๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Phosphorylation of Microtubule-Associated Protein 2 at Distinct Sites by Calmodulin-Dependent and Cyclic-AMP-Dependent Kinases

โœ Scribed by James R. Goldenring; Mary Lou Vallano; Robert J. DeLorenzo


Book ID
111173194
Publisher
John Wiley and Sons
Year
1985
Tongue
English
Weight
693 KB
Volume
45
Category
Article
ISSN
0022-3042

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Differential regulation of basic protein
โœ Glyn Dawson; Patrick McAtee ๐Ÿ“‚ Article ๐Ÿ“… 1989 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 584 KB

Myelin basic protein, an 80-kilodalton (kDa) protein in rat oligodendrocytes, and an 80-kDa basic protein in neuroblastoma x neonatal Chinese hamster brain explant hybrids were phosphorylated extensively when the cells were treated with either phorbol esters (TPA) or diacylglycerols (e.g., oleyoyl-a

Calpain-mediated proteolysis of microtub
โœ Dr. Gail V. W. Johnson; V. G. Foley ๐Ÿ“‚ Article ๐Ÿ“… 1993 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 686 KB

## B i k n g h a m , Alabama - The effects of CAMP-dependent protein kinase (CAMP-PK) and CaZf/calmodulin-dependent protein kinase I1 (CaMKII) phosphorylation on the calpainmediated degradation of microtubule-associated protein 2 (MAP-2) were studied. Both CAMP-PK and CaMKII readily phosphorylated