Smooth muscle caldesmon is an extended flexible monomeric protein in solution that can readily undergo reversible intra- and intermolecular sulfhydryl cross-linking. A mechanism for caldesmon's F-actin bundling activity.
Open Access
- 1 May 1987
- journal article
- abstracts
- Published by Elsevier
- Vol. 262 (15), 7429-7437
- https://doi.org/10.1016/s0021-9258(18)48255-5
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Functional domain of caldesmonFEBS Letters, 1986
- Bundling of actin filaments by aorta caldesmon is not related to its regulatory functionFEBS Letters, 1985
- Crosslinking of actin filaments is caused by caldesmon aggregates, but not by its dimersFEBS Letters, 1985
- Detection of caldesmon in muscle and non-muscle tissues of the chicken using polyclonal antibodiesBiochemical and Biophysical Research Communications, 1985
- Caldesmon, a calmodulin‐binding, F actin‐interacting protein, is present in aorta, uterus and plateletsFEBS Letters, 1983
- Tropomyosin from bovine brain contains two polypeptide chains of slightly different molecular weightsFEBS Letters, 1978
- Rabbit skeletal α-tropomyosin chains are in registerBiochemical and Biophysical Research Communications, 1975
- Tropomyosin: Evidence for no stagger between chainsFEBS Letters, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Substructure of the myosin moleculeJournal of Molecular Biology, 1969