The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Creation of "Amyloid" Fibrils from Bence Jones Proteins in vitro
Abstract
"Amyloid" fibrils have been created from some human Bence Jones proteins by proteolytic digestion under physiologic conditions. These fibrils with an antiparallel, β-pleated sheet conformation consist of only a portion of the variable region of the immunoglobulin light polypeptide chain and share the physical properties of amyloid fibrils. The relation between amyloidosis and immunoglobulins is thus more firmly established and a pathogenetic mechanism for amyloid fibril formation is suggested.
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
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 20,298
Edman, P., & Begg, G. (1967) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1967.tb00047.x · Cited by 2,845
ON THE BINDING OF CONGO RED BY AMYLOID
PUCHTLER, H., SWEAT, F., & LEVINE, M. (1962) · Journal of Histochemistry & Cytochemistry · doi:10.1177/10.3.355 · Cited by 1,128
X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS
EANES, E. D., & GLENNER, G. G. (1968) · Journal of Histochemistry & Cytochemistry · doi:10.1177/16.11.673 · Cited by 823
Self-citationPeptide Separation by Two-dimensional Chromatography and Electrophoresis
Katz, A. M., Dreyer, W. J., & Anfinsen, C. B. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69690-5 · Cited by 726
Electron Microscopic Observations on a Fibrous Component in Amyloid of Diverse Origins
COHEN, A. S., & CALKINS, E. (1959) · Nature · doi:10.1038/1831202a0 · Cited by 638
Fish, W. W., Mann, K. G., & Tanford, C. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94300-0 · Cited by 601
Amyloid Fibril Proteins: Proof of Homology with Immunoglobulin Light Chains by Sequence Analyses
Glenner, G. G., Terry, W., Harada, M., Isersky, C., & Page, D. (1971) · Science · doi:10.1126/science.172.3988.1150 · Cited by 590
Self-citationHIGH-RESOLUTION ELECTRON MICROSCOPIC ANALYSIS OF THE AMYLOID FIBRIL
Shirahama, T., & Cohen, A. S. (1967) · The Journal of Cell Biology · doi:10.1083/jcb.33.3.679 · Cited by 383
Edelman, G. M., & Gall, W. E. (1969) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.38.070169.002215 · Cited by 343
Cited by
Protein aggregation: folding aggregates, inclusion bodies and amyloid
Fink, A. L. (1998) · Folding and Design · doi:10.1016/s1359-0278(98)00002-9 · Cited by 1,157
Breathnach, S. M. (1988) · Journal of the American Academy of Dermatology · doi:10.1016/s0190-9622(88)70001-8 · Cited by 615
Alternative conformations of amyloidogenic proteins govern their behavior
Kelly, J. W. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80089-3 · Cited by 593
Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
Colon, W., & Kelly, J. W. (1992) · Biochemistry · doi:10.1021/bi00151a036 · Cited by 573
Amyloid fibrils: Abnormal protein assembly
Rambaran, R. N., & Serpell, L. C. (2008) · Prion · doi:10.4161/pri.2.3.7488 · Cited by 511
Metadata
- Authors
- Glenner, G. G., Ein, D., Eanes, E. D., Bladen, H. A., Terry, W., & Page, D. L.
- Venue
- Science
- Published
- 1971-11-12
- Volume
- 174
- Issue
- 4010
- Pages
- 712-714
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2054733764
- Cited by
- 377
- References
- 14
- FWCI
- 8.25
- 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: Creation of "Amyloid" Fibrils from Bence Jones Proteins in vitro. https://app.cochat.ai/papers/10.1126/science.174.4010.712
- The paper
- Glenner, G. G., Ein, D., Eanes, E. D., Bladen, H. A., Terry, W., & Page, D. L. (1971). Creation of "Amyloid" Fibrils from Bence Jones Proteins in vitro. Science. https://doi.org/10.1126/science.174.4010.712
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.