A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression.
Open Access
- 1 December 1991
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (35) , 23521-23524
- https://doi.org/10.1016/s0021-9258(18)54312-x
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domainNature, 1991
- ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGFCell, 1991
- Max: A Helix-Loop-Helix Zipper Protein That Forms a Sequence-Specific DNA-Binding Complex with MycScience, 1991
- Methylation-Sensitive Sequence-Specific DNA Binding by the c-Myc Basic RegionScience, 1991
- New light on Myc and Myb. Part I. Myc.Genes & Development, 1990
- An Insulin-Stimulated Protein Kinase Similar to Yeast Kinases Involved in Cell Cycle ControlScience, 1990
- Casein kinase II enhances the DNA binding activity of serum response factor.Genes & Development, 1990
- Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activationNature, 1990
- GAL4-VP16 is an unusually potent transcriptional activatorNature, 1988
- c-myc oncogene protein synthesis is independent of the cell cycle in human and avian cellsNature, 1985