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

Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays

Mosmann, T. (1983) · Journal of Immunological Methods · doi:10.1016/0022-1759(83)90303-4 · Cited by 56,104 · see citing works

Alzheimer's Disease Is a Synaptic Failure

Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420 · see citing works

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works

Diffusible, nonfibrillar ligands derived from Aβ _1–42 are potent central nervous system neurotoxins

Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506 · see citing works

Phase I clinical trial of curcumin, a chemopreventive agent, in patients with high-risk or pre-malignant lesions.

Cheng, A., Hsu, C., Lin, J., Hsu, M. M., Ho, Y., Shen, T. S., Ko, J. Y., Lin, J.-T., Lin, B., Ming-Shiang, W., et al. (2001) · PubMed · Cited by 2,071 · see citing works

Molecular mechanisms underlying chemopreventive activities of anti-inflammatory phytochemicals: down-regulation of COX-2 and iNOS through suppression of NF-κB activation

Surh, Y., Chun, K., Cha, H.-H., Han, S. S., Keum, Y., Park, K.-K., & Lee, S. S. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00183-x · Cited by 1,620 · see citing works

The Curry Spice Curcumin Reduces Oxidative Damage and Amyloid Pathology in an Alzheimer Transgenic Mouse

Lim, G. P., Chu, T., Yang, F., Beech, W., Frautschy, S. A., & Cole, G. M. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-21-08370.2001 · Cited by 1,530 · see citing works

Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447 · see citing works

A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity

Weggen, S., Eriksen, J. L., Das, P., Sagi, S. A., Wang, R., Pietrzik, C. U., Findlay, K. A., Smith, T. E., Murphy, M. P., Bulter, T., et al. (2001) · Nature · doi:10.1038/35102591 · Cited by 1,388 · see citing works

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 · see citing works

Curcumin has potent anti‐amyloidogenic effects for Alzheimer's β‐amyloid fibrils in vitro

Ono, K., Hasegawa, K., Naiki, H., & Yamada, M. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20025 · Cited by 1,254 · see citing works

Nonsteroidal Antiinflammatory Drugs and the Risk of Alzheimer's Disease

in 't Veld, B. A., Ruitenberg, A., Hofman, A., Launer, L. J., van Duijn, C. M., Stijnen, T., Breteler, M. M. B., & Stricker, B. H. C. (2001) · New England Journal of Medicine · doi:10.1056/nejmoa010178 · Cited by 1,196 · see citing works

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 1,136 · see citing works

Safety and Anti-Inflammatory Activity of Curcumin: A Component of Tumeric ( <i>Curcuma longa</i> )

Chainani-Wu, N. (2003) · The Journal of Alternative and Complementary Medicine · doi:10.1089/107555303321223035 · Cited by 1,106 · see citing works

Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss

Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061 · see citing works

Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease

Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · see citing works

Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?

Klein, W. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01749-5 · Cited by 989 · see citing works

Metal-Protein Attenuation With Iodochlorhydroxyquin (Clioquinol) Targeting Aβ Amyloid Deposition and Toxicity in Alzheimer Disease: A Pilot Phase 2 Clinical Trial

Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988 · see citing works

Biotransformation of Curcumin Through Reduction and Glucuronidation in Mice

Pan, M., Huang, T., & Lin, J. (1999) · Drug Metabolism and Disposition · doi:10.1016/s0090-9556(24)15211-7 · Cited by 950 · see citing works

Ibuprofen Suppresses Plaque Pathology and Inflammation in a Mouse Model for Alzheimer's Disease

Lim, G. P., Yang, F., Chu, T., Chen, P., Beech, W. K., Teter, B., Tran, T., Ubeda, O. J., Ashe, K. H., Frautschy, S. A., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-15-05709.2000 · Cited by 876 · see citing works

Alzheimer's Disease--Genotypes, Phenotype, and Treatments

Selkoe, D. J. (1997) · Science · doi:10.1126/science.275.5300.630 · Cited by 871 · see citing works

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 829 · see citing works

Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model

Calon, F., Lim, G. P., Yang, F., Morihara, T., Teter, B., Ubeda, O., Rostaing, P., Triller, A., Salem, N., Ashe, K. H., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.08.013 · Cited by 707 · see citing works

Structure‐Activity Analyses of β‐Amyloid Peptides: Contributions of the β25–35 Region to Aggregation and Neurotoxicity

Pike, C. J., Walencewicz‐Wasserman, A. J., Kosmoski, J., Cribbs, D. H., Glabe, C. G., & Cotman, C. W. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64010253.x · Cited by 699 · see citing works

Characterization of Copper Interactions with Alzheimer Amyloid β Peptides: Identification of an Attomolar‐Affinity Copper Binding Site on Amyloid β1‐42

Atwood, C. S., Scarpa, R. C., Huang, X., Moir, R. D., Jones, W. D., Fairlie, D. P., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751219.x · Cited by 641 · see citing works

Inhibition of cyclo-oxygenase 2 expression in colon cells by the chemopreventive agent curcumin involves inhibition of NF-κB activation via the NIK/IKK signalling complex

Plummer, S. M., Holloway, K., Manson, M. M., Munks, R. J. L., Kaptein, A., Farrow, S. N., & Howells, L. M. (1999) · Oncogene · doi:10.1038/sj.onc.1202980 · Cited by 627 · see citing works

Self-Assembly of Aβ ₁ _- ₄₂ into Globular Neurotoxins

Chromy, B. A., Nowak, R. J., Lambert, M. P., Viola, K. L., Chang, L., Velasco, P. T., Jones, B. W., Fernandez, S. J., Lacor, P. N., Horowitz, P., et al. (2003) · Biochemistry · doi:10.1021/bi030029q · Cited by 522 · see citing works

Alzheimer's disease

Cummings, J. L., Vinters, H. V., Cole, G. M., & Khachaturian, Z. S. (1998) · Neurology · doi:10.1212/wnl.51.1_suppl_1.s2 · Cited by 515 · see citing works

Phenolic anti-inflammatory antioxidant reversal of Aβ-induced cognitive deficits and neuropathology

Frautschy, S. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00300-1 · Cited by 514 · see citing works

Effect of non-steroidal anti-inflammatory drugs on risk of Alzheimer's disease: systematic review and meta-analysis of observational studies

Etminan, M., Gill, S., & Samii, A. (2003) · BMJ · doi:10.1136/bmj.327.7407.128 · Cited by 511 · see citing works

Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer’s disease animal models

Baum, L., & Ng, A. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6403 · Cited by 483 · see citing works

Curcuminoids as Potent Inhibitors of Lipid Peroxidation

Sreejayan, & Rao, M. (1994) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.1994.tb03258.x · Cited by 461 · see citing works

In Vivo Inhibition of Nitric Oxide Synthase Gene Expression by Curcumin, a Cancer Preventive Natural Product with Anti-Inflammatory Properties

Chan, M. M.-Y., Huang, H., Fenton, M. R., & Fong, D. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00114-2 · Cited by 398 · see citing works

Direct evidence of oxidative injury produced by the Alzheimer's β-Amyloid peptide (1–40) in cultured hippocampal neurons

Harris‐White, M. E., Hensley, K., Butterfield, D. A., Leedle, R. A., & Carney, J. M. (1995) · Experimental Neurology · doi:10.1016/0014-4886(95)90041-1 · Cited by 331 · see citing works

Scavenging effect of extracts of green tea and natural antioxidants on active oxygen radicals

Zhao, B., Li, X., He, R., Cheng, S., & Wenjuan, X. (1989) · Cell Biophysics · doi:10.1007/bf02797132 · Cited by 322 · see citing works

Reduced incidence of AD with NSAID but not H2receptor antagonists

Zandi, P. P., Anthony, J. C., Hayden, K. M., Mehta, K. M., Mayer, L. S., & Breitner, J. C. S. (2002) · Neurology · doi:10.1212/wnl.59.6.880 · Cited by 314 · see citing works

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

Klunk, W. E., Jacob, R. F., & Mason, R. P. (1999) · Analytical Biochemistry · doi:10.1006/abio.1998.2933 · Cited by 310 · see citing works

Neuroprotective effects of resveratrol against β‐amyloid‐induced neurotoxicity in rat hippocampal neurons: involvement of protein kinase C

Han, Y.-S., Zheng, W., Bastianetto, S., Chabot, J., & Quirion, R. (2004) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705688 · Cited by 300 · see citing works

Curcumin inhibits phorbol ester-induced expression of cyclooxygenase-2 in mouse skin through suppression of extracellular signal-regulated kinase activity and NF- B activation

Chun, K. (2003) · Carcinogenesis · doi:10.1093/carcin/bgg107 · Cited by 297 · see citing works

Antibody to caspase-cleaved actin detects apoptosis in differentiated neuroblastoma and plaque-associated neurons and microglia in Alzheimer's disease.

Yang, F., Sun, X., Beech, W. K., Teter, B., Wu, S. S. H., Sigel, J. J., Vinters, H. V., Frautschy, S. A., & Cole, G. M. (1998) · Europe PMC (PubMed Central) · Cited by 245 · see citing works

Reduced prevalence of AD in users of NSAIDs and H2 receptor antagonists

Anthony, J. C., Breitner, J., Zandi, P., Meyer, M., Jurasová, I., Norton, M., & Stone, S. (2000) · Neurology · doi:10.1212/wnl.54.11.2066 · Cited by 222 · see citing works

Oligomerization of Endogenous and Synthetic Amyloid β-Protein at Nanomolar Levels in Cell Culture and Stabilization of Monomer by Congo Red

Podlisny, M. B., Walsh, D. M., Amarante, P., Ostaszewski, B. L., Stimson, E. R., Maggio, J. E., Teplow, D. B., & Selkoe, D. J. (1998) · Biochemistry · doi:10.1021/bi972029u · Cited by 181 · see citing works

Inhibition of fibril formation in beta-amyloid peptide by a novel series of benzofurans.

Howlett, D. R., Perry, A. E., GODFREY, F., et al. (1999) · PubMed · Cited by 180 · see citing works

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 · see citing works

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 · see citing works

Residues 17–20 and 30–35 of beta‐amyloid play critical roles in aggregation

Liu, R., McAllister, C., Lyubchenko, Y. L., & Sierks, M. R. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10859 · Cited by 165 · see citing works

Reduced effectiveness of Aβ1-42 immunization in APP transgenic mice with significant amyloid deposition

Das, P., Murphy, M. P., Younkin, L. H., Younkin, S. G., & Golde, T. E. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00245-7 · Cited by 150 · see citing works

NSAIDs and incident Alzheimer’s disease. The Rotterdam study

In ’t Veld, B. A., Launer, L. J., Hoes, A. W., Ott, A., Hofman, A., Breteler, M. M. B., & Stricker, B. H. C. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00096-7 · Cited by 145 · see citing works

Aspirin and non-steroidal anti-inflammatory drugs inhibit amyloid-β aggregation

Thomas, T., Nadackal, T. G., & Thomas, K. (2001) · Neuroreport · doi:10.1097/00001756-200110290-00024 · Cited by 127 · see citing works

Intrastriatal Dopamine Injection Induces Apoptosis Through Oxidation-Involved Activation of Transcription Factors AP-1 and NF-κB in Rats

Luo, Y., Hattori, A., Munoz, J. R., Qin, Z.-H., & Roth, G. S. (1999) · Molecular Pharmacology · doi:10.1124/mol.56.2.254 · Cited by 120 · see citing works

Inhibition of fibril formation in β-amyloid peptide by a novel series of benzofurans

Howlett, D. R., PERRY, A. E., GODFREY, F., et al. (1999) · Biochemical Journal · doi:10.1042/bj3400283 · Cited by 112 · see citing works

Effect of Different Anti-Aβ Antibodies on Aβ Fibrillogenesis as Assessed by Atomic Force Microscopy

Legleiter, J. A., Czilli, D. L., Gitter, B. D., Demattos, R. B., Holtzman, D. M., & Kowalewski, T. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.019 · Cited by 104 · see citing works

Protective effects of BDNF and NT-3 but not PDGF against hypoglycemic injury to cultured striatal neurons

Nakao, N. (1995) · Experimental Neurology · doi:10.1016/0014-4886(95)90002-0 · Cited by 99 · see citing works

Modulation of β‐amyloid metabolism by non‐steroidal anti‐inflammatory drugs in neuronal cell cultures

Gasparini, L., Rusconi, L., Xu, H., Soldato, P. D., & Ongini, E. (2003) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02154.x · Cited by 97 · see citing works

A novelβ‐sheet breaker, RS‐0406, reverses amyloidβ‐induced cytotoxicity and impairment of long‐term potentiationin vitro

Nakagami, Y., Nishimura, S., Murasugi, T., Kaneko, I., Meguro, M., Marumoto, S., Kogen, H., Koyama, K., & Oda, T. (2002) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704911 · Cited by 94 · see citing works

Cytokines and chemokines as mediators of protection and injury in the central nervous system assessed in transgenic mice.

Wang, J., Asensio, V., & Campbell, I. (2002) · Current Topics in Microbiology and Immunology · doi:10.1007/978-3-662-09525-6_2 · Cited by 77 · see citing works

The Non-cyclooxygenase Targets of Non-steroidal Anti-inflammatory Drugs, Lipoxygenases, Peroxisome Proliferator-activated Receptor, Inhibitor of κB Kinase, and NFκB, Do Not Reduce Amyloid β42 Production

Sagi, S. A., Weggen, S., Eriksen, J. L., Golde, T. E., & Koo, E. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303588200 · Cited by 76 · see citing works

Non-steroidal anti-inflammatory drug (NSAID) use and Alzheimer disease in community-dwelling elderly patients.

Landi, F., Cesari, M., Onder, G., Russo, A., Torre, S., & Bernabei, R. (2003) · The American journal of geriatric psychiatry · doi:10.1097/00019442-200303000-00008 · Cited by 55 · see citing works

Nonsteroidal anti-inflammatory drugs and Alzheimer disease: what's next?

Launer, L. (2003) · Journal of the American Medical Association (JAMA) · doi:10.1001/jama.289.21.2865 · Cited by 37 · see citing works

Congo red reverses amyloid β protein-induced cellular stress in astrocytes

Abe, K., Kato, M., & Saitō, H. (1997) · Neuroscience Research · doi:10.1016/s0168-0102(97)00081-3 · Cited by 14 · see citing works

Use of Race and Ethnicity in Biomedical Publication

Ozuah, P. O., & Stick, S. L. (2003) · JAMA · doi:10.1001/jama.290.9.1154-a · Cited by 6 · see citing works

The Essential Medicinal Chemistry of Curcumin

Nelson, K. M., Dahlin, J. L., Bisson, J., Graham, J., Pauli, G. F., & Walters, M. A. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00975 · Cited by 1,956 · see citing works

Design, functionalization strategies and biomedical applications of targeted biodegradable/biocompatible polymer-based nanocarriers for drug delivery

Nicolas, J., Mura, S., Brambilla, D., Mackiewicz, N., & Couvreur, P. (2013) · Chem. Soc. Rev. · doi:10.1039/c2cs35265f · Cited by 1,270 · see citing works

Pharmacological basis for the role of curcumin in chronic diseases: an age-old spice with modern targets

Aggarwal, B. B., & Sung, B. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.11.002 · Cited by 1,140 · see citing works

Oxidative Stress in Neurodegenerative Diseases: From Molecular Mechanisms to Clinical Applications

Liu, Z., Zhou, T., Ziegler, A. C., Dimitrion, P., & Zuo, L. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2525967 · Cited by 810 · see citing works

Microglia constitute a barrier that prevents neurotoxic protofibrillar Aβ42 hotspots around plaques

Condello, C., Yuan, P., Schain, A., & Grutzendler, J. (2015) · Nature Communications · doi:10.1038/ncomms7176 · Cited by 718 · see citing works

Identification of amyloid plaques in retinas from Alzheimer's patients and noninvasive in vivo optical imaging of retinal plaques in a mouse model

Koronyo-Hamaoui, M., Koronyo, Y., Ljubimov, A. V., Miller, C. A., Ko, M. K., Black, K. L., Schwartz, M., & Farkas, D. L. (2011) · NeuroImage · doi:10.1016/j.neuroimage.2010.06.020 · Cited by 672 · see citing works

Amyloid β oligomers in Alzheimer’s disease pathogenesis, treatment, and diagnosis

Viola, K. L., & Klein, W. L. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1386-3 · Cited by 628 · see citing works

Alzheimer's Disease: From Pathology to Therapeutic Approaches

Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802808 · Cited by 626 · see citing works

The redox chemistry of the Alzheimer's disease amyloid β peptide

Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608 · see citing works

Curcumin Structure-Function, Bioavailability, and Efficacy in Models of Neuroinflammation and Alzheimer’s Disease

Begum, A. N., Jones, M. R., Lim, G. P., Morihara, T., Kim, P., Heath, D. D., Rock, C. L., Pruitt, M. A., Yang, F., Hudspeth, B., et al. (2008) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.108.137455 · Cited by 604 · see citing works

The effect of curcumin (turmeric) on Alzheimer’s disease: An overview

Mishra, S., & Palanivelu, K. (2008) · Annals of Indian Academy of Neurology · doi:10.4103/0972-2327.40220 · Cited by 599 · see citing works

Neuroprotective effects of curcumin

Cole, G. M., Teter, B., & Frautschy, S. A. (2007) · ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY · doi:10.1007/978-0-387-46401-5_8 · Cited by 516 · see citing works

Targeting the TLR4 signaling pathway by polyphenols: A novel therapeutic strategy for neuroinflammation

Rahimifard, M., Maqbool, F., Moeini-Nodeh, S., Niaz, K., Abdollahi, M., Braidy, N., Nabavi, S. M., & Nabavi, S. F. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.02.004 · Cited by 481 · see citing works

Green tea epigallocatechin-3-gallate (EGCG) reduces β-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice

Rezai-Zadeh, K., Arendash, G. W., Hou, H., Fernandez, F., Jensen, M., Runfeldt, M., Shytle, R. D., & Tan, J. (2008) · Brain Research · doi:10.1016/j.brainres.2008.02.107 · Cited by 459 · see citing works

REVIEW: Curcumin and Alzheimer’s disease

Hamaguchi, T., Ono, K., & Yamada, M. (2010) · CNS Neuroscience &amp; Therapeutics · doi:10.1111/j.1755-5949.2010.00147.x · Cited by 450 · see citing works

Natural products as a source of Alzheimer's drug leads

Williams, P., Sorribas, A., & Howes, M.-J. R. (2011) · Nat. Prod. Rep. · doi:10.1039/c0np00027b · Cited by 404 · see citing works

Neuroprotective strategies involving ROS in Alzheimer disease

Dumont, M., & Beal, M. F. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.026 · Cited by 402 · see citing works

Abnormal mitochondrial dynamics and synaptic degeneration as early events in Alzheimer’s disease: Implications to mitochondria-targeted antioxidant therapeutics

Reddy, P. H., Tripathi, R., Troung, Q., Tirumala, K., Reddy, T. P., Anekonda, V., Shirendeb, U. P., Calkins, M. J., Reddy, A. P., Mao, P., et al. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.011 · Cited by 394 · see citing works

Matrix Metalloproteinase-9 Degrades Amyloid-β Fibrils in Vitro and Compact Plaques in Situ

Yan, P., Hu, X., Song, H., Yin, K., Bateman, R. J., Cirrito, J. R., Xiao, Q., Hsu, F. F., Turk, J. W., Xu, J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602440200 · Cited by 380 · see citing works

Investigation of the effects of solid lipid curcumin on cognition and mood in a healthy older population

Cox, K. H., Pipingas, A., & Scholey, A. B. (2015) · Journal of Psychopharmacology · doi:10.1177/0269881114552744 · Cited by 368 · see citing works

Protective Effects of Indian Spice Curcumin Against Amyloid-β in Alzheimer’s Disease

Reddy, P. H., Manczak, M., Yin, X., Grady, M. C., Mitchell, A., Tonk, S., Kuruva, C. S., Bhatti, J. S., Kandimalla, R., Vijayan, M., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170512 · Cited by 354 · see citing works

Inflammaging as a prodrome to Alzheimer's disease

Giunta, B., Fernandez, F., Nikolic, W. V., Obregon, D., Rrapo, E., Town, T., & Tan, J. (2008) · Journal of Neuroinflammation · doi:10.1186/1742-2094-5-51 · Cited by 327 · see citing works

Nanotechnology: A Promising Approach for Delivery of Neuroprotective Drugs

Naqvi, S., Panghal, A., & Flora, S. J. S. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00494 · Cited by 305 · see citing works

Inhibitory effect of curcuminoids on acetylcholinesterase activity and attenuation of scopolamine-induced amnesia may explain medicinal use of turmeric in Alzheimer’s disease

Ahmed, T., & Gilani, A.-H. (2009) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2008.09.010 · Cited by 301 · see citing works

Revenge of the “Sit”: How lifestyle impacts neuronal and cognitive health through molecular systems that interface energy metabolism with neuronal plasticity

Vaynman, S., & Gomez‐Pinilla, F. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20979 · Cited by 299 · see citing works

Optimization of curcumin nanoemulsion for intranasal delivery using design of experiment and its toxicity assessment

Sood, S., Jain, K., & Gowthamarajan, K. (2014) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2013.09.030 · Cited by 289 · see citing works

Development of tau aggregation inhibitors for alzheimer's disease

Bulic, B., Pickhardt, M., Schmidt, B., Mandelkow, E., Waldmann, H., & Mandelkow, E. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802621 · Cited by 286 · see citing works

Multifunctional Nanoliposomes with Curcumin-Lipid Derivative and Brain Targeting Functionality with Potential Applications for Alzheimer Disease

Mourtas, S., Lazar, A. N., Markoutsa, E., Duyckaerts, C., & Antimisiaris, S. G. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.04.050 · Cited by 263 · see citing works

Natural Compounds for Alzheimer’s Disease Therapy: A Systematic Review of Preclinical and Clinical Studies

Andrade, S., Ramalho, M. J., Loureiro, J. A., & Pereira, M. D. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092313 · Cited by 240 · see citing works

Amelioration of cognitive deficits and neurodegeneration by curcumin in rat model of sporadic dementia of Alzheimer’s type (SDAT)

Ishrat, T., Hoda, M. N., Khan, M. B., Yousuf, S., Ahmad, M., Khan, M. M., Ahmad, A., & Islam, F. (2009) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2009.02.002 · Cited by 230 · see citing works

Neurotherapeutic applications of nanoparticles in Alzheimer’s disease

Sahni, J. K., Doggui, S., Ali, J., Baboota, S., Dao, L., & Ramassamy, C. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2010.11.033 · Cited by 219 · see citing works

Ayurvedic medicinal plants for Alzheimer’s disease: A review

Rao, R. V., Descamps, O., John, V., & Bredesen, D. E. (2012) · Alzheimer's Research &amp; Therapy · doi:10.1186/alzrt125 · Cited by 213 · see citing works

Development of an optimized hyaluronic acid-based lipidic nanoemulsion co-encapsulating two polyphenols for nose to brain delivery

Nasr, M. (2016) · Drug Delivery · doi:10.3109/10717544.2015.1092619 · Cited by 208 · see citing works

Curcumin Protected PC12 Cells against Beta-Amyloid-Induced Toxicity through the Inhibition of Oxidative Damage and Tau Hyperphosphorylation

Park, S.-Y., Kim, H.-S., Cho, E.-K., Kwon, B.-Y., Phark, S., Hwang, K.-W., & Sul, D. (2008) · Food and Chemical Toxicology · doi:10.1016/j.fct.2008.05.030 · Cited by 209 · see citing works

Nanotechnology—novel therapeutics for CNS disorders

Srikanth, M., & Kessler, J. A. (2012) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.76 · Cited by 198 · see citing works

Formulations of Curcumin Nanoparticles for Brain Diseases

Del Prado-Audelo, M. L., Caballero-Florán, I. H., Meza-Toledo, J. A., Mendoza-Muñoz, N., González-Torres, M., Florán, B., Cortés, H., & Leyva-Gómez, G. (2019) · Biomolecules · doi:10.3390/biom9020056 · Cited by 191 · see citing works

Clinical development of curcumin in neurodegenerative disease

Hu, S., Maiti, P., Ma, Q., Zuo, X., Jones, M. R., Cole, G. M., & Frautschy, S. A. (2015) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2015.1044981 · Cited by 179 · see citing works

A novel LDL-mimic nanocarrier for the targeted delivery of curcumin into the brain to treat Alzheimer's disease

Meng, F., Asghar, S., Gao, S., Su, Z., Song, J., Huo, M., Meng, W., Ping, Q., & Xiao, Y. (2015) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2015.06.025 · Cited by 176 · see citing works

Iron dysregulation in Alzheimer's disease: Multimodal brain permeable iron chelating drugs, possessing neuroprotective-neurorescue and amyloid precursor protein-processing regulatory activities as therapeutic agents

Mandel, S., Amit, T., Bar-Am, O., & Youdim, M. B. H. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.06.001 · Cited by 164 · see citing works

Significance of NF-κB as a pivotal therapeutic target in the neurodegenerative pathologies of Alzheimer’s disease and multiple sclerosis

Srinivasan, M., & Lahiri, D. K. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2014.989834 · Cited by 164 · see citing works

Curcuminoids enhance memory in an amyloid-infused rat model of Alzheimer’s disease

Ahmed, T., Enam, S. A., & Gilani, A. H. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.05.078 · Cited by 156 · see citing works

The art of building multifunctional metal-binding agents from basic molecular scaffolds for the potential application in neurodegenerative diseases

Rodríguez-Rodríguez, C., Telpoukhovskaia, M., & Orvig, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.008 · Cited by 151 · see citing works

Effect of Curcumin-Associated and Lipid Ligand-Functionalized Nanoliposomes on Aggregation of the Alzheimer's Aβ Peptide

Taylor, M., Moore, S., Mourtas, S., Niarakis, A., Re, F., Zona, C., Ferla, B. L., Nicotra, F., Masserini, M., Antimisiaris, S. G., et al. (2011) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2011.06.015 · Cited by 149 · see citing works

Neuroprotective mechanisms of ayurvedic antidementia botanical <i>Bacopa monniera</i>

Dhanasekaran, M., Tharakan, B., Holcomb, L. A., Hitt, A. R., Young, K. A., & Manyam, B. V. (2007) · Phytotherapy Research · doi:10.1002/ptr.2195 · Cited by 148 · see citing works

Amyloid beta-induced glycogen synthase kinase 3β phosphorylated VDAC1 in Alzheimer's disease: Implications for synaptic dysfunction and neuronal damage

Reddy, P. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.06.012 · Cited by 147 · see citing works

Can herbs provide a new generation of drugs for treating Alzheimer’s disease?

Anekonda, T. S., & Reddy, P. H. (2005) · Brain Research Reviews · doi:10.1016/j.brainresrev.2005.09.001 · Cited by 140 · see citing works

Polyphenols and neuroprotection: therapeutic implications for cognitive decline

Caruso, G., Torrisi, S. A., Mogavero, M. P., Currenti, W., Castellano, S., Godos, J., Ferri, R., Galvano, F., Leggio, G. M., Grosso, G., et al. (2022) · Pharmacology &amp; Therapeutics · doi:10.1016/j.pharmthera.2021.108013 · Cited by 140 · see citing works

Alzheimer's-associated Aβ oligomers show altered structure, immunoreactivity and synaptotoxicity with low doses of oleocanthal

Pitt, J., Roth, W., Lacor, P., Smith, A. B., Blankenship, M., Velasco, P., De Felice, F., Breslin, P., & Klein, W. L. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.07.018 · Cited by 134 · see citing works

Effect of curcumin on brain insulin receptors and memory functions in STZ (ICV) induced dementia model of rat

Agrawal, R., Mishra, B., Tyagi, E., Nath, C., & Shukla, R. (2010) · Pharmacological Research · doi:10.1016/j.phrs.2009.12.008 · Cited by 133 · see citing works

Contribution of reactive oxygen species to cerebral amyloid angiopathy, vasomotor dysfunction, and microhemorrhage in aged Tg2576 mice

Han, B. H., Zhou, M.-L., Johnson, A. W., Singh, I., Liao, F., Vellimana, A. K., Nelson, J. W., Milner, E., Cirrito, J. R., Basak, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414930112 · Cited by 131 · see citing works

Alzheimer’s disease as oligomeropathy

Ono, K. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.010 · Cited by 129 · see citing works

Targeting multiple Alzheimer's disease etiologies with multimodal neuroprotective and neurorestorative iron chelators

Amit, T., Avramovich‐Tirosh, Y., Youdim, M. B. H., & Mandel, S. (2008) · The FASEB Journal · doi:10.1096/fj.07-8627rev · Cited by 126 · see citing works

Disease-Modifying Therapies for Alzheimer’s Disease: More Questions than Answers

Golde, T. E. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01201-2 · Cited by 119 · see citing works

An update on the novel and approved drugs for Alzheimer disease

Alhazmi, H. A., & Albratty, M. (2022) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2022.10.004 · Cited by 122 · see citing works

Alzheimer’s Disease, Inflammation, and the Role of Antioxidants

Sinyor, B., Mineo, J., & Ochner, C. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200171 · Cited by 120 · see citing works

Disease modifying therapy for AD?¹

Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117 · see citing works

Design, Synthesis and Evaluation of Genistein-O-Alkylbenzylamines as Potential Multifunctional Agents for the Treatment of Alzheimer's Disease

Qiang, X., Sang, Z., Yuan, W., Li, Y., Liu, Q., Bai, P., Shi, Y., Ang, W., Tan, Z., & Deng, Y. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.02.045 · Cited by 113 · see citing works

Indian Medicinal Herbs and Formulations for Alzheimer’s Disease, from Traditional Knowledge to Scientific Assessment

Mehla, J., Gupta, P., Pahuja, M., Diwan, D., & Diksha, D. (2020) · Brain Sciences · doi:10.3390/brainsci10120964 · Cited by 108 · see citing works

Natural Compounds as Beneficial Antioxidant Agents in Neurodegenerative Disorders: A Focus on Alzheimer’s Disease

Amato, A., Terzo, S., & Mulè, F. (2019) · Antioxidants · doi:10.3390/antiox8120608 · Cited by 107 · see citing works

Curcumin Ameliorates Neuroinflammation, Neurodegeneration, and Memory Deficits in p25 Transgenic Mouse Model that Bears Hallmarks of Alzheimer’s Disease

Sundaram, J. R., Poore, C. P., Sulaimee, N. H. B., Pareek, T., Cheong, W. F., Wenk, M. R., Pant, H. C., Frautschy, S. A., Low, C.-M., & Kesavapany, S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170093 · Cited by 105 · see citing works

A Theranostic Agent for in Vivo Near-Infrared Imaging of β-Amyloid Species and Inhibition of β-Amyloid Aggregation

Li, Y., Xu, D., Ho, S.-L., Li, H.-W., Yang, R., & Wong, M. S. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.03.047 · Cited by 102 · see citing works

Dietary plant polyphenols as the potential drugs in neurodegenerative diseases: current evidence, advances, and opportunities

Yan, L., Guo, M.-S., Zhang, Y., Yu, L., Wu, J.-M., Tang, Y., Ai, W., Zhu, F.-D., Law, B. Y.-K., Chen, Q., et al. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/5288698 · Cited by 97 · see citing works

Neuroprotective effects of Bacopa monnieri in experimental model of dementia

Saini, N., Singh, D., & Sandhir, R. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0811-4 · Cited by 95 · see citing works

New Insights in Amyloid Beta Interactions with Human Telomerase

Wang, J., Zhao, C., Zhao, A., Li, M., Ren, J., & Qu, X. (2015) · Journal of the American Chemical Society · doi:10.1021/ja511030s · Cited by 90 · see citing works

Development of Phenothiazine-Based Theranostic Compounds That Act Both as Inhibitors of β-Amyloid Aggregation and as Imaging Probes for Amyloid Plaques in Alzheimer’s Disease

Dao, P., Ye, F., Liu, Y., Du, Z. Y., Zhang, K., Dong, C. Z., Meunier, B., & Chen, H. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00380 · Cited by 80 · see citing works

Curcumin ameliorates impaired insulin/IGF signalling and memory deficit in a streptozotocin-treated rat model

Isik, A. T., Celik, T., Ulusoy, G., Ongoru, O., Elibol, B., Doruk, H., Bozoglu, E., Kayir, H., Mas, M. R., & Akman, S. (2009) · AGE · doi:10.1007/s11357-008-9078-8 · Cited by 76 · see citing works

Potential Role of Natural Polyphenols against Protein Aggregation Toxicity: In Vitro, In Vivo, and Clinical Studies

Henríquez, G., Gomez, A., Guerrero, E., & Narayan, M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00381 · Cited by 83 · see citing works

Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes

Piccialli, I., Tedeschi, V., Caputo, L., D’Errico, S., Ciccone, R., De Feo, V., Secondo, A., & Pannaccione, A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.876614 · Cited by 73 · see citing works

Anti-inflammatory and Immune Therapy for Alzheimers Disease: Current Status and Future Directions

Walker, D., & Lue, L.-F. (2007) · Current Neuropharmacology · doi:10.2174/157015907782793667 · Cited by 66 · see citing works

Design, synthesis, and evaluation of multitarget-directed ligands against Alzheimer’s disease based on the fusion of donepezil and curcumin

Yan, J., Hu, J., Liu, A., He, L., Li, X., & Wei, H. (2017) · Bioorganic &amp; Medicinal Chemistry · doi:10.1016/j.bmc.2017.02.048 · Cited by 65 · see citing works

Multimodal Nanoprobes to Target Cerebrovascular Amyloid in Alzheimer’s Disease Brain

Jaruszewski, K. M., Curran, G. L., Swaminathan, S. K., Rosenberg, J. T., Grant, S. C., Ramakrishnan, S., Lowe, V. J., Poduslo, J. F., & Kandimalla, K. K. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2013.10.075 · Cited by 64 · see citing works

Alzheimer’s Disease as a Major Public Health Concern: Role of Dietary Saponins in Mitigating Neurodegenerative Disorders and Their Underlying Mechanisms

Abduljawad, A. A., Elawad, M. A., Elkhalifa, M. E. M., Ahmed, A., Hamdoon, A. A. E., Salim, L. H. M., Ashraf, M., Ayaz, M., Hassan, S. S. U., & Bungau, S. (2022) · Molecules · doi:10.3390/molecules27206804 · Cited by 63 · see citing works

Dietary Regulation of Gut-Brain Axis in Alzheimer’s Disease: Importance of Microbiota Metabolites

Frausto, D. M., Forsyth, C. B., Keshavarzian, A., & Voigt, R. M. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.736814 · Cited by 61 · see citing works

The Positive Role of Curcumin-Loaded Salmon Nanoliposomes on the Culture of Primary Cortical Neurons

Hasan, M., Latifi, S., Kahn, C. J. F., Tamayol, A., Habibey, R., Passeri, E., Linder, M., & Arab-Tehrany, E. (2018) · Marine Drugs · doi:10.3390/md16070218 · Cited by 54 · see citing works

The Natural Product Curcumin as a Potential Coadjuvant in Alzheimer's Treatment

Morales, I., Cerda-Troncoso, C., Andrade, V., & Maccioni, R. B. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170354 · Cited by 51 · see citing works

Protective effects of plant‐derived natural products on renal complications

Yaribeygi, H., Simental‐Mendía, L. E., Butler, A. E., & Sahebkar, A. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.27950 · Cited by 46 · see citing works

Effect of Curcumin on Intracerebroventricular Colchicine-Induced Cognitive Impairment and Oxidative Stress in Rats

Kumar, A., Naidu, P. S., Seghal, N., & Padi, S. S. V. (2007) · Journal of Medicinal Food · doi:10.1089/jmf.2006.076 · Cited by 45 · see citing works

Vitamin E, Turmeric and Saffron in Treatment of Alzheimer’s Disease

Adalier, N., & Parker, H. (2016) · Antioxidants · doi:10.3390/antiox5040040 · Cited by 40 · see citing works

Amelioration of β-amyloid-induced cognitive dysfunction and hippocampal axon degeneration by curcumin is associated with suppression of CRMP-2 hyperphosphorylation

Wang, Y., Yin, H., Li, J., Zhang, Y., Han, B., Zeng, Z., Qiao, N., Cui, X., Lou, J., & Li, J. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.10.024 · Cited by 36 · see citing works

Secondary Metabolites from Plants Possessing Inhibitory Properties against Beta-Amyloid Aggregation as Revealed by Thioflavin-T Assay and Correlations with Investigations on Transgenic Mouse Models of Alzheimer's Disease

Stefanescu, R., Stanciu, G. D., Luca, A., Paduraru, L., & Tamba, B.-I. (2020) · Biomolecules · doi:10.3390/biom10060870 · Cited by 35 · see citing works

Screening Assay for Metal-Catalyzed Oxidation Inhibitors Using Liquid Chromatography−Mass Spectrometry with an N-Terminal β-Amyloid Peptide

Inoue, K., Nakagawa, A., Hino, T., & Oka, H. (2009) · Analytical Chemistry · doi:10.1021/ac802162n · Cited by 32 · see citing works

The Multifaceted Role of Neuroprotective Plants in Alzheimer’s Disease Treatment

Zieneldien, T., Kim, J., & Cao, C. (2022) · Geriatrics · doi:10.3390/geriatrics7020024 · Cited by 29 · see citing works

Investigation of therapeutic effect of curcumin α and β glucoside anomers against Alzheimer’s disease by the nose to brain drug delivery

Ahmadi, N., Hosseini, M.-J., Rostamizadeh, K., & Anoush, M. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147517 · Cited by 28 · see citing works

Sensitized ZnO nanorod assemblies to detect heavy metal contaminated phytomedicines: Spectroscopic and simulation studies

Bagchi, D., Maji, T. K., Sardar, S., Lemmens, P., Bhattacharya, C., Karmakar, D., & Pal, S. K. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp08016b · Cited by 25 · see citing works

Exploring the effects of methylene blue on amyloid fibrillogenesis of lysozyme

How, S.-C., Cheng, Y.-H., Lo, C.-H., Lai, J.-T., Lin, T.-H., Bednarikova, Z., Antosova, A., Gazova, Z., Wu, J. W., & Wang, S. S.-S. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.08.038 · Cited by 25 · see citing works

Detoxification of amyloid β fibrils by curcumin derivatives and their verification in a <i>Drosophila</i> Alzheimer's model

Utomo, R. Y., Sugie, A., Okada, S., Miura, K., & Nakamura, H. (2022) · Chemical Communications · doi:10.1039/d1cc07000b · Cited by 18 · see citing works

Research Mechanism and Progress of the Natural Compound Curcumin in Treating Alzheimer’s Disease

Li, L., Wang, F., Jia, X., Yao, L., & Liu, Y. (2024) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/0113895575263783231009051957 · Cited by 11 · see citing works

Binding Behavior and Energetics between Curcumin and Amyloid-β Aggregates at the Molecular Scale

Martin, T. D., Malagodi, A. J., Chi, E. Y., et al. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.1262

High-definition characterization of cerebral β-amyloid angiopathy in Alzheimer's disease

Soontornniyomkij, V., Choi, C., Pomakian, J., & Vinters, H. V. (2010) · Human Pathology · doi:10.1016/j.humpath.2010.04.011 · Cited by 28 · see citing works

Cerebrospinal fluid amyloid β₄₀ is decreased in cerebral amyloid angiopathy

Verbeek, M. M., Kremer, B. P. H., Rikkert, M. O., Van Domburg, P. H. M. F., Skehan, M. E., & Greenberg, S. M. (2009) · Annals of Neurology · doi:10.1002/ana.21694 · Cited by 202 · see citing works

Familial cerebral amyloid angiopathy (British type) with nonneuritic amyloid plaque formation may be due to a novel amyloid protein

Ghiso, J. A., Plant, G. T., Révész, T., Wısnıewskı, T., & Frangione, B. (1995) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(94)00274-r · Cited by 28 · see citing works

Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils*

O'Nuallain, B., Williams, A. D., Westermark, P., & Wetzel, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311300200 · Cited by 406 · see citing works