Bacterial chemoreceptors: high-performance signaling in networked arrays.
The C2 domain calcium‐binding motif: Structural and functional diversity
The present review summarizes the information currently available regarding the structure and function of the C2 domain and provides a novel sequence alignment of 65 C2domain primary structures that predicts that C2 domains form two distinct topological folds.
Molecular Tuning of Ion Binding to Calcium Signaling Proteins
- J. Falke, S. K. Drake, A. Hazard, O. Peersen
- BiologyQuarterly Reviews of Biophysics (print)
- 1 August 1994
Intracellular calcium plays an essential role in the transduction of most hormonal, neuronal, visual, and muscle stimuli. (Recent reviews include Putney, 1993; Berridge, 1993a,b; Tsunoda, 1993;…
The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes.
- J. Falke, R. Bass, S. Butler, S. Chervitz, M. A. Danielson
- Biology, ChemistryAnnual Review of Cell and Developmental Biology
The chemosensory pathway of bacterial chemotaxis has become a paradigm for the two-component superfamily of receptor-regulated phosphorylation pathways and provides an ideal system in which to probe molecular principles underlying complex cellular signaling and behavior.
Evidence that opioids may have toll-like receptor 4 and MD-2 effects
Transmembrane signaling in bacterial chemoreceptors.
Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update.
Purification of proteins using polyhistidine affinity tags.
Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
Recent results from x-ray crystallographic, solution 19F NMR, and engineered disulfide studies probing the aspartate-induced structural change within the periplasmic and transmembrane regions of the receptor provide evidence that aspartates binding triggers a "swinging-piston" displacement of the second membrane-spanning helix, which is proposed to communicate the signal across the bilayer.