| pubmed-article:9826174 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9826174 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:9826174 | lifeskim:mentions | umls-concept:C0039938 | lld:lifeskim |
| pubmed-article:9826174 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:9826174 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:9826174 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:9826174 | lifeskim:mentions | umls-concept:C1511539 | lld:lifeskim |
| pubmed-article:9826174 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9826174 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9826174 | pubmed:dateCreated | 1998-12-7 | lld:pubmed |
| pubmed-article:9826174 | pubmed:abstractText | The mechanism of disulfide reduction by thioredoxin in the cell is thought to occur through the formation and subsequent destruction of a mixed-disulfide intermediate between thioredoxin and the substrate. In order to model the interaction, we have prepared a mutant of Escherichia coli thioredoxin where the second cysteine residue of the active site has been replaced by an alanine residue. A specific covalent complex has been prepared between the remaining cysteine residue and a short cysteine-containing peptide. This paper describes the preparation and characterization of the mutant protein both free and in the peptide complex. | lld:pubmed |
| pubmed-article:9826174 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9826174 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9826174 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9826174 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9826174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9826174 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9826174 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9826174 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9826174 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:9826174 | pubmed:author | pubmed-author:HolmgrenAA | lld:pubmed |
| pubmed-article:9826174 | pubmed:author | pubmed-author:TennantL LLL | lld:pubmed |
| pubmed-article:9826174 | pubmed:author | pubmed-author:DysonH JHJ | lld:pubmed |
| pubmed-article:9826174 | pubmed:author | pubmed-author:ReymondM TMT | lld:pubmed |
| pubmed-article:9826174 | pubmed:author | pubmed-author:JengM FMF | lld:pubmed |
| pubmed-article:9826174 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9826174 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9826174 | pubmed:volume | 257 | lld:pubmed |
| pubmed-article:9826174 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9826174 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9826174 | pubmed:pagination | 299-308 | lld:pubmed |
| pubmed-article:9826174 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:9826174 | pubmed:meshHeading | pubmed-meshheading:9826174-... | lld:pubmed |
| pubmed-article:9826174 | pubmed:meshHeading | pubmed-meshheading:9826174-... | lld:pubmed |
| pubmed-article:9826174 | pubmed:meshHeading | pubmed-meshheading:9826174-... | lld:pubmed |
| pubmed-article:9826174 | pubmed:meshHeading | pubmed-meshheading:9826174-... | lld:pubmed |
| pubmed-article:9826174 | pubmed:meshHeading | pubmed-meshheading:9826174-... | lld:pubmed |
| pubmed-article:9826174 | pubmed:meshHeading | pubmed-meshheading:9826174-... | lld:pubmed |
| pubmed-article:9826174 | pubmed:meshHeading | pubmed-meshheading:9826174-... | lld:pubmed |
| pubmed-article:9826174 | pubmed:meshHeading | pubmed-meshheading:9826174-... | lld:pubmed |
| pubmed-article:9826174 | pubmed:meshHeading | pubmed-meshheading:9826174-... | lld:pubmed |
| pubmed-article:9826174 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9826174 | pubmed:articleTitle | NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex. | lld:pubmed |
| pubmed-article:9826174 | pubmed:affiliation | Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. | lld:pubmed |
| pubmed-article:9826174 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9826174 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9826174 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9826174 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9826174 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9826174 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9826174 | lld:pubmed |
