 36748-36754
- https://doi.org/10.1074/jbc.m204317200
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Subunit Organization in a Soluble Complex of Tar, CheW, and CheA by Electron MicroscopyPublished by Elsevier ,2002
- Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial ChemotaxisPublished by Elsevier ,2001
- Mechanism of CheA Protein Kinase Activation in Receptor Signaling ComplexesBiochemistry, 1999
- THE TWO-COMPONENT SIGNALING PATHWAY OF BACTERIAL CHEMOTAXIS: A Molecular View of Signal Transduction by Receptors, Kinases, and Adaptation EnzymesAnnual Review of Cell and Developmental Biology, 1997
- High-resolution Structures of the Ligand Binding Domain of the Wild-type Bacterial Aspartate ReceptorJournal of Molecular Biology, 1996
- Role of α-Helical Coiled-coil Interactions in Receptor Dimerization, Signaling, and Adaptation during Bacterial ChemotaxisPublished by Elsevier ,1996
- Imitation of Escherichia coli Aspartate Receptor Signaling in Engineered Dimers of the Cytoplasmic DomainScience, 1996
- Dimerization Is Required for the Activity of the Protein Histidine Kinase CheA That Mediates Signal Transduction in Bacterial ChemotaxisPublished by Elsevier ,1996
- The serine receptor of bacterial chemotaxis exhibits half-site saturation for serine bindingBiochemistry, 1994
- Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativityBiochemistry, 1994