pubmed-article:12427017 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12427017 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:12427017 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:12427017 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:12427017 | pubmed:issue | 46 | lld:pubmed |
pubmed-article:12427017 | pubmed:dateCreated | 2002-11-12 | lld:pubmed |
pubmed-article:12427017 | pubmed:abstractText | It has become increasingly evident that nitric oxide exerts its effects, in part, by S-nitrosylation of cysteine residues. We tested in vitro whether nitric oxide may indirectly control p53 by S-nitrosylation and inactivation of the p53 negative regulator, Hdm2. Treatment of Hdm2 with a nitric oxide donor inhibits Hdm2-p53 binding, a critical step in Hdm2 regulation of p53. The presence of excess amounts of cysteine or dithiothreitol blocks this inhibition of binding. Moreover, nitric oxide inhibition of Hdm2-p53 binding was found to be reversible. Sulfhydryl sensitivity and reversibility are consistent with nitrosylation. Finally, we have identified a critical cysteine residue that nitric oxide modifies to disrupt Hdm2-p53 binding. This cysteine is proximal to the Hdm2-p53 binding interface and is conserved across species from zebrafish to humans. Mutation of this residue from a cysteine to an alanine does not interfere with binding but rather eliminates the sensitivity of Hdm2 to nitric oxide inactivation. | lld:pubmed |
pubmed-article:12427017 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:language | eng | lld:pubmed |
pubmed-article:12427017 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12427017 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12427017 | pubmed:month | Nov | lld:pubmed |
pubmed-article:12427017 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:12427017 | pubmed:author | pubmed-author:SchifferCelia... | lld:pubmed |
pubmed-article:12427017 | pubmed:author | pubmed-author:JonesStephen... | lld:pubmed |
pubmed-article:12427017 | pubmed:author | pubmed-author:RossAlonzo... | lld:pubmed |
pubmed-article:12427017 | pubmed:author | pubmed-author:SchonhoffChri... | lld:pubmed |
pubmed-article:12427017 | pubmed:author | pubmed-author:DaouMarie-Cla... | lld:pubmed |
pubmed-article:12427017 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12427017 | pubmed:day | 19 | lld:pubmed |
pubmed-article:12427017 | pubmed:volume | 41 | lld:pubmed |
pubmed-article:12427017 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12427017 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12427017 | pubmed:pagination | 13570-4 | lld:pubmed |
pubmed-article:12427017 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:12427017 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12427017 | pubmed:articleTitle | Nitric oxide-mediated inhibition of Hdm2-p53 binding. | lld:pubmed |
pubmed-article:12427017 | pubmed:affiliation | Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA. | lld:pubmed |
pubmed-article:12427017 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12427017 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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