Alzheimer's Disease: From Pathology to Therapeutic Approaches

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744

Inflammation and Alzheimer’s disease

Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514

Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B

Klunk, W. E., Engler, H., Nordberg, A., Wang, Y., Blomqvist, G., Holt, D. P., Bergström, M., Savitcheva, I., Huang, G., Estrada, S., et al. (2004) · Annals of Neurology · doi:10.1002/ana.20009 · Cited by 4,496

Alzheimer's Disease Is a Synaptic Failure

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

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

Mild cognitive impairment

Gauthier, S. G., Reisberg, ‌., Zaudig, M., Petersen, R. C., Ritchie, K. A., Broich, K., Belleville, S., Brodaty, H., Bennett, D. A., Chertkow, H. M., et al. (2006) · The Lancet · doi:10.1016/s0140-6736(06)68542-5 · Cited by 4,094

β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876

Oxidative stress and the amyloid beta peptide in Alzheimer’s disease

Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185

Compromised MAPK signaling in human diseases: an update

Kim, E., & Choi, E. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1472-2 · Cited by 1,033

Bioinorganic Chemistry of Alzheimer’s Disease

Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 683

Mitochondria-Targeting Ceria Nanoparticles as Antioxidants for Alzheimer’s Disease

Kwon, H. J., Cha, M.-Y., Kim, D., Kim, D., Soh, M., Shin, K., Hyeon, T., & Mook‐Jung, I. (2016) · ACS Nano · doi:10.1021/acsnano.5b08045 · Cited by 667

New Horizons for Diagnostics and Therapeutic Applications of Graphene and Graphene Oxide

Feng, L., Wu, L. J., & Qu, X. (2012) · Advanced Materials · doi:10.1002/adma.201203229 · Cited by 634

Development of Multifunctional Molecules as Potential Therapeutic Candidates for Alzheimer’s Disease, Parkinson’s Disease, and Amyotrophic Lateral Sclerosis in the Last Decade

Savelieff, M. G., Nam, G., Kang, J., Lee, H. J., Lee, M., & Lim, M. H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00138 · Cited by 612

Using Graphene Oxide High Near‐Infrared Absorbance for Photothermal Treatment of Alzheimer's Disease

Li, M., Yang, X., Ren, J., Qu, K., & Qu, X. (2012) · Advanced Materials · doi:10.1002/adma.201104864 · Cited by 535

Antioxidant Cerium Oxide Nanoparticles in Biology and Medicine

Nelson, B. C., Johnson, M. E., Walker, M. L., Riley, K., & Sims, C. M. (2016) · Antioxidants · doi:10.3390/antiox5020015 · Cited by 500

Rational Design of Near-Infrared Aggregation-Induced-Emission-Active Probes: In Situ Mapping of Amyloid-β Plaques with Ultrasensitivity and High-Fidelity

Fu, W., Yan, C., Guo, Z., Zhang, J., Zhang, H., Tian, H., & Zhu, W. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b12820 · Cited by 448

Recent advances in the multitarget‐directed ligands approach for the treatment of Alzheimer's disease

Leon, R. M., García, A. G., & Marco, J. L. (2011) · Medicinal Research Reviews · doi:10.1002/med.20248 · Cited by 447

Copper, zinc and iron in neurodegenerative diseases (Alzheimer's, Parkinson's and prion diseases)

Kozłowski, H., Łuczkowski, M., Remelli, M., & Valensin, D. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.013 · Cited by 446

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

Untangling Amyloid-β, Tau, and Metals in Alzheimer’s Disease

Savelieff, M. G., Lee, S., Liu, Y., & Lim, M. H. (2013) · ACS Chemical Biology · doi:10.1021/cb400080f · Cited by 407

Chiral gold nanoparticles enantioselectively rescue memory deficits in a mouse model of Alzheimer’s disease

Hou, K., Zhao, J., Wang, H., Li, B., Li, K., Shi, X., Wan, K., Ai, J., Lv, J., Wang, D., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18525-2 · Cited by 373

Misfolded proteins in Alzheimer's disease and type II diabetes

DeToma, A. S., Salamekh, S., Ramamoorthy, A., & Lim, M. H. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15112f · Cited by 363

Design and Synthesis of Curcumin Analogues for in Vivo Fluorescence Imaging and Inhibiting Copper-Induced Cross-Linking of Amyloid Beta Species in Alzheimer’s Disease

Zhang, X., Tian, Y., Zeng, L., Tian, X., Sun, H., Liu, H., Moore, A. V., & Ran, C. (2013) · Journal of the American Chemical Society · doi:10.1021/ja405239v · Cited by 354

Microglia in the Neuroinflammatory Pathogenesis of Alzheimer’s Disease and Related Therapeutic Targets

Cai, Y., Liu, J., Wang, B., Sun, M., & Yang, H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.856376 · Cited by 351

Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity

Fändrich, M. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.006 · Cited by 346

Negatively Charged Gold Nanoparticles Inhibit Alzheimer's Amyloid‐β Fibrillization, Induce Fibril Dissociation, and Mitigate Neurotoxicity

Liao, Y., Chang, Y., Yoshiike, Y., Chang, Y. C., & Chen, Y. (2012) · Small · doi:10.1002/smll.201201068 · Cited by 324

Nrf2 reduces levels of phosphorylated tau protein by inducing autophagy adaptor protein NDP52

Jo, C., Gundemir, S., Pritchard, S., Jin, Y. N., Rahman, I., & Johnson, G. V. W. (2014) · Nature Communications · doi:10.1038/ncomms4496 · Cited by 323

Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity

Choi, J.-S., Braymer, J. J., Nanga, R. P. R., Ramamoorthy, A., & Lim, M. H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006091107 · Cited by 264

Metal-associated amyloid-β species in Alzheimer's disease

Pithadia, A. S., & Lim, M. H. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.01.016 · Cited by 259

Cognitive Dysfunction Syndrome

Landsberg, G. M., Nichol, J., & Araujo, J. A. (2012) · Veterinary Clinics of North America Small Animal Practice · doi:10.1016/j.cvsm.2012.04.003 · Cited by 277

Specific Knockdown of Endogenous Tau Protein by Peptide-Directed Ubiquitin-Proteasome Degradation

Chu, T.-T., Gao, N., Li, Q.-Q., Chen, P.-G., Yang, X.-F., Chen, Y.-X., Zhao, Y.-F., & Li, Y.-M. (2016) · Cell Chemical Biology · doi:10.1016/j.chembiol.2016.02.016 · Cited by 247

Mitochondrial dysfunction in neurodegenerative diseases and cancer

de Moura, M. B., Santana‐Santos, L., & Houten, B. V. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20575 · Cited by 247

Insights into antiamyloidogenic properties of the green tea extract (−)-epigallocatechin-3-gallate toward metal-associated amyloid-β species

Hyung, S., DeToma, A. S., Brender, J., Lee, S., Vivekanandan, S., Kochi, A., Choi, J.-S., Ramamoorthy, A., Ruotolo, B. T., & Lim, M. H. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220326110 · Cited by 240

Protein misfolding and aggregation in Alzheimer’s disease and type 2 diabetes mellitus

Ashraf, G., Greig, N., Khan, T., Hassan, I., Tabrez, S., Shakil, S., Sheikh, I., Zaidi, S., Akram, M., Jabir, N., et al. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527313666140917095514 · Cited by 236

Near-infrared fluorescence molecular imaging of amyloid beta species and monitoring therapy in animal models of Alzheimer’s disease

Zhang, X., Tian, Y., Zhang, C. M., Tian, X., Ross, A., Moir, R. D., Sun, H., Tanzi, R. E., Moore, A. V., & Ran, C. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1505420112 · Cited by 228

The Supramolecular Chemistry of β-Sheets

Cheng, P.-N., Pham, J. D., & Nowick, J. S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja3088407 · Cited by 235

Synthesis, Biological Evaluation, and Molecular Modeling of Donepezil and N-[(5-(Benzyloxy)-1-methyl-1H-indol-2-yl)methyl]-N-methylprop-2-yn-1-amine Hybrids as New Multipotent Cholinesterase/Monoamine Oxidase Inhibitors for the Treatment of Alzheimer’s Disease

Bolea, I., Juárez‐Jiménez, J., Rı́os, C. D. L., Chioua, M., Pouplana, R., Luque, F. J., Unzeta, M., Marco, J. L., & Samadi, A. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200853t · Cited by 220

Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide

Sharma, A. K., Pavlova, S. T., Kim, J., Finkelstein, D., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210588m · Cited by 202

18F Stilbenes and Styrylpyridines for PET Imaging of Aβ Plaques in Alzheimer’s Disease: A Miniperspective

Kung, H. F., Choi, S., Qü, W., Zhang, W., & Skovronsky, D. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901039z · Cited by 201

Design of PLGA-functionalized quercetin nanoparticles for potential use in Alzheimer’s disease

Sun, D., Li, N., Zhang, W., Zhao, Z., Mou, Z., Huang, D., Liu, J., & Wang, W. (2016) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2016.08.052 · Cited by 202

Rethinking CRITID Procedure of Brain Targeting Drug Delivery: Circulation, Blood Brain Barrier Recognition, Intracellular Transport, Diseased Cell Targeting, Internalization, and Drug Release

Ruan, S., Zhou, Y., Jiang, X., & Gao, H. (2021) · Advanced Science · doi:10.1002/advs.202004025 · Cited by 200

PROTACs to address the challenges facing small molecule inhibitors

Martín-Acosta, P., & Xiao, X. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112993 · Cited by 192

Rational Design of a Structural Framework with Potential Use to Develop Chemical Reagents That Target and Modulate Multiple Facets of Alzheimer’s Disease

Lee, S., Zheng, X., Krishnamoorthy, J., Savelieff, M. G., Park, H. M., Brender, J., Kim, J. H., Derrick, J. S., Kochi, A., Lee, H. J., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja409801p · Cited by 186

Aβ Toxicity in Alzheimer's Disease

Cavallucci, V., D’Amelio, M., & Cecconi, F. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8251-3 · Cited by 179

Pyrano[3,2-c]quinoline−6-Chlorotacrine Hybrids as a Novel Family of Acetylcholinesterase- and β-Amyloid-Directed Anti-Alzheimer Compounds

Camps, P., Formosa, X., Galdeano, C., Muñoz‐Torrero, D., Ramírez, L., Gómez, E., Isambert, N., Lavilla, R., Badı́a, A., Clos, M. V., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900859q · Cited by 174

The Ongoing Search for Small Molecules to Study Metal-Associated Amyloid-β Species in Alzheimer’s Disease

Savelieff, M. G., DeToma, A. S., Derrick, J. S., & Lim, M. H. (2014) · Accounts of Chemical Research · doi:10.1021/ar500152x · Cited by 174

Nanotechnology-based drug delivery for central nervous system disorders

Nguyen, T. T., Nguyen, T. T. D., Vo, T. K., An, T. N. M., Nguyen, M. K., Toi, V. V., & Vo, G. V. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112117 · Cited by 182

Brazilin inhibits amyloid β-protein fibrillogenesis, remodels amyloid fibrils and reduces amyloid cytotoxicity

Du, W., Guo, J., Gao, M., Hu, S., Dong, X., Han, Y., Liu, F., Jiang, S., & Sun, Y. P. (2015) · Scientific Reports · doi:10.1038/srep07992 · Cited by 171

Recent progress in understanding Alzheimer's β-amyloid structures

Fändrich, M., Schmidt, M., & Grigorieff, N. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.02.002 · Cited by 168

Cerium oxide caged metal chelator: anti-aggregation and anti-oxidation integrated H2O2-responsive controlled drug release for potential Alzheimer's disease treatment

Li, M., Shi, P., Xu, C., Ren, J., & Qu, X. (2013) · Chemical Science · doi:10.1039/c3sc50697e · Cited by 166

γ-Secretase Modulators as Potential Disease Modifying Anti-Alzheimer’s Drugs

Oehlrich, D., Berthelot, D., & Gijsen, H. J. M. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm101168r · Cited by 163

Chiral Metallohelical Complexes Enantioselectively Target Amyloid β for Treating Alzheimer’s Disease

Li, M. C., Howson, S. E., Dong, K., Gao, N., Ren, J., Scott, P., & Qu, X. (2014) · Journal of the American Chemical Society · doi:10.1021/ja502789e · Cited by 163

Metallobiology and therapeutic chelation of biometals (copper, zinc and iron) in Alzheimer’s disease: Limitations, and current and future perspectives

Fasae, K. D., Abolaji, A. O., Faloye, T. R., Odunsi, A., Oyetayo, B. O., Enya, J. I., Rotimi, J. A., Akinyemi, R., Whitworth, A. J., & Aschner, M. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126779 · Cited by 161

Maintenance of Amyloid β Peptide Homeostasis by Artificial Chaperones Based on Mixed‐Shell Polymeric Micelles

Huang, F., Wang, J., Qu, A., Shen, L., Liu, J., Liu, J., Zhang, Z., An, Y., & Shi, L. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201400735 · Cited by 152

Time-Course and Regional Analyses of the Physiopathological Changes Induced after Cerebral Injection of an Amyloid β Fragment in Rats

Zussy, C., Brureau, A., Delair, B., Marchal, S., Keller, E., IXART, G., Naert, G., Meunier, J., Chevallier, N., Maurice, T., et al. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.03.021 · Cited by 154

6-Shogaol, an active constituent of ginger, attenuates neuroinflammation and cognitive deficits in animal models of dementia

Moon, M., Kim, H. G., Choi, J. G., Oh, H., Lee, P. K. J., Ha, S. K., Kim, S. Y., Park, Y., Huh, Y., & Oh, M. S. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.04.121 · 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

Recent progress in multifunctional metal chelators as potential drugs for Alzheimer's disease

Santos, M. A., Chand, K., & Chaves, S. (2016) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2016.04.013 · Cited by 152

Coumarin: A Privileged Scaffold for the Design and Development of Antineurodegenerative Agents

Jameel, E., Umar, T., Kumar, J., & Hoda, N. (2015) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12629 · Cited by 150

Pathways of Amyloid-β Aggregation Depend on Oligomer Shape

Barz, B., Liao, Q., & Strodel, B. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b10343 · Cited by 144

β-Secretase (BACE1) inhibitors with high in vivo efficacy suitable for clinical evaluation in Alzheimer's disease.

Hilpert, H., Guba, W., Woltering, T., Wostl, W., Pinard, E., Mauser, H., Mayweg, A., Rogers-Evans, M., Humm, R., Krummenacher, D., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400225m · Cited by 119

Molecular Insight into Conformational Transition of Amyloid β-Peptide 42 Inhibited by (−)-Epigallocatechin-3-gallate Probed by Molecular Simulations

Liu, F., Dong, X., He, L., Middelberg, A. P. J., & Sun, Y. P. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp202640b · Cited by 144

Hydroxypyridinones as “privileged” chelating structures for the design of medicinal drugs

Santos, M. A., Marques, S. M., & Chaves, S. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.08.008 · Cited by 131

Multi-targetable chalcone analogs to treat deadly Alzheimer’s disease: Current view and upcoming advice

Zhang, X., Rakesh, K. P., Bukhari, S. N. A., Moku, B., Manukumar, H. M. G., & Qin, H. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.06.009 · Cited by 132

Impact of aging, Alzheimer's disease and Parkinson's disease on the blood-brain barrier transport of therapeutics

Pan, Y., & Nicolazzo, J. A. (2018) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2018.04.009 · Cited by 131

Inhibition of beta-amyloid peptide aggregation by multifunctional carbazole-based fluorophores.

Yang, W.-G., Wong, Y., Ng, O. T. W., Bai, L.-P., Kwong, D., Ke, Y., Jiang, Z.-H., Li, H.-W., Yung, K. K. L., & Wong, M. (2012) · Angewandte Chemie · doi:10.1002/anie.201104150 · Cited by 120

Black Tea Theaflavins Inhibit Formation of Toxic Amyloid-β and α-Synuclein Fibrils

Grelle, G., Otto, A., Lorenz, M., Frank, R. F., Wanker, E. E., & Bieschke, J. (2011) · Biochemistry · doi:10.1021/bi2012383 · Cited by 133

Redox Reactions of the α-Synuclein−Cu2+ Complex and Their Effects on Neuronal Cell Viability

Wang, C., Liu, L., Zhang, L., Peng, Y., & Zhou, F. (2010) · Biochemistry · doi:10.1021/bi1010909 · Cited by 126

Microbubbles in combination with focused ultrasound for the delivery of quercetin-modified sulfur nanoparticles through the blood brain barrier into the brain parenchyma and relief of endoplasmic reticulum stress to treat Alzheimer's disease

Liu, Y., Gong, Y., Xie, W., Huang, A., Yuan, X., Zhou, H., Zhu, X., Chen, X., Liu, J., Liu, J., et al. (2020) · Nanoscale · doi:10.1039/c9nr09713a · Cited by 123

Turn-on chemiluminescence probes and dual-amplification of signal for detection of amyloid beta species in vivo

Yang, J., Yin, W., Van, R., Yin, K., Wang, P., Zheng, C., Zhu, B., Ran, K., Zhang, C., Kumar, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17783-4 · Cited by 123

Design, Synthesis, and Evaluation of Orally Available Clioquinol-Moracin M Hybrids as Multitarget-Directed Ligands for Cognitive Improvement in a Rat Model of Neurodegeneration in Alzheimer’s Disease

Wang, Z., Wang, Y., Wang, B., Li, W., Huang, L., & Li, X. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01222 · Cited by 120

Gold nanoparticle-capped mesoporous silica-based H2O2-responsive controlled release system for Alzheimer’s disease treatment

Yang, L., Yin, T., Liu, Y., Sun, J., Zhou, Y., & Liu, J. (2016) · Acta Biomaterialia · doi:10.1016/j.actbio.2016.09.010 · 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

Alzheimer's Disease Related Markers, Cellular Toxicity and Behavioral Deficits Induced Six Weeks after Oligomeric Amyloid-β Peptide Injection in Rats

Zussy, C., Brureau, A., Keller, E., Marchal, S., Blayo, C., Delair, B., IXART, G., Maurice, T., & Givalois, L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053117 · Cited by 118

Chiral bis(amino acid)- and bis(amino alcohol)-oxalamidegelators. Gelation properties, self-assembly motifs and chirality effects

Frkanec, L., & Žinić, M. (2009) · Chemical Communications · doi:10.1039/b920353m · Cited by 117

The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity

Cecchi, C., & Stefani, M. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.06.003 · Cited by 117

Fisetin stimulates autophagic degradation of phosphorylated tau via the activation of TFEB and Nrf2 transcription factors

Kim, S., Choi, K. J., Cho, S., Yun, S., Jeon, J., Koh, Y. H., Song, J., Johnson, G. V. W., & Jo, C. (2016) · Scientific Reports · doi:10.1038/srep24933 · Cited by 116

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

Fucoidan, a sulfated polysaccharide from brown algae, improves cognitive impairment induced by infusion of Aβ peptide in rats

Gao, Y., Li, C., Yin, J., Shen, J., Wang, H., Wu, Y., & Jin, H. (2011) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2011.12.022 · Cited by 114

Novel insights for the treatment of Alzheimer's disease

Kurz, A., & Perneczky, R. (2010) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2010.07.018 · Cited by 115

Self‐Assembled Peptide–Polyoxometalate Hybrid Nanospheres: Two in One Enhances Targeted Inhibition of Amyloid β‐Peptide Aggregation Associated with Alzheimer's Disease

Li, M. C., Xu, C., Wu, L. J., Ren, J., Wang, E., & Qu, X. (2013) · Small · doi:10.1002/smll.201202612 · Cited by 111

Ellagic acid promotes Aβ42 fibrillization and inhibits Aβ42-induced neurotoxicity

Feng, Y. N., Yang, S., Du, X., Zhang, X., Sun, X., Zhao, M., Sun, G., & Liu, R. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.10.130 · Cited by 110

Vitamin B12 offers neuronal cell protection by inhibiting Aβ-42 amyloid fibrillation

Alam, P., Siddiqi, M. K., Chaturvedi, S. K., Zaman, M., & Khan, R. H. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.03.001 · Cited by 109

Advances in developing therapeutic strategies for Alzheimer's disease

Nguyen, T. T., Nguyen, T. T. D., Nguyen, T. K. O., Vo, T. K., & Giau, V. V. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111623 · Cited by 108

Noncancerous disease-targeting AIEgens

Duo, Y., Luo, G., Zhang, W., Wang, R., Xiao, G. G., Li, Z., Li, X., Chen, M., Yoon, J., & Tang, B. Z. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00610c · Cited by 106

Design, synthesis and neuroprotective evaluation of novel tacrine–benzothiazole hybrids as multi-targeted compounds against Alzheimer’s disease

Keri, R. S., Quintanova, C., Marques, S. M., Esteves, A. R., Cardoso, S. M., & Santos, M. A. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.05.028 · Cited by 107

A bifunctional curcumin analogue for two-photon imaging and inhibiting crosslinking of amyloid beta in Alzheimer's disease

Zhang, X., Tian, Y., Yuan, P., Li, Y., Yaseen, M. A., Grutzendler, J., Moore, A. V., & Ran, C. (2014) · Chemical Communications · doi:10.1039/c4cc03731f · Cited by 106

Recent Advances in the Identification of γ-Secretase Inhibitors To Clinically Test the Aβ Oligomer Hypothesis of Alzheimer’s Disease

Kreft, A. F., Martone, R. L., & Porte, A. M. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900188z · Cited by 105

How Can Insulin Resistance Cause Alzheimer’s Disease?

Yoon, J. H., Hwang, J., Son, S. U., Choi, J., You, S.-W., Park, H., Cha, S.-Y., & Maeng, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043506 · Cited by 106

A Step into the Future: Applications of Nanoparticle Enzyme Mimics

Korschelt, K., Tahir, M. N., & Tremel, W. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201800384 · Cited by 102

Current progress of mitochondrial transplantation that promotes neuronal regeneration

Chang, C.-Y., Liang, M.-Z., & Chen, L. (2019) · Translational Neurodegeneration · doi:10.1186/s40035-019-0158-8 · Cited by 102

Enzyme-mimetic antioxidant nanomaterials for ROS scavenging: Design, classification, and biological applications

Zhou, S., Cai, H., He, X., Tang, Z., & Lu, S. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215536 · Cited by 102

α-Helix Mimetics as Modulators of Aβ Self-Assembly

Kumar, S., & Hamilton, A. D. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b09734 · Cited by 99

Copper-Targeting Approaches in Alzheimer’s Disease: How To Improve the Fallouts Obtained from in Vitro Studies

Esmieu, C., Guettas, D., Conte‐Daban, A., Sabater, L., Faller, P., & Hureau, C. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b00995 · Cited by 103

Myricetin: A Naturally Occurring Regulator of Metal‐Induced Amyloid‐β Aggregation and Neurotoxicity

DeToma, A. S., Choi, J., Braymer, J. J., & Lim, M. H. (2011) · ChemBioChem · doi:10.1002/cbic.201000790 · Cited by 99

Combined Treatment with a BACE Inhibitor and Anti-Aβ Antibody Gantenerumab Enhances Amyloid Reduction in APP London Mice

Jacobsen, H., Ozmen, L., Caruso, A., Narquizian, R., Hilpert, H., Jacobsen, B., Terwel, D., Tanghe, A., & Bohrmann, B. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1405-14.2014 · Cited by 96

A Functionalized Octahedral Palladium Nanozyme as a Radical Scavenger for Ameliorating Alzheimer’s Disease

Zhi, J., Yuan, X., Wei, J., Guo, X., Gong, Y., Li, J., Zhou, H., Zhang, L., & Liu, J. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c06687 · Cited by 97

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Guo, X., Lie, Q., Liu, Y., Zhi, J., Gong, Y., Yuan, X., & Liu, J. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c00690 · Cited by 96

Protective Effects of Ginger Root Extract on Alzheimer Disease-Induced Behavioral Dysfunction in Rats

Zeng, G., Zhang, Z., Lü, L., Xiao, D.-Q., Zong, S., & He, J.-M. (2013) · Rejuvenation Research · doi:10.1089/rej.2012.1389 · Cited by 94

Structure-mechanism-based engineering of chemical regulators targeting distinct pathological factors in Alzheimer’s disease

Beck, M. W., Derrick, J. S., Kerr, R. A., Oh, S. B., Cho, W. J., Lee, S. J. C., Ji, Y., Han, J., Tehrani, Z. A., Suh, N., et al. (2016) · Nature Communications · doi:10.1038/ncomms13115 · Cited by 93

Synthesis and biological evaluation of deferiprone-resveratrol hybrids as antioxidants, Aβ 1–42 aggregation inhibitors and metal-chelating agents for Alzheimer's disease

Xu, P., Zhang, M., Sheng, R., & Ma, Y. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.12.045 · Cited by 92

Crystal structure of thioflavin-T and its binding to amyloid fibrils: insights at the molecular level

Rodríguez‐Rodríguez, C., Rimola, A., Rodrı́guez-Santiago, L., Ugliengo, P., Álvarez‐Larena, Á., Gutiérrez‐de‐Terán, H., Sodupe, M., & Gonzalez-Duarte, P. (2010) · Chemical Communications · doi:10.1039/b912396b · Cited by 91

Zinc and Copper Differentially Modulate Amyloid Precursor Protein Processing by γ-Secretase and Amyloid-β Peptide Production

Gerber, H., Wu, F., Dimitrov, M. I., Osuna, G. M. G., & Fraering, P. C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.754101 · Cited by 89

5-Hydroxymethylfurfural, an antioxidant agent from Alpinia oxyphylla Miq. improves cognitive impairment in Aβ1–42 mouse model of Alzheimer's disease

Liu, A., Zhao, X. D., Li, H., Liu, Z., Liu, B., Mao, X., Guo, L., Bi, K., & Jia, Y. (2014) · International Immunopharmacology · doi:10.1016/j.intimp.2014.10.028 · Cited by 89

Chemically exfoliated WS2 nanosheets efficiently inhibit amyloid β-peptide aggregation and can be used for photothermal treatment of Alzheimer’s disease

Li, M. C., Zhao, A., Dong, K., Li, W., Ren, J., & Qu, X. (2015) · Nano Research · doi:10.1007/s12274-015-0821-z · Cited by 91

Development of Bifunctional Stilbene Derivatives for Targeting and Modulating Metal-Amyloid-β Species

Braymer, J. J., Choi, J.-S., DeToma, A. S., Wang, C., Nam, K., Kampf, J. W., Ramamoorthy, A., & Lim, M. H. (2011) · Inorganic Chemistry · doi:10.1021/ic2012205 · Cited by 89

Dietary Polyphenols: A Multifactorial Strategy to Target Alzheimer’s Disease

Dhakal, S., Kushairi, N., Phan, C., Adhikari, B., Sabaratnam, V., & Macreadie, I. G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205090 · Cited by 92

Die Alzheimer‐Demenz: von der Pathologie zu therapeutischen Ansätzen

Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie · doi:10.1002/ange.200802808 · Cited by 41

The Role and Therapeutic Targeting of α-, β- and γ-Secretase in Alzheimer's Disease

MacLeod, R., Hillert, E., Cameron, R. T., & Baillie, G. S. (2015) · Future Science OA · doi:10.4155/fso.15.9 · Cited by 136

Progress towards testing the amyloid hypothesis: inhibitors of APP processing.

Olson, R. E., Copeland, R. A., & Seiffert, D. (2001) · PubMed · Cited by 20

β-Amyloid therapies in Alzheimer’s disease

Jhee, S. S., Shiovitz, T. M., Crawford, A. W., & Cutler, N. R. (2001) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.10.4.593 · Cited by 25

Views on Amyloid Hypothesis and Secretase Inhibitors for Treating Alzheimers Disease: Progress and Problems

Nguyen, J., Yamani, A., & Kiso, Y. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206778792976 · Cited by 36