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Antimicrobial Properties of Amyloid Peptides

Molecular pharmaceutics, 2012-04, Vol.9 (4), p.708-717

2012

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Truncated β-amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndrome

Proceedings of the National Academy of Sciences - PNAS, 2010-04, Vol.107 (14), p.6538-6543

2010

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Ion Channel Formation by Tau Protein: Implications for Alzheimer’s Disease and Tauopathies

Biochemistry (Easton), 2015-12, Vol.54 (50), p.7320-7325

2015

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Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs

Chemical Society reviews, 2014-10, Vol.43 (19), p.675-6764

2014

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Mechanisms for the Insertion of Toxic, Fibril-like β‑Amyloid Oligomers into the Membrane

Journal of chemical theory and computation, 2013-01, Vol.9 (1), p.822-833

2013

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Bipolar spectrum disorder masquerading as treatment resistant unipolar depression

CNS spectrums, 2022-02, Vol.27 (1), p.4-6

2022

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Antimicrobial Amyloids?

Biophysical journal, 2011-04, Vol.100 (7), p.1597-1598

Kagan, Bruce L.

2011

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Membrane Pores in the Pathogenesis of Neurodegenerative Disease

Molecular Biology of Neurodegenerative Diseases, 2012, Vol.107, p.295-325

Kagan, Bruce L.

2012

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Amyloid Ion Channels: A Common Structural Link for Protein-Misfolding Disease

Proceedings of the National Academy of Sciences - PNAS, 2005-07, Vol.102 (30), p.10427-10432

2005

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Atomic Force Microscopy and MD Simulations Reveal Pore-Like Structures of All-d-Enantiomer of Alzheimer’s β-Amyloid Peptide: Relevance to the Ion Channel Mechanism of AD Pathology

The journal of physical chemistry. B, 2012-02, Vol.116 (5), p.1728-1735

2012

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Ion channel formation by N-terminally truncated Aβ (4–42): relevance for the pathogenesis of Alzheimer's disease

Nanomedicine, 2020-10, Vol.29, p.102235-102235, Article 102235

2020

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Alzheimer's disease: which type of amyloid-preventing drug agents to employ?

Physical chemistry chemical physics : PCCP, 2013-06, Vol.15 (23), p.8868-8877

2013

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Amyloid β Ion Channels in a Membrane Comprising Brain Total Lipid Extracts

ACS chemical neuroscience, 2017-06, Vol.8 (6), p.1348-1357

2017

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Probing Structural Features of Alzheimer’s Amyloid-β Pores in Bilayers Using Site-Specific Amino Acid Substitutions

Biochemistry (Easton), 2012-01, Vol.51 (3), p.776-785

2012

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Activity and Architecture of Pyroglutamate-Modified Amyloid‑β (AβpE3‑42) Pores

The journal of physical chemistry. B, 2014-07, Vol.118 (26), p.7335-7344

2014

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Role of the Fast Kinetics of Pyroglutamate-Modified Amyloid‑β Oligomers in Membrane Binding and Membrane Permeability

Biochemistry (Easton), 2014-07, Vol.53 (28), p.4704-4714

2014

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Effects of Point Substitutions on the Structure of Toxic Alzheimer’s β-Amyloid Channels: Atomic Force Microscopy and Molecular Dynamics Simulations

Biochemistry (Easton), 2012-04, Vol.51 (14), p.3031-3038

2012

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Familial Alzheimer’s Disease Osaka Mutant (ΔE22) β‑Barrels Suggest an Explanation for the Different Aβ1–40/42 Preferred Conformational States Observed by Experiment

The journal of physical chemistry. B, 2013-10, Vol.117 (39), p.11518-11529

2013

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The channel hypothesis of Alzheimer’s disease: current status

Peptides (New York, N.Y. : 1980), 2002-07, Vol.23 (7), p.1311-1315

2002

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Computational Methods for Structural and Functional Studies of Alzheimer's Amyloid Ion Channels

Methods in molecular biology (Clifton, N.J.), 2016, Vol.1345, p.251

2016

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Amyloid peptide pores and the beta sheet conformation

Advances in experimental medicine and biology, 2010, Vol.677, p.150

2010

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All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers

Journal of chemical theory and computation, 2012-03, Vol.8 (3), p.1143-1152

2012

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Amyloidosis and Protein Folding

Science (American Association for the Advancement of Science), 2005-01, Vol.307 (5706), p.42-43

2005

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Electrophysiologic properties of channels induced by Aβ25–35 in planar lipid bilayers

Peptides (New York, N.Y. : 1980), 2002-07, Vol.23 (7), p.1215-1228

2002

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Channel formation by serum amyloid A: a potential mechanism for amyloid pathogenesis and host defense

Amyloid, 2002, Vol.9 (1), p.13-23

2002

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Antimicrobial Properties of Amyloid Peptides

Truncated β-amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndrome

Ion Channel Formation by Tau Protein: Implications for Alzheimer’s Disease and Tauopathies

Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs

Mechanisms for the Insertion of Toxic, Fibril-like β‑Amyloid Oligomers into the Membrane

Bipolar spectrum disorder masquerading as treatment resistant unipolar depression

Antimicrobial Amyloids?

Membrane Pores in the Pathogenesis of Neurodegenerative Disease

Amyloid Ion Channels: A Common Structural Link for Protein-Misfolding Disease

Atomic Force Microscopy and MD Simulations Reveal Pore-Like Structures of All-d-Enantiomer of Alzheimer’s β-Amyloid Peptide: Relevance to the Ion Channel Mechanism of AD Pathology

Ion channel formation by N-terminally truncated Aβ (4–42): relevance for the pathogenesis of Alzheimer's disease

Alzheimer's disease: which type of amyloid-preventing drug agents to employ?

Amyloid β Ion Channels in a Membrane Comprising Brain Total Lipid Extracts

Probing Structural Features of Alzheimer’s Amyloid-β Pores in Bilayers Using Site-Specific Amino Acid Substitutions

Activity and Architecture of Pyroglutamate-Modified Amyloid‑β (AβpE3‑42) Pores

Role of the Fast Kinetics of Pyroglutamate-Modified Amyloid‑β Oligomers in Membrane Binding and Membrane Permeability

Effects of Point Substitutions on the Structure of Toxic Alzheimer’s β-Amyloid Channels: Atomic Force Microscopy and Molecular Dynamics Simulations

Familial Alzheimer’s Disease Osaka Mutant (ΔE22) β‑Barrels Suggest an Explanation for the Different Aβ1–40/42 Preferred Conformational States Observed by Experiment

The channel hypothesis of Alzheimer’s disease: current status

Computational Methods for Structural and Functional Studies of Alzheimer's Amyloid Ion Channels

Amyloid peptide pores and the beta sheet conformation

All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers

Amyloidosis and Protein Folding

Electrophysiologic properties of channels induced by Aβ25–35 in planar lipid bilayers

Channel formation by serum amyloid A: a potential mechanism for amyloid pathogenesis and host defense

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