Results 261 to 270 of about 60,031 (297)
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S-Adenosylmethionine

The International Journal of Biochemistry & Cell Biology, 2000
S-Adenosyl-Lmethionine (SAM) is an important molecule in normal cell function and survival. SAM is utilized by three key metabolic pathways: transmethylation; transsulfuration; and polyamine synthesis. In transmethylation reactions, the methyl group of SAM is donated to a large variety of acceptor substrates including DNA, phospholipids and proteins ...
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S-adenosylmethionine and affective disorder

The American Journal of Medicine, 1987
Several open and double-blind studies suggest that SAMe may have an anti-depressant effect, and further studies are indicated. SAMe may exert a beneficial effect selectively on endogenous rather than neurotic depression. SAMe crosses the blood-brain barrier. SAMe is involved in several central enzyme pathways relating to transmethylation and folate and
M W, Carney, B K, Toone, E H, Reynolds
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S-adenosylmethionine and its products

Amino Acids, 2007
S-adenosylmethionine is involved in many processes, mainly methylation, polyamine synthesis and radical-based catalysis. It is synthesised through the catalysis of differently regulated enzyme forms. When it is used, the compounds formed are reutilized in different ways: in case of methylation, its end product is homocysteine, which can be remethylated
GRILLO MA, COLOMBATTO, Sebastiano
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Potential inhibitors of S-adenosylmethionine-dependent methyltransferases. 6. Structural modifications of S-adenosylmethionine

Journal of Medicinal Chemistry, 1976
Structural analogues of S-adenosyl-L-methionine (SAM), with modifications in the amino acid, sugar, or base portions of the molecule, have been synthesized and evaluated as either inhibitors and/or substrates for the enzymes catechol O-methyltransferase, phenylethanolamine N-methyltransferase, histamine N-methyltransferase, and hydroxyindole O ...
R T, Borchardt   +3 more
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On Lowering S-Adenosylmethionine

1978
L-Dopa produces a marked lowering of brain S-adenosylmethionine (8), but nicotinamide, although also a methyl group acceptor, does not (3). It would be interesting to have a theoretical explanation for this difference in activity, especially if it would help in the selection of new agents which might have S-adenosylmethionine lowering activity.
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SAMe: S-Adenosylmethionine

American Journal of Health-System Pharmacy, 2000
J C, Echols, U, Naidoo, C, Salzman
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Assay for S-adenosylmethionine: Methionine methyltransferase

Analytical Biochemistry, 1973
Abstract A quantitative assay for S-adenosylmethionine: methionine methyltransferase in phosphate buffer extracts has been developed. This enzyme catalyzes the biosynthesis of S-methylmethionine from methionine and S-adenosylmethionine. The radioactively labeled product, S-methylmethionine, is first separated from the radioactively labeled substrate,
B D, Allamong, L, Abrahamson
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S-adenosylmethionine decarboxylase from human placenta

International Journal of Biochemistry, 1977
Abstract 1. 1. S-adenosylmethionine decarboxylase from human placenta has been purified more than 1200-fold by use of Chromatographic techniques. 2. 2. The molecular weight was determined as approx 53,000 by gel nitration. 3. 3. The enzyme preparations were quite unstable in the absence of reducing agents; the crude enzyme was rapidly ...
PORTA, RAFFAELE   +2 more
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Inhibition of angiogenesis by S-adenosylmethionine

Biochemical and Biophysical Research Communications, 2011
Metastasis is a leading cause of mortality and morbidity in cancer. One of the steps in metastasis process is the formation of new blood vessels. Aberrant DNA methylation patterns are common in cancer cells. In recent studies, S-adenosylmethionine (SAM), which is a DNA methylating agent, has been found to have inhibitory effects on some carcinoma cells
Mehmet, Sahin   +4 more
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The synthesis of S-adenosylmethionine by mutants with defects in S-adenosylmethionine synthetase

Molecular and General Genetics MGG, 1976
Some metK mutants of Salmonella typhimurium with constitutive methionine biosynthesis have no detectable S-adenosylmethionine (SAM) synthetase, the enzyme which converts methionine to SAM, the postulated corepressor of the methionine pathway. However, these mutants are not auxotrophic for SAM, an essential compound for many reactions.
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