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A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers

Nature structural & molecular biology, 2015-03, Vol.22 (3), p.207

2015

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Functionalization of amyloid fibrils via the Bri2 BRICHOS domain

Scientific reports, 2020-12, Vol.10 (1), p.21765-21765, Article 21765

2020

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Food protein-derived amyloids do not accelerate amyloid β aggregation

Scientific reports, 2023, Vol.13 (1), p.985-985, Article 985

2023

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Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity

Biochimie, 2017-09, Vol.140, p.176-192

2017

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Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain

Nature communications, 2024-02, Vol.15 (1), p.965-965, Article 965

2024

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High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

Scientific reports, 2020-01, Vol.10 (1), p.235-235, Article 235

2020

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Identification of cytoskeletal proteins as binding partners of Bri2 BRICHOS domain

Molecular and cellular neuroscience, 2023-06, Vol.125, p.103843-103843, Article 103843

2023

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Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering

Proceedings of the National Academy of Sciences - PNAS, 2010-08, Vol.107 (35), p.15595-15600

2010

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Amyloid-β-induced action potential desynchronization and degradation of hippocampal gamma oscillations is prevented by interference with peptide conformation change and aggregation

The Journal of neuroscience, 2014-08, Vol.34 (34), p.11416-11425

2014

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BRICHOS Domains Efficiently Delay Fibrillation of Amyloid β-Peptide

The Journal of biological chemistry, 2012-09, Vol.287 (37), p.31608-31617

2012

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Molecular Structure of Cu(II)-Bound Amyloid‑β Monomer Implicated in Inhibition of Peptide Self-Assembly in Alzheimer’s Disease

JACS Au, 2022-11, Vol.2 (11), p.2571-2584

2022

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Blood–brain and blood–cerebrospinal fluid passage of BRICHOS domains from two molecular chaperones in mice

The Journal of biological chemistry, 2019-02, Vol.294 (8), p.2606-5220

2019

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Dementia-related Bri2 BRICHOS is a versatile molecular chaperone that efficiently inhibits Aβ42 toxicity in Drosophila

Biochemical journal, 2016-10, Vol.473 (20), p.3683-3704

2016

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Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation

Chemical science (Cambridge), 2022-01, Vol.13 (2), p.536-553

2022

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Specific inhibition of α‐synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS

Protein science, 2024-08, Vol.33 (8), p.e5091-n/a

2024

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Amyloid Fibril Formation of Arctic Amyloid‑β 1–42 Peptide is Efficiently Inhibited by the BRICHOS Domain

ACS chemical biology, 2022-08, Vol.17 (8), p.2201-2211

2022

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Pro-resolving lipid mediator reduces amyloid-β42– induced gene expression in human monocyte-derived microglia

Neural regeneration research, 2025-03, Vol.20 (3), p.873-886

2025

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Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro

Communications biology, 2020-01, Vol.3 (1), p.32, Article 32

2020

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High intracellular stability of the spidroin N‐terminal domain in spite of abundant amyloidogenic segments revealed by in‐cell hydrogen/deuterium exchange mass spectrometry

The FEBS journal, 2020-07, Vol.287 (13), p.2823-2833

2020

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Amyloid‑β Peptide Targeting Peptidomimetics for Prevention of Neurotoxicity

ACS chemical neuroscience, 2019-03, Vol.10 (3), p.1462-1477

2019

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Dissociation of a BRICHOS trimer into monomers leads to increased inhibitory effect on Aβ42 fibril formation

Biochimica et biophysica acta, 2015-08, Vol.1854 (8), p.835-843

2015

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Molecular Chaperone BRICHOS Inhibits CADASIL-Mutated NOTCH3 Aggregation In Vitro

Frontiers in molecular biosciences, 2022-02, Vol.9, p.812808-812808

2022

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Improved method for cannula fixation for long-term intracerebral brain infusion

Journal of neuroscience methods, 2017-10, Vol.290, p.145-150

2017

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Expression of endogenous mouse APP modulates β-amyloid deposition in hAPP-transgenic mice

Acta neuropathologica communications, 2017-06, Vol.5 (1), p.49-49, Article 49

2017

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Abilities of the BRICHOS domain to prevent neurotoxicity and fibril formation are dependent on a highly conserved Asp residue

RSC chemical biology, 2022-11, Vol.3 (11), p.1342-1358

2022

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A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers

Functionalization of amyloid fibrils via the Bri2 BRICHOS domain

Food protein-derived amyloids do not accelerate amyloid β aggregation

Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity

Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain

High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

Identification of cytoskeletal proteins as binding partners of Bri2 BRICHOS domain

Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering

Amyloid-β-induced action potential desynchronization and degradation of hippocampal gamma oscillations is prevented by interference with peptide conformation change and aggregation

BRICHOS Domains Efficiently Delay Fibrillation of Amyloid β-Peptide

Molecular Structure of Cu(II)-Bound Amyloid‑β Monomer Implicated in Inhibition of Peptide Self-Assembly in Alzheimer’s Disease

Blood–brain and blood–cerebrospinal fluid passage of BRICHOS domains from two molecular chaperones in mice

Dementia-related Bri2 BRICHOS is a versatile molecular chaperone that efficiently inhibits Aβ42 toxicity in Drosophila

Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation

Specific inhibition of α‐synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS

Amyloid Fibril Formation of Arctic Amyloid‑β 1–42 Peptide is Efficiently Inhibited by the BRICHOS Domain

Pro-resolving lipid mediator reduces amyloid-β42– induced gene expression in human monocyte-derived microglia

Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro

High intracellular stability of the spidroin N‐terminal domain in spite of abundant amyloidogenic segments revealed by in‐cell hydrogen/deuterium exchange mass spectrometry

Amyloid‑β Peptide Targeting Peptidomimetics for Prevention of Neurotoxicity

Dissociation of a BRICHOS trimer into monomers leads to increased inhibitory effect on Aβ42 fibril formation

Molecular Chaperone BRICHOS Inhibits CADASIL-Mutated NOTCH3 Aggregation In Vitro

Improved method for cannula fixation for long-term intracerebral brain infusion

Expression of endogenous mouse APP modulates β-amyloid deposition in hAPP-transgenic mice

Abilities of the BRICHOS domain to prevent neurotoxicity and fibril formation are dependent on a highly conserved Asp residue

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