New proteins involved in cell regulation by Ca2+ and phospholipids
- 31 October 1986
- journal article
- review article
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 11 (10) , 420-423
- https://doi.org/10.1016/0968-0004(86)90176-3
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Common domain structure of Ca2+ and lipid‐binding proteinsFEBS Letters, 1986
- Binding sites for calcium, lipid and p11 on p36, the substrate of retroviral tyrosine‐specific protein kinasesFEBS Letters, 1986
- Phosphorylation of p36 in vitro with pp60srcFEBS Letters, 1985
- Isolation of calelectrin-like proteins associated with smooth muscle plasma membranesBiochemical and Biophysical Research Communications, 1985
- Characterization of Calelectrin, a Ca2+‐Binding Protein Isolated from the Electric Organ of Torpedo marmorataJournal of Neurochemistry, 1985
- Identification of calcium-binding proteins associated with the lymphocyte plasma membraneBiochemical and Biophysical Research Communications, 1985
- Synthesis of novel calcium-dependent proteins associated with mammary epithelial cell migration and differentiationExperimental Cell Research, 1984
- Calelectrins are a ubiquitous family of Ca2+-binding proteins purified by Ca2+-dependent hydrophobic affinity chromatography by a mechanism distinct from that of calmodulinBiochemical and Biophysical Research Communications, 1984
- The 46,000-dalton tyrosine protein kinase substrate is widespread, whereas the 36,000-dalton substrate is only expressed at high levels in certain rodent tissues.The Journal of cell biology, 1984
- Synhibin: A new calcium‐dependent membrane‐binding protein that inhibits synexin‐induced chromaffin granule aggregation and fusionFEBS Letters, 1982