Side Chains at the Membrane−Water Interface Modulate the Signaling State of a Transmembrane Receptor
- 29 January 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 43 (7), 1763-1770
- https://doi.org/10.1021/bi0360206
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Mapping Out Regions on the Surface of the Aspartate Receptor That Are Essential for Kinase ActivationBiochemistry, 2003
- Quantitative Analysis of Aspartate Receptor Signaling Complex Reveals that the Homogeneous Two-state Model is Inadequate: Development of a Heterogeneous Two-state ModelJournal of Molecular Biology, 2003
- Common Extracellular Sensory Domains in Transmembrane Receptors for Diverse Signal Transduction Pathways inBacteriaandArchaeaJournal of Bacteriology, 2003
- Collaborative signaling by mixed chemoreceptor teams in Escherichia coliProceedings of the National Academy of Sciences, 2002
- Molecular Information Processing: Lessons from Bacterial ChemotaxisPublished by Elsevier BV ,2002
- Site-Directed Rotational Resonance Solid-State NMR Distance Measurements Probe Structure and Mechanism in the Transmembrane Domain of the Serine Bacterial ChemoreceptorBiochemistry, 2002
- How proteins adapt to a membrane–water interfaceTrends in Biochemical Sciences, 2000
- Attractant Regulation of the Aspartate Receptor−Kinase Complex: Limited Cooperative Interactions between Receptors and Effects of the Receptor Modification StateBiochemistry, 2000
- Chimeric chemosensory transducers of Escherichia coli.Proceedings of the National Academy of Sciences, 1985
- A diffusion assay for detection and quantitation of methyl-esterified proteins on polyacrylamide gelsAnalytical Biochemistry, 1984