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Ge, Y., Rybakova, I. N., Xu, Q., Moss, R. L. (2009) Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state. Proceedings of the National Academy of Sciences, 106 (31) 12658-12663 doi:10.1073/pnas.0813369106

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Reference TypeJournal (article/letter/editorial)
TitleTop-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state
JournalProceedings of the National Academy of Sciences
AuthorsGe, Y.Author
Rybakova, I. N.Author
Xu, Q.Author
Moss, R. L.Author
Year2009 (August 4)Volume106
Issue31
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0813369106Search in ResearchGate
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Mindat Ref. ID1765910Long-form Identifiermindat:1:5:1765910:9
GUID0
Full ReferenceGe, Y., Rybakova, I. N., Xu, Q., Moss, R. L. (2009) Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state. Proceedings of the National Academy of Sciences, 106 (31) 12658-12663 doi:10.1073/pnas.0813369106
Plain TextGe, Y., Rybakova, I. N., Xu, Q., Moss, R. L. (2009) Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state. Proceedings of the National Academy of Sciences, 106 (31) 12658-12663 doi:10.1073/pnas.0813369106
In(2009, August) Proceedings of the National Academy of Sciences Vol. 106 (31) Proceedings of the National Academy of Sciences

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Colson, B. A., Rybakova, I. N., Prochniewicz, E., Moss, R. L., Thomas, D. D. (2012) Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner. Proceedings of the National Academy of Sciences, 109 (50) 20437-20442 doi:10.1073/pnas.1213027109
Kensler, Robert W., Craig, Roger, Moss, Richard L. (2017) Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments. Proceedings of the National Academy of Sciences, 114 (8) doi:10.1073/pnas.1614020114
Moss, Richard L. (2016) Cardiac myosin-binding protein C: A protein once at loose ends finds its regulatory groove. Proceedings of the National Academy of Sciences, 113 (12) 3133-3135 doi:10.1073/pnas.1602568113
Weisberg, A., Winegrad, S. (1996) Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle. Proceedings of the National Academy of Sciences, 93 (17) 8999-9003 doi:10.1073/pnas.93.17.8999
Colson, Brett A., Thompson, Andrew R., Espinoza-Fonseca, L. Michel, Thomas, David D. (2016) Site-directed spectroscopy of cardiac myosin-binding protein C reveals effects of phosphorylation on protein structural dynamics. Proceedings of the National Academy of Sciences, 113 (12) 3233-3238 doi:10.1073/pnas.1521281113
Sadayappan, S., Osinska, H., Klevitsky, R., Lorenz, J. N., Sargent, M., Molkentin, J. D., Seidman, C. E., Seidman, J. G., Robbins, J. (2006) Cardiac myosin binding protein c phosphorylation is cardioprotective. Proceedings of the National Academy of Sciences, 103 (45) 16918-16923 doi:10.1073/pnas.0607069103
Ponnam, Saraswathi, Sevrieva, Ivanka, Sun, Yin-Biao, Irving, Malcolm, Kampourakis, Thomas (2019) Site-specific phosphorylation of myosin binding protein-C coordinates thin and thick filament activation in cardiac muscle. Proceedings of the National Academy of Sciences, 116 (31) 15485-15494 doi:10.1073/pnas.1903033116
Wang, G., Abzalimov, R. R., Bobst, C. E., Kaltashov, I. A. (2013) Conformer-specific characterization of nonnative protein states using hydrogen exchange and top-down mass spectrometry. Proceedings of the National Academy of Sciences, 110 (50) 20087-20092 doi:10.1073/pnas.1315029110
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Whitten, A. E., Jeffries, C. M., Harris, S. P., Trewhella, J. (2008) Cardiac myosin-binding protein C decorates F-actin: Implications for cardiac function. Proceedings of the National Academy of Sciences, 105 (47) 18360-18365 doi:10.1073/pnas.0808903105
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