• Publications
  • Influence
Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase,
Kinetic analysis indicated that H-89 inhibits protein kinase A, in competitive fashion against ATP, and the forskolin- and dibutyryl cAMP-induced neurite outgrowth is apparently mediated by protein Kinase A while the NGF- induced neuriteOutgrowth is mediated by a protein kinases A-independent pathway. Expand
Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C.
Both the holoenzyme and the catalytic subunit (or fragment), which is active without an enzyme activator, are susceptible to these compounds with a similar concentration dependency, thereby indicating that the inhibitory effect is attributed to the direct interaction of the compound with the active center of the enzyme but not with the enzymeactivator. Expand
Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase.
Findings suggest that the ATP-binding site at the active center of smooth muscle myosin light chain kinase is located in a hydrophobic environment. Expand
The newly synthesized selective Ca2+/calmodulin dependent protein kinase II inhibitor KN-93 reduces dopamine contents in PC12h cells.
Investigation of the inhibitory property of a newly synthesized methoxybenzenesulfonamide, KN-93, on CaMKII activity in situ and in vitro suggests that it inhibits DA formation by modulating the reaction rate of TH to reduce the Ca(2+)-mediated phosphorylation levels of the TH molecule. Expand
KN-62, 1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenylpiperazi ne, a specific inhibitor of Ca2+/calmodulin-dependent protein kinase II.
Results suggest that KN-62 affects the interaction between calmodulin and Ca2+/CaM kinase II following inhibition of this kinase activity by directly binding to theCalmodulin binding site of the enzyme but does not affect the cal modulin-independent activity of already autophosphorylated (activated) enzyme. Expand
Pharmacology of protein kinase inhibitors.
MAPKAP kinase‐2; a novel protein kinase activated by mitogen‐activated protein kinase.
Results indicate that MAP kinase activates at least two distinct protein kinases, suggesting that it represents a point at which the growth factor‐stimulated protein kinase cascade bifurcates. Expand
The novel and specific Rho-kinase inhibitor (S)-(+)-2-methyl-1-[(4-methyl-5-isoquinoline)sulfonyl]-homopiperazine as a probing molecule for Rho-kinase-involved pathway.
The results show that the Rho-kinase inhibitor targets a protein with a well-known function, MARC KS in neuronal cells, and raises the possibility that MARCKS is a target protein of Rho -kinase in neuronal Cells. Expand
N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, a calmodulin antagonist, inhibits cell proliferation.
This pharmacological demonstration that cytoplasmic calmodulin is involved in cell proliferation is significant; W-7 and its derivatives may be useful tools for research oncalmodulin and cell biology-related studies. Expand
Development of specific Rho-kinase inhibitors and their clinical application.
These results demonstrate that the new 5-isoquinolinesulfonylamides are not only potent ROCK selective compounds, but are also useful compounds for clinical applications. Expand