Dev Thacker

Lund, M 22100, Sweden

Last Updated: 09/26/2026

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Found 18 publications

The chaperone DNAJB6b halts amyloid formation through association with transient Aβ oligomers.

The chaperone DNAJB6b halts amyloid formation through association with transient Aβ oligomers.

Journal: Physical chemistry chemical physics : PCCP

Published: May 01, 2026

The temperature dependence of amyloid β solubility reveals the hydrophobic effect as the main driving force for fibril formation.

The temperature dependence of amyloid β solubility reveals the hydrophobic effect as the main driving force for fibril formation.

Journal: Proceedings of the National Academy of Sciences of the United States of America

Published: April 20, 2026

Human chaperone DNAJB6b suppresses tau fibril formation through co-aggregation.

Human chaperone DNAJB6b suppresses tau fibril formation through co-aggregation.

Journal: Communications chemistry

Published: January 26, 2026

Aducanumab binding to Aβ1-42 fibrils alters dynamics of the N-terminal tail while preserving the fibril core.

Aducanumab binding to Aβ1-42 fibrils alters dynamics of the N-terminal tail while preserving the fibril core.

Journal: Proceedings of the National Academy of Sciences of the United States of America

Published: December 22, 2025

Aducanumab Binding to Aβ1-42 Fibrils Alters Dynamics of the N-Terminal Tail While Preserving the Fibril Core.

Aducanumab Binding to Aβ1-42 Fibrils Alters Dynamics of the N-Terminal Tail While Preserving the Fibril Core.

Journal: bioRxiv : the preprint server for biology

Published: November 24, 2025

On the self-assembly of αB-crystallin.

On the self-assembly of αB-crystallin.

Journal: Soft matter

Published: September 02, 2025

The Role of α-Synuclein-DNAJB6b Coaggregation in Amyloid Suppression.

The Role of α-Synuclein-DNAJB6b Coaggregation in Amyloid Suppression.

Journal: ACS chemical neuroscience

Published: April 30, 2025

Residues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways.

Residues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways.

Journal: Proceedings of the National Academy of Sciences of the United States of America

Published: August 12, 2024

Structural defects in amyloid-β fibrils drive secondary nucleation.

Structural defects in amyloid-β fibrils drive secondary nucleation.

Journal: Nature communications

Published: June 29, 2024

The role of shear forces in primary and secondary nucleation of amyloid fibrils.

The role of shear forces in primary and secondary nucleation of amyloid fibrils.

Journal: Proceedings of the National Academy of Sciences of the United States of America

Published: June 14, 2024

Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces.

Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces.

Journal: ACS chemical neuroscience

Published: May 24, 2024

Direct observation of secondary nucleation along the fibril surface of the amyloid β 42 peptide.

Direct observation of secondary nucleation along the fibril surface of the amyloid β 42 peptide.

Journal: Proceedings of the National Academy of Sciences of the United States of America

Published: June 12, 2023

Showing 1-12 of 18

Last Updated: 09/26/2026