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

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

Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status

Groenning, M. (2009) · Journal of Chemical Biology · doi:10.1007/s12154-009-0027-5 · Cited by 655

The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

Hudson, S. A., Ecroyd, H. W., Kee, T. W., & Carver, J. A. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07307.x · Cited by 614

Protein misfolding, congophilia, oligomerization, and defective amyloid processing in preeclampsia

Buhimschi, I. A., Nayeri, U. A., Zhao, G., Shook, L. L., Pensalfini, A., Funai, E. F., Bernstein, I. M., Glabe, C. G., & Buhimschi, C. S. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3008808 · Cited by 476

Binding Characteristics of Radiofluorinated 6-Dialkylamino-2-Naphthylethylidene Derivatives as Positron Emission Tomography Imaging Probes for β-Amyloid Plaques in Alzheimer's Disease

Agdeppa, E. D., Kepe, V., Liu, J., Flores-Torres, S., Satyamurthy, N., Petrič, A., Cole, G. M., Small, G. W., Huang, S., & Barrio, J. R. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-24-j0004.2001 · Cited by 421

Imaging Aβ Plaques in Living Transgenic Mice with Multiphoton Microscopy and Methoxy-X04, a Systemically Administered Congo Red Derivative

Klunk, W. E., Bacskai, B. J., Mathis, C. A., Kajdasz, S. T., McLellan, M. E., Frosch, M. P., Debnath, M. L., Holt, D. P., Wang, Y., & Hyman, B. T. (2002) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/61.9.797 · Cited by 412

Structure of an Intermediate State in Protein Folding and Aggregation

Neudecker, P., Robustelli, P., Cavalli, A., Walsh, P., Lundström, P., Zarrine‐Afsar, A., Sharpe, S. J., Vendruscolo, M., & Kay, L. E. (2012) · Science · doi:10.1126/science.1214203 · Cited by 397

[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

Insight Into the Kinetic of Amyloid β (1–42) Peptide Self‐Aggregation: Elucidation of Inhibitors’ Mechanism of Action

Bartolini, M., Bertucci, C., Bolognesi, M. L., Cavalli, A., Melchiorre, C., & Andrisano, V. (2007) · ChemBioChem · doi:10.1002/cbic.200700427 · Cited by 355

Curcumin Modulates α-Synuclein Aggregation and Toxicity

Singh, P. K., Kotia, V., Ghosh, D., Mohite, G. M., Kumar, A., & Maji, S. K. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn3001203 · Cited by 308

X-34, A Fluorescent Derivative of Congo Red: A Novel Histochemical Stain for Alzheimer's Disease Pathology

Styren, S. D., Hamilton, R. L., Styren, G. C., & Klunk, W. E. (2000) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540004800906 · Cited by 279

Studies on the in Vitro Assembly of Aβ 1–40: Implications for the Search for Aβ Fibril Formation Inhibitors

Goldsbury, C. S., Wirtz, S., Müller, S. A., Sunderji, S., Wicki, P., Aebi, U., & Frey, P. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4259 · Cited by 279

Structure and Aggregation Mechanisms in Amyloids

Almeida, Z. L., & Brito, R. M. M. (2020) · Molecules · doi:10.3390/molecules25051195 · Cited by 258

Aβ40-Lactam(D23/K28) Models a Conformation Highly Favorable for Nucleation of Amyloid

Sciarretta, K. L., Gordon, D. J., Petkova, A. T., Tycko, R., & Meredith, S. C. (2005) · Biochemistry · doi:10.1021/bi0474867 · Cited by 245

Inhibition of Fibrillization and Accumulation of Prefibrillar Oligomers in Mixtures of Human and Mouse α-Synuclein

Rochet, J., Conway, K. A., & Lansbury, P. T. (2000) · Biochemistry · doi:10.1021/bi001315u · Cited by 221

Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution

Goda, S., Takano, K., Yutani, K., Yamagata, Y., Nagata, R., Akutsu, H., Maki, S., & Namba, K. (2000) · Protein Science · doi:10.1110/ps.9.2.369 · Cited by 218

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

Pignataro, M. F., Herrera, M. G., & Dodero, V. I. (2020) · Molecules · doi:10.3390/molecules25204854 · Cited by 224

Radioiodinated Styrylbenzenes and Thioflavins as Probes for Amyloid Aggregates

Zhuang, Z.-P., KUNG, M. ‐., Hou, C., Skovronsky, D., Gur, T., Plößl, K., Trojanowski, J. Q., Lee, V. M.-Y., & Kung, H. F. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010045q · Cited by 196

Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly

Otzen, D. E., Kristensen, O., & Oliveberg, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160086297 · Cited by 177

Development of Positron Emission Tomography β-Amyloid Plaque Imaging Agents

Mathis, C. A., Mason, N. S., Lopresti, B. J., & Klunk, W. E. (2012) · Seminars in Nuclear Medicine · doi:10.1053/j.semnuclmed.2012.07.001 · Cited by 181

Alzheimer's disease cybrids replicate beta-amyloid abnormalities through cell death pathways.

Khan, S. M., Cassarino, D. S., Abramova, N. N., Keeney, P. M., Borland, M. K., Pa, T., Krebs, C. T., Bennett, J. C., Parks, J. K., Swerdlow, R. H., et al. (2000) · PubMed · Cited by 176

Dual Binding Modes of Congo Red to Amyloid Protofibril Surface Observed in Molecular Dynamics Simulations

Wu, C. F., Wang, Z., Lei, H., Zhang, W., & Duan, Y. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0662772 · Cited by 177

In vitro detection of (S)-naproxen and ibuprofen binding to plaques in the Alzheimer’s brain using the positron emission tomography molecular imaging probe 2-(1-{6-[(2-[18F]fluoroethyl)(methyl)amino]-2-naphthyl}ethylidene)malononitrile

Agdeppa, E. D., Kepe, V., Petri, A., Satyamurthy, N., Liu, J., Huang, S. C., Small, G. W., Cole, G. M., & Barrio, J. R. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00907-7 · Cited by 172

Selection of D ‐Amino‐Acid Peptides That Bind to Alzheimer's Disease Amyloid Peptide Aβ 1–42 by Mirror Image Phage Display

Wiesehan, K., Buder, K., LINKE, R. P., Patt, S., Stoldt, M., Unger, E., Schmitt, B., Bucci, E. M., & Willbold, D. (2003) · ChemBioChem · doi:10.1002/cbic.200300631 · Cited by 171

Melatonin alleviates behavioral deficits associated with apoptosis and cholinergic system dysfunction in the APP 695 transgenic mouse model of Alzheimer's disease

Zheng, F., Chang, Y. S., Cheng, Y., Zhang, B. W., Qu, Z., Qin, C., & Zhang, J. (2004) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2004.00144.x · Cited by 169

Binding of Congo Red to Amyloid Protofibrils of the Alzheimer Aβ9–40 Peptide Probed by Molecular Dynamics Simulations

Wu, C. F., Scott, J., & Shea, J. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.07.008 · Cited by 168

Beta transition and stress-induced phase separation in the spinning of spider dragline silk

Knight, D. P., Knight, M. M., & Vollrath, F. W. (2000) · International Journal of Biological Macromolecules · doi:10.1016/s0141-8130(00)00124-0 · Cited by 150

Dye-Binding Assays for Evaluation of the Effects of Small Molecule Inhibitors on Amyloid (Aβ) Self-Assembly

Jameson, L. P., Smith, N. W., & Dzyuba, S. V. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300076x · Cited by 150

Functional amyloid formation by Streptococcus mutans

Oli, M. W., Otoo, H. N., Crowley, P. J., Heim, K. P., Nascimento, M. M., Ramsook, C. B., Lipke, P. N., & Brady, L. J. (2012) · Microbiology · doi:10.1099/mic.0.060855-0 · Cited by 144

Acceleration of Amyloid β-Peptide Aggregation by Physiological Concentrations of Calcium

Isaacs, A. M., Senn, D. B., Yuan, M., Shine, J. P., & Yankner, B. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602061200 · Cited by 149

The Binding of Thioflavin T and Its Neutral Analog BTA-1 to Protofibrils of the Alzheimer’s Disease Aβ16–22 Peptide Probed by Molecular Dynamics Simulations

Wu, C. F., Wang, Z., Lei, H., Duan, Y., Bowers, M. T., & Shea, J. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.09.062 · Cited by 141

A comparison of amyloid fibrillogenesis using the novel fluorescent compound K114

Crystal, A., Giasson, B. I., Crowe, A., Kung, M., Zhuang, Z., Trojanowski, J. Q., & Lee, V. M. ‐. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01949.x · Cited by 138

Site-Specific Blockade of RAGE-VdPrevents Amyloid-β Oligomer Neurotoxicity

Sturchler, E., Galichet, A., Weibel, M., Leclerc, E., & Heizmann, C. W. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4878-07.2008 · Cited by 136

Assessing the potential of whey protein fibril as emulsifier

Mantovani, R. A., Furtado, G. D. F., Netto, F. M., & Cunha, R. L. (2017) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2017.12.006 · Cited by 132

Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody

Utsunomiya-Tate, N., Kubo, K.-I., Tate, S.-I., Kainosho, M., Katayama, E., Nakajima, K., & Mikoshiba, K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160272497 · Cited by 131

Repeated Rapid Shear-Responsiveness of Peptide Hydrogels with Tunable Shear Modulus

Ramachandran, S., Tseng, Y., & Yu, Y. B. (2005) · Biomacromolecules · doi:10.1021/bm049284w · Cited by 128

Human Apolipoprotein C-II Forms Twisted Amyloid Ribbons and Closed Loops

Hatters, D. M., MacPhee, C. E., Lawrence, L. J., Sawyer, W. H., & Howlett, G. J. (2000) · Biochemistry · doi:10.1021/bi000002w · Cited by 124

A Systematic Study of the Effect of Physiological Factors on β2-Microglobulin Amyloid Formation at Neutral pH

Myers, S. L., Jones, S., Jahn, T. R., Morten, I. J., Tennent, G. A., Hewitt, E. W., & Radford, S. E. (2006) · Biochemistry · doi:10.1021/bi052434i · Cited by 124

Peptides for Therapy and Diagnosis of Alzheimer's Disease

Funke, S. A., & Willbold, D. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799277752 · Cited by 120

Modulation of S6 Fibrillation by Unfolding Rates and Gatekeeper Residues

Pedersen, J. S., Christensen, G., & Otzen, D. E. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.06.020 · Cited by 118

Oral Treatment with the d -Enantiomeric Peptide D3 Improves the Pathology and Behavior of Alzheimer’s Disease Transgenic Mice

Funke, S. A., van Groen, T., Kadish, I., Bartnik, D., Nagel‐Steger, L., Brener, O., Sehl, T., Batra, R., Moriscot, C., Schoehn, G., et al. (2010) · ACS Chemical Neuroscience · doi:10.1021/cn100057j · Cited by 114

2-dialkylamino-6-acylmalononitrile substituted naphthalenes (DDNP analogs): novel diagnostic and therapeutic tools in Alzheimer's disease

Agdeppa, E. D. (2003) · Molecular Imaging and Biology · doi:10.1016/j.mibio.2003.09.010 · Cited by 113

β‐Amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH

Klug, G. M., Lošić, D., Supundi, Subasinghe, S., Aguilar, M., Martin, L. L., & Small, D. H. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03815.x · Cited by 109

Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils

Hatters, D. M., Zhong, N., Rutenber, E., & Weisgraber, K. H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.080 · Cited by 105

Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Aβ fibril formation pathway

Lee, S., Fernández, E., & Good, T. A. (2007) · Protein Science · doi:10.1110/ps.062514807 · Cited by 104

On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2

Sabaté, R., Lascu, I., & Saupe, S. J. (2008) · Journal of Structural Biology · doi:10.1016/j.jsb.2008.02.002 · Cited by 103

Cholesterol is necessary both for the toxic effect of Aβ peptides on vascular smooth muscle cells and for Aβ binding to vascular smooth muscle cell membranes

Subasinghe, S., Unabia, S. E., Barrow, C. J., Mok, S. S., Aguilar, M., & Small, D. H. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01552.x · Cited by 104

Small surfactant-like peptides can drive soluble proteins into active aggregates

Zhou, B., Xing, L., Wu, W., Zhang, X., & Lin, Z. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-10 · Cited by 101

α-to-β Structural Transformation of Ovalbumin: Heat and pH Effects

Hu, H. Y., & Du, H. (2000) · Journal of Protein Chemistry · doi:10.1023/a:1007099502179 · Cited by 96

Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction

Peruško, M., Al-Hanish, A., Veličković, T. Ć., & Stanić-Vučinić, D. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.01.042 · Cited by 91

Small Molecule Microarrays Enable the Discovery of Compounds That Bind the Alzheimer’s Aβ Peptide and Reduce its Cytotoxicity

Chen, J., Armstrong, A. H., Koehler, A. N., & Hecht, M. H. (2010) · Journal of the American Chemical Society · doi:10.1021/ja107552s · Cited by 89

PEGylated phospholipid nanomicelles interact with β-amyloid(1–42) and mitigate its β-sheet formation, aggregation and neurotoxicity in vitro

Pai, A., Rubinstein, I., & Önyüksel, H. (2006) · Peptides · doi:10.1016/j.peptides.2006.04.022 · Cited by 83

Promotion of Amyloid β Protein Misfolding and Fibrillogenesis by a Lipid Oxidation Product

Liu, L., Komatsu, H., Murray, I. V. J., & Axelsen, P. H. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.057 · Cited by 81

Poly‐(L‐alanine) expansions form core β‐sheets that nucleate amyloid assembly

Shinchuk, L. M., Sharma, D., Blondelle, S., Reixach, N., Inouye, H., & Kirschner, D. A. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20536 · Cited by 76

PrP(106-126) Does Not Interact with Membranes under Physiological Conditions

Henriques, S. T., Pattenden, L. K., Aguilar, M., & Castanho, M. A. R. B. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.131458 · Cited by 78

Synthesis and Characterization of68Ga-Labeled Curcumin and Curcuminoid Complexes as Potential Radiotracers for Imaging of Cancer and Alzheimer’s Disease

Asti, M., Ferrari, É., Croci, S., Atti, G., Rubagotti, S., Iori, M., Capponi, P. C., Zerbini, A., Saladini, M., & Versari, A. (2014) · Inorganic Chemistry · doi:10.1021/ic403113z · Cited by 78

Effects of the sequence and size of non-polar residues on self-assembly of amphiphilic peptides.

Wang, K., Keasling, J., & Muller, S. (2005) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2005.06.006 · Cited by 63

Aggregation of Congo red with surfactants and Ag-nanoparticles in an aqueous solution

Al-Thabaiti, S. A., Aazam, E. S., Khan, Z. A., & Bashir, O. (2015) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2015.11.015 · Cited by 73

On the Binding of Congo Red to Amyloid Fibrils

Espargaró, A., Llabrés, S., Saupe, S. J., Curutchet, C., Luque, F. J., & Sabaté, R. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.201916630 · Cited by 73

Shear Pulses Nucleate Fibril Aggregation

Akkermans, C., Venema, P., Rogers, S. S., van der Goot, A. J., Boom, R. M., & van der Linden, E. (2006) · Food Biophysics · doi:10.1007/s11483-006-9012-5 · Cited by 76

Inhibition of amyloid fibril formation of lysozyme by ascorbic acid and a probable mechanism of action

Patel, P. N., Parmar, K., Patel, D., Kumar, S., Trivedi, M., & Das, M. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.03.152 · Cited by 71

Hsp20, a novel α‐crystallin, prevents Aβ fibril formation and toxicity

Lee, S., Carson, K. H., Rice‐Ficht, A. C., & Good, T. A. (2005) · Protein Science · doi:10.1110/ps.041020705 · Cited by 72

Fabrication of Nanofibers with Uniform Morphology by Self‐Assembly of Designed Peptides

Matsumura, S., Uemura, S., & Mihara, H. (2004) · Chemistry - A European Journal · doi:10.1002/chem.200305735 · Cited by 73

In vitro model of neurotoxicity of A? 1?42 and neuroprotection by a pentapeptide: irreversible events during the first hour

Datki, Z., Papp, R., Zádori, D., Soós, K., Fülöp, L., Juhász, A., Laskay, G., Hetényi, C., MIHALIK, E., & Zarándi, M. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.08.007 · Cited by 72

Role of the single disulphide bond of β2‐microglobulin in amyloidosis in vitro

Smith, D. P., & Radford, S. E. (2001) · Protein Science · doi:10.1110/ps.4901 · Cited by 73

Modulation of Fluorescence through Coassembly of Molecules in Organic Nanostructures

Behanna, H. A., Rajangam, K. L., & Stupp, S. I. (2006) · Journal of the American Chemical Society · doi:10.1021/ja062415b · Cited by 72

Novel Molecular Hybrids of N-Benzylpiperidine and 1,3,4-Oxadiazole as Multitargeted Therapeutics to Treat Alzheimer’s Disease

Sharma, P. A., Tripathi, A., Tripathi, P. N., Singh, S. S., Singh, S. P., & Shrivastava, S. K. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00430 · Cited by 75

Human neutrophil alpha‐defensins induce formation of fibrinogen and thrombospondin‐1 amyloid‐like structures and activate platelets via glycoprotein IIb/IIIa

HORN, M., Bertling, A., Brodde, M. F., Müller, A., Roth, J., Aken, H. V., Jurk, K., Heilmann, C., Peters, G., & Kehrel, B. E. (2012) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2012.04640.x · Cited by 69

Olive Biophenols Reduces Alzheimer’s Pathology in SH-SY5Y Cells and APPswe Mice

Omar, S. H., Scott, C., Hamlin, A. S., & Obied, H. K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010125 · Cited by 71

Solution conformation and amyloid-like fibril formation of a polar peptide derived from a β-hairpin in the OspA single-layer β-sheet

Ohnishi, S., Koide, A., & Koide, S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3980 · Cited by 68

Enhancement of thermal stability and inhibition of protein aggregation by osmolytic effect of hydroxyproline

Kar, K., & Kishore, N. (2007) · Biopolymers · doi:10.1002/bip.20834 · Cited by 67

Bovine serum albumin observed by infrared spectrometry. I. Methodology, structural investigation, and water uptake

Grdadolnik, J., & Mar�chal, Y. (2000) · Biopolymers · doi:10.1002/1097-0282(2001)62:1 · Cited by 172

Prediction of Nucleating Sequences from Amyloidogenic Propensities of Tau-Related Peptides

Quijano, F. A. R., Morrow, D., Wise, B. M., Brancia, F. L., & Goux, W. J. (2006) · Biochemistry · doi:10.1021/bi052226q · Cited by 70

Temperature dependence of the nucleation constant rate in β amyloid fibrillogenesis

Sabaté, R., Gallardo, M., & Estelrich, J. (2005) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2004.11.001 · Cited by 65

Construction of a chemically and conformationally self-replicating system of amyloid-like fibrils

Takahashi, Y., & Mihara, H. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2003.11.022 · Cited by 65

Protective Effects of Ginger Extract against Glycation and Oxidative Stress-Induced Health Complications: An In Vitro Study

Anwar, S., Almatroudi, A., Allemailem, K. S., Joseph, R. J., Khan, A. A., & Rahmani, A. H. (2020) · Processes · doi:10.3390/pr8040468 · Cited by 62

Early Steps in Oxidation-Induced SOD1 Misfolding: Implications for Non-Amyloid Protein Aggregation in Familial ALS

Mulligan, V. K., Kerman, A., Laister, R. C., Sharda, P. R., Arslan, P. E., & Chakrabartty, A. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.04.016 · Cited by 60

Structural Differences between Aβ(1-40) Intermediate Oligomers and Fibrils Elucidated by Proteolytic Fragmentation and Hydrogen/Deuterium Exchange

Zhang, A., Qi, W., Good, T. A., & Fernández, E. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.10.022 · Cited by 60

Self-Assembly of a Designed Protein Polymer into β-Sheet Fibrils and Responsive Gels

Goeden-Wood, N. L., Keasling, J. D., & Muller, S. J. (2003) · Macromolecules · doi:10.1021/ma025952z · Cited by 60

Ile‐Lys‐Val‐Ala‐Val (IKVAV)‐containing laminin α1 chain peptides form amyloid‐like fibrils

YAMADA, M., Kadoya, Y., Kasai, S., Kato, K., Mochizuki, M., Nishi, N., Watanabe, N., Kleinman, H. K., Yamada, Y., & Nomizu, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03393-8 · Cited by 59

Search for dual function inhibitors for Alzheimer’s disease: Synthesis and biological activity of acetylcholinesterase inhibitors of pyridinium-type and their Aβ fibril formation inhibition capacity

Kapková, P., Alptüzün, V., Frey, P., Erciyas, E., & Holzgrabe, U. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.08.034 · Cited by 54

Self-assembling peptides: Structure, function, in silico prediction and applications

Vahedifar, A., & Wu, J. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.11.020 · Cited by 53

Specific glycosaminoglycans promote unseeded amyloid formation from β2-microglobulin under physiological conditions

Borysik, A. J., Morten, I. J., Radford, S. E., & Hewitt, E. W. (2007) · Kidney International · doi:10.1038/sj.ki.5002270 · Cited by 53

Synthesis of superparamagnetic iron oxide nanoparticles coated with a DDNP-carboxyl derivative for in vitro magnetic resonance imaging of Alzheimer's disease

Zhou, J., Fa, H., Yin, W. H., Zhang, J., Hou, C., Huo, D., Zhang, D., & Zhang, H. (2014) · Materials Science and Engineering C · doi:10.1016/j.msec.2014.01.005 · Cited by 53

Curcumin-glucoside, A Novel Synthetic Derivative of Curcumin, Inhibits α-Synuclein Oligomer Formation: Relevance to Parkinson's Disease

Gadad, B. S., Subramanya, P. K., Srinivas, P., Shantharam, I. S., & Rao, K. S. J. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212798919093 · Cited by 54

Two Disaccharides and Trimethylamine N-Oxide Affect Aβ Aggregation Differently, but All Attenuate Oligomer-Induced Membrane Permeability

Qi, W., Zhang, A., Good, T. A., & Fernández, E. (2009) · Biochemistry · doi:10.1021/bi9006397 · Cited by 52

Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation.

Espargaró, A., Sabaté, R., & Ventura, S. (2012) · Molecular Biosystems · doi:10.1039/c2mb25214g · Cited by 56

Biosynthesis of silver nanoparticles using Tamarix articulata leaf extract: an effective approach for attenuation of oxidative stress mediated diseases

Anwar, S., Almatroodi, S. A., Almatroudi, A., Allemailem, K. S., Joseph, R. J., Khan, A. A., Alrumaihi, F., Alsahli, M. A., & Rahmani, A. H. (2021) · International Journal of Food Properties · doi:10.1080/10942912.2021.1914083 · Cited by 50

In vivo amyloid imaging in Alzheimer?s disease

Sair, H. I., Doraiswamy, P. M., & Petrella, J. R. (2004) · Neuroradiology · doi:10.1007/s00234-003-1034-9 · Cited by 50

Urinary congophilia in women with hypertensive disorders of pregnancy and preexisting proteinuria or hypertension

McCarthy, F. P., Adetoba, A., Gill, C. A., Bramham, K., Bertolaccini, M. L., Burton, G. J., Girardi, G., Seed, P. T., Poston, L., & Chappell, L. C. (2016) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2016.04.041 · Cited by 49

Cu II Binding to Various Forms of Amyloid‐β Peptides: Are They Friends or Foes?

Borghesani, V., Aliès, B., & Hureau, C. (2017) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201700776 · Cited by 50

Thermoresponsive BSA hydrogels with phase tunability

Khanna, S., Singh, A. K., Behera, S. P., & Gupta, S. (2020) · Materials Science and Engineering C · doi:10.1016/j.msec.2020.111590 · Cited by 51

Inhibition of Alzheimer's amyloid-beta aggregation in-vitro by carbenoxolone: Insight into mechanism of action

Sharma, S., Nehru, B., & Saini, A. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.06.011 · Cited by 48

β-Amyloid-derived pentapeptide RIIGLa inhibits Aβ1–42 aggregation and toxicity

Fülöp, L., Zarándi, M., Datki, Z., Soós, K., & Penke, B. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.09.024 · Cited by 47

Aβ Fibrillogenesis: Kinetic Parameters for Fibril Formation from Congo Red Binding

Inouye, H., & Kirschner, D. A. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4258 · Cited by 47

Chemical Probes for Visualizing Intact Animal and Human Brain Tissue

Lai, H. M., Ng, W., Gentleman, S., & Wu, W. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.05.015 · Cited by 48

[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