ArticleBiophysical journal1999
Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 62 citations in OpenAlex.
- No Difference in Myosin Kinetics and Spatial Distribution of the Lever Arm in the Left and Right Ventricles of Human Hearts.Frontiers in physiology · 2017Article
- Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II.Scientific reports · 2016Article
- Effect of a myosin regulatory light chain mutation K104E on actin-myosin interactions.American journal of physiology. Heart and circulatory physiology · 2015Article
- The endothermic ATP hydrolysis and crossbridge attachment steps drive the increase of force with temperature in isometric and shortening muscle.The Journal of physiology · 2015Article
- The spatial distribution of actin and mechanical cycle of myosin are different in right and left ventricles of healthy mouse hearts.Biochemistry · 2014Article
- Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.American journal of physiology. Regulatory, integrative and comparative physiology · 2014Article
- Comparison of orientation and rotational motion of skeletal muscle cross-bridges containing phosphorylated and dephosphorylated myosin regulatory light chain.The Journal of biological chemistry · 2013Article
- Mesoscopic analysis of motion and conformation of cross-bridges.Biophysical reviews · 2012Review
- Myosin cross-bridges do not form precise rigor bonds in hypertrophic heart muscle carrying troponin T mutations.Journal of molecular and cellular cardiology · 2011Article
- Evidence for pre- and post-power stroke of cross-bridges of contracting skeletal myofibrils.Biophysical journal · 2011Article
- Myosin heads contribute to the maintenance of filament order in relaxed rabbit muscle.Biophysical journal · 2010Article
- Electron tomography of cryofixed, isometrically contracting insect flight muscle reveals novel actin-myosin interactions.PloS one · 2010Article
- Direct modeling of X-ray diffraction pattern from contracting skeletal muscle.Biophysical journal · 2008Article
- The structural basis of the increase in isometric force production with temperature in frog skeletal muscle.The Journal of physiology · 2005Article
- Endothermic force generation, temperature-jump experiments and effects of increased [MgADP] in rabbit psoas muscle fibres.The Journal of physiology · 2005Article
- Orientation of the myosin light chain region by single molecule total internal reflection fluorescence polarization microscopy.Biophysical journal · 2005Article
- Coupling between phosphate release and force generation in muscle actomyosin.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
- Kinetic effects of fiber type on the two subcomponents of the Huxley-Simmons phase 2 in muscle.Biophysical journal · 2003Article
- Temperature dependence of the force-generating process in single fibres from frog skeletal muscle.The Journal of physiology · 2003Article
- Force enhancement by PEG during ramp stretches of skeletal muscle.Journal of muscle research and cell motility · 2003Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural changes induced by Joule temperature jumps (T-jumps) in frog muscle fibers were monitored using time-resolved x-ray diffraction. Experiments made use of single, permeabilized fibers that were fully activated after slight cross-linking with 1-ethyl-3-[3-dimethylamino)propyl]carbodiimide to preserve their structural order. After T-jumps from 5-6 to approximately 17 degrees C and then on to approximately 30 degrees C, tension increased by a factor of 1.51 and 1.84, respectively, whereas fiber stiffness did not change with temperature. The tension rise was accompanied by a decrease in the intensity of the (1, 0) equatorial x-ray reflection by 15 and 26% (at approximately 17 and approximately 30 degrees C) and by an increase in the intensity of the M3 myosin reflection by 20% and 41%, respectively. The intensity of the (1,1) equatorial reflection increased slightly. The peak of the intensity on the 6th actin layer line shifted toward the meridian with temperature. The intensity of the 1st actin layer line increased from 12% (of its rigor value) at 5-6 degrees C to 36% at approximately 30 degrees C, so that the fraction of the cross-bridges labeling the actin helix estimated from this intensity increased proportionally to tension from approximately 35% at 5-6 degrees C to approximately 60% at approximately 30 degrees C. This suggests that force is generated during a transition of nonstereo-specifically attached myosin cross-bridges to a stereo-specific binding state.
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