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Metal Binding of Alzheimer’s Amyloid‑β and Its Effect on Peptide Self-Assembly

Accounts of chemical research, 2023-10, Vol.56 (19), p.2653-2663

Abelein, Axel

2023

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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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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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Increased CSF-decorin predicts brain pathological changes driven by Alzheimer’s Aβ amyloidosis

Acta neuropathologica communications, 2022, Vol.10 (1), p.1-96, Article 96

2022

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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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Amyloid inhibition by molecular chaperones in vitro can be translated to Alzheimer's pathology in vivo

RSC medicinal chemistry, 2023-05, Vol.14 (5), p.848-857

2023

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Ionic Strength Modulation of the Free Energy Landscape of Aβ40 Peptide Fibril Formation

Journal of the American Chemical Society, 2016-06, Vol.138 (21), p.6893-6902

2016

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A new kid in the folding funnel: Molecular chaperone activities of the BRICHOS domain

Protein science, 2023-06, Vol.32 (6), p.e4645-n/a

2023

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Metal ion coordination delays amyloid-β peptide self-assembly by forming an aggregation–inert complex

The Journal of biological chemistry, 2020-05, Vol.295 (21), p.7224-7234

2020

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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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Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state

Nature communications, 2017-12, Vol.8 (1), p.2081-14, Article 2081

2017

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Intravenous treatment with a molecular chaperone designed against β-amyloid toxicity improves Alzheimer’s disease pathology in mouse models

Molecular therapy, 2023-02, Vol.31 (2), p.487-502

2023

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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 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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Smallest Secondary Nucleation Competent Aβ Aggregates Probed by an ATP-Independent Molecular Chaperone Domain

Biochemistry (Easton), 2021-03, Vol.60 (9), p.678-688

2021

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Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform

Nature communications, 2022-08, Vol.13 (1), p.4695-4695, Article 4695

2022

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Isotope‐labeled amyloid‐β does not transmit to the brain in a prion‐like manner after peripheral administration

EMBO reports, 2022-07, Vol.23 (7), p.e54405-n/a

2022

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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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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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Exploring the potential of the Bri2 BRICHOS domain as a drug-carrier for lysosomal storage disorders

EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2023, Vol.52 (SUPPL 1), p.S96

2023

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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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Autophagy Impairment in App Knock-in Alzheimer's Model Mice

Frontiers in aging neuroscience, 2022-05, Vol.14, p.878303-878303

2022

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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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The synthesis and characterization of Bri2 BRICHOS coated magnetic particles and their application to protein fishing: Identification of novel binding proteins

Journal of pharmaceutical and biomedical analysis, 2021-05, Vol.198, p.113996-113996, Article 113996

2021

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A “spindle and thread” mechanism unblocks p53 translation by modulating N-terminal disorder

Structure (London), 2022-05, Vol.30 (5), p.733-742.e7

2022

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Metal Binding of Alzheimer’s Amyloid‑β and Its Effect on Peptide Self-Assembly

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

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

Increased CSF-decorin predicts brain pathological changes driven by Alzheimer’s Aβ amyloidosis

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

Amyloid inhibition by molecular chaperones in vitro can be translated to Alzheimer's pathology in vivo

Ionic Strength Modulation of the Free Energy Landscape of Aβ40 Peptide Fibril Formation

A new kid in the folding funnel: Molecular chaperone activities of the BRICHOS domain

Metal ion coordination delays amyloid-β peptide self-assembly by forming an aggregation–inert complex

Functionalization of amyloid fibrils via the Bri2 BRICHOS domain

Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state

Intravenous treatment with a molecular chaperone designed against β-amyloid toxicity improves Alzheimer’s disease pathology in mouse models

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

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

Smallest Secondary Nucleation Competent Aβ Aggregates Probed by an ATP-Independent Molecular Chaperone Domain

Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform

Isotope‐labeled amyloid‐β does not transmit to the brain in a prion‐like manner after peripheral administration

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

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

Exploring the potential of the Bri2 BRICHOS domain as a drug-carrier for lysosomal storage disorders

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

Autophagy Impairment in App Knock-in Alzheimer's Model Mice

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 synthesis and characterization of Bri2 BRICHOS coated magnetic particles and their application to protein fishing: Identification of novel binding proteins

A “spindle and thread” mechanism unblocks p53 translation by modulating N-terminal disorder

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