August 20, 1996Proceedings of the National Academy of SciencesOpen Access

Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle.

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Population

Natural thick filaments isolated from cardiac muscle

Design

Preclinical

Authors

AWAndrea S. WeisbergNational Institutes of Health SWSaul WinegradRutgers, The State University of New Jersey

Discussion

Member takes

Implication

May modulate cardiac force in animals; hypothesis-generating for human contractility and disease.

Structured PICO

Population

Natural thick filaments isolated from cardiac muscle

Intervention

Phosphorylation of myosin-binding protein C (MBP-C) by protein kinase A

Outcome

Structural changes in cross bridges (filament thickness, intensity of reflections, distance of first peak reflection)surrogate

Phosphorylation of MBP-C extends cross bridges and alters their orientation, providing a structural basis for how it may modify force production in activated cardiac muscle.

Cite This Study

Weisberg et al. (1996) studied this question.

synapsesocial.com/papers/6a1241809b33f06ee260d543 https://doi.org/10.1073/pnas.93.17.8999

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Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider