Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide - Wikidata - awgldk - TriplyDB

Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

http://www.wikidata.org/entity/Q57209091

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Recent advances in the molecular genetics of type 2 diabetes mellitus On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.Effects of several quinones on insulin aggregation.Amyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.Structure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Facet-Dependent Interactions of Islet Amyloid Polypeptide with Gold Nanoparticles: Implications for Fibril Formation and Peptide-Induced Lipid Membrane Disruption.Regulation of the aggregation behavior of human islet amyloid polypeptide fragment by titanocene complexes.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Structural studies and cytotoxicity assays of "aggregation-prone" IAPP(8-16) and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin.Inhibition of Insulin Amyloid Fibrillation by a Novel Amphipathic Heptapeptide: MECHANISTIC DETAILS STUDIED BY SPECTROSCOPY IN COMBINATION WITH MICROSCOPY From Peptide Fragments to Whole Protein: Copper(II) Load and Coordination Features of IAPP.New Insight in Copper-Ion Binding to Human Islet Amyloid: The Contribution of Metal-Complex Speciation To Reveal the Polypeptide Toxicity.Membrane-mediated amyloid deposition of human islet amyloid polypeptide.The effect of aluminum ion on the aggregation of human islet amyloid polypeptide (11-28).Effect of Zn(2+) ions on the assembly of amylin oligomers: insight into the molecular mechanisms.Zinc-coordination and C-peptide complexation: a potential mechanism for the endogenous inhibition of IAPP aggregation.Coordination of Zn(2+) and Cu(2+) to the membrane disrupting fragment of amylin.

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Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

http://www.wikidata.org/entity/Q57209091

description

im Januar 2013 veröffentlichter wissenschaftlicher Artikel

@de

wetenschappelijk artikel

@nl

наукова стаття, опублікована у 2013

@uk

name

Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

@en

Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

@nl

type

label

Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

@en

Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

@nl

prefLabel

Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

@en

Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

@nl

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Chemical Communications

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Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

@en

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Aniruddha Deb

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

Ayyalusamy Ramamoorthy

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

Carmelo La Rosa

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

Grazia M. L. Messina

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

James E. Penner-Hahn

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

Janarthanan Krishnamoorthy

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

Jeffrey R. Brender

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

Subramanian Vivekanandan

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P2860

Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy

A genome-wide association study identifies novel risk loci for type 2 diabetes

Elemental composition of secretory granules in pancreatic islets of Langerhans.

The molecular basis of distinct aggregation pathways of islet amyloid polypeptide.

Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide.

Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective

Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers

Investigating metal-binding in proteins by nuclear magnetic resonance.

Islet amyloid polypeptide, islet amyloid, and diabetes mellitus.

Effect of zinc binding on β-amyloid structure and dynamics: implications for Aβ aggregation.

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3339

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scholarly article

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10.1039/C3CC40383A

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32

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49

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2013-01-01T00:00:00Z

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23505632

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