Results 171 to 180 of about 6,839 (201)
Some of the next articles are maybe not open access.
The Journal of Pharmacology and Experimental Therapeutics, 1982
To evaluate the role of ornithine decarboxylase (ODC) and the polyamines in tissue growth and development, neonatal rats were given daily injections of alpha-difluoromethylornithine, a specific, irreversible inhibitor of ODC. Enzyme activity in brain, heart and kidney was effectively inhibited, leading to prompt reductions in putrescine levels which ...
T A, Slotkin +7 more
openaire +2 more sources
To evaluate the role of ornithine decarboxylase (ODC) and the polyamines in tissue growth and development, neonatal rats were given daily injections of alpha-difluoromethylornithine, a specific, irreversible inhibitor of ODC. Enzyme activity in brain, heart and kidney was effectively inhibited, leading to prompt reductions in putrescine levels which ...
T A, Slotkin +7 more
openaire +2 more sources
Journal of Medicinal Chemistry, 1981
alpha-Ethynyl- and alpha-vinylornithine were designed and synthesized as potential enzyme-activated inhibitors of mammalian ornithine decarboxylase. These two new inhibitors produce both immediate and time-dependent inhibition of rat liver ornithine decarboxylase in vitro. The inhibitions exhibition saturation kinetics.
C, Danzin +3 more
openaire +2 more sources
alpha-Ethynyl- and alpha-vinylornithine were designed and synthesized as potential enzyme-activated inhibitors of mammalian ornithine decarboxylase. These two new inhibitors produce both immediate and time-dependent inhibition of rat liver ornithine decarboxylase in vitro. The inhibitions exhibition saturation kinetics.
C, Danzin +3 more
openaire +2 more sources
Journal of Medicinal Chemistry, 1978
Fourteen structural analogues of ornithine were synthesized and evaluated as inhibitors of preparations of the enzyme L-ornithine carboxylase (ODC) (E.C. 4.1.1.17) obtained from rat liver, rat hepatoma cells in culture, or bull prostate. The synthesis of these compounds was achieved either via a Bucherer type reaction or via alkylation of carbanions ...
P, Bey +5 more
openaire +2 more sources
Fourteen structural analogues of ornithine were synthesized and evaluated as inhibitors of preparations of the enzyme L-ornithine carboxylase (ODC) (E.C. 4.1.1.17) obtained from rat liver, rat hepatoma cells in culture, or bull prostate. The synthesis of these compounds was achieved either via a Bucherer type reaction or via alkylation of carbanions ...
P, Bey +5 more
openaire +2 more sources
Ornithine decarboxylase antizyme inhibitor 2 regulates intracellular vesicle trafficking
Experimental Cell Research, 2010Antizyme inhibitor 1 (AZIN1) and 2 (AZIN2) are proteins that activate ornithine decarboxylase (ODC), the key enzyme of polyamine biosynthesis. Both AZINs release ODC from its inactive complex with antizyme (AZ), leading to formation of the catalytically active ODC.
Kristiina, Kanerva +3 more
openaire +2 more sources
Regulation of ornithine decarboxylase by antizymes and antizyme inhibitor in zebrafish (Danio rerio)
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2002Mammalian polyamine synthesis is regulated by a unique feedback mechanism. When cellular polyamine levels increase, antizyme, an ornithine decarboxylase (ODC) inhibitory protein, is induced by polyamine-dependent translational frameshifting. Antizyme not only inhibits ODC, a key enzyme in polyamine synthesis, it also targets the enzyme degradation by ...
Tomasz, Hascilowicz +3 more
openaire +2 more sources
Cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme inhibitor
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1997We report here cloning and sequencing human antizyme inhibitor from a human kidney cDNA library. Amino acid sequence deduced from the nucleotide sequence shows 92.9% identity to that of rat antizyme inhibitor. Northern blot analysis reveals that antizyme inhibitor is expressed in human liver.
K, Koguchi +5 more
openaire +2 more sources
International Journal of Biochemistry, 1989
1. Ornithine decarboxylase (ODC) was measured in human mononuclear leucocytes (HML) by retention of putrescine on cation exchange paper. 2. The method was validated with unstimulated HML, phytohemagglutinin-stimulated HML, and a commercial preparation of ODC.
D B, Johnson +4 more
openaire +2 more sources
1. Ornithine decarboxylase (ODC) was measured in human mononuclear leucocytes (HML) by retention of putrescine on cation exchange paper. 2. The method was validated with unstimulated HML, phytohemagglutinin-stimulated HML, and a commercial preparation of ODC.
D B, Johnson +4 more
openaire +2 more sources
Purification and characterization of antizyme inhibitor of ornithine decarboxylase from rat liver
Biochimica et Biophysica Acta (BBA) - General Subjects, 1989A protein inhibiting a protein inhibitor (antizyme) to ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) (ODC), antizyme inhibitor, was purified from the liver cytosol of thioacetamide-treated rats by procedures including antizyme affinity chromatography. Overall purification was roughly estimated to be about 17,000,000-fold and recovery
T, Kitani, H, Fujisawa
openaire +2 more sources
Journal of Cellular Physiology, 1982
AbstractThe role of polyamines in myoblast proliferation was studied by treating cells of Yaffe's L6 line of rat myoblasts with inhibitors of polyamine synthesis. Both an irreversible inhibitor of ornithine decarboxylase—difluoromethyl‐ornithine (DFMO)—and a competitive inhibitor of S‐adenosyl‐methionine decarboxylase—methylglyoxal‐bis(guanylhydrazone)
C M, Stoscheck +4 more
openaire +2 more sources
AbstractThe role of polyamines in myoblast proliferation was studied by treating cells of Yaffe's L6 line of rat myoblasts with inhibitors of polyamine synthesis. Both an irreversible inhibitor of ornithine decarboxylase—difluoromethyl‐ornithine (DFMO)—and a competitive inhibitor of S‐adenosyl‐methionine decarboxylase—methylglyoxal‐bis(guanylhydrazone)
C M, Stoscheck +4 more
openaire +2 more sources
Induction of ornithine decarboxylase by transcriptional inhibitors in quiescent thymocytes.
Biochemistry international, 1992The transcriptional inhibitors actinomycin D and dichlororibofuranosylbenzimidazole induced ornithine decarboxylase activity in isolated, quiescent thymocytes, which otherwise did not show detectable levels of the enzyme. This paradoxical induction was transient and dependent on the presence of serum and continuous protein synthesis.
C, Stefanelli +4 more
openaire +1 more source

