| pubmed-article:9202340 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C0524851 | lld:lifeskim |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C0033679 | lld:lifeskim |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C0032214 | lld:lifeskim |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C1441290 | lld:lifeskim |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9202340 | lifeskim:mentions | umls-concept:C0384782 | lld:lifeskim |
| pubmed-article:9202340 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9202340 | pubmed:dateCreated | 1997-7-24 | lld:pubmed |
| pubmed-article:9202340 | pubmed:abstractText | Huntington's disease and six other neurodegenerative diseases are associated with abnormal gene products containing expanded polyglutamine (poly-Q; Qn) domains (n > or = 40). In the present work, we show that glutathione S-transferase (GST) fusion proteins containing a small, physiological-length poly-Q domain (GSTQ10) or a large, pathological-length poly-Q domain (GSTQ62) are excellent substrates of guinea pig liver (tissue) transglutaminase and that both GSTQ10 and GSTQ62 are activators of tissue transglutaminase-catalyzed hydroxaminolysis of N-alpha-carbobenzoxyglutaminylglycine. The present findings have implications for understanding the pathophysiological mechanisms of expanded CAG/poly-Q domain diseases. | lld:pubmed |
| pubmed-article:9202340 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202340 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9202340 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202340 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9202340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9202340 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9202340 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9202340 | pubmed:issn | 0022-3042 | lld:pubmed |
| pubmed-article:9202340 | pubmed:author | pubmed-author:RosesA DAD | lld:pubmed |
| pubmed-article:9202340 | pubmed:author | pubmed-author:CooperA JAJ | lld:pubmed |
| pubmed-article:9202340 | pubmed:author | pubmed-author:StrittmatterW... | lld:pubmed |
| pubmed-article:9202340 | pubmed:author | pubmed-author:BlassJ PJP | lld:pubmed |
| pubmed-article:9202340 | pubmed:author | pubmed-author:BurkaJ FJF | lld:pubmed |
| pubmed-article:9202340 | pubmed:author | pubmed-author:SheuK FKF | lld:pubmed |
| pubmed-article:9202340 | pubmed:author | pubmed-author:OnoderaOO | lld:pubmed |
| pubmed-article:9202340 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9202340 | pubmed:volume | 69 | lld:pubmed |
| pubmed-article:9202340 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9202340 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9202340 | pubmed:pagination | 431-4 | lld:pubmed |
| pubmed-article:9202340 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9202340 | pubmed:meshHeading | pubmed-meshheading:9202340-... | lld:pubmed |
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| pubmed-article:9202340 | pubmed:meshHeading | pubmed-meshheading:9202340-... | lld:pubmed |
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| pubmed-article:9202340 | pubmed:meshHeading | pubmed-meshheading:9202340-... | lld:pubmed |
| pubmed-article:9202340 | pubmed:meshHeading | pubmed-meshheading:9202340-... | lld:pubmed |
| pubmed-article:9202340 | pubmed:meshHeading | pubmed-meshheading:9202340-... | lld:pubmed |
| pubmed-article:9202340 | pubmed:meshHeading | pubmed-meshheading:9202340-... | lld:pubmed |
| pubmed-article:9202340 | pubmed:meshHeading | pubmed-meshheading:9202340-... | lld:pubmed |
| pubmed-article:9202340 | pubmed:meshHeading | pubmed-meshheading:9202340-... | lld:pubmed |
| pubmed-article:9202340 | pubmed:meshHeading | pubmed-meshheading:9202340-... | lld:pubmed |
| pubmed-article:9202340 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9202340 | pubmed:articleTitle | Polyglutamine domains are substrates of tissue transglutaminase: does transglutaminase play a role in expanded CAG/poly-Q neurodegenerative diseases? | lld:pubmed |
| pubmed-article:9202340 | pubmed:affiliation | Department of Biochemistry, Cornell University Medical College, New York, New York, U.S.A. | lld:pubmed |
| pubmed-article:9202340 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9202340 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9202340 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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