Oligomeric and Fibrillar Species of Amyloid-β Peptides Differentially Affect Neuronal Viability

Alzheimer's Disease: Genes, Proteins, and Therapy

Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659

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

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

Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975

Huntingtin Acts in the Nucleus to Induce Apoptosis but Death Does Not Correlate with the Formation of Intranuclear Inclusions

Saudou, F., Finkbeiner, S. M., Devys, D., & Greenberg, M. E. (1998) · Cell · doi:10.1016/s0092-8674(00)81782-1 · Cited by 1,598

Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy

Conway, K. A., Lee, S., Rochet, J., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,559

Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease

Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530

A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N–terminus of β–amyloid

Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B., & Lannfelt, L. (1992) · Nature Genetics · doi:10.1038/ng0892-345 · Cited by 1,513

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

Is Targeting the Inflammasome a Way Forward for Neuroscience Drug Discovery?

Swanton, T., Cook, J., Beswick, J. A., Freeman, S., Lawrence, C. B., & Brough, D. (2018) · SLAS DISCOVERY · doi:10.1177/2472555218786210 · Cited by 26

Murine Beta-Amyloid (1–42) Oligomers Disrupt Endothelial Barrier Integrity and VEGFR Signaling via Activating Astrocytes to Release Deleterious Soluble Factors

Yue, Q., Zhou, X., Zhang, Z., & Hoi, M. P. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031878 · Cited by 26

Enhancing the Amyloid-β Anti-Aggregation Properties of Curcumin via Arene-Ruthenium(II) Derivatization

Cuccioloni, M., Cecarini, V., Bonfili, L., Pettinari, R., Tombesi, A., Pagliaricci, N., Petetta, L., Angeletti, M., & Eleuteri, A. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158710 · Cited by 27

Unveiling the Potential of Polyphenols as Anti-Amyloid Molecules in Alzheimer’s Disease

Kabir, E. R., Chowdhury, N. M., Yasmin, H., Kabir, M. T., Akter, R., Perveen, A., Ashraf, G. M., Akter, S., Rahman, M. H., & Sweilam, S. H. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666221010113812 · Cited by 26

The Conformational Stability of Nonfibrillar Amyloid-β Peptide Oligomers Critically Depends on the C-Terminal Peptide Length

Socher, E., Sticht, H., & Horn, A. H. C. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn400208r · Cited by 25

Glycyrrhiza and Uncaria Hook contribute to protective effect of traditional Japanese medicine yokukansan against amyloid β oligomer-induced neuronal death

Kanno, H., Kawakami, Z., Iizuka, S., Tabuchi, M., Mizoguchi, K., Ikarashi, Y., & Kase, Y. (2013) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2013.06.052 · Cited by 25

Effects of concentration of amyloid β (Aβ) on viability of cultured retinal pigment epithelial cells

Masuda, N., Tsujinaka, H., Hirai, H., Yamashita, M., Ueda, T., & Ogata, N. (2019) · BMC Ophthalmology · doi:10.1186/s12886-019-1076-3 · Cited by 25

The Intact Human Acetylcholinesterase C-Terminal Oligomerization Domain Is α-Helical in Situ and in Isolation, but a Shorter Fragment Forms β-Sheet-Rich Amyloid Fibrils and Protofibrillar Oligomers

Cottingham, M. G., Voskuil, J. L. A., & Vaux, D. J. (2003) · Biochemistry · doi:10.1021/bi034768i · Cited by 25

Dendrimers antiamyloidogenic potential in neurodegenerative diseases

Benseny‐Cases, N., Klementieva, O. L., & Cladera, J. (2011) · New Journal of Chemistry · doi:10.1039/c1nj20469f · Cited by 25

Amyloid β oligomers induce interleukin-1β production in primary microglia in a cathepsin B- and reactive oxygen species-dependent manner

Taneo, J., Adachi, T., Yoshida, A., Takayasu, K., Takahara, K., & Inaba, K. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.006 · Cited by 25

Antiamyloidogenic Activity of Aβ42-Binding Peptoid in Modulating Amyloid Oligomerization

Zhao, Z., Zhu, L., Li, H., Cheng, P., Peng, J., Yin, Y., Yang, Y., Wang, C., Hu, Z., & Yang, Y. (2016) · Small · doi:10.1002/smll.201602857 · Cited by 24

Neuroprotective effects of brain‐derived neurotrophic factor against amyloid beta 1‐40‐induced retinal and optic nerve damage

Lazaldin, M. A. M., Iezhitsa, I. N., Agarwal, R., Bakar, N. S., Agarwal, P., & Ismail, N. M. (2019) · European Journal of Neuroscience · doi:10.1111/ejn.14662 · Cited by 24

The Role of Age on Beta-Amyloid1–42 Plasma Levels in Healthy Subjects

Zecca, C., Pasculli, G., Tortelli, R., Dell’Abate, M. T., Capozzo, R., Barulli, M. R., Barone, R., Accogli, M., Arima, S., Pollice, A., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.698571 · Cited by 26

Ca2+, within the physiological concentrations, selectively accelerates Aβ42 fibril formation and not Aβ40 in vitro

Ahmad, A., Muzaffar, M., & Ingram, V. M. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.06.022 · Cited by 26

Dynamin 1 depletion and memory deficits in rats treated with Aβ and cerebral ischemia

Watanabe, T., Iwasaki, K., Takasaki, K., Yamagata, N., Fujino, M., Nogami, A., Ii, M., Katsurabayashi, S., Mishima, K., & Fujiwara, M. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22346 · Cited by 23

Translational, rotational and internal dynamics of amyloid β-peptides (Aβ40 and Aβ42) from molecular dynamics simulations

Bora, R. P., & Prabhakar, R. S. (2009) · The Journal of Chemical Physics · doi:10.1063/1.3249609 · Cited by 24

A New Amyloid-Like β-Aggregate with Amyloid Characteristics, Except Fibril Morphology

Chang, E. S. ‐., Liao, T., Lim, T., Fann, W. S., & Chen, R. P. ‐. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.11.009 · Cited by 24

The novel RAGE interactor PRAK is associated with autophagy signaling in Alzheimer’s disease pathogenesis

Kim, Y., Kim, C., Son, S. M., Song, H., Hong, H., Han, S.-H., & Mook‐Jung, I. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0068-5 · Cited by 25

N-Terminus Binding Preference for Either Tanshinone or Analogue in Both Inhibition of Amyloid Aggregation and Disaggregation of Preformed Amyloid Fibrils—Toward Introducing a Kind of Novel Anti-Alzheimer Compounds

Dong, M., Zhao, W., Hu, D., Ai, H., & Kang, B. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00080 · Cited by 24

Site-specific glycation of Aβ1–42 affects fibril formation and is neurotoxic

Ng, J., Kaur, H., Collier, T. A., Chang, K., Brooks, A. E. S., Allison, J. R., Brimble, M. A., Hickey, A. J., & Birch, N. P. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006846 · Cited by 24

Novel Disassembly Mechanisms of Sigmoid Aβ42 Protofibrils by Introduced Neutral and Charged Drug Molecules

Xing, X., Liu, C., Ali, A., Kang, B., Li, P., & Ai, H. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00550 · Cited by 24

Resveratrol targeting tau proteins, amyloid‐beta aggregations, and their adverse effects: An updated review

Ashrafizadeh, M., Zarrabi, A., Najafi, M., Samarghandian, S., Mohammadinejad, R., & Ahn, K. S. (2020) · Phytotherapy Research · doi:10.1002/ptr.6732 · Cited by 24

The Peptide KLVFF-K6 Promotes β-Amyloid(1–40) Protofibril Growth by Association but Does Not Alter Protofibril Effects on Cellular Reduction of 3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium Bromide (MTT)

Moss, M. A., Nichols, M. R., Reed, D. K., Hoh, J. H., & Rosenberry, T. L. (2003) · Molecular Pharmacology · doi:10.1124/mol.64.5.1160 · Cited by 25

Replicating neuroblastoma cells in different cell cycle phases display different vulnerability to amyloid toxicity

Cecchi, C., Pensalfini, A., Stefani, M., Baglioni, S., Fiorillo, C., Cappadona, S., Caporale, R., Nosi, D., Ruggiero, M., & Liguri, G. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0265-3 · Cited by 24

Not Oligomers but Amyloids are Cytotoxic in the Membrane‐Mediated Amyloidogenesis of Amyloid‐β Peptides

Itoh, N., Takada, E., Okubo, K., Yano, Y., Hoshino, M., Sasaki, A., Kinjo, M., & Matsuzaki, K. (2017) · ChemBioChem · doi:10.1002/cbic.201700576 · Cited by 24

Therapeutic targets from a Drosophila model of Alzheimer’s disease

Crowther, D. C., Kinghorn, K. J., Page, R., & Lomas, D. A. (2004) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2004.07.001 · Cited by 23

Aggregating the amyloid Aβ11–25 peptide into a four‐stranded β‐sheet structure

Boucher, G., Mousseau, N., & Derreumaux, P. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21134 · Cited by 24

Glossopharyngeal and vagal neuralgia secondary to vascular compression of the nerves.

Morales-Zavala, F., Albert, P., Alberca, R., de Valle, B., & Narros, A. (1977) · PubMed · Cited by 24

A single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer’s disease CSF

Bigi, A., Napolitano, L., Vadukul, D. M., Chiti, F., Cecchi, C., Aprile, F. A., & Cascella, R. (2024) · Alzheimer s Research & Therapy · doi:10.1186/s13195-023-01361-z · Cited by 23

Heparin Nanoparticles for β Amyloid Binding and Mitigation of β Amyloid Associated Cytotoxicity

Wang, P., Kouyoumdjian, H., Zhu, D. C., & Huang, X. (2014) · Carbohydrate Research · doi:10.1016/j.carres.2014.07.020 · Cited by 16

Caprospinol: Discovery of a Steroid Drug Candidate to Treat Alzheimer’s Disease Based on 22R‐Hydroxycholesterol Structure and Properties

Papadopoulos, V., & Lecanu, L. (2011) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2011.02167.x · Cited by 23

Dual functions of β-amyloid oligomer and fibril in Cu(II)-induced H2O2 production

Fang, C.-L., Wu, W., Liu, Q. R., Sun, X., Ma, Y., Zhao, Y., & Li, Y. (2010) · Regulatory Peptides · doi:10.1016/j.regpep.2010.05.001 · Cited by 23

Modulators of amyloid protein aggregation and toxicity: EGCG and CLR01

Attar, A., Rahimi, F., & Bitan, G. (2013) · Translational Neuroscience · doi:10.2478/s13380-013-0137-y · Cited by 24

Pramlintide Antagonizes Beta Amyloid (Aβ)- and Human Amylin-Induced Depression of Hippocampal Long-Term Potentiation

Kimura, R., MacTavish, D., Yang, J., Westaway, D. A., & Jhamandas, J. H. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9684-x · Cited by 24

Vitamin D 3 protects against Aβ peptide cytotoxicity in differentiated human neuroblastoma SH- SY5Y cells: A role for S1P1/p38MAPK/ATF4 axis

Pierucci, F., Garcia‐Gil, M., Frati, A., Bini, F., Martinesi, M., Vannini, E., Mainardi, M., Luzzati, F., Peretto, P. M., Caleo, M., et al. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.01.003 · Cited by 24

The Effects of N-terminal Mutations on β-amyloid Peptide Aggregation and Toxicity

Foroutanpay, B. V., Kumar, J., Kang, S., Danaei, N., Westaway, D. A., Sim, V. L., & Kar, S. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.03.014 · Cited by 24

Amyloid-β1–40 Inhibits Amyloid-β1–42 Induced Activation of Cytoplasmic Phospholipase A2 and Synapse Degeneration

Bate, C., & Williams, A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100528 · Cited by 23

Design and synthesis of new theranostic agents for near-infrared imaging of β-amyloid plaques and inhibition of β-amyloid aggregation in Alzheimer's disease

Dao, P., Ye, F., Du, Z. Y., Qian, C., Zhang, K., Dong, C., Meunier, B., & Chen, H. (2017) · Dyes and Pigments · doi:10.1016/j.dyepig.2017.07.071 · Cited by 23

Pirh2 modulates the mitochondrial function and cytochrome c-mediated neuronal death during Alzheimer’s disease

Singh, A., Tiwari, S., & Singh, S. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06662-1 · Cited by 23

Critical role of C-terminal residues of the Alzheimer's associated β-amyloid protein in mediating antiviral activity and modulating viral and bacterial interactions with neutrophils

White, M. R., Kandel, R., Hsieh, I.-N., Luna, X. D., & Hartshorn, K. L. (2018) · PLoS ONE · doi:10.1371/journal.pone.0194001 · Cited by 23

SSH1 impedes SQSTM1/p62 flux and MAPT/Tau clearance independent of CFL (cofilin) activation

Fang, C. C., Woo, J. A., Liu, T., Zhao, X., Cazzaro, S., Yan, Y., Matlack, J. K., Kee, T. R., LePochat, P., & Kang, D. E. (2020) · Autophagy · doi:10.1080/15548627.2020.1816663 · Cited by 22

Agomelatine prevents angiotensin II-induced endothelial and mononuclear cell adhesion

Hong, N., Ye, Z., Lin, Y., Liu, W., Xu, N., & Wang, Y. (2021) · Aging · doi:10.18632/aging.203299 · Cited by 22

Anti-inflammatory Activity of a Polypeptide Fraction From Achyranthes bidentate in Amyloid β Oligomers Induced Model of Alzheimer’s Disease

Ge, X., Wang, Y., Yu, S., Cao, X., Chen, Y., Cheng, Q., & Ding, F. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.716177 · Cited by 22

Co-Ultramicronized Palmitoylethanolamide/Luteolin Restores Oligodendrocyte Homeostasis via Peroxisome Proliferator-Activated Receptor-α in an In Vitro Model of Alzheimer’s Disease

Facchinetti, R., Valenza, M., Gomiero, C., Mancini, G. F., Steardo, L., Campolongo, P., & Scuderi, C. (2022) · Biomedicines · doi:10.3390/biomedicines10061236 · Cited by 23

Dissecting the Molecular Mechanisms of the Co-Aggregation of Aβ40 and Aβ42 Peptides: A REMD Simulation Study

Li, X., Yang, Z., Chen, Y., Zhang, S., Wei, G., & Zhang, L. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c01078 · Cited by 22

The pro-domains of neurotrophins, including BDNF, are linked to Alzheimer's disease through a toxic synergy with Aβ

Lim, J. Y., Reighard, C., & Crowther, D. C. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv130 · Cited by 24

Pathogenic Mutations within the Hydrophobic Domain of the Prion Protein Lead to the Formation of Protease-Sensitive Prion Species with Increased Lethality

Coleman, B. M., Harrison, C. F., Guo, B. B., Masters, C. L., Barnham, K. J., Lawson, V., & Hill, A. F. (2013) · Journal of Virology · doi:10.1128/jvi.02720-13 · Cited by 22

Different electrophysiological actions of 24- and 72-hour aggregated amyloid-beta oligomers on hippocampal field population spike in both anesthetized and awake rats

Orbán, G., Völgyi, K., Juhász, G. D., Penke, B., Kékesi, K. A., Kardos, J., & Czurkó, A. (2010) · Brain Research · doi:10.1016/j.brainres.2010.07.061 · Cited by 22

Earliest events in α-synuclein fibrillation probed with the fluorescence of intrinsic tyrosines

Saraiva, M. A., Jorge, C. D., Santos, H., & Maçanita, A. L. (2015) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2015.11.006 · Cited by 22

(R)‐α‐trifluoromethylalanine containing short peptide in the inhibition of amyloid peptide fibrillation

Botz, A., Gasparik, V., Devillers, E., Hoffmann, A. R. F., Caillon, L., Chelain, E., Lequin, O., Brigaud, T., & Khemtemourian, L. (2015) · Biopolymers · doi:10.1002/bip.22670 · Cited by 18

3D compartmented model to study the neurite-related toxicity of Aβ aggregates included in collagen gels of adaptable porosity

Labour, M.-N., Vigier, S., Lerner, D. A., Marcilhac, A., & Belamie, E. (2016) · Acta Biomaterialia · doi:10.1016/j.actbio.2016.04.001 · Cited by 22

Synthesis and Characterization of Hairpin Mimics that Modulate the Early Oligomerization and Fibrillization of Amyloid β‐Peptide

Vahdati, L., Kaffy, J., Brinet, D., Bernadat, G., Correia, I., Panzeri, S., Fanelli, R., Lequin, O., Taverna, M., Ongeri, S., et al. (2017) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201700010 · Cited by 22

Amyloid, tau, and astrocyte pathology in autosomal-dominant Alzheimer’s disease variants: AβPParc and PSEN1DE9

Lemoine, L., Gillberg, P., Bogdanović, N., Nennesmo, I., Saint‐Aubert, L., Viitanen, M. H., Graff, C., Ingelsson, M., & Nordberg, A. K. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-0817-2 · Cited by 23

Fluorescence resonance energy transfer analysis of apolipoprotein E C-terminal domain and amyloid β peptide (1-42) interaction

Phu, M.-J., Hawbecker, S. K., & Narayanaswami, V. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20503 · Cited by 21

Relative paucity of tau accumulation in the small areas with abundant Aβ42-positive capillary amyloid angiopathy within a given cortical region in the brain of patients with Alzheimer pathology

Oshima, K., Akiyama, H., Tsuchiya, K., Kondo, H., Haga, C., Shimomura, Y., Iseki, E., Uchikado, H., Kato, M., Niizato, K., et al. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0070-z · Cited by 22

Aβ1–42 disrupts the expression and function of KLF2 in Alzheimer’s disease mediated by p53

Wu, C., Li, F., Guo-sheng, H., & Liu, Z. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.01.008 · Cited by 22

Alzheimer’s Amyloid-β Sequesters Caspase-3 in Vitro via Its C-Terminal Tail

Chang, Y., Nguyen, H. L., Shih, Y., Yu, H., Li, M. S., & Chen, Y. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00049 · Cited by 22

Divalent copper ion bound amyloid-β(40) and amyloid-β(42) alloforms are less preferred than divalent zinc ion bound amyloid-β(40) and amyloid-β(42) alloforms

Coskuner‐Weber, O. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-016-1392-5 · Cited by 22

APOE2 protects against Aβ pathology by improving neuronal mitochondrial function through ERRα signaling

Ning, Z., Liu, Y., Wan, M., Zuo, Y., Chen, S., Shi, Z., Xu, Y., Li, H., Ko, H., Zhang, J., et al. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00600-x · Cited by 20

TAR DNA‐binding protein 43 oligomers in physiology and pathology

Lye, Y. S., & Chen, Y. (2022) · IUBMB Life · doi:10.1002/iub.2603 · Cited by 22

Tachykinin Neuropeptides and Amyloid β (25–35) Assembly: Friend or Foe?

Liu, X., Ganguly, P., Jin, Y., Jhatro, M. J., Shea, J., Buratto, S. K., & Bowers, M. T. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c03845 · Cited by 22

Initial stages of beta-amyloid Aβ1−40and Aβ1−42oligomerization observed using fluorescence decay and molecular dynamics analyses of tyrosine

Amaro, M., Kubiak-Ossowska, K., Birch, D. J. S., & Rolinski, O. J. (2013) · Methods and Applications in Fluorescence · doi:10.1088/2050-6120/1/1/015006 · Cited by 21

Development and Expression of Amyloid‐β Peptide 42 in Retinal Ganglion Cells in Rats

Wang, J., Zhu, C., Xu, Y., Liu, B., Wang, M., & Wu, K. (2011) · The Anatomical Record · doi:10.1002/ar.21438 · Cited by 21

Role and regulation of p27 in neuronal apoptosis

Jaiswal, S., & Sharma, P. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13918 · Cited by 21

Oligomeric amyloid β preferentially targets neuronal and not glial mitochondrial‐encoded mRNAs

Mastroeni, D., Nolz, J., Khdour, O. M., Sekar, S., Delvaux, E., Cuyugan, L., Liang, W. S., Hecht, S. M., & Coleman, P. D. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.12.005 · Cited by 21

Mesenchymal Stem Cell-Derived Extracellular Vesicle-Based Therapy for Alzheimer’s Disease: Progress and Opportunity

Chen, Y., Lu, C.-H., Ke, C., & Liu, R.-S. (2021) · Membranes · doi:10.3390/membranes11100796 · Cited by 23

An aminopeptidase from Streptomyces sp. KK565 degrades beta amyloid monomers, oligomers and fibrils

Yoo, C., Ahn, K., Park, J., Kim, M.-J., & Jo, S. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.08.048 · Cited by 20

Fibrillar and Oligomeric β‐Amyloid as Distinct Local Biomarkers for Alzheimer's Disease

Montalto, M., Farrar, G., & Hehir, C. A. T. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1379.023 · Cited by 22

A new naphthalene derivative with anti-amyloidogenic activity as potential therapeutic agent for Alzheimer's disease

Rivera-Marrero, S., Bencomo-Martínez, A., Salazar, E. O., Sablón-Carrazana, M., García-Pupo, L., Zoppolo, F., Arredondo, F., Dapueto, R., Santi, M. D., Kreimerman, I., et al. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115700 · Cited by 20

Antenatal Hypoxia Accelerates the Onset of Alzheimer’s Disease Pathology in 5xFAD Mouse Model

Shen, G., Hu, S. X., Zhao, Z., Zhang, L., & Ma, Q. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00251 · Cited by 20

The Hidden Role of Non-Canonical Amyloid β Isoforms in Alzheimer’s Disease

Busch, L., Eggert, S., Endres, K., & Bufe, B. (2022) · Cells · doi:10.3390/cells11213421 · Cited by 20

Bioinformatics investigation on blood-based gene expressions of Alzheimer's disease revealed ORAI2 gene biomarker susceptibility: An explainable artificial intelligence-based approach

Sekaran, K., Alsamman, A. M., Doss, C. G. P., & Zayed, H. (2023) · Metabolic Brain Disease · doi:10.1007/s11011-023-01171-0 · Cited by 22

Mass spectrometry imaging highlights dynamic patterns of lipid co‐expression with Aβ plaques in mouse and human brains

Huang, H. X., Inglese, P., Tang, J., Yagoubi, R., Correia, G. D. S., der Sluis, V. M. H.-V., Camuzeaux, S., Wu, V., Kopanitsa, M. V., Willumsen, N., et al. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16042 · Cited by 22

Hydrophobic C-Terminal Peptide Analog Aβ31–41 Protects the Neurons from Aβ-Induced Toxicity

Mallesh, R., Khan, J., Gharai, P. K., Arshi, M. U., Garg, S., Gupta, S., & Ghosh, S. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00032 · Cited by 20

Point Mutations in Aβ Induce Polymorphic Aggregates at Liquid/Solid Interfaces

Yates, E. A., Cucco, E. M., & Legleiter, J. A. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn200001k · Cited by 20

Effect of liposome membranes on disaggregation of amyloid β fibrils by dopamine

Vu, H. T., Shimanouchi, T., Ishikawa, D., Matsumoto, T., Yagi, H., Goto, Y., Umakoshi, H., & Kuboi, R. (2012) · Biochemical Engineering Journal · doi:10.1016/j.bej.2012.12.012 · Cited by 20

Physiological Transgene Regulation and Functional Complementation of a Neurological Disease Gene Deficiency in Neurons

Peruzzi, P. P., Lawler, S. E., Senior, S. L., Dmitrieva, N., Edser, P. A. H., Gianni, D., Chiocca, E. A., & Wade‐Martins, R. (2009) · Molecular Therapy · doi:10.1038/mt.2009.64 · Cited by 20

Stability of Aβ (1-42) peptide fibrils as consequence of environmental modifications

Gregori, M., Cassina, V., Brogioli, D., Salerno, D., Kimpe, L. D., Scheper, W., Masserini, M., & Mantegazza, F. (2010) · European Biophysics Journal · doi:10.1007/s00249-010-0619-6 · Cited by 20

Expression of the plant viral protease NIa in the brain of a mouse model of Alzheimer's disease mitigates Aβ pathology and improves cognitive function

Kim, T., Han, H.-E., Kim, H., Lee, J. E., Choi, D., Park, W. J., & Han, P. (2012) · Experimental & Molecular Medicine · doi:10.3858/emm.2012.44.12.082 · Cited by 20

N-benzylcinnamide protects rat cultured cortical neurons from β-amyloid peptide-induced neurotoxicity

Thangnipon, W., Puangmalai, N., Chinchalongporn, V., Jantrachotechatchawan, C., Kitiyanant, N., Soi‐ampornkul, R., Tuchinda, P., & Nobsathian, S. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.09.071 · Cited by 20

NMR structure of the Arctic mutation of the Alzheimer’s Aβ(1–40) peptide docked to SDS micelles

Usachev, K. S., Filippov, A. V., Khairutdinov, B. I., Antzutkin, O. N., & Klochkov, V. V. (2014) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2014.08.030 · Cited by 20

Inhibition of Aβ42 oligomerization in yeast by a PICALM ortholog and certain FDA approved drugs

Park, S.-K., Ratia, K. M., Ba, M. A., Valencik, M. L., & Liebman, S. W. (2016) · Microbial Cell · doi:10.15698/mic2016.02.476 · Cited by 21

Citrullination and deamidation affect aggregation properties of amyloidβ-proteins

Osaki, D., & Hiramatsu, H. (2016) · Amyloid · doi:10.1080/13506129.2016.1240076 · Cited by 22

Immunoglobulin G transport increases in an in vitro blood–brain barrier model with amyloid‐β and with neuroinflammatory cytokines

Mantle, J. L., & Lee, K. H. (2019) · Biotechnology and Bioengineering · doi:10.1002/bit.26967 · Cited by 20

Plasmon-Activated Water Reduces Amyloid Burden and Improves Memory in Animals with Alzheimer’s Disease

Cheng, C., Lin, K., Hong, C., Wu, D., Chang, H., Liu, C.-H., Hsiao, I., Yang, C.-P., Liu, Y., & Hu, C. (2019) · Scientific Reports · doi:10.1038/s41598-019-49731-8 · Cited by 20

Kinetic Transition in Amyloid Assembly as a Screening Assay for Oligomer-Selective Dyes

Barton, J., Arias, D. S., Niyangoda, C., Borjas, G. J., Le, N., Mohamed, S., & Muschol, M. (2019) · Biomolecules · doi:10.3390/biom9100539 · Cited by 20

Fibrillar Aβ1-42 Enhances NMDA Receptor Sensitivity via the Integrin Signaling Pathway

Juhász, G., Barkóczi, B., Vass, G., Datki, Z., Hunya, Á. G., Fülöp, L., Budai, D., Penke, B., & Szegedi, V. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1301 · Cited by 20

Engineering of a peptide probe for β-amyloid aggregates

Aoraha, E., Candreva, J., & Kim, J. R. (2015) · Molecular BioSystems · doi:10.1039/c5mb00280j · Cited by 20

Granular Non-Fibrillar Aggregates and Toxicity in Alzheimer’s Disease

Benseny‐Cases, N., Klementieva, O. L., Malý, J., & Cladera, J. (2012) · Current Alzheimer Research · doi:10.2174/156720512803251129 · Cited by 19

EGb761 protects against Aβ1-42 oligomer-induced cell damage via endoplasmic reticulum stress activation andHsp70 protein expression increase in SH-SY5Y cells

Liu, L., Zhang, C., Kalionis, B., Wan, W., Murthi, P., Chen, C., Li, Y., & Xia, S. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.01.003 · Cited by 20

The Amyloid Hypothesis and the clearance and degradation of Alzheimer's β-peptide

LeVine, H. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6311 · Cited by 20

Copper(ii) and zinc(ii) dependent effects on Aβ42 aggregation: a CD, Th-T and SFM study

Attanasio, F., Bona, P. D., Cataldo, S., Sciacca, M. F. M., Milardi, D., Pignataro, B., & Pappalardo, G. (2013) · New Journal of Chemistry · doi:10.1039/c3nj40999f · Cited by 20

Controlling Amyloid Fibril Properties Via Ionic Liquids: The Representative Case of Ethylammonium Nitrate and Tetramethylguanidinium Acetate on the Amyloidogenesis of Lysozyme

Pillai, V. V. S., Kumari, P., Kolagatla, S., Sakai, V. G., Rudić, S., Rodriguez, B. J., Rubini, M., Tych, K. M., & Benedetto, A. (2022) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.2c01505 · Cited by 19

T cells promote the regeneration of neural precursor cells in the hippocampus of Alzheimer′s disease mice

Da-chuan, X., Liu, J., Ma, Y., Tian, S., Zhang, L., Zhao, M., & Zhang, Y. (2014) · Neural Regeneration Research · doi:10.4103/1673-5374.139481 · Cited by 19

Stability of early-stage amyloid-β(1–42) aggregation species

Coalier, K. A., Paranjape, G. S., Karki, S., & Nichols, M. R. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.08.017 · Cited by 20

Bag5 Protects Neuronal Cells from Amyloid β-induced Cell Death

Guo, K., Li, L., Yin, G., Zi, X., & Liu, L. (2014) · Journal of Molecular Neuroscience · doi:10.1007/s12031-014-0433-1 · Cited by 19

Different effects of soluble and aggregated amyloid β42 on gene/protein expression and enzyme activity involved in insulin and APP pathways

Bartl, J., Meyer, A. H., Brendler, S., Riederer, P., & Grünblatt, E. (2012) · Journal of Neural Transmission · doi:10.1007/s00702-012-0852-5 · Cited by 19

Biological Membranes as Protein Aggregation Matrices and Targets of Amyloid Toxicity

Bucciantini, M., & Cecchi, C. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-756-3_15 · Cited by 19

Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions

Cieplak, A. S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180905 · Cited by 21

Aptamers Selected for Recognizing Amyloid β-Protein—A Case for Cautious Optimism

Rahimi, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030668 · Cited by 18

In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis

Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015

P1‐167: Effects of beta‐amyloid oligomers on neuronal viability and microglial activation

Ferrera, D., Canale, C., Benfenati, F., & Gasparini, L. (2009) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.04.173

Effect of different Aβ1-42 assemblies on neuronal cell viability

Morkūnienė, R., Čižas, P., Budvytytė, R., Valinčius, G., & Borutaitė, V. (2010) · Lithuanian University of Health Sciences

P4–014: Divergent cytotoxic mechanisms of soluble and fibrillar forms of AAY in human cortical neurons

Deshpande, A. M., Mina, E. W., Glabe, C. G., & Busciglio, J. A. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.1752

Fractionation and characterization of oligomeric, protofibrillar and fibrillar forms of β-amyloid peptide

Ward, R. V., JENNINGS, K. H., Jepras, R., Neville, W. A., OWEN, D. E., HAWKINS, J., Christie, G., Davis, J. B., George, A. R., Karran, E. H., et al. (2000) · Biochemical Journal · doi:10.1042/bj3480137 · Cited by 153