| http://purl.uniprot.org/citations/23017368 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23017368 | http://www.w3.org/2000/01/rdf-schema#comment | "S-adenosyl-L-methionine (AdoMet)-dependent methylation is central to the regulation of many biological processes: more than 50 AdoMet-dependent methyltransferases methylate a broad spectrum of cellular compounds including nucleic acids, proteins and lipids. Common to all AdoMet-dependent methyltransferase reactions is the release of the strong product inhibitor S-adenosyl-L-homocysteine (AdoHcy), as a by-product of the reaction. S-adenosyl-L-homocysteine hydrolase is the only eukaryotic enzyme capable of reversible AdoHcy hydrolysis to adenosine and homocysteine and, thus, relief from AdoHcy inhibition. Impaired S-adenosyl-L-homocysteine hydrolase activity in humans results in AdoHcy accumulation and severe pathological consequences. Hyperhomocysteinemia, which is characterized by elevated levels of homocysteine in blood, also exhibits a similar phenotype of AdoHcy accumulation due to the reversal of the direction of the S-adenosyl-L-homocysteine hydrolase reaction. Inhibition of S-adenosyl-L-homocysteine hydrolase is also linked to antiviral effects. In this review the advantages of yeast as an experimental system to understand pathologies associated with AdoHcy accumulation will be discussed."xsd:string |
| http://purl.uniprot.org/citations/23017368 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbadis.2012.09.007"xsd:string |
| http://purl.uniprot.org/citations/23017368 | http://purl.uniprot.org/core/author | "Pavkov-Keller T."xsd:string |
| http://purl.uniprot.org/citations/23017368 | http://purl.uniprot.org/core/author | "Keller W."xsd:string |
| http://purl.uniprot.org/citations/23017368 | http://purl.uniprot.org/core/author | "Tehlivets O."xsd:string |
| http://purl.uniprot.org/citations/23017368 | http://purl.uniprot.org/core/author | "Malanovic N."xsd:string |
| http://purl.uniprot.org/citations/23017368 | http://purl.uniprot.org/core/author | "Visram M."xsd:string |
| http://purl.uniprot.org/citations/23017368 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23017368 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta"xsd:string |
| http://purl.uniprot.org/citations/23017368 | http://purl.uniprot.org/core/pages | "204-215"xsd:string |
| http://purl.uniprot.org/citations/23017368 | http://purl.uniprot.org/core/title | "S-adenosyl-L-homocysteine hydrolase and methylation disorders: yeast as a model system."xsd:string |
| http://purl.uniprot.org/citations/23017368 | http://purl.uniprot.org/core/volume | "1832"xsd:string |
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