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

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

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

http://www.wikidata.org/entity/Q27639526

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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 Fully Convergent Chemical Synthesis of Ester Insulin: Determination of the High Resolution X-ray Structure by Racemic Protein Crystallography Conformational dynamics of insulin.Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B chain Proinsulin is refractory to protein fibrillation: topological protection of a precursor protein from cross-beta assembly.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.Deciphering the hidden informational content of protein sequences: foldability of proinsulin hinges on a flexible arm that is dispensable in the mature hormone Proinsulin misfolding and diabetes: mutant INS gene-induced diabetes of youth.Proinsulin and the genetics of diabetes mellitus The structure and function of insulin: decoding the TR transition The structure of a mutant insulin uncouples receptor binding from protein allostery. An electrostatic block to the TR transition.Proinsulin disulfide maturation and misfolding in the endoplasmic reticulum Insulin: a model system for nanomedicine?Diabetes mellitus due to the toxic misfolding of proinsulin variants.Insulin: a small protein with a long journey.Nisin-inducible secretion of a biologically active single-chain insulin analog by Lactococcus lactis NZ9000.A conserved histidine in insulin is required for the foldability of human proinsulin: structure and function of an ALAB5 analog.Role of the connecting peptide in insulin biosynthesis.Design and folding of [GluA4(ObetaThrB30)]insulin ("ester insulin"): a minimal proinsulin surrogate that can be chemically converted into human insulin Biomimetic synthesis of lispro insulin via a chemically synthesized "mini-proinsulin" prepared by oxime-forming ligation.In vitro refolding of human proinsulin. Kinetic intermediates, putative disulfide-forming pathway folding initiation site, and potential role of C-peptide in folding process.Transdermal Protein Delivery Using Choline and Geranate (CAGE) Deep Eutectic Solvent.Insulin in motion: The A6-A11 disulfide bond allosterically modulates structural transitions required for insulin activity.Unfolding of human proinsulin. Intermediates and possible role of its C-peptide in folding/unfolding.

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

http://www.wikidata.org/entity/Q27639526

description

2002 nî lūn-bûn

@nan

2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

name

Mechanism of insulin chain com ...... a-helices in disulfide pairing

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Mechanism of insulin chain com ...... a-helices in disulfide pairing

@en

Mechanism of insulin chain com ...... a-helices in disulfide pairing

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type

label

Mechanism of insulin chain com ...... a-helices in disulfide pairing

@ast

Mechanism of insulin chain com ...... a-helices in disulfide pairing

@en

Mechanism of insulin chain com ...... a-helices in disulfide pairing

@nl

prefLabel

Mechanism of insulin chain com ...... a-helices in disulfide pairing

@ast

Mechanism of insulin chain com ...... a-helices in disulfide pairing

@en

Mechanism of insulin chain com ...... a-helices in disulfide pairing

@nl

P1433

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P1433

Journal of Biological Chemistry

P1476

Mechanism of insulin chain com ...... a-helices in disulfide pairing

@en

P2093

Michael A Weiss

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

Nelson F B Phillips

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

Panayotis G Katsoyannis

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

Qing-Xin Hua

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

Run-Ying Wang

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

Wenhua Jia

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

Ying-Chi Chu

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

P2860

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

Receptor binding redefined by a structural switch in a mutant human insulin

Structure of a protein in a kinetic trap

Solution structure of an engineered insulin monomer at neutral pH

Mapping the functional surface of insulin by design: structure and function of a novel A-chain analogue

The relationship between insulin bioactivity and structure in the NH2-terminal A-chain helix

Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin

The role of assembly in insulin's biosynthesis

Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain.

Protein structure and the spandrels of San Marco: insulin's receptor-binding surface is buttressed by an invariant leucine essential for its stability.

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43443-53

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scholarly article

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10.1074/JBC.M206107200

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45

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277

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2002-11-08T00:00:00Z

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12196530

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