ArticleBiophysical journal2006
Catch force links and the low to high force transition of myosin.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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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
15 citing papers in PubMed, 32 citations in OpenAlex.
- Differences between fast and slow muscles in scallops revealed through proteomics and transcriptomics.BMC genomics · 2018Article
- 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
- Serotonin modulates muscle function in the medicinal leech Hirudo verbana.Biology letters · 2011Article
- 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
- Rhythmic contraction generates adjustable passive stiffness in rabbit detrusor.Journal of applied physiology (Bethesda, Md. : 1985) · 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
- Myosin loop 2 is involved in the formation of a trimeric complex of twitchin, actin, and myosin.The Journal of biological chemistry · 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
- Small-angle X-ray diffraction studies of a molluscan smooth muscle in the catch state.Journal of muscle research and cell motility · 2008Article
- Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch.The Journal of experimental biology · 2007Article
- Myosin cross-bridge kinetics and the mechanism of catch.Biophysical journal · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Catch is characterized by maintenance of force with very low energy utilization in some invertebrate muscles. Catch is regulated by phosphorylation of the mini-titin, twitchin, and a catch component of force exists at all [Ca2+] except those resulting in maximum force. The mechanism responsible for catch force was characterized by determining how the effects of agents that inhibit the low to high force transition of the myosin cross-bridge (inorganic phosphate, butanedione monoxime, trifluoperazine, and blebbistatin) are modified by twitchin phosphorylation and [Ca2+]. In permeabilized anterior byssus retractor muscles from Mytilus edulis, catch force was identified as being sensitive to twitchin phosphorylation, whereas noncatch force was insensitive. In all cases, inhibition of the low to high force transition caused an increase in catch force. The same relationship exists between catch force and noncatch force whether force is varied by changes in [Ca2+] and/or agents that inhibit cross-bridge force production. This suggests that myosin in the high force state detaches catch force maintaining structures, whereas myosin in the low force state promotes their formation. It is unlikely that the catch structure is the myosin cross-bridge; rather, it appears that myosin interacts with the structure, most likely twitchin, and regulates its attachment and detachment.
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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.