Conformational changes due to calcium-induced calmodulin dissociation in brush border MyosinI-decorated F-actin revealed by cryoelectron microscopy and image analysis
- 1 June 1997
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 269 (4) , 548-557
- https://doi.org/10.1006/jmbi.1997.1058
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Fifty Ways to Love Your Lever: Myosin MotorsCell, 1996
- Zipper Protein, a B-G Protein with the Ability to Regulate Actin/Myosin 1 Interactions in the Intestinal Brush BorderJournal of Biological Chemistry, 1996
- Helical Processing Using PHOELIXJournal of Structural Biology, 1996
- Differential regulation of skeletal muscle myosin‐II and brush border myosin‐I enzymology and mechanochemistry by bacterially produced tropomyosin isoformsCell Motility, 1994
- Unconventional myosinsCurrent Opinion in Cell Biology, 1992
- Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro.The Journal of cell biology, 1990
- Mapping of the microvillar 110K-calmodulin complex: calmodulin-associated or -free fragments of the 110-kD polypeptide bind F-actin and retain ATPase activityThe Journal of cell biology, 1988
- The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase.The Journal of cell biology, 1987
- Calcium-regulated cooperative binding of the microvillar 110K-calmodulin complex to F-actin: formation of decorated filaments.The Journal of cell biology, 1987
- Localization of myosin, actin, and tropomyosin in rat intestinal epithelium: immunohistochemical studies at the light and electron microscope levels.The Journal of cell biology, 1980