| pubmed-article:10623879 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10623879 | lifeskim:mentions | umls-concept:C0017037 | lld:lifeskim |
| pubmed-article:10623879 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10623879 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10623879 | pubmed:dateCreated | 2000-1-27 | lld:pubmed |
| pubmed-article:10623879 | pubmed:abstractText | Glutathione is an important antioxidant that is involved in numerous cellular activities. gamma-Glutamylcysteine synthetase (gammaGCS) is a key regulatory enzyme in the synthesis of glutathione. It is a heterodimeric zinc metalloprotein that belongs to a unique class of proteins that gain activity due to formation of a reversible disulfide bond. The two subunits of gammaGCS exhibit differential and coordinate transcription regulation. In addition, the subunits are regulated at the posttranscriptional and posttranslational levels. These various levels of regulation allow numerous stimuli to induce or inhibit activity. | lld:pubmed |
| pubmed-article:10623879 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10623879 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10623879 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10623879 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10623879 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10623879 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10623879 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10623879 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10623879 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:10623879 | pubmed:issn | 0021-9541 | lld:pubmed |
| pubmed-article:10623879 | pubmed:author | pubmed-author:FreemanM LML | lld:pubmed |
| pubmed-article:10623879 | pubmed:author | pubmed-author:MeredithM JMJ | lld:pubmed |
| pubmed-article:10623879 | pubmed:author | pubmed-author:SekharK RKR | lld:pubmed |
| pubmed-article:10623879 | pubmed:author | pubmed-author:Soltaninassab... | lld:pubmed |
| pubmed-article:10623879 | pubmed:copyrightInfo | Copyright 2000 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:10623879 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10623879 | pubmed:volume | 182 | lld:pubmed |
| pubmed-article:10623879 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10623879 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10623879 | pubmed:pagination | 163-70 | lld:pubmed |
| pubmed-article:10623879 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:10623879 | pubmed:meshHeading | pubmed-meshheading:10623879... | lld:pubmed |
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| pubmed-article:10623879 | pubmed:meshHeading | pubmed-meshheading:10623879... | lld:pubmed |
| pubmed-article:10623879 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10623879 | pubmed:articleTitle | Multi-faceted regulation of gamma-glutamylcysteine synthetase. | lld:pubmed |
| pubmed-article:10623879 | pubmed:affiliation | Department of Radiation Oncology, Vanderbilt University School of Medicine and Vanderbilt-Ingram Cancer Center, Nashville, TN 37232, USA. | lld:pubmed |
| pubmed-article:10623879 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10623879 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10623879 | pubmed:publicationType | Review | lld:pubmed |
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