The DOI matches its Crossref record; 100 of the 100 references it cites were found in a registry or an index.
Untangling Amyloid-β, Tau, and Metals in Alzheimer’s Disease
Abstract
Protein misfolding and metal ion dyshomeostasis are believed to underlie numerous neurodegenerative diseases, including Alzheimer's disease (AD). The pathological hallmark of AD is accumulation of misfolded amyloid-β (Aβ) peptides and hyperphosphorylated tau (ptau) proteins in the brain. Since AD etiology remains unclear, several hypotheses have emerged to elucidate its pathological pathways. The amyloid cascade hypothesis, a leading hypothesis for AD development, advocates Aβ as the principal culprit. Additionally, evidence suggests that tau may contribute to AD pathology. Aβ and tau have also been shown to impact each other's pathology either directly or indirectly. Furthermore, metal ion dyshomeostasis is associated with these misfolded proteins. Metal interactions with Aβ and tau/ptau also influence their aggregation properties and neurotoxicity. Herein, we present current understanding on the roles of Aβ, tau, and metal ions, placing equal emphasis on each of these proposed features, as well as their inter-relationships in AD pathogenesis.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedVMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,423
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174
Metals in Neurobiology: Probing Their Chemistry and Biology with Molecular Imaging
Que, E. L., Domaille, D. W., & Chang, C. J. (2008) · Chemical Reviews · doi:10.1021/cr078203u · Cited by 2,061
Buée, L., Bussière, T., Buée-Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,015
3D structure of Alzheimer's amyloid-β(1–42) fibrils
Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 1,996
Cited by
Synthetic fluorescent probes for studying copper in biological systems
Cotruvo, Jr., Aron, A. T., Ramos-Torres, K. M., & Chang, C. J. (2015) · Chemical Society Reviews · doi:10.1039/c4cs00346b · Cited by 558
Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation
Tamás, M., Sharma, S., Ibstedt, S., Jacobson, T., & Christen, P. (2014) · Biomolecules · doi:10.3390/biom4010252 · Cited by 468
Chemically diverse small molecule fluorescent chemosensors for copper ion
Sivaraman, G., Iniya, M., Anand, T., Kotla, N. G., Sunnapu, O., Singaravadivel, S., Gulyani, A., & Chellappa, D. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.11.020 · Cited by 391
The biological pathways of Alzheimer disease: a review
Calabrò, M., Department of Biomedical and Dental Sciences and Morphofunctional Imaging, U. O. M., Rinaldi, C., Santoro, G., & Crisafulli, C. (2021) · AIMS Neuroscience · doi:10.3934/neuroscience.2021005 · Cited by 265
Rajasekhar, K., & Govindaraju, T. (2018) · RSC Advances · doi:10.1039/c8ra03620a · Cited by 150
Role of natural products for the treatment of Alzheimer’s disease
Noori, T., Dehpour, A. R., Sureda, A., Sobarzo-Sanchez, E., & Shirooie, S. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173974 · Cited by 141
Multitarget Therapeutic Strategies for Alzheimer’s Disease: Review on Emerging Target Combinations
Maramai, S., Benchekroun, M., Gabr, M. T., & Yahiaoui, S. (2020) · BioMed Research International · doi:10.1155/2020/5120230 · Cited by 121
Microbiota‐microglia connections in age‐related cognition decline
Zhou, R., Qian, S., Cho, W. C. S., Zhou, J., Jin, C., Zhong, Y., Wang, J., Zhang, X., Xu, Z., Tian, M., et al. (2022) · Aging Cell · doi:10.1111/acel.13599 · Cited by 71
Hybrid Multifunctional Modulators Inhibit Multifaceted Aβ Toxicity and Prevent Mitochondrial Damage
Rajasekhar, K., Mehta, K., & Govindaraju, T. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00033 · Cited by 69
Chen, Y.-Y., Wang, M.-C., Wang, Y.-N., Hu, H.-H., Liu, Q.-Q., Liu, H.-J., & Zhao, Y.-Y. (2020) · Biomarker Research · doi:10.1186/s40364-020-00218-z · Cited by 33
Liu, Y., Kochi, A., Pithadia, A. S., Lee, S., Nam, Y., Beck, M. W., He, X., Lee, D., & Lim, M. H. (2013) · Inorganic Chemistry · doi:10.1021/ic400851w · Cited by 30
Self-citationTomasello, M. F., Di Rosa, M. C., Naletova, I., Sciacca, M. F. M., Giuffrida, A., Maccarrone, G., & Attanasio, F. (2025) · Bioinorganic Chemistry and Applications · doi:10.1155/bca/4226220 · Cited by 3
“Several studies have shown that the AD-afected brain contains elevated concentrations of transition metals accumulated in amyloid plaques, mainly copper, zinc, and iron, suggesting that these metal ions actively take part in the etiology of the pathology by interacting with a β peptide [3, 9, 12].”
Metadata
- Authors
- Savelieff, M. G., Lee, S., Liu, Y., & Lim, M. H.
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2013-03-18
- Volume
- 8
- Issue
- 5
- Pages
- 856-865
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- OpenAlex
- W2029119021
- Cited by
- 400
- References
- 100
- FWCI
- 17.95
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
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.
