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| pubmed-article:2649090 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:2649090 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:2649090 | lifeskim:mentions | umls-concept:C1150171 | lld:lifeskim |
| pubmed-article:2649090 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:2649090 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2649090 | pubmed:dateCreated | 1989-5-4 | lld:pubmed |
| pubmed-article:2649090 | pubmed:abstractText | Inhibitor studies were performed on the two endopeptidase activities involved in proinsulin conversion in isolated insulin secretory granules [Davidson, Rhodes & Hutton (1988) Nature (London) 333, 93-96]. The active-site-directed peptides L-alanyl-L-arginyl-L-arginylmethyldimethylsulphonium and L-alanyl-L-lysyl-L-arginylmethyldimethylsulphonium inhibited these activities in accordance with the observed cleavage pattern, suggesting that the primary amino acid sequence of the dibasic site was an important determinant of the endopeptidase substrate specificities. | lld:pubmed |
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| pubmed-article:2649090 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2649090 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2649090 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2649090 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2649090 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2649090 | pubmed:author | pubmed-author:HuttonJ CJC | lld:pubmed |
| pubmed-article:2649090 | pubmed:author | pubmed-author:ShawEE | lld:pubmed |
| pubmed-article:2649090 | pubmed:author | pubmed-author:RhodesC JCJ | lld:pubmed |
| pubmed-article:2649090 | pubmed:author | pubmed-author:BailyesE MEM | lld:pubmed |
| pubmed-article:2649090 | pubmed:author | pubmed-author:ZumbrunnAA | lld:pubmed |
| pubmed-article:2649090 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2649090 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2649090 | pubmed:volume | 258 | lld:pubmed |
| pubmed-article:2649090 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2649090 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2649090 | pubmed:pagination | 305-8 | lld:pubmed |
| pubmed-article:2649090 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2649090 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2649090 | pubmed:articleTitle | The inhibition of proinsulin-processing endopeptidase activities by active-site-directed peptides. | lld:pubmed |
| pubmed-article:2649090 | pubmed:affiliation | Department of Clinical Biochemistry, University of Cambridge, Addenbrooke's Hospital, U.K. | lld:pubmed |
| pubmed-article:2649090 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2649090 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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