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General amyloid inhibitors? A critical examination of the inhibition of IAPP amyloid formation by inositol stereoisomers

PloS one, 2014-09, Vol.9 (9), p.e104023

2014

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Analysis of the Inhibition and Remodeling of Islet Amyloid Polypeptide Amyloid Fibers by Flavanols

Biochemistry (Easton), 2012-04, Vol.51 (13), p.2670-2683

2012

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Linking Gas-Phase and Solution-Phase Protein Unfolding via Mobile Proton Simulations

Analytical chemistry (Washington), 2022-11, Vol.94 (46), p.16113-16121

2022

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On the plasticity of amyloid formation: The impact of destabilizing small to large substitutions on islet amyloid polypeptide amyloid formation

Protein science, 2023-02, Vol.32 (2), p.e4539-n/a

2023

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Ion Mobility Spectrometry–Mass Spectrometry Defines the Oligomeric Intermediates in Amylin Amyloid Formation and the Mode of Action of Inhibitors

Journal of the American Chemical Society, 2014-01, Vol.136 (2), p.660-670

2014

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Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology

Current opinion in structural biology, 2013-02, Vol.23 (1), p.82-89

2013

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Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry

Nature chemistry, 2015-01, Vol.7 (1), p.73

2015

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Islet amyloid polypeptide toxicity and membrane interactions

Proceedings of the National Academy of Sciences - PNAS, 2013-11, Vol.110 (48), p.19279-19284

2013

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The Flavanol (−)-Epigallocatechin 3-Gallate Inhibits Amyloid Formation by Islet Amyloid Polypeptide, Disaggregates Amyloid Fibrils, and Protects Cultured Cells against IAPP-Induced Toxicity

Biochemistry (Easton), 2010-09, Vol.49 (37), p.8127-8133

2010

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Ionic Strength Effects on Amyloid Formation by Amylin Are a Complicated Interplay among Debye Screening, Ion Selectivity, and Hofmeister Effects

Biochemistry (Easton), 2012-10, Vol.51 (43), p.8478-8490

2012

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A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP

Journal of the American Chemical Society, 2017-11, Vol.139 (46), p.16748-16758

2017

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Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet

Proceedings of the National Academy of Sciences - PNAS, 2013-11, Vol.110 (48), p.19285-19290

2013

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Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity

FEBS letters, 2013-04, Vol.587 (8), p.1106-1118

2013

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A role for helical intermediates in amyloid formation by natively unfolded polypeptides?

Physical biology, 2009-02, Vol.6 (1), p.015005-015005 (6)

2009

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Two-Dimensional IR Spectroscopy and Isotope Labeling Defines the Pathway of Amyloid Formation with Residue-Specific Resolution

Proceedings of the National Academy of Sciences - PNAS, 2009-04, Vol.106 (16), p.6614-6619

2009

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Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology

Journal of Diabetes Research, 2016-01, Vol.2016, p.2798269-18

2016

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Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure

Proceedings of the National Academy of Sciences - PNAS, 2013-02, Vol.110 (6), p.2123-2128

2013

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Defining the Molecular Basis of Amyloid Inhibitors: Human Islet Amyloid Polypeptide–Insulin Interactions

Journal of the American Chemical Society, 2014-09, Vol.136 (37), p.12912-12919

2014

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The Role of His-18 in Amyloid Formation by Human Islet Amyloid Polypeptide

Biochemistry (Easton), 2005-12, Vol.44 (49), p.16284-16291

2005

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Energetically significant networks of coupled interactions within an unfolded protein

Proceedings of the National Academy of Sciences - PNAS, 2014-08, Vol.111 (33), p.12079-12084

2014

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The triphenylmethane dye brilliant blue G is only moderately effective at inhibiting amyloid formation by human amylin or at disaggregating amylin amyloid fibrils, but interferes with amyloid assays; Implications for inhibitor design

PloS one, 2019-08, Vol.14 (8), p.e0219130-e0219130

2019

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Rational design of potent domain antibody inhibitors of amyloid fibril assembly

Proceedings of the National Academy of Sciences - PNAS, 2012-12, Vol.109 (49), p.19965-19970

2012

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Deamidation Accelerates Amyloid Formation and Alters Amylin Fiber Structure

Journal of the American Chemical Society, 2012-08, Vol.134 (30), p.12658-12667

2012

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Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers

Chemical science (Cambridge), 2017-07, Vol.8 (7), p.5030-5040

2017

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General amyloid inhibitors? A critical examination of the inhibition of IAPP amyloid formation by inositol stereoisomers

Analysis of the Inhibition and Remodeling of Islet Amyloid Polypeptide Amyloid Fibers by Flavanols

Linking Gas-Phase and Solution-Phase Protein Unfolding via Mobile Proton Simulations

On the plasticity of amyloid formation: The impact of destabilizing small to large substitutions on islet amyloid polypeptide amyloid formation

Ion Mobility Spectrometry–Mass Spectrometry Defines the Oligomeric Intermediates in Amylin Amyloid Formation and the Mode of Action of Inhibitors

Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology

Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry

Islet amyloid polypeptide toxicity and membrane interactions

The Flavanol (−)-Epigallocatechin 3-Gallate Inhibits Amyloid Formation by Islet Amyloid Polypeptide, Disaggregates Amyloid Fibrils, and Protects Cultured Cells against IAPP-Induced Toxicity

Ionic Strength Effects on Amyloid Formation by Amylin Are a Complicated Interplay among Debye Screening, Ion Selectivity, and Hofmeister Effects

A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP

Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet

Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity

A role for helical intermediates in amyloid formation by natively unfolded polypeptides?

Two-Dimensional IR Spectroscopy and Isotope Labeling Defines the Pathway of Amyloid Formation with Residue-Specific Resolution

Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics

Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology

Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure

Defining the Molecular Basis of Amyloid Inhibitors: Human Islet Amyloid Polypeptide–Insulin Interactions

The Role of His-18 in Amyloid Formation by Human Islet Amyloid Polypeptide

Energetically significant networks of coupled interactions within an unfolded protein

The triphenylmethane dye brilliant blue G is only moderately effective at inhibiting amyloid formation by human amylin or at disaggregating amylin amyloid fibrils, but interferes with amyloid assays; Implications for inhibitor design

Rational design of potent domain antibody inhibitors of amyloid fibril assembly

Deamidation Accelerates Amyloid Formation and Alters Amylin Fiber Structure

Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers

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