| pubmed-article:9655824 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9655824 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:9655824 | lifeskim:mentions | umls-concept:C0017837 | lld:lifeskim |
| pubmed-article:9655824 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:9655824 | lifeskim:mentions | umls-concept:C1511997 | lld:lifeskim |
| pubmed-article:9655824 | lifeskim:mentions | umls-concept:C0205430 | lld:lifeskim |
| pubmed-article:9655824 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:9655824 | pubmed:dateCreated | 1998-8-12 | lld:pubmed |
| pubmed-article:9655824 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9655824 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9655824 | pubmed:abstractText | Glutathione S-transferases (GSTs) are a multifunctional group of enzymes, widely distributed in aerobic organisms, that have a critical role in the cellular detoxification process. Unlike their mammalian counterparts, bacterial GSTs often catalyze quite specific reactions, suggesting that their roles in bacteria might be different. The GST from Proteus mirabilis (PmGST B1-1) is known to bind certain antibiotics tightly and reduce the antimicrobial activity of beta-lactam drugs. Hence, bacterial GSTs may play a part in bacterial resistance towards antibiotics and are the subject of intense interest. | lld:pubmed |
| pubmed-article:9655824 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9655824 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9655824 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9655824 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9655824 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:9655824 | pubmed:author | pubmed-author:ParkerM WMW | lld:pubmed |
| pubmed-article:9655824 | pubmed:author | pubmed-author:AllocatiNN | lld:pubmed |
| pubmed-article:9655824 | pubmed:author | pubmed-author:PolekhinaGG | lld:pubmed |
| pubmed-article:9655824 | pubmed:author | pubmed-author:FeilS CSC | lld:pubmed |
| pubmed-article:9655824 | pubmed:author | pubmed-author:RossjohnJJ | lld:pubmed |
| pubmed-article:9655824 | pubmed:author | pubmed-author:MasulliMM | lld:pubmed |
| pubmed-article:9655824 | pubmed:author | pubmed-author:De IllioCC | lld:pubmed |
| pubmed-article:9655824 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9655824 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9655824 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:9655824 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9655824 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9655824 | pubmed:pagination | 721-34 | lld:pubmed |
| pubmed-article:9655824 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:9655824 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9655824 | pubmed:articleTitle | A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. | lld:pubmed |
| pubmed-article:9655824 | pubmed:affiliation | The Ian Potter Foundation Protein Crystallography Laboratory St Vincent's Institute of Medical Research 41 Victoria Parade, Fitzroy, Victoria, 3065, Australia. | lld:pubmed |
| pubmed-article:9655824 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9655824 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9655824 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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