Dilated cardiomyopathy myosin mutants have reduced force-generating capacity
Journal Article
Overview
publication date
- June 8, 2018
has subject area
- Adenosine Triphosphatases - Cardiac Myosins
- Adenosine Triphosphatases - Myosin Heavy Chains
- Animals
- Biochemical Phenomena - Amino Acid Sequence
- Biochemical Phenomena - Kinetics
- Cardiomyopathies - Cardiomyopathy, Dilated
- Cell Line
- Cytoskeletal Proteins - Actins
- Cytoskeletal Proteins - Cardiac Myosins
- Cytoskeletal Proteins - Myosin Heavy Chains
- Heart Diseases - Cardiomyopathy, Dilated
- Humans
- Laminopathies - Cardiomyopathy, Dilated
- Macromolecular Substances - Actins
- Macromolecular Substances - Cardiac Myosins
- Macromolecular Substances - Myosin Heavy Chains
- Mechanical Phenomena - Kinetics
- Mice
- Models, Molecular
- Molecular Sequence Data - Amino Acid Sequence
- Muscle Proteins - Actins
- Muscle Proteins - Cardiac Myosins
- Muscle Proteins - Myosin Heavy Chains
- Nucleic Acids, Nucleotides, and Nucleosides - Adenosine Triphosphate
- Point Mutation
- Protein Structural Elements - Protein Domains
- Protein Structure, Tertiary - Protein Domains
- Purines - Adenosine Triphosphate
- Ribonucleotides - Adenosine Triphosphate
has restriction
- hybrid
Date in CU Experts
- April 27, 2018 2:10 AM
Full Author List
- Ujfalusi Z; Vera CD; Mijailovich SM; Svicevic M; Yu EC; Kawana M; Ruppel KM; Spudich JA; Geeves MA; Leinwand LA
author count
- 10
citation count
- 42
published in
- Journal of Biological Chemistry Journal
Other Profiles
Electronic International Standard Serial Number (EISSN)
- 1083-351X
Digital Object Identifier (DOI)
Additional Document Info
start page
- 9017
end page
- 9029
volume
- 293
issue
- 23