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- W2142381589 endingPage "488" @default.
- W2142381589 startingPage "459" @default.
- W2142381589 abstract "Cells can sense and transduce a broad range of mechanical forces into distinct sets of biochemical signals that ultimately regulate cellular processes, including adhesion, proliferation, differentiation, and apoptosis. Deciphering at the nanoscale the design principles by which sensory elements are integrated into structural protein motifs whose conformations can be switched mechanically is crucial to understand the process of transduction of force into biochemical signals that are then integrated to regulate mechanoresponsive pathways. While the major focus in the search for mechanosensory units has been on membrane proteins such as ion channels, integrins, and associated cytoplasmic complexes, a multimodular design of tandem repeats of various structural motifs is ubiquitously found among extracellular matrix proteins, as well as cell adhesion molecules, and among many intracellular players that physically link transmembrane proteins to the contractile cytoskeleton. Single-molecule studies have revealed an unexpected richness of mechanosensory motifs, including force-regulated conformational changes of loop-exposed molecular recognition sites, intermediate states in the unraveling pathway that might either expose cryptic binding or phosphorylation sites, or regions that display enzymatic activity only when unmasked by force. Insights into mechanochemical signal conversion principles will also affect various technological fields, from biotechnology to tissue engineering and drug development." @default.
- W2142381589 created "2016-06-24" @default.
- W2142381589 creator A5040449994 @default.
- W2142381589 date "2006-06-01" @default.
- W2142381589 modified "2023-09-30" @default.
- W2142381589 title "MECHANOTRANSDUCTION INVOLVING MULTIMODULAR PROTEINS: Converting Force into Biochemical Signals" @default.
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