| pubmed-article:11576537 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11576537 | lifeskim:mentions | umls-concept:C0331570 | lld:lifeskim |
| pubmed-article:11576537 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:11576537 | lifeskim:mentions | umls-concept:C0039938 | lld:lifeskim |
| pubmed-article:11576537 | lifeskim:mentions | umls-concept:C0065559 | lld:lifeskim |
| pubmed-article:11576537 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11576537 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11576537 | pubmed:dateCreated | 2001-9-28 | lld:pubmed |
| pubmed-article:11576537 | pubmed:abstractText | The activation pathway of the chloroplastic NADP-dependent malate dehydrogenase (MDH) by reduced thioredoxin has been examined using a method based on the mechanism of thiol/disulfide interchanges, i.e. the transient formation of a mixed disulfide between the target and the reductant. This disulfide can be stabilized when each of the partners is mutated in the less reactive cysteine of the disulfide/dithiol pair. As NADP-MDH has two regulatory disulfides per monomer, four different single cysteine mutants were examined, two for the C-terminal bridge and two for the N-terminal bridge. The results clearly show that the nucleophilic attack of thioredoxin on the C-terminal bridge proceeds through the formation of a disulfide with the most external Cys377. The results are less clear-cut for the N-terminal cysteines and suggest that the Cys24-Cys207 disulfide bridge previously proposed to be an intermediary step in MDH activation can form only when the C-terminal disulfide is reduced. | lld:pubmed |
| pubmed-article:11576537 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11576537 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11576537 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11576537 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11576537 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11576537 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11576537 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11576537 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11576537 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:11576537 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:11576537 | pubmed:author | pubmed-author:GreenH THT | lld:pubmed |
| pubmed-article:11576537 | pubmed:author | pubmed-author:DecottigniesP... | lld:pubmed |
| pubmed-article:11576537 | pubmed:author | pubmed-author:Miginiac-Masl... | lld:pubmed |
| pubmed-article:11576537 | pubmed:author | pubmed-author:Issakidis-Bou... | lld:pubmed |
| pubmed-article:11576537 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11576537 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:11576537 | pubmed:volume | 505 | lld:pubmed |
| pubmed-article:11576537 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11576537 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11576537 | pubmed:pagination | 405-8 | lld:pubmed |
| pubmed-article:11576537 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:11576537 | pubmed:meshHeading | pubmed-meshheading:11576537... | lld:pubmed |
| pubmed-article:11576537 | pubmed:meshHeading | pubmed-meshheading:11576537... | lld:pubmed |
| pubmed-article:11576537 | pubmed:meshHeading | pubmed-meshheading:11576537... | lld:pubmed |
| pubmed-article:11576537 | pubmed:meshHeading | pubmed-meshheading:11576537... | lld:pubmed |
| pubmed-article:11576537 | pubmed:meshHeading | pubmed-meshheading:11576537... | lld:pubmed |
| pubmed-article:11576537 | pubmed:meshHeading | pubmed-meshheading:11576537... | lld:pubmed |
| pubmed-article:11576537 | pubmed:meshHeading | pubmed-meshheading:11576537... | lld:pubmed |
| pubmed-article:11576537 | pubmed:meshHeading | pubmed-meshheading:11576537... | lld:pubmed |
| pubmed-article:11576537 | pubmed:meshHeading | pubmed-meshheading:11576537... | lld:pubmed |
| pubmed-article:11576537 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11576537 | pubmed:articleTitle | Sites of interaction of thioredoxin with sorghum NADP-malate dehydrogenase. | lld:pubmed |
| pubmed-article:11576537 | pubmed:affiliation | Institut de Biotechnologie des Plantes, UMR CNRS 8618, Université Paris-Sud, Orsay, France. | lld:pubmed |
| pubmed-article:11576537 | pubmed:publicationType | Journal Article | lld:pubmed |
