The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Manipulating the Amyloid-β Aggregation Pathway with Chemical Chaperones
Open accessAbstract
Amyloid-beta (Abeta) assembly into fibrillar structures is a defining characteristic of Alzheimer's disease that is initiated by a conformational transition from random coil to beta-sheet and a nucleation-dependent aggregation process. We have investigated the role of organic osmolytes as chemical chaperones in the amyloid pathway using glycerol to mimic the effects of naturally occurring molecules. Osmolytes such as the naturally occurring trimethylamine N-oxide and glycerol correct folding defects by preferentially hydrating partially denatured proteins and entropically stabilize native conformations and polymeric states. Trimethylamine N-oxide and glycerol were found to rapidly accelerate the Abeta random coil-to-beta-sheet conformational change necessary for fiber formation. This was accompanied by an immediate conversion of amorphous unstructured aggregates into uniform globular and possibly nucleating structures. Osmolyte-facilitated changes in Abeta hydration also affected the final stages of amyloid formation and mediated transition from the protofibrils to mature fibers that are observed in vivo. These findings suggest that hydration forces can be used to control fibril assembly and may have implications for the accumulation of Abeta within intracellular compartments such as the endoplasmic reticulum and in vitro modeling of the amyloid pathway.
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Cites
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
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Cited by
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
Ehrnhoefer, D. E., Bieschke, J., Boeddrich, A., Herbst, M., Masino, L., Lurz, R., Engemann, S., Pastore, A., & Wanker, E. E. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1437 · Cited by 1,434
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015
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Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
Ignatova, Z., & Gierasch, L. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603772103 · Cited by 320
The therapeutic potential of chemical chaperones in protein folding diseases
Cortez, L., & Sim, V. (2014) · Prion · doi:10.4161/pri.28938 · Cited by 254
Metadata
- Authors
- Yang, D.-S., Yip, C. M., Huang, T. H. J., Chakrabartty, A., & Fraser, P. E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-11
- Volume
- 274
- Issue
- 46
- Pages
- 32970-32974
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1966771308
- Cited by
- 268
- References
- 33
- FWCI
- 5.02
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Yang, D.-S., Yip, C. M., Huang, T. H. J., Chakrabartty, A., & Fraser, P. E. (1999). Manipulating the Amyloid-β Aggregation Pathway with Chemical Chaperones. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.46.32970
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
