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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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Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction

Nature chemical biology, 2011-02, Vol.7 (2), p.113

2011

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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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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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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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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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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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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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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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Rational modification of protein stability by targeting surface sites leads to complicated results

Proceedings of the National Academy of Sciences - PNAS, 2013-07, Vol.110 (28), p.11337-11342

2013

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Efficient Microwave-Assisted Synthesis of Human Islet Amyloid Polypeptide Designed to Facilitate the Specific Incorporation of Labeled Amino Acids

Organic letters, 2010-11, Vol.12 (21), p.4848-4851

2010

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Mutational Analysis of Preamyloid Intermediates: The Role of His-Tyr Interactions in Islet Amyloid Formation

Biophysical journal, 2014-04, Vol.106 (7), p.1520-1527

2014

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Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics

Angewandte Chemie (International ed.), 2010-10, Vol.49 (41), p.7473-7475

2010

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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

Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction

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

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

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

Islet amyloid polypeptide toxicity and membrane interactions

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

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

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

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

Rational modification of protein stability by targeting surface sites leads to complicated results

Efficient Microwave-Assisted Synthesis of Human Islet Amyloid Polypeptide Designed to Facilitate the Specific Incorporation of Labeled Amino Acids

Mutational Analysis of Preamyloid Intermediates: The Role of His-Tyr Interactions in Islet Amyloid Formation

Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics

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