Reassessing the unifying hypothesis for hypercontractility caused by myosin mutations in hypertrophic cardiomyopathy
Author:
Funder
HHS | NIH | National Institute of General Medical Sciences
Agence Nationale de la Recherche
American Heart Association
Publisher
Springer Science and Business Media LLC
Link
https://www.embopress.org/doi/epdf/10.1038/s44318-024-00199-x
Reference136 articles.
1. Ababou A, Gautel M, Pfuhl M (2007) Dissecting the N-terminal myosin binding site of human cardiac myosin-binding protein C. J Biol Chem 282:9204–9215
2. Ababou A, Rostkova E, Mistry S, Le Masurier C, Gautel M, Pfuhl M (2008) Myosin binding protein C positioned to play a key role in regulation of muscle contraction: structure and interactions of domain C1. J Mol Biol 384:615–630
3. Adhikari AS, Kooiker KB, Sarkar SS, Liu C, Bernstein D, Spudich JA, Ruppel KM (2016) Early-onset hypertrophic cardiomyopathy mutations significantly increase the velocity, force, and actin-activated ATPase activity of human β-cardiac myosin. Cell Rep 17:2857–2864
4. Adhikari AS, Trivedi DV, Sarkar SS, Song D, Kooiker KB, Bernstein D, Spudich JA, Ruppel KM (2019) β-Cardiac myosin hypertrophic cardiomyopathy mutations release sequestered heads and increase enzymatic activity. Nat Commun 10:2685
5. Alamo L, Li X, (Edward), Espinoza-Fonseca LM, Pinto A, Thomas DD, Lehman W, Padrón R (2015) Tarantula myosin free head regulatory light chain phosphorylation stiffens N-terminal extension, releasing it and blocking its docking back. Mol Biosyst 11:2180–2189
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