ArticleBiochemistry2014
The C-terminal threonine of Aβ43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Small-Molecule Targeting of the Iron-Responsive Element in the APP mRNA 5'-UTR to Control Amyloid Translation in Alzheimer's Disease.International journal of molecular sciences · 2026Review
- Targeting Iron Responsive Elements (IREs) of APP mRNA into Novel Therapeutics to Control the Translation of Amyloid-β Precursor Protein in Alzheimer's Disease.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Expanding the molecular grammar of polar residues and arginine in FUS prion-like domain phase separation and aggregation.bioRxiv : the preprint server for biology · 2024Article
- TMEM106B core deposition associates with TDP-43 pathology and is increased in risk SNP carriers for frontotemporal dementia.Science translational medicine · 2024Article
- Senile plaques and phosphorylated tau deposition in a super-aged rhesus monkey (Macaca mulatta).The Journal of veterinary medical science · 2023Article
- Different Aβ43 deposition patterns in the brains of aged dogs, sea lions, and cats.The Journal of veterinary medical science · 2022Article
- NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions.Progress in nuclear magnetic resonance spectroscopy · 2022Review
- Reversible Kinetic Trapping of FUS Biomolecular Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Aβ43 aggregates exhibit enhanced prion-like seeding activity in mice.Acta neuropathologica communications · 2021Article
- Quantitative Measurement of Cerebrospinal Fluid Amyloid-β Species by Mass Spectrometry.Journal of Alzheimer's disease : JAD · 2021Article
- Enhancement of Amyloid βBiomedicines · 2020Article
- Reduced Influence of apoE on Aβ43 Aggregation and Reduced Vascular Aβ43 Toxicity as Compared with Aβ40 and Aβ42.Molecular neurobiology · 2020Article
- Exchange saturation transfer and associated NMR techniques for studies of protein interactions involving high-molecular-weight systems.Journal of biomolecular NMR · 2019Article
- The combined force field-sampling problem in simulations of disordered amyloid-β peptides.The Journal of chemical physics · 2019Article
- Lysines in the RNA Polymerase II C-Terminal Domain Contribute to TAF15 Fibril Recruitment.Biochemistry · 2018Article
- The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Journal of Alzheimer's disease : JAD · 2018Review
- Induction of Amyloid-β42 Production by Fipronil and Other Pyrazole Insecticides.Journal of Alzheimer's disease : JAD · 2018Article
- Cerebrospinal Fluid Levels of Amyloid Beta 1-43 Mirror 1-42 in Relation to Imaging Biomarkers of Alzheimer's Disease.Frontiers in aging neuroscience · 2017Article
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- Cerebrospinal Fluid Aβ43 Is Reduced in Early-Onset Compared to Late-Onset Alzheimer's Disease, But Has Similar Diagnostic Accuracy to Aβ42.Frontiers in aging neuroscience · 2017Article
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2 authors.
Funding
Abstract
Recent studies suggest that deposition of amyloid β (Aβ) into oligomeric aggregates and fibrils, hallmarks of Alzheimer's disease, may be initiated by the aggregation of Aβ species other than the well-studied 40- and 42-residue forms, Aβ40 and Aβ42, respectively. Here we report on key structural, dynamic, and aggregation kinetic parameters of Aβ43, extended by a single threonine at the C-terminus relative to Aβ42. Using aggregation time course experiments, electron microscopy, and a combination of nuclear magnetic resonance measurements including backbone relaxation, dark-state exchange saturation transfer, and quantification of chemical shift differences and scalar coupling constants, we demonstrate that the C-terminal threonine in Aβ43 increases the rate and extent of protofibril aggregation and confers slow C-terminal motions in the monomeric and protofibril-bound forms of Aβ43. Relative to the neighboring residues, the hydrophilic Thr43 of Aβ43 favors direct contact with the protofibril surface more so than the C-terminus of Aβ40 or Aβ42. Taken together, these results demonstrate the potential of a small chemical modification to affect the properties of Aβ structure and aggregation, providing a mechanism for the potential role of Aβ43 as a primary nucleator of Aβ aggregates in Alzheimer's disease.
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