Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B chain
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Landmarks in insulin researchDesign of an Active Ultrastable Single-chain Insulin Analog: SYNTHESIS, STRUCTURE, AND THERAPEUTIC IMPLICATIONSEnhancing the Activity of a Protein by Stereospecific Unfolding: CONFORMATIONAL LIFE CYCLE OF INSULIN AND ITS EVOLUTIONARY ORIGINSCrystal Structure of a"Nonfoldable"Insulin: IMPAIRED FOLDING EFFICIENCY DESPITE NATIVE ACTIVITYInsulin analog with additional disulfide bond has increased stability and preserved activityInsight into the Structural and Biological Relevance of the T/R Transition of the N-Terminus of the B-Chain in Human InsulinConformational dynamics of insulin.A comparative structural bioinformatics analysis of the insulin receptor family ectodomain based on phylogenetic information.Contribution of residue B5 to the folding and function of insulin and IGF-I: constraints and fine-tuning in the evolution of a protein family.Biophysical optimization of a therapeutic protein by nonstandard mutagenesis: studies of an iodo-insulin derivativeDeciphering a molecular mechanism of neonatal diabetes mellitus by the chemical synthesis of a protein diastereomer, [D-AlaB8]human proinsulin.Deciphering the hidden informational content of protein sequences: foldability of proinsulin hinges on a flexible arm that is dispensable in the mature hormoneThe first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.Proinsulin and the genetics of diabetes mellitusAdditional disulfide bonds in insulin: Prediction, recombinant expression, receptor binding affinity, and stability.The structure and function of insulin: decoding the TR transitionInsulin gene mutations as a cause of permanent neonatal diabetes.The structure of a mutant insulin uncouples receptor binding from protein allostery. An electrostatic block to the TR transition.Diabetes mellitus due to the toxic misfolding of proinsulin variants.Insulin: a small protein with a long journey.The insulin receptor changes conformation in unforeseen ways on ligand binding: sharpening the picture of insulin receptor activation.A conserved histidine in insulin is required for the foldability of human proinsulin: structure and function of an ALAB5 analog.Decoding the cryptic active conformation of a protein by synthetic photoscanning: insulin inserts a detachable arm between receptor domains.All-atom structural models of insulin binding to the insulin receptor in the presence of a tandem hormone-binding element.
P2860
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P2860
Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B chain
description
2005 nî lūn-bûn
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2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2005 թվականի ապրիլին հրատարակված գիտական հոդված
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2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年學術文章
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Chiral mutagenesis of insulin. ...... specific switch in the B chain
@ast
Chiral mutagenesis of insulin. ...... specific switch in the B chain
@en
type
label
Chiral mutagenesis of insulin. ...... specific switch in the B chain
@ast
Chiral mutagenesis of insulin. ...... specific switch in the B chain
@en
prefLabel
Chiral mutagenesis of insulin. ...... specific switch in the B chain
@ast
Chiral mutagenesis of insulin. ...... specific switch in the B chain
@en
P2093
P2860
P356
P1433
P1476
Chiral mutagenesis of insulin. ...... specific switch in the B chain
@en
P2093
Michael A Weiss
Qing-xin Hua
Satoe H Nakagawa
Shi-Quan Hu
Wenhua Jia
Zhu-li Wan
P2860
P304
P356
10.1021/BI048025O
P407
P577
2005-04-01T00:00:00Z