ReviewJournal of muscle research and cell motility2003
Why choose myofibrils to study muscle myosin ATPase?
Review in Journal of muscle research and cell motility, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- MyosinA is a druggable target in the widespread protozoan parasite Toxoplasma gondii.PLoS biology · 2023Article
- Are there two different binding sites for ATP on the myosin head, or only one that switches between two conformers?Journal of muscle research and cell motility · 2017Article
- Effect of N-Terminal Extension of Cardiac Troponin I on the Ca(2+) Regulation of ATP Binding and ADP Dissociation of Myosin II in Native Cardiac Myofibrils.Biochemistry · 2016Article
- The rates of Ca2+ dissociation and cross-bridge detachment from ventricular myofibrils as reported by a fluorescent cardiac troponin C.The Journal of biological chemistry · 2012Article
- Correlation between cross-bridge kinetics obtained from Trp fluorescence of myofibril suspensions and mechanical studies of single muscle fibers in rabbit psoas.Journal of muscle research and cell motility · 2011Article
- Single actomyosin motor interactions in skeletal muscle.Biochimica et biophysica acta · 2011Article
- Micromechanical function of myofibrils isolated from skeletal and cardiac muscles of the zebrafish.The Journal of general physiology · 2011Article
- Observing cycling of a few cross-bridges during isometric contraction of skeletal muscle.Cytoskeleton (Hoboken, N.J.) · 2010Article
- Single molecule kinetics in the familial hypertrophic cardiomyopathy D166V mutant mouse heart.Journal of molecular and cellular cardiology · 2010Article
- Insights into human beta-cardiac myosin function from single molecule and single cell studies.Journal of cardiovascular translational research · 2009Review
- Insights into the kinetics of Ca2+-regulated contraction and relaxation from myofibril studies.Pflugers Archiv : European journal of physiology · 2009Article
- Fluorescence lifetime of actin in the familial hypertrophic cardiomyopathy transgenic heart.Biochemistry · 2009Article
- Sarcomere dynamics during muscular contraction and their implications to muscle function.Journal of muscle research and cell motility · 2007Review
- Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles.Biophysical journal · 2005Article
- Myofibrillar myosin ATPase activity in hindlimb muscles from young and aged rats.Mechanisms of ageing and development · 2004Article
- Does phosphate release limit the ATPases of soleus myofibrils? Evidence that (A)M. ADP.Pi states predominate on the cross-bridge cycle.Journal of muscle research and cell motility · 2004Article
- At physiological temperatures the ATPase rates of shortening soleus and psoas myofibrils are similar.Biophysical journal · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Our objective is to propose an overview of the usefulness of skeletal myofibril as an experimental system for studying mechanochemical coupling of skeletal muscles and myosin ATPase activity. The myofibril is a true functional mini-muscle that is able to contract in the presence of ATP. It also contains the machinery necessary for the calcium sensitivity of the contraction. In the absence of calcium, myofibrillar ATPase activity is basal, no shortening occurs and no active force is developed. In the presence of calcium, myofibrillar ATPase is activated and myofibrils either shorten with no external load (native myofibrils) or contract isometrically (cross-linked myofibrils). With this organised system, both chemical and mechanical studies can be carried out. For a decade, our laboratory has been using rabbit psoas myofibrils for exploring myosin ATPase activity. The first challenge was to successfully apply rapid kinetic approaches, such as rapid-flow-quench, to this organised system. Another challenge was to work with myofibrils in cryoenzymic conditions, i.e. in the presence of organic solvents and at sub-zero temperatures. In this overview, we highlight differences between the myosin ATPase in organised systems (myofibrils or fibres) and that of contractile proteins in solution (S1 or actoS1) that we observed using these approaches. We discuss the importance of these differences in terms of mechanochemical coupling. It is concluded that great care should be taken when extrapolating mechanochemical properties of the contractile proteins in solution to the whole muscle.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.