Cross-bridge binding to actin and force generation in skinned fibers of the rabbit psoas muscle in the presence of antibody fragments against the N-terminus of actin
- 31 January 1996
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 70 (1) , 48-56
- https://doi.org/10.1016/s0006-3495(96)79579-6
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Equilibration and exchange of fluorescently labeled molecules in skinned skeletal muscle fibers visualized by confocal microscopy.Biophysical Journal, 1995
- Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generationBiophysical Journal, 1995
- The actomyosin interaction and its control by tropomyosin.1995
- The mechanism of force generation in myosin: a disorder-to-order transition, coupled to internal structural changes.1995
- Millisecond time resolution electron cryo-microscopy of the M-ATP transient kinetic state of the acto-myosin ATPase.1995
- Microsecond rotational motion of spin-labeled myosin heads during isometric muscle contraction. Saturation transfer electron paramagnetic resonanceBiophysical Journal, 1989
- Antibody against the amino terminus of α-actin inhibits actomyosin interactions in the presence of ATPJournal of Molecular Biology, 1989
- Functional characterization of skeletal F‐actin labeled on the NH2‐terminal segment of residues 1–28European Journal of Biochemistry, 1989
- Nucleotide-induced states of myosin subfragment 1 cross-linked to actinBiochemistry, 1989
- Modifying preselected sites on proteins: the stretch of residues 633-642 of the myosin heavy chain is part of the actin-binding site.Proceedings of the National Academy of Sciences, 1988