Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B chain - Wikidata - awgldk - TriplyDB

Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B chain

Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B chain

http://www.wikidata.org/entity/Q31156781

about

Landmarks in insulin research Design of an Active Ultrastable Single-chain Insulin Analog: SYNTHESIS, STRUCTURE, AND THERAPEUTIC IMPLICATIONS Enhancing the Activity of a Protein by Stereospecific Unfolding: CONFORMATIONAL LIFE CYCLE OF INSULIN AND ITS EVOLUTIONARY ORIGINS Crystal Structure of a"Nonfoldable"Insulin: IMPAIRED FOLDING EFFICIENCY DESPITE NATIVE ACTIVITY Insulin analog with additional disulfide bond has increased stability and preserved activity Insight into the Structural and Biological Relevance of the T/R Transition of the N-Terminus of the B-Chain in Human Insulin Conformational 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 derivative Deciphering 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 hormone The 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 mellitus Additional disulfide bonds in insulin: Prediction, recombinant expression, receptor binding affinity, and stability.The structure and function of insulin: decoding the TR transition Insulin 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.

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Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B chain

http://www.wikidata.org/entity/Q31156781

description

2005 nî lūn-bûn

@nan

2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2005年の論文

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2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

name

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

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Chiral mutagenesis of insulin. ...... specific switch in the B chain

@en

P2093

Michael A Weiss

http://www.w3.org/2001/XMLSchema#string

Ming Zhao

http://www.w3.org/2001/XMLSchema#string

Qing-xin Hua

http://www.w3.org/2001/XMLSchema#string

Satoe H Nakagawa

http://www.w3.org/2001/XMLSchema#string

Shi-Quan Hu

http://www.w3.org/2001/XMLSchema#string

Wenhua Jia

http://www.w3.org/2001/XMLSchema#string

Zhu-li Wan

http://www.w3.org/2001/XMLSchema#string

P2860

Structural consequences of the B5 histidine --> tyrosine mutation in human insulin characterized by X-ray crystallography and conformational analysis

R6 hexameric insulin complexed with m-cresol or resorcinol

Crystal structure of human insulin-like growth factor-1: detergent binding inhibits binding protein interactions

A cavity-forming mutation in insulin induces segmental unfolding of a surrounding α-helix

Non-standard insulin design: structure-activity relationships at the periphery of the insulin receptor

Chiral mutagenesis of insulin's hidden receptor-binding surface: structure of an allo-isoleucine(A2) analogue

Mechanism of insulin chain combination. Asymmetric roles of A-chain alpha-helices in disulfide pairing

Structure of insulin in 4-zinc insulin

Crystal structure of allo-Ile(A2)-insulin, an inactive chiral analogue: implications for the mechanism of receptor binding

X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue.

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4984-4999

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scholarly article

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10.1021/BI048025O

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13

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44

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2005-04-01T00:00:00Z

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15794637

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3845378

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