ArticleJournal of muscle research and cell motility2011
Tropomyosin is in a reduced state in rabbit psoas muscle.
Article in Journal of muscle research and cell motility, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Impact of A134 and E218 Amino Acid Residues of Tropomyosin on Its Flexibility and Function.International journal of molecular sciences · 2020Article
- Functional outcomes of structural peculiarities of striated muscle tropomyosin.Journal of muscle research and cell motility · 2020Review
- Effects of an Interchain Disulfide Bond on Tropomyosin Structure: A Molecular Dynamics Study.International journal of molecular sciences · 2018Article
- Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin.Journal of muscle research and cell motility · 2017Article
- The Relaxation Properties of Myofibrils Are Compromised by Amino Acids that Stabilize α-Tropomyosin.Biophysical journal · 2017Article
- In vitro formation and characterization of the skeletal muscle α·β tropomyosin heterodimers.Biochemistry · 2012Article
- Structural analysis of smooth muscle tropomyosin α and β isoforms.The Journal of biological chemistry · 2012Article
- Tropomyosin is in a reduced state in rat cardiac muscle.Journal of muscle research and cell motility · 2011Article
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3 authors at 2 institutions in 1 country.
Funding
Abstract
Tropomyosin (Tm) purified from skeletal and cardiac muscle often contains disulfide bonds due to oxidation of cysteine groups that are in close proximity in the coiled-coil structure. Are these disulfide crosslinks present in the muscle or produced by oxidation during preparation? To answer this question we reacted one part of freshly dissected rabbit psoas muscle fibers, which was permeabilized with Triton X-100, with N-ethyl maleimide (NEM) to block cysteine groups and another part with 5,5'-dithiobis(2-nitro benzoate) (DTNB) to facilitate disulfide bond formation by interchain sulfhydryl-disulfide exchange. We found, by high resolution gradient SDS polyacrylamide gels, that the NEM-treated muscle was only composed of uncrosslinked Tm and the DTNB treated muscle was composed of disulfide-crosslinked Tm. This work indicates that Tm exists in a reduced state in rabbit psoas muscle.
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