Zobrazeno 1 - 10
of 14
pro vyhledávání: '"B C Wise"'
Publikováno v:
Molecular pharmacology. 40(2)
Neonatal rat cortical astrocytes in primary culture synthesize and secrete nerve growth factor (NGF). Interleukin-1 beta(IL-1) and basic fibroblast growth factor (bFGF) treatment of astrocytes increased NGF mRNA content by about 2-fold. The effect of
Publikováno v:
Biochemical Journal. 209:189-195
Cardiac phospholipid-sensitive Ca2+-dependent protein kinase phosphorylated cardiac troponin inhibitory subunit (troponin I) and tropomyosin-binding subunit (troponin T), present either as the free form or as the troponin-tropomyosin complex. Exhaust
Publikováno v:
Journal of Biological Chemistry. 255:12042-12046
The Ca2+-dependent phosphorylation of a number of proteins in the cytosol of the rat or guinea pig cerebral cortex was profoundly stimulated by phosphatidylserine; calmodulin, on the other hand, had only a minimal effect. The Ca2+-dependent phosphory
Autor:
J.F. Kuo, Robert F. Kibler, D. B. Glass, C. H. J. Chou, N. Katoh, R C Schatzman, R S Turner, Robert L. Raynor, B. C. Wise
Publikováno v:
Journal of Biological Chemistry. 257:8489-8495
Publikováno v:
Journal of Biological Chemistry. 257:8481-8488
Publikováno v:
Experientia. 45:879-881
The effects of serotonin on the formation of inositol phosphates and protein phosphorylation were examined in cultured smooth muscle cells. Serotonin stimulated the formation of [3H]inositol monophosphate, [3H]inositol bisphosphate and [3H]inositol t
Publikováno v:
Advances in cyclic nucleotide and protein phosphorylation research. 17
GABA- modulin , a regulatory component of the GABA/benzodiazepine receptor complex, is phosphorylated by cyclic-AMP-, Ca/calmodulin-, and Ca/phospholipid-dependent protein kinases at distinct sites in the molecule. Phosphorylation of GM by the cyclic
Publikováno v:
The Journal of biological chemistry. 255(24)
The Ca2+-dependent phosphorylation of a number of proteins in the cytosol of the rat or guinea pig cerebral cortex was profoundly stimulated by phosphatidylserine; calmodulin, on the other hand, had only a minimal effect. The Ca2+-dependent phosphory
Adriamycin, a lipid-interacting anti-cancer agent, was found to inhibit phospholipid-sensitive Ca2+-dependent phosphorylation of endogenous proteins from the cytosol of the guinea-pig heart. The drug, unexpectedly, also inhibited phosphorylation of s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46db21bd9f5f01538f7ca62501c93105
https://europepmc.org/articles/PMC1163227/
https://europepmc.org/articles/PMC1163227/