| pubmed-article:1879526 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1879526 | lifeskim:mentions | umls-concept:C1261322 | lld:lifeskim |
| pubmed-article:1879526 | lifeskim:mentions | umls-concept:C0178555 | lld:lifeskim |
| pubmed-article:1879526 | lifeskim:mentions | umls-concept:C0066319 | lld:lifeskim |
| pubmed-article:1879526 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:1879526 | pubmed:dateCreated | 1991-9-27 | lld:pubmed |
| pubmed-article:1879526 | pubmed:abstractText | A model of tryptophan tryptophylquinone (TTQ), recently proposed by McIntire et al. (Science (1991) 252, 817-824) to be the prosthetic group of the quinoprotein methylamine dehydrogenase, has been compared with electron density maps of this dehydrogenase from Thiobacillus versutus and Paracoccus denitrificans. The comparison shows that the TTQ model can be neatly accommodated, providing strong supportive evidence that TTQ is indeed the cofactor for this group of quinoproteins. | lld:pubmed |
| pubmed-article:1879526 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1879526 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1879526 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1879526 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1879526 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1879526 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1879526 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:1879526 | pubmed:author | pubmed-author:HolW GWG | lld:pubmed |
| pubmed-article:1879526 | pubmed:author | pubmed-author:DuineJ AJA | lld:pubmed |
| pubmed-article:1879526 | pubmed:author | pubmed-author:MathewsF SFS | lld:pubmed |
| pubmed-article:1879526 | pubmed:author | pubmed-author:DYALJ AJA | lld:pubmed |
| pubmed-article:1879526 | pubmed:author | pubmed-author:DavidsonV LVL | lld:pubmed |
| pubmed-article:1879526 | pubmed:author | pubmed-author:HuizingaE GEG | lld:pubmed |
| pubmed-article:1879526 | pubmed:author | pubmed-author:VellieuxF MFM | lld:pubmed |
| pubmed-article:1879526 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1879526 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1879526 | pubmed:volume | 287 | lld:pubmed |
| pubmed-article:1879526 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1879526 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1879526 | pubmed:pagination | 163-6 | lld:pubmed |
| pubmed-article:1879526 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:1879526 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1879526 | pubmed:articleTitle | Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase. | lld:pubmed |
| pubmed-article:1879526 | pubmed:affiliation | Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110. | lld:pubmed |
| pubmed-article:1879526 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1879526 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1879526 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1879526 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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