Solution state structures of human pancreatic amylin and pramlintide. - Wikidata - awgldk - TriplyDB

Solution state structures of human pancreatic amylin and pramlintide.

Solution state structures of human pancreatic amylin and pramlintide.

http://www.wikidata.org/entity/Q33481542

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NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP 248−286 Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment Structure of micelle-bound adrenomedullin: a first step toward the analysis of its interactions with receptors and small molecules Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.Stable and metastable states of human amylin in solution.Macromolecular crowding as a suppressor of human IAPP fibril formation and cytotoxicity.Structural similarities and differences between amyloidogenic and non-amyloidogenic islet amyloid polypeptide (IAPP) sequences and implications for the dual physiological and pathological activities of these peptides.A multi-pronged search for a common structural motif in the secretion signal of Salmonella enterica serovar Typhimurium type III effector proteins.α-helix to β-hairpin transition of human amylin monomer.Effect of Pramlintide on Postprandial Glucose Fluxes in Type 1 Diabetes.Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization.Effect of proline mutations on the monomer conformations of amylin.Effect of Post-Translational Amidation on Islet Amyloid Polypeptide Conformational Ensemble: Implications for Its Aggregation Early Steps.Designed hairpin peptides interfere with amyloidogenesis pathways: fibril formation and cytotoxicity inhibition, interception of the preamyloid state 2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.Probing the binding affinity of amyloids to reduce toxicity of oligomers in diabetes.Peptide Inhibitors of the amyloidogenesis of IAPP: verification of the hairpin-binding geometry hypothesis.A two-site mechanism for the inhibition of IAPP amyloidogenesis by zinc.Effects of forcefield and sampling method in all-atom simulations of inherently disordered proteins: Application to conformational preferences of human amylin.Role of zinc in human islet amyloid polypeptide aggregation.Click Peptide concept: o-acyl isopeptide of islet amyloid polypeptide as a nonaggregative precursor molecule.Dynamics of the conformational transitions during the dimerization of an intrinsically disordered peptide: a case study on the human islet amyloid polypeptide fragment.

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P2860

Solution state structures of human pancreatic amylin and pramlintide.

http://www.wikidata.org/entity/Q33481542

description

2009 nî lūn-bûn

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2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հուլիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Solution state structures of human pancreatic amylin and pramlintide.

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Solution state structures of human pancreatic amylin and pramlintide.

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type

label

Solution state structures of human pancreatic amylin and pramlintide.

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Solution state structures of human pancreatic amylin and pramlintide.

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prefLabel

Solution state structures of human pancreatic amylin and pramlintide.

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Solution state structures of human pancreatic amylin and pramlintide.

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Protein Engineering Design and Selection

P1476

Solution state structures of human pancreatic amylin and pramlintide.

@en

P2093

Gregory M Lee

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John R Cort

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K N L Huggins

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Kathryn Prickett

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Niels H Andersen

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Susan Janes

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

Zhihong Liu

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

P2860

Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin

Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells

Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients

Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy

A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity

Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis

Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states

Conformational preferences of the amylin nucleation site in SDS micelles: an NMR study

Conformational isomerism of endothelin in acidic aqueous media: a quantitative NOESY analysis

Dynamic -Helix Structure of Micelle-bound Human Amylin

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497-513

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scholarly article

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10.1093/PROTEIN/GZP029

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8

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22

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2009-07-12T00:00:00Z

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19596697

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2719500

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