The DOI matches its Crossref record; 1,144 of the 1,144 references it cites were found in a registry or an index.
Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis
Open accessAbstract
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting either the central nervous system or a variety of peripheral tissues. Structural and dynamic characterization of all species along the pathways from monomers to fibrils is challenging by experimental and computational means because they involve intrinsically disordered proteins in most diseases. Yet understanding how amyloid species become toxic is the challenge in developing a treatment for these diseases. Here we review what computer, in vitro, in vivo, and pharmacological experiments tell us about the accumulation and deposition of the oligomers of the (Aβ, tau), α-synuclein, IAPP, and superoxide dismutase 1 proteins, which have been the mainstream concept underlying Alzheimer’s disease (AD), Parkinson’s disease (PD), type II diabetes (T2D), and amyotrophic lateral sclerosis (ALS) research, respectively, for many years.
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4 retracted
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RetractedRETRACTED: Soluble α-Synuclein Is a Novel Modulator of Alzheimer's Disease Pathophysiology
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Self-citationRetractedVMD: visual molecular dynamics
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The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
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Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
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Cited by
Alrouji, M., Al-Kuraishy, H. M., Al-Gareeb, A. I., Saad, H. M., & Batiha, G. E.-S. (2023) · Inflammopharmacology · doi:10.1007/s10787-023-01192-2 · Cited by 47
Liquid − liquid phase separation of tau: Driving forces, regulation, and biological implications
Li, P., Chen, J., Wang, X., Su, Z., Gao, M., & Huang, Y. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106167 · Cited by 30
Self-citationBerbon, M., Martinez, D., Morvan, E., Grélard, A., Kauffmann, B., Waeytens, J., Wien, F., Arluison, V., & Habenstein, B. (2023) · Communications Biology · doi:10.1038/s42003-023-05462-1 · Cited by 14
Self-citationHitschler, L., & Lang, T. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101911 · Cited by 11
AmyloGram reveals amyloidogenic potential in stroke thrombus proteomes
Kell, D. B., Doyle, K. M., Salcedo-Sora, J. E., Sekhar, A., Walker, M., & Pretorius, E. (2025) · Biochemical Journal · doi:10.1042/bcj20253317 · Cited by 4
“The highest-scoring proteins included amyloid precursor protein (APP, part of whose sequence forms the highly amyloidogenic Aβ protein [65]) and islet amyloid polypeptide (IAPP or amylin [66–70]), both exceeding 0.95.”
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Metadata
- Authors
- Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., Ma, B., Nussinov, R., Najafi, S., Ngo, S. T., Loquet, A., Chiricotto, M., Ganguly, P., McCarty, J., Li, M. S., Hall, C., Wang, Y., Miller, Y., Melchionna, S., Habenstein, B., Timr, S., Chen, J., Hnath, B., Strodel, B., Kayed, R., Lesné, S., Wei, G., Sterpone, F., Doig, A. J., & Derreumaux, P.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2021-02-05
- Volume
- 121
- Issue
- 4
- Pages
- 2545-2647
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W3127602688
- Cited by
- 678
- References
- 1,144
- FWCI
- 22.06
- Type
- journal article
- Language
- en
- Open access
- green
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- Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., Ma, B., Nussinov, R., Najafi, S., Ngo, S. T., Loquet, A., Chiricotto, M., Ganguly, P., McCarty, J., Li, M. S., . . . Derreumaux, P. (2021). Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis. Chemical Reviews. https://doi.org/10.1021/acs.chemrev.0c01122
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
