A hIAPP-derived all-D-amino-acid inhibits hIAPP fibrillation efficiently at membrane surface by targeting α-helical oligomeric intermediates (Q24338147)

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English	A hIAPP-derived all-D-amino-acid inhibits hIAPP fibrillation efficiently at membrane surface by targeting α-helical oligomeric intermediates	scientific article

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scholarly article

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A hIAPP-derived all-D-amino-acid inhibits hIAPP fibrillation efficiently at membrane surface by targeting α-helical oligomeric intermediates (English)

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islet amyloid polypeptide

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GOA release 2020-03-11

identical protein binding

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GOA release 2020-03-11

author name string

Li Wang

1

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Liyan Lei

2

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Yang Li

3

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Liping Wang

4

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Fei Li

5

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language of work or name

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publication date

18 March 2014

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588

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884-91

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6

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Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Islet amyloid and type 2 diabetes mellitus

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Therapeutic approaches to protein-misfolding diseases

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

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Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Coffee components inhibit amyloid formation of human islet amyloid polypeptide in vitro: possible link between coffee consumption and diabetes mellitus

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Small-molecule inhibitors of islet amyloid polypeptide fibril formation

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Suppression of IAPP fibrillation at anionic lipid membranes via IAPP-derived amyloid inhibitors and insulin

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

The polyphenol EGCG inhibits amyloid formation less efficiently at phospholipid interfaces than in bulk solution.

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Lipid membranes modulate the structure of islet amyloid polypeptide.

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Islet amyloid polypeptide forms rigid lipid-protein amyloid fibrils on supported phospholipid bilayers

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Phospholipid catalysis of diabetic amyloid assembly

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Mechanistic studies of peptide self-assembly: transient α-helices to stable β-sheets

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Helix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptide

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assemblies

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Design of peptide-based inhibitors of human islet amyloid polypeptide fibrillogenesis

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid peptide abeta1-42 by mirror image phage display

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Reduction of Alzheimer's disease amyloid plaque load in transgenic mice by D3, A D-enantiomeric peptide identified by mirror image phage display

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Oral treatment with the d-enantiomeric peptide D3 improves the pathology and behavior of Alzheimer's Disease transgenic mice

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Stereoselective interactions of peptide inhibitors with the beta-amyloid peptide

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Controlling amyloid beta-peptide fibril formation with protease-stable ligands

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins.

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

21 January 2018

A comparison of the immunogenicity of a pair of enantiomeric proteins

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

7 January 2021

based on heuristic

inferred from DOI database lookup

Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

7 January 2021

based on heuristic

inferred from DOI database lookup

Inhibition of hIAPP amyloid-fibril formation and apoptotic cell death by a designed hIAPP amyloid- core-containing hexapeptide

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

7 January 2021

based on heuristic

inferred from DOI database lookup

Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

7 January 2021

based on heuristic

inferred from DOI database lookup

The Human Islet Amyloid Polypeptide Forms Transient Membrane-Active Prefibrillar Assemblies†

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

7 January 2021

based on heuristic

inferred from DOI database lookup

Pore formation by the cytotoxic islet amyloid peptide amylin

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2014.02.020

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/J.FEBSLET.2014.02.020

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