Quantifying Amyloid β-Peptide (Aβ) Aggregation Using the Congo Red-Aβ (CR–Aβ) Spectrophotometric Assay

Thioflavine T interaction with synthetic Alzheimer's disease β ‐amyloid peptides: Detection of amyloid aggregation in solution

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

Amyloid-associated proteins α1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments

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

On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants.

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

Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation.

Klunk, W. E., Pettegrew, J. W., & Abraham, D. J. (1989) · Journal of Histochemistry & Cytochemistry · doi:10.1177/37.8.2666510 · Cited by 618

A 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

Physical, morphological and functional differences between ph 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Abeta.

Wood, S. J., Maleeff, B., Hart, T., & Wetzel, R. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0133 · Cited by 337

Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB

Jarrett, J. T., & Lansbury, P. T. (1992) · Biochemistry · doi:10.1021/bi00164a008 · Cited by 325

Selective Inhibition of Aβ Fibril Formation

Wood, S. J., MacKenzie, L., Maleeff, B. E., Hurle, M. R., & Wetzel, R. B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4086 · Cited by 234

In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to alzheimer's disease β-protein

Castaño, E. M., Ghiso, J. A., Prelli, F. C., Gorevic, P. D., Migheli, A., & Frangione, B. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80241-8 · Cited by 225

The Toxicity of the Alzheimer's β-Amyloid Peptide Correlates with a Distinct Fiber Morphology

Seilheimer, B., Bohrmann, B., Bondolfi, L., Müller, F., Stüber, D., & Döbeli, H. (1997) · Journal of Structural Biology · doi:10.1006/jsbi.1997.3859 · Cited by 207

Aggregation State and Neurotoxic Properties of Alzheimer Beta-Amyloid Peptide

Howlett, D. R., JENNINGS, K. H., Lee, D. C., Clark, M. S. G., Brown, F., Wetzel, R. B., Wood, S. J., Camilleri, P., & Roberts, G. W. (1995) · Neurodegeneration · doi:10.1006/neur.1995.0003 · Cited by 204

THE RELATION OF THE PROPERTIES OF CONGO RED-STAINED AMYLOID FIBRILS TO THE β-CONFORMATION

Glenner, G. G., Page, D. L., & Eanes, E. D. (1972) · Journal of Histochemistry & Cytochemistry · doi:10.1177/20.10.821 · Cited by 192

Binding of the dye congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences

Turnell, W. G., & Finch, J. T. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90532-o · Cited by 181

Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease.

Klunk, W., Debnath, M., & Pettegrew, J. (1994) · Neurobiology of Aging · doi:10.1016/0197-4580(94)90050-7 · Cited by 180

Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods.

Jh, C. (1974) · PubMed · Cited by 137

A Model for Structure-Dependent Binding of Congo Red to Alzheimer β-Amyloid Fibrils

Carter, D. B., & Chou, K.-C. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00164-4 · Cited by 131

Two simple methods for quantifying low-affinity dye-substrate binding.

Klunk, W. E., Pettegrew, J. W., & Abraham, D. J. (1989) · Journal of Histochemistry & Cytochemistry · doi:10.1177/37.8.2666512 · Cited by 99

Double-Refringence of the Amyloid-Congo-Red-Complex in Histological Sections

Ladewig, P. P. (1945) · Nature · doi:10.1038/156081a0 · Cited by 96

Light scattering analysis of fibril growth from the amino-terminal fragment beta(1–28) of beta-amyloid peptide

Shen, C. L., Scott, G., Merchant, F., & Murphy, R. M. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81312-2 · Cited by 93

Aβ deposition inhibitor screen using synthetic amyloid

Esler, W. P., Stimson, E. R., Ghilardi, J. R., Felix, A. M., Lu, Y., Vinters, H. V., Mantyh, P. W., & Maggio, J. E. (1997) · Nature Biotechnology · doi:10.1038/nbt0397-258 · Cited by 69

Selective Aggregation of Endogenous β‐Amyloid Peptide and Soluble Amyloid Precursor Protein in Cerebrospinal Fluid by Zinc

Brown, A. M., Tummolo, D. M., Rhodes, K. J., Hofmann, J. R., Jacobsen, J. S., & Sonnenberg‐Reines, J. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69031204.x · Cited by 55

HISTOCHEMICAL OBSERVATIONS ON AMYLOID WITH REFERENCE TO POLARIZATION MICROSCOPY

DeLellis, R. A., Glenner, G. G., & Ram, J. S. (1968) · Journal of Histochemistry & Cytochemistry · doi:10.1177/16.10.663-a · Cited by 39

Predicting the In Vitro Toxicity of Synthetic Beta-Amyloid (1-40)

Brining, S. K. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00153-x · Cited by 25

Identification of the importance of the secondary structure of Alzheimer's disease amyloid

Cavillon, F., Elhaddaoui, A., Alix, A. J. P., Turrell, S., & Dauchez, M. (1997) · Journal of Molecular Structure · doi:10.1016/s0022-2860(96)09673-1 · Cited by 13

Curcumin Inhibits Formation of Amyloid β Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo

Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336

Amyloid β-Protein Fibrillogenesis

Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046

Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in Cortical Neurons

Hartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B., & Selkoe, D. J. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 817

Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid

Conway, K. A., Harper, J. D., & Lansbury, P. T. (2000) · Biochemistry · doi:10.1021/bi991447r · Cited by 786

11C-PiB PET assessment of change in fibrillar amyloid-β load in patients with Alzheimer's disease treated with bapineuzumab: a phase 2, double-blind, placebo-controlled, ascending-dose study

Rinne, J. O., Brooks, D. J., Rossor, M. N., Fox, N. C., Bullock, R., Klunk, W. E., Mathis, C. A., Blennow, K., Barakos, J., Okello, A. A., et al. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70043-0 · Cited by 701

[19] Quantifying amyloid by congo red spectral shift assay

Klunk, W. E., Jacob, R. F., & Mason, R. P. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)09021-7 · Cited by 352

A new molecular model for Congo Red-β amyloid interaction: implications for diagnosis and inhibition of brain plaque formation in Alzheimer’s disease

Zhang, K. A., & Li, Y. (2015) · Proceedings of SPIE, the International Society for Optical Engineering/Proceedings of SPIE · doi:10.1117/12.2186236

Effects of Congo Red on Aβ1−40 Fibril Formation Process and Morphology

Bose, P. P., Chatterjee, U., Xie, L., Johansson, J., Göthelid, E., & Arvidsson, P. I. (2010) · ACS Chemical Neuroscience · doi:10.1021/cn900041x · Cited by 52

Insight into Amyloid Formation Using Congo Red as the Electrochemical Probe

Veloso, A. J., Chan, T., Hung, V. W. S., Lam, L., & Kerman, K. (2011) · Electroanalysis · doi:10.1002/elan.201100329 · Cited by 11

Detergent-like Interaction of Congo Red with the Amyloid β Peptide

Lendel, C., Bolognesi, B., Wahlström, A., Dobson, C. M., & Gräslund, A. (2010) · Biochemistry · doi:10.1021/bi902005t · Cited by 75