The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Folding proteins in fatal ways
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
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Self-citationWalsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Self-citationInherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline
Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268
Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227 · cited 1×
“In α-synuclein aggregation in Parkinson's disease, loss of dopaminergic neurons in a Drosophila model expressing human α-synuclein was prevented by co-expressing the heat shock protein Hsp70, one of numerous molecular chaperones that guide the correct folding of polypeptide”
BackgroundPlaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123
Water-soluble Aβ(N-40, N-42) oligomers in normal and Alzheimer disease brains
Kuo, Y.-M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., Ball, M. J., & Roher, A. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4077 · Cited by 618
Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats
Perutz, M. F., & Windle, A. H. (2001) · Nature · doi:10.1038/35084141 · Cited by 199
Cited by
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
Mechanisms of Diabetic Complications
Forbes, J. M., & Cooper, M. E. (2013) · Physiological Reviews · doi:10.1152/physrev.00045.2011 · Cited by 2,890
Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971
Opposing activities protect against age-onset proteotoxicity
Cohen, E., Bieschke, J., Perciavalle, R. M., Kelly, J. W., & Dillin, A. (2006) · Science · doi:10.1126/science.1124646 · Cited by 843
Molecular pathways to neurodegeneration
Bossy-Wetzel, E., Schwarzenbacher, R., & Lipton, S. A. (2004) · Nature Medicine · doi:10.1038/nm1067 · Cited by 740
Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs
Forman, M. S., Trojanowski, J. Q., & Lee, V. M.-Y. (2004) · Nature Medicine · doi:10.1038/nm1113 · Cited by 715
Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
Hetz, C., & Mollereau, B. (2014) · Nature Reviews Neuroscience · doi:10.1038/nrn3689 · Cited by 684
Trushina, E., Dutta, T., Persson, X.-M. T., Mielke, M. M., & Petersen, R. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063644 · Cited by 438
Contribution of inflammatory processes to Alzheimer's disease: molecular mechanisms
Sastre, M., Klockgether, T., & Heneka, M. T. (2006) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2005.11.014 · Cited by 426
Induction of cerebral β-amyloidosis: Intracerebral versus systemic Aβ inoculation
Eisele, Y. S., Bolmont, T., Heikenwalder, M., Langer, F., Jacobson, L. H., Yan, Z.-X., Roth, K., Aguzzi, A., Staufenbiel, M., Walker, L. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903200106 · Cited by 279
Emerging roles of ER stress in the etiology and pathogenesis of Alzheimer's disease
Gerakis, Y., & Hetz, C. (2018) · The FEBS Journal · doi:10.1111/febs.14332 · Cited by 226
Wogulis, M., Wright, S., Cunningham, D., Chilcote, T., Powell, K., & Rydel, R. E. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2381-04.2005 · Cited by 233
The Silver locus product Pmel17/gp100/Silv/ME20: controversial in name and in function
Theos, A. C., Truschel, S. T., Raposo, G., & Marks, M. S. (2005) · Pigment Cell Research · doi:10.1111/j.1600-0749.2005.00269.x · Cited by 224
Rodríguez-Rodríguez, C., Telpoukhovskaia, M., & Orvig, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.008 · Cited by 151
Pihlaja, R., Koistinaho, J., Kauppinen, R., Sandholm, J., Tanila, H., & Koistinaho, M. (2011) · Glia · doi:10.1002/glia.21212 · Cited by 96
Hsp90 inhibitors as senolytic drugs to extend healthy aging
Fuhrmann-Stroissnigg, H., Niedernhofer, L. J., & Robbins, P. D. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1475828 · Cited by 92
Garcia, P., Jürgens‐Wemheuer, W., Uriarte Huarte, O., Michelucci, A., Masuch, A., Brioschi, S., Weihofen, A., Koncina, E., Coowar, D., Heurtaux, T., et al. (2022) · Glia · doi:10.1002/glia.24149 · Cited by 65
Puentes-Díaz, N., Chaparro, D., Morales-Morales, D., Flores-Gaspar, A., & Alí-Torres, J. (2023) · ACS Omega · doi:10.1021/acsomega.2c06939 · Cited by 67
Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ
Malet, H., Canellas, F., Sawa, J., Yan, J., Thalassinos, K., Ehrmann, M., Clausen, T., & Saibil, H. R. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2210 · Cited by 61
Suttkus, A., Holzer, M., Morawski, M., & Arendt, T. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2015.11.040 · Cited by 50
Oligodendrocytes are a Novel Source of Amyloid Peptide Generation
Skaper, S. D., Evans, N. A., Soden, P. E., Rosin, C., Facci, L., & Richardson, J. C. (2009) · Neurochemical Research · doi:10.1007/s11064-009-0022-9 · Cited by 43
Microglial autophagy in Alzheimer’s disease and Parkinson’s disease
Wang, Z., Wang, Q., Li, S., Li, X.-J., Yang, W., & He, D. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1065183 · Cited by 35
Monomeric Aβ1–42 and RAGE: key players in neuronal differentiation
Piras, S., Furfaro, A. L., Piccini, A., Passalacqua, M., Borghi, R., Carminati, E., Parodi, A., Colombo, L., Salmona, M., Pronzato, M. A., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.01.002 · Cited by 27
Balancing speed and precision in protein folding: a comparison of AlphaFold2, ESMFold, and OmegaFold
Hýsková, A., Maršálková, E., & Šimeček, P. (2026) · Frontiers in Genetics · doi:10.3389/fgene.2025.1715037 · Cited by 16
Revealing Free Energy Landscape From MD Data via Conditional Angle Partition Tree
Jiang, H., Li, H., Wong, W. H., & Fan, X. (2023) · IEEE/ACM Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2022.3172352 · Cited by 4
Metadata
- Authors
- Selkoe, D. J.
- Venue
- Nature
- Published
- 2003-12-18
- Volume
- 426
- Issue
- 6968
- Pages
- 900-904
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2042036635
- Cited by
- 1,417
- References
- 8
- FWCI
- 31.67
- 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.
