Effect of Removing the Amino-Terminal Hexapeptide of Tropomyosin on the Properties of the Thin Filament
Author:
Affiliation:
1. Department of Biochemistry, Memorial University, St. John’s, Newfoundland, Canada A1B 3X9
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi802004j
Reference51 articles.
1. The structure of F-actin and of actin filaments isolated from muscle
2. Calcium and muscle contraction
3. Solution NMR Structure of the Junction between Tropomyosin Molecules: Implications for Actin Binding and Regulation
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1. Further Investigation into the Biochemical Effects of Phosphorylation of Tropomyosin Tpm1.1(α). Serine-283 Is in Communication with the Midregion;Biochemistry;2020-12-08
2. Demonstration of beta-tropomyosin (Tpm2) and duplication of the alpha-slow tropomyosin gene (TPM3) in Atlantic salmon Salmo salar;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;2020-07
3. Biochemical Comparison of Tpm1.1 (α) and Tpm2.2 (β) Tropomyosins from Rabbit Skeletal Muscle;Biochemistry;2016-02-26
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