| pubmed-article:11394913 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11394913 | lifeskim:mentions | umls-concept:C0132555 | lld:lifeskim |
| pubmed-article:11394913 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:11394913 | lifeskim:mentions | umls-concept:C0085862 | lld:lifeskim |
| pubmed-article:11394913 | lifeskim:mentions | umls-concept:C1299583 | lld:lifeskim |
| pubmed-article:11394913 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:11394913 | lifeskim:mentions | umls-concept:C1608386 | lld:lifeskim |
| pubmed-article:11394913 | lifeskim:mentions | umls-concept:C1549571 | lld:lifeskim |
| pubmed-article:11394913 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11394913 | pubmed:dateCreated | 2001-6-7 | lld:pubmed |
| pubmed-article:11394913 | pubmed:abstractText | Ca2+-independent forms of nitric-oxide synthase have significant activity when the endogenous calmodulin subunit is Ca2+ free. Further activation is seen when Ca2+ is added. We have examined the activation of a Ca2+-independent nitric-oxide synthase variant and its two point mutants that are more dependent on Ca2+ for activation using mutant calmodulins containing non-functional Ca2+-binding sites. These studies provide evidence that the Ca2+-independent activity of these enzymes can be exerted through specific adapted interactions between the enzyme and the Ca2+-binding site 2 of calmodulin. Further, the results suggest that EGTA-sensitive metals other than Ca2+ complexed to calmodulin may be involved in maximal activation of these nitric-oxide synthase variants. | lld:pubmed |
| pubmed-article:11394913 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:keyword | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11394913 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11394913 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11394913 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11394913 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:11394913 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:11394913 | pubmed:author | pubmed-author:StullJ TJT | lld:pubmed |
| pubmed-article:11394913 | pubmed:author | pubmed-author:LeeS JSJ | lld:pubmed |
| pubmed-article:11394913 | pubmed:author | pubmed-author:BeckinghamKK | lld:pubmed |
| pubmed-article:11394913 | pubmed:copyrightInfo | Copyright 2001 Academic Press. | lld:pubmed |
| pubmed-article:11394913 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11394913 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:11394913 | pubmed:volume | 284 | lld:pubmed |
| pubmed-article:11394913 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11394913 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11394913 | pubmed:pagination | 526-30 | lld:pubmed |
| pubmed-article:11394913 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:meshHeading | pubmed-meshheading:11394913... | lld:pubmed |
| pubmed-article:11394913 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11394913 | pubmed:articleTitle | Ca2+-independent activity of nitric oxide synthase. | lld:pubmed |
| pubmed-article:11394913 | pubmed:affiliation | Department of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9040, USA. slee@resgen.com | lld:pubmed |
| pubmed-article:11394913 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11394913 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11394913 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:36329 | entrezgene:pubmed | pubmed-article:11394913 | lld:entrezgene |
