Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Henry G. Zot"'
Autor:
Henry G. Zot, Javier E. Hasbun
Publikováno v:
Frontiers in Physiology, Vol 7 (2016)
To explain disparate decay rates of cytosolic Ca2+ and structural changes in the thin filaments during a twitch, we model the time course of Ca2+ bound troponin (Tn) resulting from the free Ca2+ transient of fast skeletal muscle. In fibers stretched
Externí odkaz:
https://doaj.org/article/206676ca55424dab91b5894f99ba5bfd
Autor:
Henry G. Zot, Javier E. Hasbun
Publikováno v:
Biophysical Journal. 122:118a
Publikováno v:
J Biol Chem
Vertebrate striated muscle thin filaments are thought to be thermodynamically activated in response to an increase in Ca(2+) concentration. We tested this hypothesis by measuring time intervals for gliding runs and pauses of individual skeletal muscl
Publikováno v:
Biophysical Journal. 120:60a
Publikováno v:
Biophysical Journal. 118:258a
Publikováno v:
Biophysical Journal. 116:177a-178a
Autor:
Javier E. Hasbun, Henry G. Zot
Publikováno v:
Frontiers in Physiology, Vol 7 (2016)
To explain disparate decay rates of cytosolic Ca2+ and structural changes in the thin filaments during a twitch, we model the time course of Ca2+ bound troponin (Tn) resulting from the free Ca2+ transient of fast skeletal muscle. In fibers stretched
Autor:
Henry G, Zot, Javier E, Hasbun
Publikováno v:
Frontiers in Physiology
To explain disparate decay rates of cytosolic Ca2+ and structural changes in the thin filaments during a twitch, we model the time course of Ca2+-bound troponin (Tn) resulting from the free Ca2+ transient of fast skeletal muscle. In fibers stretched
Publikováno v:
Biophysical Journal. 110(3)
We have uncovered a statistical mechanical basis for recurring interactions of unit and ensemble biomolecules in motion. Motility is characteristic of life, but a common basis for movement has remained to be identified. Diverse systems in motion shif
Autor:
Svetlana B. Tikunova, Javier E. Hasbun, Henry G. Zot, Ryan S. Lee, Jack A. Rall, Jonathan P. Davis, Nguyen Van Minh, Kristopher P. Kline, Darl R. Swartz
Publikováno v:
American Journal of Physiology-Cell Physiology. 299:C1091-C1099
To investigate effects of altering troponin (Tn)C Ca2+binding properties on rate of skeletal muscle contraction, we generated three mutant TnCs with increased or decreased Ca2+sensitivities. Ca2+binding properties of the regulatory domain of TnC with