The DOI matches its Crossref record; 137 of the 137 references it cites were found in a registry or an index.
PATHOLOGIC CONFORMATIONS OF PRION PROTEINS
Abstract
While many aspects of prion disease biology are unorthodox, perhaps the most fundamental paradox is posed by the coexistence of inherited, sporadic, and infectious forms of these diseases. Sensible molecular mechanisms for prion propagation must explain all three forms of prion diseases in a manner that is compatible with the formidable array of experimental data derived from histopathological, biochemical, biophysical, human genetic, and transgenetic studies. In this review, we explore prion disease pathogenesis initially from the perspective of an autosomal dominant inherited disease. Subsequently, we examine how an intrinsically inherited disease could present in sporadic and infectious forms. Finally, we explore the phenomenologic constraints on models of prion replication with a specific emphasis on biophysical studies of prion protein structures.
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
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,118
Self-citationPan, K. M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., & Cohen, F. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10962 · Cited by 2,277
Self-citationMice devoid of PrP are resistant to scrapie
Büeler, H., Aguzzi, A., Sailer, A., Greiner, R.-A., Autenried, P., Aguet, M., & Weissmann, C. (1993) · Cell · doi:10.1016/0092-8674(93)90360-3 · Cited by 2,100
Molecular Biology of Prion Diseases
Prusiner, S. B. (1991) · Science · doi:10.1126/science.1675487 · Cited by 1,988
Self-citationAmyloid Deposits and Amyloidosis: The β-Fibrilloses(First of Two Parts)
Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006053022305 · Cited by 1,790
A cellular gene encodes scrapie PrP 27-30 protein
Oesch, B., Westaway, D., Wälchli, M., McKinley, M. P., Kent, S. B. H., Aebersold, R., Barry, R. A., Tempst, P., Teplow, D. B., Hood, L. E., et al. (1985) · Cell · doi:10.1016/0092-8674(85)90333-2 · Cited by 1,513
Self-citationNMR structure of the mouse prion protein domain PrP(121–231)
Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., & Wüthrich, K. (1996) · Nature · doi:10.1038/382180a0 · Cited by 1,257
Scrapie prions aggregate to form amyloid-like birefringent rods
Prusiner, S. B., McKinley, M. P., Bowman, K. A., Bolton, D. C., Bendheim, P. E., Groth, D. F., & Glenner, G. G. (1983) · Cell · doi:10.1016/0092-8674(83)90168-x · Cited by 1,043
Self-citationPrion Diseases and the BSE Crisis
Prusiner, S. B. (1997) · Science · doi:10.1126/science.278.5336.245 · Cited by 954
Self-citation
Cited by
Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine System
Abeliovich, A., Schmitz, Y., Fariñas, I., Choi-Lundberg, D., Ho, W.-H., Castillo, P. E., Shinsky, N., Verdugo, J. M. G., Armanini, M., Ryan, A., et al. (2000) · Neuron · doi:10.1016/s0896-6273(00)80886-7 · Cited by 1,722
3D domain swapping: As domains continue to swap
Liu, Y., & Eisenberg, D. (2002) · Protein Science · doi:10.1110/ps.0201402 · Cited by 684
Amyloid Structure: Conformational Diversity and Consequences
Toyama, B. H., & Weissman, J. S. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-090908-120656 · Cited by 304
Inhibitors of Amyloid Toxicity Based on β-sheet Packing of Aβ40 and Aβ42
Sato, T., Kienlen-Campard, P., Ahmed, M., Liu, W., Li, H., Elliott, J. I., Aimoto, S., Constantinescu, S. N., Octave, J.-N., & Smith, S. O. (2006) · Biochemistry · doi:10.1021/bi052485f · Cited by 191
Shaked, G. M., Kummer, M. P., Lu, D. C., Galvan, V., Bredesen, D. E., Koo, E. H., Shaked, G. M., Kummer, M. P., Lu, D. C., Galvan, V., et al. (2006) · The FASEB Journal · doi:10.1096/fj.05-5032fje · Cited by 132
Metadata
- Authors
- Cohen, F. E., & Prusiner, S. B.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1998-06
- Volume
- 67
- Issue
- 1
- Pages
- 793-819
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2148130200
- Cited by
- 533
- References
- 137
- FWCI
- 2.09
- 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: PATHOLOGIC CONFORMATIONS OF PRION PROTEINS. https://app.cochat.ai/papers/10.1146/annurev.biochem.67.1.793
- The paper
- Cohen, F. E., & Prusiner, S. B. (1998). PATHOLOGIC CONFORMATIONS OF PRION PROTEINS. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.67.1.793
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.