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Phosphorylation of both serine residues in cardiac troponin I is required to decrease the Ca2+ affinity of cardiac troponin C.
Zhang R, Zhao J, Potter JD. Zhang R, et al. Among authors: zhao j. J Biol Chem. 1995 Dec 22;270(51):30773-80. doi: 10.1074/jbc.270.51.30773. J Biol Chem. 1995. PMID: 8530519 Free article.
Phosphorylation of these residues has been shown to reduce the Ca2+ affinity of the single Ca(2+)-specific regulatory site of cardiac troponin C (CTnC) and to increase the rate of Ca2+ dissociation from this site (Robertson, S. P., Johnson, J. D., Holroyde, M. J., K …
Phosphorylation of these residues has been shown to reduce the Ca2+ affinity of the single Ca(2+)-specific regulatory site of cardiac tropon …
The regulatory light chains of myosin modulate cross-bridge cycling in skeletal muscle.
Szczesna D, Zhao J, Potter JD. Szczesna D, et al. Among authors: zhao j. J Biol Chem. 1996 Mar 1;271(9):5246-50. doi: 10.1074/jbc.271.9.5246. J Biol Chem. 1996. PMID: 8617809 Free article.
Previously we showed that partial extraction of the 18-kDa regulatory light chains (RLCs) of myosin decreased the rate of force development and was subsequently increased by approximately 20% following reconstitution with RLCs (Potter, J. D., Zhao, J. and Pan …
Previously we showed that partial extraction of the 18-kDa regulatory light chains (RLCs) of myosin decreased the rate of force development …
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