ArticleBiophysical journal1998
Regulation of catch muscle by twitchin phosphorylation: effects on force, ATPase, and shortening.
Article in Biophysical journal, 1998. 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.
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Who cites it
17 citing papers in PubMed, 47 citations in OpenAlex.
- Mechanism and Function of the Catch State in Molluscan Smooth Muscle: A Historical Perspective.International journal of molecular sciences · 2020Review
- Calcium-dependent titin-thin filament interactions in muscle: observations and theory.Journal of muscle research and cell motility · 2020Review
- Basic science and clinical use of eccentric contractions: History and uncertainties.Journal of sport and health science · 2018Review
- Myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro.Journal of muscle research and cell motility · 2013Article
- A force-activated kinase in a catch smooth muscle.Journal of muscle research and cell motility · 2011Article
- The N-terminal region of twitchin binds thick and thin contractile filaments: redundant mechanisms of catch force maintenance.The Journal of biological chemistry · 2010Article
- The highly efficient holding function of the mollusc 'catch' muscle is not based on decelerated myosin head cross-bridge cycles.Proceedings. Biological sciences · 2010Article
- Mechanism of catch force: tethering of thick and thin filaments by twitchin.Journal of biomedicine & biotechnology · 2010Article
- Twitchin of mollusc smooth muscles can induce "catch"-like properties in human skeletal muscle: support for the assumption that the "catch" state involves twitchin linkages between myofilaments.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2009Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- Molecular basis of the catch state in molluscan smooth muscles: a catchy challenge.Journal of muscle research and cell motility · 2008Review
- Myosin cross-bridge kinetics and the mechanism of catch.Biophysical journal · 2007Article
- Catch force links and the low to high force transition of myosin.Biophysical journal · 2006Article
- No effect of twitchin phosphorylation on the rate of myosin head detachment in molluscan catch muscle: are myosin heads involved in the catch state?Pflugers Archiv : European journal of physiology · 2005Article
- Effects of vanadate, phosphate and 2,3-butanedione monoxime (BDM) on skinned molluscan catch muscle.Pflugers Archiv : European journal of physiology · 2005Article
- Myorod, a thick filament protein in molluscan smooth muscles: isolation, polymerization and interaction with myosin.Journal of muscle research and cell motility · 2001Article
- The myosin cross-bridge cycle and its control by twitchin phosphorylation in catch muscle.Biophysical journal · 2001Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Recent experiments on permeabilized anterior byssus retractor muscle (ABRM) of Mytilus edulis have shown that phosphorylation of twitchin releases catch force at pCa > 8 and decreases force at suprabasal but submaximum [Ca2+]. Twitchin phosphorylation decreases force with no detectable change in ATPase activity, and thus increases the energy cost of force maintenance at subsaturating [Ca2+]. Similarly, twitchin phosphorylation causes no change in unloaded shortening velocity (Vo) at any [Ca2+], but when compared at equal submaximum forces, there is a higher Vo when twitchin is phosphorylated. During calcium activation, the force-maintaining structure controlled by twitchin phosphorylation adjusts to a 30% Lo release to maintain force at the shorter length. The data suggest that during both catch and calcium-mediated submaximum contractions, twitchin phosphorylation removes a structure that maintains force with a very low ATPase, but which can slowly cycle during submaximum calcium activation. A quantitative cross-bridge model of catch is presented that is based on modifications of the Hai and Murphy (1988. Am. J. Physiol. 254:C99-C106) latch bridge model for regulation of mammalian smooth muscle.
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What OpenQuestion holds
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.