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pro vyhledávání: '"J E, Andrea"'
Autor:
Michael P. Walsh, J E Andrea
Publikováno v:
Biochemical Journal. 310:835-843
Protein kinase C (PKC), a widely-distributed enzyme implicated in the regulation of many physiological processes, consists of a family of at least twelve isoenzymes which differ in tissue distribution, subcellular localization, regulatory properties,
Autor:
Michael P. Walsh, J E Andrea
Publikováno v:
Hypertension. 20:585-595
The primary mechanism of regulation of smooth muscle contraction involves the phosphorylation of myosin catalyzed by Ca2+/calmodulin-dependent myosin light chain kinase. However, additional mechanisms, both Ca(2+)-dependent and Ca(2+)-independent, ca
Publikováno v:
Biochemistry and cell biology = Biochimie et biologie cellulaire. 75(6)
A full-length cDNA encoding smooth muscle calcyclin (S100A6) was cloned from chicken gizzard, using reverse transcription--polymerase chain reaction techniques. The deduced amino acid sequence contains 92 residues with 12 substitutions and a 2 amino
Publikováno v:
The Journal of biological chemistry. 269(46)
Two immunoreactive proteins (75 and 80 kDa) were detected in rat brain and rabbit aorta using a polyclonal peptide-directed antibody to the C terminus of the zeta isoenzyme of protein kinase C (PKC). The 75-kDa protein resembled authentic PKC zeta; i
Publikováno v:
Molecular pharmacology. 40(4)
We have introduced the novel application of a simple ethidium fluorescence assay, using covalently closed circular DNA, for the study of topoisomerase-targeted drugs. With the specificity of camptothecin for eukaryotic topoisomerases I and of VM26 fo