Amyloid-β oligomers are captured by the DNAJB6 chaperone: Direct detection of interactions that can prevent primary nucleation
Open Access
- 1 June 2020
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 295 (24) , 8135-8144
Abstract
No abstract availableKeywords
All Related Versions
Funding Information
- Crafoordska Stiftelsen
- Alzheimerfonden
- the Swedish Research Council
- Science for Life Laboratory
This publication has 44 references indexed in Scilit:
- Relative Solvent Accessible Surface Area Predicts Protein Conformational Changes upon BindingStructure, 2011
- Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineeringProceedings of the National Academy of Sciences, 2010
- Molecular mechanism of Thioflavin-T binding to amyloid fibrilsBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2010
- A DNAJB Chaperone Subfamily with HDAC-Dependent Activities Suppresses Toxic Protein AggregationMolecular Cell, 2010
- Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: Conformational heterogeneity of α‐synucleinProteins: Structure, Function, and Bioinformatics, 2009
- Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's diseaseNature Chemistry, 2009
- A facile method for expression and purification of the Alzheimer’s disease‐associated amyloid β‐peptideThe FEBS Journal, 2009
- Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formationProceedings of the National Academy of Sciences, 2008
- Structural Reorganisation and Potential Toxicity of Oligomeric Species Formed during the Assembly of Amyloid FibrilsPLOS Computational Biology, 2007
- Aβ Oligomers – a decade of discoveryJournal of Neurochemistry, 2007