The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant
Open accessAbstract
Prion proteins can serve as genetic elements by adopting distinct physical and functional states that are self-perpetuating and heritable. The critical region of one prion protein, Sup35, is initially unstructured in solution and then forms self-seeded amyloid fibers. We examined in vitro the mechanism by which this state is attained and replicated. Structurally fluid oligomeric complexes appear to be crucial intermediates in de novo amyloid nucleus formation. Rapid assembly ensues when these complexes conformationally convert upon association with nuclei. This model for replicating protein-based genetic information, nucleated conformational conversion, may be applicable to other protein assembly processes.
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
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,118
Jarrett, J. T., & Lansbury, P. T. (1993) · Cell · doi:10.1016/0092-8674(93)90635-4 · Cited by 2,178
Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen
Sunde, M., Serpell, L. C., Bartlam, M., Fraser, P. E., Pepys, M. B., & Blake, C. C. F. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1348 · Cited by 1,707
Self-citationHarper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
The interaction of a naphthalene dye with apomyoglobin and apohemoglobin
Stryer, L. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80111-5 · Cited by 1,497
Glover, J. R., & Lindquist, S. (1998) · Cell · doi:10.1016/s0092-8674(00)81223-4 · Cited by 1,357
Self-citationNature of the Scrapie Agent: Self-replication and Scrapie
GRIFFITH, J. S. (1967) · Nature · doi:10.1038/2151043a0 · Cited by 1,161
Role of the Chaperone Protein Hsp104 in Propagation of the Yeast Prion-Like Factor [ psi + ]
Chernoff, Y. O., Lindquist, S. L., Ono, B.-I., Inge-Vechtomov, S. G., & Liebman, S. W. (1995) · Science · doi:10.1126/science.7754373 · Cited by 1,027
Self-citationSupport for the Prion Hypothesis for Inheritance of a Phenotypic Trait in Yeast
Patino, M. M., Liu, J.-J., Glover, J. R., & Lindquist, S. (1996) · Science · doi:10.1126/science.273.5275.622 · Cited by 611
Self-citationGlover, J. R., Kowal, A. S., Schirmer, E. C., Patino, M. M., Liu, J.-J., & Lindquist, S. (1997) · Cell · doi:10.1016/s0092-8674(00)80264-0 · Cited by 597
Self-citation
Cited by
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein
Cremades, N., Cohen, S. I. A., Deas, E., Abramov, A. Y., Chen, A. Y., Orte, A., Sandal, M., Clarke, R. W., Dunne, P., Aprile, F. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.037 · Cited by 911
Metadata
- Authors
- Serio, T. R., Cashikar, A. G., Kowal, A. S., Sawicki, G. J., Moslehi, J. J., Serpell, L., Arnsdorf, M. F., & Lindquist, S. L.
- Venue
- Science
- Published
- 2000-08-25
- Volume
- 289
- Issue
- 5483
- Pages
- 1317-1321
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2068334126
- Cited by
- 963
- References
- 25
- FWCI
- 9.35
- Type
- journal article
- Language
- en
- Open access
- green
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: Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant. https://app.cochat.ai/papers/10.1126/science.289.5483.1317
- The paper
- Serio, T. R., Cashikar, A. G., Kowal, A. S., Sawicki, G. J., Moslehi, J. J., Serpell, L., Arnsdorf, M. F., & Lindquist, S. L. (2000). Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant. Science. https://doi.org/10.1126/science.289.5483.1317
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.
