Article

A FRET assay to quantitate levels of the human β-cardiac myosin interacting heads motif based on its near-atomic resolution structure

2024-12-10

Abstract excerpt

In cardiac muscle, many myosin molecules are in a resting or “OFF” state with their catalytic heads in a folded structure known as the interacting heads motif (IHM). Many mutations in the human β-cardiac myosin gene that cause hypertrophic cardiomyopathy (HCM) are thought to destabilize (decrease the population of) the IHM state. The effects of pathogenic mutations on the IHM structural state are often studied usi...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 90980f6f-0786-55b7-a0b9-d4de02833e7e
DOI: 10.1101/2024.12.05.626936

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

A FRET assay to quantitate levels of the human β-cardiac myosin interacting heads motif based on its near-atomic resolution structureDOI 10.1101/2024.12.05.626936Read

Direct detection of the myosin super-relaxed state and interacting heads motif in solutionSemantic proximity Read

Dilated cardiomyopathy mutation E525K in human beta-cardiac myosin stabilizes the interacting-heads motif and super-relaxed state of myosin.Semantic proximity Read

Dilated cardiomyopathy mutation E525K in human beta-cardiac myosin stabilizes the interacting heads motif and super-relaxed state of myosinSemantic proximity Read

Tail length and E525K dilated cardiomyopathy mutant alter human β-cardiac myosin super-relaxed state.Semantic proximity Read

β-Cardiac myosin hypertrophic cardiomyopathy mutations release sequestered heads and increase enzymatic activitySemantic proximity Read

Tail Length and E525K Dilated Cardiomyopathy Mutant Alter Human β-Cardiac Myosin Super-Relaxed StateSemantic proximity Read

Hypertrophic cardiomyopathy mutations at the folded-back sequestered β-cardiac myosin S1-S2 and S1-S1 interfaces release sequestered heads and increase myosin enzymatic activitySemantic proximity Read

Hypertrophic cardiomyopathy mutations Y115H and E497D disrupt the folded-back state of human beta-cardiac myosin allostericallySemantic proximity Read

Human skeletal myopathy myosin mutations disrupt myosin head sequestration.Semantic proximity Read

Cryo-EM structure of the folded-back state of human β-cardiac myosin*Semantic proximity Read

Dynamics of the β-cardiac myosin auto-inhibited state explain cardiomyopathy pathogenesis.Semantic proximity Read

A myosin hypertrophic cardiomyopathy mutation disrupts the super-relaxed state and boosts contractility by enhanced actin attachmentSemantic proximity Read