Phosphorylation controls brush border motility by regulating myosin structure and association with the cytoskeleton
- 1 December 1983
- Vol. 35 (2), 561-571
- https://doi.org/10.1016/0092-8674(83)90190-3
Abstract
No abstract availableThis publication has 42 references indexed in Scilit:
- Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin moleculesNature, 1983
- Reactivation of intestinal epithelial cell brush border motility: ATP-dependent contraction via a terminal web contractile ring.The Journal of cell biology, 1982
- The binding of smooth muscle myosin light chain kinase to actinBiochemical and Biophysical Research Communications, 1982
- Superprecipitation of gizzard actomyosin, and tension in gizzard muscle skinned fibers in the presence of nucleotides other than ATPBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Reevaluation of brush border motility: calcium induces core filament solation and microvillar vesiculationThe Journal of cell biology, 1982
- Phosphorylation of lymphocyte myosin catalyzed in vitro and in intact cells.The Journal of cell biology, 1982
- Regulation of epithelial tight junction permeability by cyclic AMPNature, 1981
- Activation of skeletal muscle myosin light chain kinase by calcium(2+) and calmodulinBiochemistry, 1980
- alpha-Actinin localization in the junctional complex of intestinal epithelial cells.The Journal of cell biology, 1979
- Phosphorylation of platelet myosin increases actin-activated myosin ATPase activityNature, 1975