ArticleBiophysical journal2009
Dynamics of thin-filament activation in rabbit skeletal muscle fibers examined by time-resolved x-ray diffraction.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Dual-filament regulation of relaxation in mammalian fast skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Activation of skeletal muscle is controlled by a dual-filament mechano-sensing mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Thick filament activation is different in fast- and slow-twitch skeletal muscle.The Journal of physiology · 2022Article
- Small Angle X-ray Diffraction as a Tool for Structural Characterization of Muscle Disease.International journal of molecular sciences · 2022Review
- Crossbridge Recruitment Capacity of Wild-Type and Hypertrophic Cardiomyopathy-Related Mutant Troponin-T Evaluated by X-ray Diffraction and Mechanical Study of Cardiac Skinned Fibers.International journal of molecular sciences · 2020Article
- Synchrotron radiation X-ray diffraction studies on muscle: past, present, and future.Biophysical reviews · 2019Review
- Myosin Head Configurations in Resting and Contracting Murine Skeletal Muscle.International journal of molecular sciences · 2018Article
- Synchrotron Radiation X-ray Diffraction Techniques Applied to Insect Flight Muscle.International journal of molecular sciences · 2018Review
- Regulation of Contraction by the Thick Filaments in Skeletal Muscle.Biophysical journal · 2017Review
- The earliest molecular response to stretch of insect flight muscle as revealed by fast X-ray diffraction recording.Scientific reports · 2017Article
- Structural dynamics of troponin during activation of skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Fast x-ray recordings reveal dynamic action of contractile and regulatory proteins in stretch-activated insect flight muscle.Biophysical journal · 2010Article
- Monitoring the structural behavior of troponin and myoplasmic free Ca2+ concentration during twitch of frog skeletal muscle.Biophysical journal · 2010Article
- A myopathy-linked tropomyosin mutation severely alters thin filament conformational changes during activation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
By using skinned-rabbit skeletal muscle fibers, the time courses of changes of thin filament-based x-ray reflections were followed at a 3.4-ms time resolution during thin-filament activation. To discriminate between the effects of calcium binding and myosin binding on thin-filament activity, measurements were performed after caged-calcium photolysis in fibers with full-filament or no-filament overlap, or during force recovery after a quick release. All three reflections examined, i.e., the second actin layer line (second ALL, reporting the tropomyosin movement), the sixth ALL (reporting actin structural change), and the meridional troponin reflections, exhibited calcium-induced and myosin-induced components, but their rate constants and polarities were different. Generally, calcium-induced components exhibited fast rate constants (>100 s(-1)). The myosin-induced components of the second ALL had a rate constant similar to that of the force (7-10 s(-1)), but that of the sixth ALL was apparently faster. The myosin-induced component of troponin reflection was the only one with negative polarity, and was too slow to be analyzed with this protocol. The results suggest that the three regulation-related proteins change their structures with different rate constants, and the significance of these findings is discussed in the context of a cooperative thin-filament activation mechanism.
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