The DOI matches its Crossref record.
X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS
Abstract
The filamentous protein component of amyloid-laden tissue was studied by x-ray diffraction procedures. The principal features of the x-ray pattern from nonoriented amyloid material consist of a sharp, intense ring at 4.75 Å overlaying a diffuse halo at 4.3 Å, and a broad and less intense ring at 9.8 Å. When oriented, the material gives a "cross-β" x-ray pattern. The x-ray findings are interpreted in terms of a "pleated sheet" structure formed by the amyloid polypeptide chain folding in a regular manner on itself such that adjacent chain segments are laterally arranged in an antiparallel manner. The x-ray patterns from oriented amyloid suggest further that the axes of the chain segments run transverse to the filament axis.
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
Cited by
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
Self-citationProtein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965
Westermark, P., Wernstedt, C., Wilander, E., Hayden, D. W., O'Brien, T. D., & Johnson, K. H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.11.3881 · Cited by 976
Common mechanisms of amyloid oligomer pathogenesis in degenerative disease
Glabe, C. G. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.04.017 · Cited by 569
Metadata
- Authors
- EANES, E. D., & GLENNER, G. G.
- Venue
- Journal of Histochemistry & Cytochemistry
- Publisher
- SAGE Publications
- Published
- 1968-11
- Volume
- 16
- Issue
- 11
- Pages
- 673-677
- ISSN
- 0022-1554 (ISSN-L)
- 1551-5044
- OpenAlex
- W2062593465
- Cited by
- 823
- References
- 0
- FWCI
- 1.74
- 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: X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS. https://app.cochat.ai/papers/10.1177/16.11.673
- The paper
- EANES, E. D., & GLENNER, G. G. (1968). X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS. Journal of Histochemistry & Cytochemistry. https://doi.org/10.1177/16.11.673
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.
