Amino acid sequence of a 15 kilodalton actin-binding fragment of turkey gizzard caldesmon: Similarity with dystrophin, tropomysin and the tropomyosin-binding region of troponin T
- 1 April 1989
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 160 (1), 210-216
- https://doi.org/10.1016/0006-291x(89)91642-2
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- A 35-kilodalton fragment from gizzard smooth muscle caldesmon that induces F-actin bundlesBiochemical and Biophysical Research Communications, 1988
- Identification of a 15 kilodalton actin binding region on gizzard caldesmon probed by chemical cross-linkingBiochemical and Biophysical Research Communications, 1988
- The complete sequence of dystrophin predicts a rod-shaped cytoskeletal proteinCell, 1988
- Bovine cardiac troponin T: amino acid sequences of the two isoformsBiochemistry, 1987
- α-Helical coiled coils — a widespread motif in proteinsTrends in Biochemical Sciences, 1986
- The influence of caldesmon on ATPase activity of the skeletal muscle actomyosin and bundling of actin filamentsBiochimica et Biophysica Acta (BBA) - General Subjects, 1985
- Analysis of the amino acid sequence of a tropomyosin-binding fragment from troponin-TJournal of Molecular Biology, 1981
- Regulation and Kinetics of the Actin-Myosin-ATP InteractionAnnual Review of Biochemistry, 1980
- Empirical Predictions of Protein ConformationAnnual Review of Biochemistry, 1978
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978