ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2002
Role of titin in vertebrate striated muscle.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 69 citations in OpenAlex.
- Cardiac function, structural, and electrical remodeling by microgravity exposure.American journal of physiology. Heart and circulatory physiology · 2023Review
- The Sarcomeric Spring Protein Titin: Biophysical Properties, Molecular Mechanisms, and Genetic Mutations Associated with Heart Failure and Cardiomyopathy.Current cardiology reports · 2021Review
- How does tissue preparation affect skeletal muscle transverse isotropy?Journal of biomechanics · 2016Article
- Theoretical Hill-type muscle and stability: numerical model and application.Computational and mathematical methods in medicine · 2013Article
- Conformational dynamics of titin PEVK explored with FRET spectroscopy.Biophysical journal · 2012Article
- Muscle performance in a soft-bodied terrestrial crawler: constitutive modelling of strain-rate dependency.Journal of the Royal Society, Interface · 2008Article
- Restoring force development by titin/connectin and assessment of Ig domain unfolding.Journal of muscle research and cell motility · 2005Article
- Can the passive elasticity of muscle be explained directly from the mechanics of individual titin molecules?Journal of muscle research and cell motility · 2005Article
- Titin PEVK segment: charge-driven elasticity of the open and flexible polyampholyte.Journal of muscle research and cell motility · 2005Article
- The elasticity of single titin molecules using a two-bead optical tweezers assay.Biophysical journal · 2004Article
- Calcium-dependent molecular spring elements in the giant protein titin.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Molecular basis of passive stress relaxation in human soleus fibers: assessment of the role of immunoglobulin-like domain unfolding.Biophysical journal · 2003Article
- Damped elastic recoil of the titin spring in myofibrils of human myocardium.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- The entire cDNA sequences of projectin isoforms of crayfish claw closer and flexor muscles and their localization.Journal of muscle research and cell motility · 2003Article
- M-band: a safeguard for sarcomere stability?Journal of muscle research and cell motility · 2003Review
- Gigantic variety: expression patterns of titin isoforms in striated muscles and consequences for myofibrillar passive stiffness.Journal of muscle research and cell motility · 2003Article
- Stretching and visualizing titin molecules: combining structure, dynamics and mechanics.Journal of muscle research and cell motility · 2002Review
- Unfolding of titin domains studied by molecular dynamics simulations.Journal of muscle research and cell motility · 2002Article
- Titin as a modular spring: emerging mechanisms for elasticity control by titin in cardiac physiology and pathophysiology.Journal of muscle research and cell motility · 2002Review
- Single-molecule measurement of elasticity of serine-, glutamate- and lysine-rich repeats of invertebrate connectin reveals that its elasticity is caused entropically by random coil structure.Journal of muscle research and cell motility · 2002Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Titin is a giant muscle protein with a molecular weight in the megaDalton range and a contour length of more than 1 microm. Its size and location within the sarcomere structure determine its important role in the mechanism of muscle elasticity. According to the current consensus, elasticity stems directly from more than one type of spring-like behaviour of the I-band portion of the molecule. Starting from slack length, extension of the sarcomere first causes straightening of the molecule. Further extension then induces local unfolding of a unique sequence, the PEVK region, which is named due to the preponderance of these amino-acid residues. High speeds of extension and/or high forces are likely to lead to unfolding of the beta-sandwich domains from which the molecule is mainly constructed. A release of tension leads to refolding and recoiling of the polypeptide. Here, we review the literature and present new experimental material related to the role of titin in muscle elasticity. In particular, we analyse the possible influence of the arrangement and environment of titin within the sarcomere structure on its extensible behaviour. We suggest that, due to the limited conformational space, elongation and compression of the molecule within the sarcomere occur in a more ordered way or with higher viscosity and higher forces than are observed in solution studies of the isolated protein.
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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.