Ontology highlight
ABSTRACT:
SUBMITTER: McConnell BK
PROVIDER: S-EPMC409819 | biostudies-literature | 1999 Nov
REPOSITORIES: biostudies-literature
McConnell B K BK Jones K A KA Fatkin D D Arroyo L H LH Lee R T RT Aristizabal O O Turnbull D H DH Georgakopoulos D D Kass D D Bond M M Niimura H H Schoen F J FJ Conner D D Fischman D A DA Seidman C E CE Seidman J G JG
The Journal of clinical investigation 19991101 9
To elucidate the role of cardiac myosin-binding protein-C (MyBP-C) in myocardial structure and function, we have produced mice expressing altered forms of this sarcomere protein. The engineered mutations encode truncated forms of MyBP-C in which the cardiac myosin heavy chain-binding and titin-binding domain has been replaced with novel amino acid residues. Analogous heterozygous defects in humans cause hypertrophic cardiomyopathy. Mice that are homozygous for the mutated MyBP-C alleles express ...[more]