The DOI matches its Crossref record; 29 of the 30 references it cites were found in a registry or an index.
Quantifying Amyloid β-Peptide (Aβ) Aggregation Using the Congo Red-Aβ (CR–Aβ) Spectrophotometric Assay
Abstract
Congo red (CR) is a histologic dye that binds to many amyloid proteins because of their extensive beta-sheet structure. The absorbance spectrum of the dye changes upon binding to amyloid. This spectral change has previously been exploited to develop a method to study the interaction of CR with fibrillar beta-sheet insulin fibrils, a model amyloid protein. The amyloid beta-peptide (Abeta) is an amyloid protein which is deposited in the brains of Alzheimer's disease victims. Abeta is toxic to neurons in vitro in a manner that is highly dependent on the assembly of this peptide into beta-sheet fibrils. The CR-insulin assay has been applied as a means of studying the aggregation of Abeta, despite the fact that the CR-insulin procedure was never adequately developed for this purpose. In this study, we modify our original CR-insulin assay specifically for the purpose of quantifying Abeta aggregation and discuss the reasons why application of the CR-insulin method is not valid for this purpose. The CR-Abeta method is equally simple and retains the advantages of speed and lack of necessity for specialized instrumentation or expensive/radioactive reagents. Furthermore, this method can directly provide quantitation of aggregated Abeta in absolute terms (i.e., microg/ml).
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Congo red is known to bind amyloid-like fibrils with a β-sheet structure in a regular parallel arrangement, which can be detected by a red-shift in the Congo red absorbance spectrum (42).”
From Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody (2000) · cites this paper as [42]
In the citing paper
“which is shorter than that of amyloid fibrils (541 nm; ref. 42).”
From Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody (2000) · cites this paper as [42]
Citations
Cites
LeVine, H. (1993) · Protein Science · doi:10.1002/pro.5560020312 · Cited by 2,284
Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324
ON THE BINDING OF CONGO RED BY AMYLOID
Puchtler, H., Sweat, F., & Levine, M. I. (1962) · Journal of Histochemistry & Cytochemistry · doi:10.1177/10.3.355 · Cited by 1,133
Ma, J., Yee, A., Brewer, H. B., Das, S., & Potter, H. (1994) · Nature · doi:10.1038/372092a0 · Cited by 871
In vitro aging of ß-amyloid protein causes peptide aggregation and neurotoxicity
Pike, C. J., Walencewicz, A. J., Glabe, C. G., & Cotman, C. W. (1991) · Brain Research · doi:10.1016/0006-8993(91)91553-d · Cited by 841
Lomakin, A., Chung, D. S., Benedek, G. B., Kirschner, D. A., & Teplow, D. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1125 · Cited by 784
Klunk, W. E., Pettegrew, J. W., & Abraham, D. J. (1989) · Journal of Histochemistry & Cytochemistry · doi:10.1177/37.8.2666510 · Cited by 618
Self-citationA kinetic model for amyloid formation in the prion diseases: importance of seeding.
Come, J. H., Fraser, P. E., & Lansbury, P. T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.13.5959 · Cited by 395
Secondary structure of amyloid beta peptide correlates with neurotoxic activity in vitro.
Simmons, L. K., May, P. C., Tomaselli, K. J., Rydel, R. E., Fuson, K. S., Brigham, E. F., Wright, S., Lieberburg, I. M., Becker, G. W., & Brems, D. N. (1994) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10007-2 · Cited by 371
Research works printed but not linked: 3
- Glenner, 1973, J. Histochem. Cytochem., 21, 406
- Cooper, 1974, Lab. Invest., 31, 232
- Bedaux, 1963, Pharm. Weekbl. Sci., 98, 189
Cited by
Sorted by citations
Items 301–311 of 311
Exosomes in Amyloid Propagation—Roles in Neurodegeneration
Mishra, R., & Upadhyay, A. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05913-w
Kurihara, T., Aoyagi, R., Kitase, S., Kuroda, S., Kaneko, M., & Miura, T. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.111013
Guo, H., Zhang, L., Zuo, Z., Li, X., Sui, L., Yan, Y., & Zhang, X. (2026) · Materials Today Communications · doi:10.1016/j.mtcomm.2026.116486
BindingDB Entry 50020816: Bioactive Isoquinoline Alkaloids with Diverse Skeletons from
BindingDB (2024) · UC San Diego · doi:10.7270/q2f19476
BindingDB (2009) · UC San Diego · doi:10.7270/q2v69hv8
Jacobsen, C. L. (2013) · ScholarsArchive (Brigham Young University)
Henriques, S. T. (2007) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Investigating the process of fibril formation of the Iowa mutant of the Alzheimer's peptide
Udad, X. (2011) · Digital Commons-DePaul (DePaul University)
Khan (2000) · doi:10.1002/1531-8249(200008)48:2
Metadata
- Authors
- Klunk, W. E., Jacob, R. F., & Mason, R. P.
- Affiliations
- University of Pittsburgh (US)
- ORCID
- Klunk, William E.
- Venue
- Analytical Biochemistry
- Publisher
- Elsevier BV
- Published
- 1999-01
- Volume
- 266
- Issue
- 1
- Pages
- 66-76
- ISSN
- 0003-2697 (ISSN-L)
- OpenAlex
- W2053546096
- Cited by
- 310
- References
- 30
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 10 · 2023: 6 · 2022: 5 · 2021: 9 · 2020: 15 · 2019: 14 · 2018: 18 · 2017: 15 · 2016: 15 · 2015: 11 · 2014: 8 · 2013: 13 · 2012: 20
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Analytical Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- amyloid-beta, Congo red, spectrophotometric assay, β-sheet fibrils, Alzheimer's disease, dye-protein binding, amyloidosis
- MeSH terms
- Congo Red, Coloring Agents, Spectrophotometry, Amyloid beta-Peptides
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
