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Human and mouse single-nucleus transcriptomics reveal TREM2-dependent and TREM2-independent cellular responses in Alzheimer's disease

Nature medicine, 2020-01, Vol.26 (1), p.131-142

2020

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Inflammatory mechanisms in neurodegeneration

Journal of neurochemistry, 2019-06, Vol.149 (5), p.562-581

2019

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A new class of monoclonal Aβ antibodies selectively targets and triggers deposition of Aβ protofibrils

Journal of neurochemistry, 2023-06, Vol.165 (6), p.860-873

2023

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Amyloid-β42 protofibrils are internalized by microglia more extensively than monomers

Brain research, 2016-10, Vol.1648 (Pt A), p.485-495

2016

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Disentangling aggregation-prone proteins: a new method for isolating α-synuclein species: An Editorial Highlight for "A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of α-synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in α-synuclein research" on page 103

Journal of neurochemistry, 2020-04, Vol.153 (1), p.7-9

Nichols, Michael R

2020

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The intricate biophysical puzzle of caspase-1 activation

Archives of biochemistry and biophysics, 2021-03, Vol.699, p.108753-108753, Article 108753

2021

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Development of β-sheet structure in Aβ aggregation intermediates diminishes exposed hydrophobic surface area and enhances proinflammatory activity

Biochimica et biophysica acta. Proteins and proteomics, 2022-09, Vol.1870 (9), p.140817-140817, Article 140817

2022

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CD47 does not mediate amyloid-β(1-42) protofibril-stimulated microglial cytokine release

Biochemical and biophysical research communications, 2014-11, Vol.454 (1), p.239-244

2014

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The influence of gold surface texture on microglia morphology and activation

Biomaterials science, 2014-01, Vol.2 (1), p.110-120

2014

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Amyloid- beta 42 protofibrils are internalized by microglia more extensively than monomers

Brain research, 2016-10, Vol.1648, p.485-495

2016

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Nascent Aβ42 Fibrillization in Synaptic Endosomes Precedes Plaque Formation in a Mouse Model of Alzheimer's-like β-Amyloidosis

The Journal of neuroscience, 2023-12, Vol.43 (50), p.8812-8824

2023

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McDonald's Blood Flow in Arteries: Theoretical, Experimental and Clinical Principles

Seventh edition, 2022

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APP Regulates Microglial Phenotype in a Mouse Model of Alzheimer's Disease

The Journal of neuroscience, 2016-08, Vol.36 (32), p.8471-8486

2016

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Toll-like receptors 2 and 4 mediate Aβ(1-42) activation of the innate immune response in a human monocytic cell line

Journal of neurochemistry, 2008, Vol.104 (2), p.524-533

2008

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Biophysical Comparison of Soluble Amyloid-β(1–42) Protofibrils, Oligomers, and Protofilaments

Biochemistry (Easton), 2015-04, Vol.54 (13), p.2193-2204

2015

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Aβ40 has a subtle effect on Aβ42 protofibril formation, but to a lesser degree than Aβ42 concentration, in Aβ42/Aβ40 mixtures

Archives of biochemistry and biophysics, 2016-05, Vol.597, p.1-11

2016

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The conformational epitope for a new Aβ42 protofibril‐selective antibody partially overlaps with the peptide N‐terminal region

Journal of neurochemistry, 2017-12, Vol.143 (6), p.736-749

2017

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Development of a Simple and Effective Lipid‑A Antagonist Based on Computational Prediction

ACS infectious diseases, 2022-06, Vol.8 (6), p.1171-1178

2022

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Isolated Amyloid-β(1–42) Protofibrils, But Not Isolated Fibrils, Are Robust Stimulators of Microglia

ACS chemical neuroscience, 2012-04, Vol.3 (4), p.302-311

2012

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Stability of early-stage amyloid-β(1–42) aggregation species

Biochimica et biophysica acta, 2013-01, Vol.1834 (1), p.65-70

2013

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Disentangling aggregation‐prone proteins: a new method for isolating α‐synuclein species

Journal of neurochemistry, 2020-04, Vol.153 (1), p.7-9

Nichols, Michael R.

2020

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Substituted tryptophans at amyloid-β(1–40) residues 19 and 20 experience different environments after fibril formation

Archives of biochemistry and biophysics, 2011-10, Vol.514 (1), p.27-32

2011

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Amyloid-β Protofibrils Differ from Amyloid-β Aggregates Induced in Dilute Hexafluoroisopropanol in Stability and Morphology

The Journal of biological chemistry, 2005-01, Vol.280 (4), p.2471-2480

2005

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Growth of β-Amyloid(1−40) Protofibrils by Monomer Elongation and Lateral Association. Characterization of Distinct Products by Light Scattering and Atomic Force Microscopy

Biochemistry (Easton), 2002-05, Vol.41 (19), p.6115-6127

2002

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Human and mouse single-nucleus transcriptomics reveal TREM2-dependent and TREM2-independent cellular responses in Alzheimer's disease

Inflammatory mechanisms in neurodegeneration

A new class of monoclonal Aβ antibodies selectively targets and triggers deposition of Aβ protofibrils

Amyloid-β42 protofibrils are internalized by microglia more extensively than monomers

The intricate biophysical puzzle of caspase-1 activation

Development of β-sheet structure in Aβ aggregation intermediates diminishes exposed hydrophobic surface area and enhances proinflammatory activity

CD47 does not mediate amyloid-β(1-42) protofibril-stimulated microglial cytokine release

The influence of gold surface texture on microglia morphology and activation

Amyloid- beta 42 protofibrils are internalized by microglia more extensively than monomers

Nascent Aβ42 Fibrillization in Synaptic Endosomes Precedes Plaque Formation in a Mouse Model of Alzheimer's-like β-Amyloidosis

McDonald's Blood Flow in Arteries: Theoretical, Experimental and Clinical Principles

APP Regulates Microglial Phenotype in a Mouse Model of Alzheimer's Disease

Toll-like receptors 2 and 4 mediate Aβ(1-42) activation of the innate immune response in a human monocytic cell line

Biophysical Comparison of Soluble Amyloid-β(1–42) Protofibrils, Oligomers, and Protofilaments

Aβ40 has a subtle effect on Aβ42 protofibril formation, but to a lesser degree than Aβ42 concentration, in Aβ42/Aβ40 mixtures

The conformational epitope for a new Aβ42 protofibril‐selective antibody partially overlaps with the peptide N‐terminal region

Development of a Simple and Effective Lipid‑A Antagonist Based on Computational Prediction

Author Correction: Human and mouse single-nucleus transcriptomics reveal TREM2-dependent and TREM2-independent cellular responses in Alzheimer's disease

Isolated Amyloid-β(1–42) Protofibrils, But Not Isolated Fibrils, Are Robust Stimulators of Microglia

Stability of early-stage amyloid-β(1–42) aggregation species

Disentangling aggregation‐prone proteins: a new method for isolating α‐synuclein species

Substituted tryptophans at amyloid-β(1–40) residues 19 and 20 experience different environments after fibril formation

Amyloid-β Protofibrils Differ from Amyloid-β Aggregates Induced in Dilute Hexafluoroisopropanol in Stability and Morphology

Growth of β-Amyloid(1−40) Protofibrils by Monomer Elongation and Lateral Association. Characterization of Distinct Products by Light Scattering and Atomic Force Microscopy

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