| pubmed-article:15369390 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15369390 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:15369390 | lifeskim:mentions | umls-concept:C0019587 | lld:lifeskim |
| pubmed-article:15369390 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:15369390 | lifeskim:mentions | umls-concept:C1412431 | lld:lifeskim |
| pubmed-article:15369390 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:15369390 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:15369390 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:15369390 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:15369390 | lifeskim:mentions | umls-concept:C1513371 | lld:lifeskim |
| pubmed-article:15369390 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:15369390 | pubmed:dateCreated | 2004-9-16 | lld:pubmed |
| pubmed-article:15369390 | pubmed:abstractText | We previously reported that substrates of semicarbazide-sensitive amine oxidase in combination with low concentrations of vanadate exert potent insulin-like effects. Here we performed homology modeling of the catalytic domain of mouse SSAO/VAP-1 and searched through chemical databases to identify novel SSAO substrates. The modeling of the catalytic domain revealed that aromatic residues Tyr384, Phe389, and Tyr394 define a pocket of stable size that may participate in the binding of apolar substrates. We identified a number of amines as substrates of human, rat, and mouse SSAO. The compounds PD0119035, 2,3-dimethoxy-benzylamine, and C-naphthalen-1-yl-methylamine showed high affinity as substrates of rat SSAO. C-Naphthalen-1-yl-methylamine was the only substrate that showed high affinity for human SSAO. C-Naphthalen-1-yl-methylamine and 4-aminomethyl-benzenesulfonamide showed the highest capacity to stimulate glucose transport in isolated rat adipocytes. The impact of these findings on the development of new treatments for diabetes is discussed. | lld:pubmed |
| pubmed-article:15369390 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15369390 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15369390 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15369390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15369390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15369390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15369390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15369390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15369390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15369390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15369390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15369390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15369390 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15369390 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15369390 | pubmed:issn | 0022-2623 | lld:pubmed |
| pubmed-article:15369390 | pubmed:author | pubmed-author:OrozcoModesto... | lld:pubmed |
| pubmed-article:15369390 | pubmed:author | pubmed-author:UnzetaMercede... | lld:pubmed |
| pubmed-article:15369390 | pubmed:author | pubmed-author:De La... | lld:pubmed |
| pubmed-article:15369390 | pubmed:author | pubmed-author:PalacínManuel... | lld:pubmed |
| pubmed-article:15369390 | pubmed:author | pubmed-author:ZorzanoAntoni... | lld:pubmed |
| pubmed-article:15369390 | pubmed:author | pubmed-author:MartiLucL | lld:pubmed |
| pubmed-article:15369390 | pubmed:author | pubmed-author:TestarXavierX | lld:pubmed |
| pubmed-article:15369390 | pubmed:author | pubmed-author:CarpénéChrist... | lld:pubmed |
| pubmed-article:15369390 | pubmed:author | pubmed-author:AbellaAnnaA | lld:pubmed |
| pubmed-article:15369390 | pubmed:author | pubmed-author:García-Vicent... | lld:pubmed |
| pubmed-article:15369390 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15369390 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:15369390 | pubmed:volume | 47 | lld:pubmed |
| pubmed-article:15369390 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15369390 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15369390 | pubmed:pagination | 4865-74 | lld:pubmed |
| pubmed-article:15369390 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:15369390 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15369390 | pubmed:articleTitle | Exploring the binding mode of semicarbazide-sensitive amine oxidase/VAP-1: identification of novel substrates with insulin-like activity. | lld:pubmed |
| pubmed-article:15369390 | pubmed:affiliation | Parc Científic de Barcelona and Departament de Bioquímica i Biologia Molecular, Facultat de Biologia, Universitat de Barcelona, Avda. Diagonal 645, E-08028 Barcelona, Spain. | lld:pubmed |
| pubmed-article:15369390 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15369390 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:15369390 | lld:chembl |
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