Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Matthew R. Locher"'
Autor:
Matthew R. Locher, Ying Ge, Yi-Chen Chen, Richard L. Moss, Nicole M. Lane, Takushi Kohmoto, Ying Peng, Lars Larsson, Serife Ayaz-Guner
Publikováno v:
Analytical Chemistry. 87:8399-8406
Actin is the major component of the cytoskeleton playing an essential role in the structure and motility of both muscle and non-muscle cells. It is highly conserved and encoded by a multigene family. α-cardiac actin (αCAA) and α-skeletal actin (α
Autor:
Tanya Bekyarova, Brett A. Colson, Daniel P. Fitzsimons, Richard L. Moss, Jitandrakumar R. Patel, Matthew R. Locher, Thomas C. Irving
Publikováno v:
The Journal of Physiology. 588:981-993
Phosphorylation of myosin regulatory light chain (RLC) by myosin light chain kinase (MLCK) and myosin binding protein-C (cMyBP-C) by protein kinase A (PKA) independently accelerate the kinetics of force development in ventricular myocardium. However,
Autor:
Julian E. Stelzer, Matthew R. Locher, Maria V. Razumova, Jitandrakumar R. Patel, Holly S. Norman, Richard L. Moss
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 297:H247-H256
The ventricles of small mammals express mostly α-myosin heavy chain (α-MHC), a fast isoform, whereas the ventricles of large mammals, including humans, express ∼10% α-MHC on a predominately β-MHC (slow isoform) background. In failing human vent
Publikováno v:
The Journal of Physiology. 579:161-173
The speed and force of myocardial contraction during systolic ejection is largely dependent on the intrinsic contractile properties of cardiac myocytes. As the myosin heavy chain (MHC) isoform of cardiac muscle is an important determinant of the cont
Publikováno v:
American journal of physiology. Heart and circulatory physiology. 300(3)
Myosin heavy chain (MHC) isoforms are principal determinants of work capacity in mammalian ventricular myocardium. The ventricles of large mammals including humans normally express ∼10% α-MHC on a predominantly β-MHC background, while in failing
Autor:
Thomas C. Irving, Matthew R. Locher, Patricia A. Powers, Tanya Bekyarova, Brett A. Colson, Carl W. Tong, Daniel P. Fitzsimons, Richard L. Moss
Publikováno v:
Biophysical Journal. 96(3)
Protein kinase A-mediated (PKA) phosphorylation of cardiac myosin binding protein-C (cMyBP-C) accelerates the kinetics of cross-bridge cycling and appears to relieve the tether-like constraint of myosin heads imposed by cMyBP-C (Colson et al., 2008,
Autor:
Tanya Bekyarova, Daniel P. Fitzsimons, Brett A. Colson, Matthew R. Locher, Richard L. Moss, Thomas C. Irving
Publikováno v:
Circulation research. 103(3)
Protein kinase A–mediated (PKA) phosphorylation of cardiac myosin binding protein C (cMyBP-C) accelerates the kinetics of cross-bridge cycling and may relieve the tether-like constraint of myosin heads imposed by cMyBP-C. We favor a mechanism in wh
Publikováno v:
Journal of Molecular and Cellular Cardiology.
Autor:
Richard L. Moss, John C. Ralphe, Willem J. de Lange, Matthew R. Locher, Laura F. Hegge, Adrian C. Grimes
Publikováno v:
Biophysical Journal. 102:351a-352a
Congestive heart failure is a debilitating disease in which the principal pathology is impaired ventricular contractility leading to diminished cardiac output, and previous work indicates that reduced contractility is based in part on the ratio of my
Autor:
Nancy K. Sweitzer, Satoru Osaki, Richard L. Moss, Holly S. Norman, Matthew R. Locher, Takushi Kohmoto
Publikováno v:
Biophysical Journal. 98:716a
The ventricles of human myocardium normally express low levels of α myosin heavy chain (MHC) on a predominately β MHC background. However, in heart failure the distribution changes to ∼100% β MHC with virtually undetectable levels of α MHC, a c