English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Cardiac myosin binding protein C (cMyBP-C) is a regulatory protein that modulates the strength and speed of heart contractions. cMyBP-C is required for normal heart function, and mutations in the gene encoding cMyBP-C are the most common cause of hypertrophic cardiomyopathy, a disease affecting an estimated 1 in 500 people. Here we used an integrated structure–function approach to determine how C0 and C1, the first two domains of cMyBP-C, interact with muscle thin filaments (composed of F-actin and regulatory proteins) to influence their ability to interact with myosin, the force-generating protein of muscle. Results reveal that C0 and C1 both bind to actin at multiple, distinct sites and that C0 and C1 exert different effects on heart muscle contraction.

C0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation