| pubmed-article:9712828 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9712828 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9712828 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
| pubmed-article:9712828 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:9712828 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9712828 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:9712828 | pubmed:dateCreated | 1998-9-24 | lld:pubmed |
| pubmed-article:9712828 | pubmed:abstractText | Arsenic is a potent toxin and carcinogen. In prokaryotes, arsenic detoxification is accomplished by chromosomal and plasmid-borne operon-encoded efflux systems. We have previously reported the cloning of hASNA-I, a human homologue of arsA encoding the ATPase component of the Escherichia coli arsenite transporter. Purified glutathione S-transferase (GST)-hASNA-I fusion protein was biochemically characterized, and its properties were compared with those of ArsA. The GST-hASNA-I exhibited a basal level of ATPase activity of 18.5 +/- 8 nmol/min/mg in the absence of arsenite. Arsenite produced a 1.6 +/- 0.1-fold stimulation of activity (p = 0. 0044), which was related to an increase in Vmax; antimonite did not stimulate activity. Two lines of evidence suggest that an oligomer is the most likely native form of hASNA-I. First, lysates of human embryo kidney 293 cells overproducing recombinant hASNA-I produced a single monomeric 37-kDa band on SDS-polyacrylamide gel electrophoresis (PAGE) and two distinct species when analyzed using nondenaturing PAGE. Second, chemical cross-linking of the 63-kDa GST-hASNA-I resulted in the formation of dimeric and tetrameric protein forms. The results indicate that hASNA-I is a distinct human arsenite-stimulated ATPase belonging to the same superfamily of ATPases represented by the E. coli ArsA protein. | lld:pubmed |
| pubmed-article:9712828 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9712828 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9712828 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9712828 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9712828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9712828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9712828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9712828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9712828 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9712828 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9712828 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9712828 | pubmed:author | pubmed-author:HeathDD | lld:pubmed |
| pubmed-article:9712828 | pubmed:author | pubmed-author:HowellS BSB | lld:pubmed |
| pubmed-article:9712828 | pubmed:author | pubmed-author:AebiSS | lld:pubmed |
| pubmed-article:9712828 | pubmed:author | pubmed-author:Kurdi-HaidarB... | lld:pubmed |
| pubmed-article:9712828 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9712828 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:9712828 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9712828 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9712828 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9712828 | pubmed:pagination | 22173-6 | lld:pubmed |
| pubmed-article:9712828 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9712828 | pubmed:meshHeading | pubmed-meshheading:9712828-... | lld:pubmed |
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| pubmed-article:9712828 | pubmed:meshHeading | pubmed-meshheading:9712828-... | lld:pubmed |
| pubmed-article:9712828 | pubmed:meshHeading | pubmed-meshheading:9712828-... | lld:pubmed |
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| pubmed-article:9712828 | pubmed:meshHeading | pubmed-meshheading:9712828-... | lld:pubmed |
| pubmed-article:9712828 | pubmed:meshHeading | pubmed-meshheading:9712828-... | lld:pubmed |
| pubmed-article:9712828 | pubmed:meshHeading | pubmed-meshheading:9712828-... | lld:pubmed |
| pubmed-article:9712828 | pubmed:meshHeading | pubmed-meshheading:9712828-... | lld:pubmed |
| pubmed-article:9712828 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9712828 | pubmed:articleTitle | Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I). | lld:pubmed |
| pubmed-article:9712828 | pubmed:affiliation | Department of Medicine and the University of California, San Diego Cancer Center, University of California, San Diego, La Jolla, California 92093-0058, USA. bhaidar@ucsd.edu | lld:pubmed |
| pubmed-article:9712828 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9712828 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9712828 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:439 | entrezgene:pubmed | pubmed-article:9712828 | lld:entrezgene |
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