| pubmed-article:8672462 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C0023690 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C0003765 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C1533698 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C0449829 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C0013845 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:8672462 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8672462 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:8672462 | pubmed:dateCreated | 1996-8-15 | lld:pubmed |
| pubmed-article:8672462 | pubmed:abstractText | The electron paramagnetic resonance spectra of the heme domain of inducible nitric oxide synthase (iNOS) demonstrate a close relationship to the corresponding spectra of the neuronal isoform (nNOS). The binding of ligands to the iNOS arginine site perturbs the environment of the high-spin ferriheme in a highly ligand-specific manner. The iNOS forms five-coordinate, high-spin complexes with arginine analogs which are clearly related to the corresponding complexes of nNOS. Studies indicate that the binding of L-arginine, N(omega)-hydroxy-L-arginine (NHA), and N(omega)-methyl-L-arginine (NMA) produces various spectroscopic species closely corresponding to the equivalent complexes of nNOS, while N(omega)-nitro-L-arginine (NNA) binding produces a state which appears intermediate in character between the nNOS NNA and arginine complexes. These spectroscopic studies have permitted the determination of ligand-specific high-spin states which reveal similarities and differences between iNOS and nNOS. | lld:pubmed |
| pubmed-article:8672462 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8672462 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8672462 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8672462 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8672462 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8672462 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8672462 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8672462 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8672462 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8672462 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8672462 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8672462 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8672462 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8672462 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8672462 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8672462 | pubmed:author | pubmed-author:MastersB SBS | lld:pubmed |
| pubmed-article:8672462 | pubmed:author | pubmed-author:SalernoJ CJC | lld:pubmed |
| pubmed-article:8672462 | pubmed:author | pubmed-author:RomanL JLJ | lld:pubmed |
| pubmed-article:8672462 | pubmed:author | pubmed-author:MartasekPP | lld:pubmed |
| pubmed-article:8672462 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8672462 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:8672462 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:8672462 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8672462 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8672462 | pubmed:pagination | 7626-30 | lld:pubmed |
| pubmed-article:8672462 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8672462 | pubmed:meshHeading | pubmed-meshheading:8672462-... | lld:pubmed |
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| pubmed-article:8672462 | pubmed:meshHeading | pubmed-meshheading:8672462-... | lld:pubmed |
| pubmed-article:8672462 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8672462 | pubmed:articleTitle | Electron paramagnetic resonance spectroscopy of the heme domain of inducible nitric oxide synthase: binding of ligands at the arginine site induces changes in the heme ligation geometry. | lld:pubmed |
| pubmed-article:8672462 | pubmed:affiliation | Rensselaer Polytechnic Institute, Troy, New York 12180, USA. | lld:pubmed |
| pubmed-article:8672462 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8672462 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8672462 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
