Mutations at the same amino acid in myosin that cause either skeletal or cardiac myopathy have distinct molecular phenotypes
Journal Article
Overview
publication date
- May 1, 2010
has subject area
- Actin Cytoskeleton
- Adenosine Triphosphatases - Myosins
- Amino Acids
- Biochemical Phenomena - Structure-Activity Relationship
- Calorimetry - Calorimetry, Differential Scanning
- Cardiomyopathies - Cardiomyopathy, Dilated
- Circular Dichroism
- Cytoskeletal Proteins - Myosin Subfragments
- Cytoskeletal Proteins - Myosins
- Diagnostic Imaging - Microscopy, Electron
- Differential Thermal Analysis - Calorimetry, Differential Scanning
- Genetic Diseases, Inborn - Distal Myopathies
- Heart Diseases - Cardiomyopathy, Dilated
- Humans
- Investigative Techniques - Microscopy, Electron
- Laminopathies - Cardiomyopathy, Dilated
- Macromolecular Substances - Myosin Subfragments
- Macromolecular Substances - Myosins
- Models, Biological
- Muscle Proteins - Myosin Subfragments
- Muscle Proteins - Myosins
- Musculoskeletal Diseases - Distal Myopathies
- Mutation
- Neuromuscular Diseases - Distal Myopathies
- Pharmacological Phenomena - Structure-Activity Relationship
- Protein Stability
- Thermodynamics
has restriction
- green
Date in CU Experts
- September 6, 2013 4:09 AM
Full Author List
- Armel TZ; Leinwand LA
author count
- 2
citation count
- 25
published in
Other Profiles
International Standard Serial Number (ISSN)
- 0022-2828
Electronic International Standard Serial Number (EISSN)
- 1095-8584
Digital Object Identifier (DOI)
Additional Document Info
start page
- 1007
end page
- 1013
volume
- 48
issue
- 5