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pubmed-article:2268358pubmed:abstractTextThe substitution of aspartic acid for the naturally-occurring histidine residue in position B10 in human insulin results in an insulin analogue which displays an in vitro potency 4- to 5-fold greater than the parent compound. This substitution has been introduced into six insulin analogues which, before modification, display potencies ranging from less than 0.01-fold to 3-fold relative to natural insulin. In each case, the resulting aspartic acid-substituted analogue is substantially more potent than the parent compound. Thus, it is now possible to prepare "tailor-made" insulins with enhanced potency.lld:pubmed
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pubmed-article:2268358pubmed:dateRevised2011-11-17lld:pubmed
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pubmed-article:2268358pubmed:articleTitleSuperactive insulins.lld:pubmed
pubmed-article:2268358pubmed:affiliationDepartment of Biochemistry, Mount Sinai School of Medicine, City University of New York, New York 10029-6574.lld:pubmed
pubmed-article:2268358pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2268358pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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