The 38 kDa Ca2+/membrane-binding protein of pig granulocytes needs a high Ca2+ concentration to be phosphorylated by protein kinase C
- 10 January 1991
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Vol. 1091 (1) , 81-86
- https://doi.org/10.1016/0167-4889(91)90225-m
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- THE PROTEIN KINASE C FAMILY: HETEROGENEITY AND ITS IMPLICATIONSAnnual Review of Biochemistry, 1989
- Alfred P. Sloan Jr. prize. Studies and prospectives of the protein kinase C family for cellular regulationCancer, 1989
- Calcium-dependent phospholipid- (and membrane-) binding proteinsBiochemistry, 1988
- The molecular heterogeneity of protein kinase C and its implications for cellular regulationNature, 1988
- In vitro protein kinase C phosphorylation sites of placental lipocortinBiochemistry, 1988
- Location of sites in human lipocortin I that are phosphorylated by protein tyrosine kinases and protein kinases A and CBiochemistry, 1988
- Phosphorylation of lipocortins invitro by protein kinase CBiochemical and Biophysical Research Communications, 1986
- Common domain structure of Ca2+ and lipid‐binding proteinsFEBS Letters, 1986
- The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo.Molecular and Cellular Biology, 1986
- PROTEIN-TYROSINE KINASESAnnual Review of Biochemistry, 1985