The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
In Situ Oxidative Catalysis by Neurofibrillary Tangles and Senile Plaques in Alzheimer’s Disease: A Central Role for Bound Transition Metals
Abstract
Abstract: There is a great deal of evidence to support a pathogenic role of oxidative stress in Alzheimer’s disease (AD), but the sources of reactive oxygen species have not been directly demonstrated. In this study, using a novel in situ detection system, we show that neurofibrillary tangles and senile plaques are major sites for catalytic redox reactivity. Pretreatment with deferoxamine or diethylenetriaminepentaacetic acid abolishes the ability of the lesions to catalyze the H 2 O 2‐dependent oxidation of 3,3′‐diaminobenzidine (DAB), strongly suggesting the involvement of associated transition metal ions. Indeed, following chelated removal of metals, incubation with iron or copper salts reestablished lesion‐dependent catalytic redox reactivity. Although DAB oxidation can also detect peroxidase activity, this was inactivated by H 2 O 2 pretreatment before use of DAB, as shown by a specific peroxidase detection method. Model studies confirmed the ability of certain copper and iron coordination complexes to catalyze the H 2 O 2‐dependent oxidation of DAB. Also, the microtubule‐associated protein τ, as an in vitro model for proteins relevant to AD pathology, was found capable of adventitious binding of copper and iron in a redox‐competent manner. Our findings suggest that neurofibrillary tangles and senile plaques contain redox‐active transition metals and may thereby exert prooxidant or possibly antioxidant activities, depending on the balance among cellular reductants and oxidants in the local microenvironment.
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
Copper, iron and zinc in Alzheimer's disease senile plaques
Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120
Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease.
Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., & Markesbery, W. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10540 · Cited by 1,296
Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009
Transition metals as catalysts of “autoxidation” reactions
Miller, D. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90148-c · Cited by 739
Good, P. F., Perl, D. P., Bierer, L. M., & Schmeidler, J. (1992) · Annals of Neurology · doi:10.1002/ana.410310310 · Cited by 476
Yan, S. D., Yan, S. F., Chen, X., Fu, J., Chen, M., Kuppusamy, P., Smith, M. A., Perry, G., Godman, G. C., Nawroth, P., et al. (1995) · Nature Medicine · doi:10.1038/nm0795-693 · Cited by 406
Self-citationAnalysis of microtubule-associated protein tau glycation in paired helical filaments.
Ledesma, M. D., Bonay, P., Colaço, C., & Avila, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31849-5 · Cited by 333
Abnormal localization of iron regulatory protein in Alzheimer’s disease
Smith, M. A., Wehr, K., Harris, P. L. R., Siedlak, S. L., Connor, J. R., & Perry, G. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00002-x · Cited by 162
Self-citationQuinone reductase (NQO1), a sensitive redox indicator, is increased in Alzheimer’s disease
Raina, A. K., Templeton, D. J., deak, J. C., Perry, G., & Smith, M. A. (1999) · Redox Report · doi:10.1179/135100099101534701 · Cited by 120
Self-citation
Cited by
Neurodegenerative diseases and oxidative stress
Barnham, K. J., Masters, C. L., & Bush, A. I. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1330 · Cited by 3,683
Oxidative Damage Is the Earliest Event in Alzheimer Disease
Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885
Self-citationThe role of iron in brain ageing and neurodegenerative disorders
Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819
Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease
Tönnies, E., & Trushina, E. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161088 · Cited by 1,750
Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729
Metadata
- Authors
- Sayre, L. M., Perry, G., Harris, P. L. R., Liu, Y., Schubert, K. A., & Smith, M. A.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2000-01
- Volume
- 74
- Issue
- 1
- Pages
- 270-279
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1731253253
- Cited by
- 540
- References
- 9
- FWCI
- 14.55
- 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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: In Situ Oxidative Catalysis by Neurofibrillary Tangles and Senile Plaques in Alzheimer’s Disease: A Central Role for Bound Transition Metals. https://app.cochat.ai/papers/10.1046/j.1471-4159.2000.0740270.x
- The paper
- Sayre, L. M., Perry, G., Harris, P. L. R., Liu, Y., Schubert, K. A., & Smith, M. A. (2000). In Situ Oxidative Catalysis by Neurofibrillary Tangles and Senile Plaques in Alzheimer’s Disease: A Central Role for Bound Transition Metals. Journal of Neurochemistry. https://doi.org/10.1046/j.1471-4159.2000.0740270.x
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.
