Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide (Q57209091)

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object named as

Ayyalusamy Ramamoorthy

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Jeffrey Brender

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object named as

Jeffrey R. Brender

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author name string

Janarthanan Krishnamoorthy

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Grazia M. L. Messina

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Aniruddha Deb

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Subramanian Vivekanandan

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Carmelo La Rosa

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James E. Penner-Hahn

Islet amyloid polypeptide, islet amyloid, and diabetes mellitus

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language of work or name

English

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publication date

2013

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published in

Chemical Communications

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volume

49

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issue

32

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page(s)

3339

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cites work

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

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Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets.

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The mechanism of insulin action on islet amyloid polypeptide fiber formation

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Elemental composition of secretory granules in pancreatic islets of Langerhans

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

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Copper(II) inhibits the formation of amylin amyloid in vitro

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Human pro-islet amyloid polypeptide (ProIAPP(1-48)) forms amyloid fibrils and amyloid spherulites in vitro.

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Role of zinc in human islet amyloid polypeptide aggregation.

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

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Association of highly compact type II diabetes related islet amyloid polypeptide intermediate species at physiological temperature revealed by diffusion NMR spectroscopy

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

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Interaction of Cd and Zn with biologically important ligands characterized using solid-state NMR and ab initio calculations

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Investigating metal-binding in proteins by nuclear magnetic resonance.

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

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High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide.

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A two-site mechanism for the inhibition of IAPP amyloidogenesis by zinc

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

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Conserved and Cooperative Assembly of Membrane-Bound α-Helical States of Islet Amyloid Polypeptide†

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The molecular basis of distinct aggregation pathways of islet amyloid polypeptide

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Amyloid peptide channels: blockade by zinc and inhibition by Congo red (amyloid channel block).

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Structure and Thermodynamics of Amylin Dimer Studied by Hamiltonian-Temperature Replica Exchange Molecular Dynamics Simulations

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Copper-mediated formation of hydrogen peroxide from the amylin peptide: A novel mechanism for degeneration of islet cells in type-2 diabetes mellitus?

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