Cardiac myosin-binding protein C interaction with actin is inhibited by compounds identified in a high-throughput fluorescence lifetime screen-Reference-Cited by-同舟云学术

Cardiac myosin-binding protein C interaction with actin is inhibited by compounds identified in a high-throughput fluorescence lifetime screen

Published:2021-07 Issue:1 Volume:297 Page:100840
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bunch Thomas A.,Guhathakurta Piyali,Lepak Victoria C.,Thompson Andrew R.^ORCID,Kanassatega Rhye-Samuel^ORCID,Wilson Anna,Thomas David D.^ORCID,Colson Brett A.

Funder

NIH

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

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4. Myosin-binding protein C displaces tropomyosin to activate cardiac thin filaments and governs their speed by an independent mechanism;Mun;Proc. Natl. Acad. Sci. U. S. A.,2014

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1. Cardiac myosin-binding protein C N-terminal interactions with myosin and actin filaments: Opposite effects of phosphorylation and M-domain mutations;Journal of Molecular and Cellular Cardiology;2024-01

2. N-Terminal Fragment of Cardiac Myosin Binding Protein-C Increases the Duration of Actin—Myosin Interaction;Bulletin of Experimental Biology and Medicine;2024-01

3. Drug discovery for heart failure targeting myosin-binding protein C;Journal of Biological Chemistry;2023-12

4. Basic science methods for the characterization of variants of uncertain significance in hypertrophic cardiomyopathy;Frontiers in Cardiovascular Medicine;2023-08-01

5. HTS driven by fluorescence lifetime detection of FRET identifies activators and inhibitors of cardiac myosin;SLAS Discovery;2023-07