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A family of cAMP-binding proteins that directly activate Rap1.
The findings suggest the need to reformulate concepts of cAMP-mediated signaling to include direct coupling to Ras superfamily signaling.
A Rap guanine nucleotide exchange factor enriched highly in the basal ganglia.
- H. Kawasaki, G. Springett, A. Graybiel
- BiologyProceedings of the National Academy of Sciences…
- 27 October 1998
It is proposed that CalDAG-GEF proteins have a critical neuronal function in determining the relative activation of Ras and Rap1 signaling induced by Ca2+ and DAG mobilization.
Neurite outgrowth of PC12 cells is suppressed by wortmannin, a specific inhibitor of phosphatidylinositol 3-kinase.
Isolation of myosin light chain kinase inhibitors from microorganisms: dehydroaltenusin, altenusin, atrovenetinone, and cyclooctasulfur.
- S. Nakanishi, S. Toki, Y. Matsuda
- Biology, ChemistryBioscience, biotechnology, and biochemistry
- 23 July 1995
Among them, dehydroaltenusin was the best MLCK inhibitor in terms of potency and selectivity examined in the purified enzyme systems.
MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.--I. Isolation, structural determination and biological properties of MS-271.
RP-1551s, a family of azaphilones produced by Penicillium sp., inhibit the binding of PDGF to the extracellular domain of its receptor.
Nine azaphilones designated RP-1551-1, -2, -3, -4, -5, -6, -7, -M1, and -M2 were isolated from the culture broth of Penicillium sp. SPC-21609 as inhibitors of PDGF binding to its receptor. RP-1551s…
Guanine nucleotide exchange factors CalDAG‐GEFI and CalDAG‐GEFII are colocalized in striatal projection neurons
- S. Toki, H. Kawasaki, N. Tashiro, D. Housman, A. Graybiel
- BiologyThe Journal of comparative neurology
- 3 September 2001
It is suggested that the CalDAG‐GEFs may be key intracellular regulators whereby calcium and diacylglycerol signals can regulate cellular functions through small GTPases in the basal ganglia circuits.
The ES-242s, novel N-methyl-D-aspartate antagonists of microbial origin, interact with both the neurotransmitter recognition site and the ion channel domain.
The neuroprotective properties of ES-242s, novel NMDA receptor antagonists, in neuronal cell culture toxicity studies.