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Indolethylamine N-methyltransferase

thioether S-methyltransferase
Top mentioned proteins: HAD, Insulin, neutrophil gelatinase-associated lipocalin, cytokeratin, alpha-adaptin
Papers on thioether S-methyltransferase
Development of the sigma-1 receptor in C-terminals of motoneurons and colocalization with the N,N'-dimethyltryptamine forming enzyme, indole-N-methyl transferase.
Ruoho et al., Madison, United States. In Neuroscience, 2012
We found that indole-N-methyl transferase is localized to postsynaptic sites of C-terminals in close proximity to the S1R
Ability of IDO to attenuate liver injury in alpha-galactosylceramide-induced hepatitis model.
Seishima et al., Gifu, Japan. In J Immunol, 2010
IDO may suppress overactive immune response in the alpha-GalCer-induced hepatitis model.
Fetal arsenic exposure appears to facilitate endocrine disruption by postnatal diethylstilbestrol in neonatal mouse adrenal.
Waalkes et al., United States. In Chem Biol Interact, 2010
The transcripts for homocysteine cycling genes (betaine-homocysteine methyltransferase and thioether S-methyltransferase) and developmental marker genes (alpha-fetoprotein, insulin-like growth factor 2 and IGF binding protein-1), were also higher with arsenic plus DES than either treatment alone.
Aberrant DNA methylation and gene expression in livers of newborn mice transplacentally exposed to a hepatocarcinogenic dose of inorganic arsenic.
Waalkes et al., United States. In Toxicology, 2007
Other expression alterations observed in the arsenic-treated male mouse newborn liver included the overexpression of cdk-inhibitors and stress response genes including increased expression of metallothionein-1 and decreased expression of betaine-homocysteine methyltransferase and thioether S-methyltransferase.
Transplacental exposure to inorganic arsenic at a hepatocarcinogenic dose induces fetal gene expression changes in mice indicative of aberrant estrogen signaling and disrupted steroid metabolism.
Waalkes et al., United States. In Toxicol Appl Pharmacol, 2007
The expression of key genes important in methionine metabolism, such as methionine adenosyltransferase-1a, betaine-homocysteine methyltransferase and thioether S-methyltransferase, were suppressed.
mRNA expression in mouse hypothalamus and basal forebrain during influenza infection: a novel model for sleep regulation.
Toth et al., Springfield, United States. In Physiol Genomics, 2006
Temt (thioether S-methyltransferase), which is located at region B3 of Chr 6, is a potential candidate gene for Srilp.
Differential gene expression in chemically induced mouse lung adenomas.
You et al., Columbus, United States. In Neoplasia, 2003
Reproducibly overexpressed genes included ERK-1, JAK-1, surfactant proteins A, B, and C, NFAT1, alpha-1 protease inhibitor, helix-loop-helix ubiquitous kinase (CHUK), alpha-adaptin, alpha-1 PI2, thioether S-methyltransferase, and CYP2C40.
Suicide inactivation of thioether S-methyltransferase by ethyl sulfide.
Hoffman et al., Bethesda, United States. In Biochemistry, 1996
Thioether S-methyltransferase is an important enzyme in the metabolism of sulfur and selenium-containing compounds in animals.
Cloning and base sequence analysis of a cDNA encoding mouse lung thioether S-methyltransferase.
Hoffman et al., Bethesda, United States. In Biochim Biophys Acta, 1995
Thioether S-methyltransferase catalyzes transfer of the methyl group from S-adenosylmethionine to X in compounds of the structure R-X-R', where X may be sulfur, selenium, or tellurium, and R and R' may be various organic groups.
Sequential methylation of 2-mercaptoethanol to the dimethyl sulfonium ion, 2-(dimethylthio)ethanol, in vivo and in vitro.
Hoffman et al., Philadelphia, United States. In Biochem Pharmacol, 1994
Thioether methyltransferase (S-adenosyl-L-methionine: thioether S-methyltransferase; EC
S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism.
Hoffman et al., Louisville, United States. In J Biol Chem, 1988
An assay has been developed for the enzyme, S-adenosylmethionine:thioether S-methyltransferase, responsible for this final methylation reaction.
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