The primary sequence of murine caveolin reveals a conserved consensus site for phosphorylation by protein kinase C
- 30 September 1994
- Vol. 147 (2) , 299-300
- https://doi.org/10.1016/0378-1119(94)90087-6
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: implications for human disease.The Journal of cell biology, 1994
- Caveolae, caveolin and caveolin-rich membrane domains: a signalling hypothesisTrends in Cell Biology, 1994
- Protein kinase C activators inhibit receptor-mediated potocytosis by preventing internalization of caveolaeThe Journal of cell biology, 1994
- Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cellsThe Journal of cell biology, 1993
- The sequence of human caveolin reveals identity with VIP21, a component of transport vesiclesFEBS Letters, 1992
- VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles.The Journal of cell biology, 1992
- Caveolin, a protein component of caveolae membrane coatsPublished by Elsevier ,1992
- Potocytosis: Sequestration and Transport of Small Molecules by CaveolaeScience, 1992
- Cellular aspects of transcapillary exchangePhysiological Reviews, 1983