In Vitro Characterization of Conditions for Amyloid-β Peptide Oligomerization and Fibrillogenesis

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

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

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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

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Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

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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

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

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Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

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C-Terminal Tetrapeptides Inhibit Aβ42-Induced Neurotoxicity Primarily through Specific Interaction at the N-Terminus of Aβ42

Li, H., Du, Z., Lopes, D. H. J., Fradinger, E. A., Wang, C., & Bitan, G. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200982p · Cited by 43

In vivo Differential Brain Clearance and Catabolism of Monomeric and Oligomeric Alzheimer's Aβ protein

McIntee, F. L., Giannoni, P., Blais, S. P., Sommer, G., Neubert, T. A., Rostagno, A. A., & Ghiso, J. A. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00223 · Cited by 42

Dual effect of chitosan-based nanoparticles on the inhibition of β-amyloid peptide aggregation and disintegration of the preformed fibrils

Jha, A., Ghormade, V., Kolge, H., & Paknikar, K. M. (2019) · Journal of Materials Chemistry B · doi:10.1039/c9tb00162j · Cited by 42

Specific Domains of Aβ Facilitate Aggregation on and Association with Lipid Bilayers

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Controlling Amyloid‐β Peptide(1–42) Oligomerization and Toxicity by Fluorinated Nanoparticles

Saraiva, A. M., Cardoso, I., Pereira, M. D. C., Coelho, M. A. N., Saraiva, M. J., Möhwald, H., & Brezesinski, G. (2010) · ChemBioChem · doi:10.1002/cbic.201000237 · Cited by 41

Quantitative detection of amyloid-β peptides by mass spectrometry: state of the art and clinical applications

Bros, P., Delatour, V., Vialaret, J., Lalère, B., Barthélemy, N. R., Gabelle, A., Lehmann, S., & Hirtz, C. (2015) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm-2014-1048 · Cited by 41

Zn2+-Aβ40 Complexes Form Metastable Quasi-spherical Oligomers That Are Cytotoxic to Cultured Hippocampal Neurons

Solomonov, I., Korkotian, E., Born, B., Feldman, Y., Bitler, A., Rahimi, F., Li, H., Bitan, G., & Sagi, I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.344036 · Cited by 41

The Molecular Mechanism of Amyloid β42 Peptide Toxicity: The Role of Sphingosine Kinase-1 and Mitochondrial Sirtuins

Cieślik, M., Czapski, G. A., & Strosznajder, J. B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137193 · Cited by 43

Neuroprotective effects of liquiritin on cognitive deficits induced by soluble amyloid-β1–42 oligomers injected into the hippocampus

Jia, S., Wu, X., Li, X., Dai, X., Gao, Z., Zheng, L., Zheng, Q., & Sun, Y. (2016) · Journal of Asian Natural Products Research · doi:10.1080/10286020.2016.1201811 · Cited by 41

The mechanisms of flavonoids inhibiting conformational transition of amyloid-β 42 monomer: a comparative molecular dynamics simulation study

Wang, L., Zeng, R., Pang, X., Gu, Q., & Tan, W. (2015) · RSC Advances · doi:10.1039/c5ra12328c · Cited by 40

TGF-β1 is increased in a transgenic mouse model of familial Alzheimer's disease and causes neuronal apoptosis

Salins, P. B., He, Y., Olson, K. L., Glazner, G. W., Kashour, T. S., & Amara, F. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.10.025 · Cited by 41

Distance Measurement between Tyr10 and Met35 in Amyloid β by Site‐Directed Spin‐Labeling ESR Spectroscopy: Implications for the Stronger Neurotoxicity of Aβ42 than Aβ40

Murakami, K., Hara, H., Masuda, Y., Ohigashi, H., & Irie, K. (2007) · ChemBioChem · doi:10.1002/cbic.200700240 · Cited by 40

Differential effect of amyloid beta on the cytochrome P450 epoxygenase activity in rat brain

Sarkar, P., Narayanan, J., & Harder, D. R. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.07.058 · Cited by 42

RNA methyltransferase NSun2 deficiency promotes neurodegeneration through epitranscriptomic regulation of tau phosphorylation

Kim, Y. A., Siddiqui, T., Blaze, J., Coşacak, M. İ., Winters, T., Kumar, A., Tein, E., Sproul, A. A., Teich, A. F., Bartolini, F., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02511-7 · Cited by 44

A Universal Method for Detection of Amyloidogenic Misfolded Proteins

Yam, A. Y.-W., Wang, X., Gao, C. M., Connolly, M. D., Zuckermann, R. N., Bleu, T., Hall, J., Fedynyshyn, J. P., Allauzen, S., Peretz, D., et al. (2011) · Biochemistry · doi:10.1021/bi200215j · Cited by 39

Aberrant activation of neuronal cell cycle caused by dysregulation of ubiquitin ligase Itch results in neurodegeneration

Chauhan, M., Modi, P. K., & Sharma, P. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2647-1 · Cited by 40

An update on the toxicity of Aβ in Alzheimer’s disease

Götz, J. (2008) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s3016 · Cited by 40

Amyloid-β reduces the expression of neuronal FAIM-L, thereby shifting the inflammatory response mediated by TNFα from neuronal protection to death

Carriba, P., Jiménez, S., Navarro, V., Moreno‐González, I., Barneda‐Zahonero, B., Moubarak, R. S., López‐Soriano, J., Gutiérrez, A., Vitórica, J., & Comella, J. X. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.6 · Cited by 40

An Azobenzene Photoswitch Sheds Light on Turn Nucleation in Amyloid-β Self-Assembly

Doran, T. M., Anderson, E. A., Latchney, S. E., Opanashuk, L. A., & Nilsson, B. L. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn2001188 · Cited by 40

Synthetic amyloid-β oligomers drive early pathological progression of Alzheimer’s disease in nonhuman primates

Yue, F., Feng, S., Lu, C., Zhang, T., Tao, G., Liu, J., Yue, C., & Jing, N. (2021) · iScience · doi:10.1016/j.isci.2021.103207 · Cited by 41

Biophysical mapping of TREM2-ligand interactions reveals shared surfaces for engagement of multiple Alzheimer's disease ligands

Greven, J. A., Wydra, J. R., Greer, R. A., Zhi, C., Price, D. A., Svoboda, J. D., Camitta, C. L. M., Washington, M., Leung, D. W., Song, Y., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00795-9 · Cited by 42

Controlled Production of Amyloid β Peptide from a Photo‐Triggered, Water‐Soluble Precursor “Click Peptide“

Taniguchi, A., Skwarczyński, M., Sohma, Y., Okada, T., Ikeda, K., Prakash, H., Mukai, H., Hayashi, Y., Kimura, T., Hirota, S., et al. (2008) · ChemBioChem · doi:10.1002/cbic.200800503 · Cited by 39

Aβ peptide conformation determines uptake and interleukin-1α expression by primary microglial cells

Parvathy, S., Rajadas, J., Ryan, H. S., Vaziri, S., Anderson, L., & Murphy, G. M. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.01.011 · Cited by 39

Amyloid β Fibril Elongation by Monomers Involves Disorder at the Tip

Bacci, M., Vymětal, J., Mihajlovic, M., Caflisch, A., & Vitalis, A. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00662 · Cited by 39

TGF-β1 protection against Aβ1–42-induced hippocampal neuronal inflammation and apoptosis by TβR-I

Fang, X.-X., Sun, G.-L., Zhou, Y., Qiu, Y., & Peng, Y.-P. (2017) · Neuroreport · doi:10.1097/wnr.0000000000000940 · Cited by 39

Rapid initiation of cell cycle reentry processes protects neurons from amyloid-β toxicity

Ippati, S., Deng, Y., van der Hoven, J., Heu, C., van Hummel, A., Chua, S. W., Parić, E., Chan, G., Feiten, A., Fath, T., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2011876118 · Cited by 39

Rapid Assembly of Amyloid-β Peptide at a Liquid/Liquid Interface Produces Unstable β-Sheet Fibers

Nichols, M. R., Moss, M. A., Reed, D. K., Hoh, J. H., & Rosenberry, T. L. (2004) · Biochemistry · doi:10.1021/bi048846t · Cited by 39

Modulation of Amyloid β Peptide1-42 Cytotoxicity and Aggregation in Vitro by Glucose and Chondroitin Sulfate

Fernàndez‐Busquets, X., Ponce, J., Bravo, R., Arimon, M., Martiáñez, T., Gella, A., Cladera, J., & Durany, N. (2010) · Current Alzheimer Research · doi:10.2174/156720510791383787 · Cited by 38

Macrophage colony stimulatory factor and interferon‐γ trigger distinct mechanisms for augmentation of β‐amyloid‐induced microglia‐mediated neurotoxicity

Li, M., Pisalyaput, K., Galvan, M. D., & Tenner, A. J. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02765.x · Cited by 38

Novel curcumin derivatives as potent inhibitors of amyloid β aggregation

Yanagisawa, D., Taguchi, H., Morikawa, S., Kato, T., Hirao, K., Shirai, N., & Tooyama, I. (2015) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2015.10.009 · Cited by 38

Simulations of monomeric amyloid β-peptide (1–40) with varying solution conditions and oxidation state of Met35: Implications for aggregation

Brown, A. M., Lemkul, J. A., Schaum, N., & Bevan, D. R. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.01.002 · Cited by 39

Genetic Inhibition of Phosphorylation of the Translation Initiation Factor eIF2α Does Not Block Aβ-Dependent Elevation of BACE1 and APP Levels or Reduce Amyloid Pathology in a Mouse Model of Alzheimer’s Disease

Sadleir, K. R., Eimer, W. A., Kaufman, R. J., Osten, P., & Vassar, R. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101643 · Cited by 40

Cajaninstilbene Acid Ameliorates Cognitive Impairment Induced by Intrahippocampal Injection of Amyloid-β1–42 Oligomers

Wang, L.-S., Xue, T., Liu, X., Zhou, Y., Zhang, M.-D., Liao, Y., Pan, R., & Chang, Q. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01084 · Cited by 38

Effect of Aβ Oligomers on Neuronal APP Triggers a Vicious Cycle Leading to the Propagation of Synaptic Plasticity Alterations to Healthy Neurons

Rolland, M., Powell, R., Jacquier‐Sarlin, M. R., Boisseau, S., Reynaud-Dulaurier, R., Hernández, J. M., André, L., Borel, E., Buisson, A., & Lanté, F. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.2501-19.2020 · Cited by 41

Out-of-Register Parallel β-Sheets and Antiparallel β-Sheets Coexist in 150-kDa Oligomers Formed by Amyloid-β(1–42)

Gao, Y., Guo, C., Watzlawik, J. O., Randolph, P. S., Lee, E. J., Huang, D., Stagg, S. M., Zhou, H., Rosenberry, T. L., & Paravastu, A. K. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.05.018 · Cited by 38

Advances on the Understanding of the Origins of Synaptic Pathology in AD

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Ac‐LPFFD‐Th: A Trehalose‐Conjugated Peptidomimetic as a Strong Suppressor of Amyloid‐β Oligomer Formation and Cytotoxicity

Sinopoli, A., Giuffrida, A., Tomasello, M. F., Giuffrida, M. L., Leone, M., Attanasio, F., Caraci, F., Bona, P. D., Николаевна, Н. И., Saviano, M., et al. (2016) · ChemBioChem · doi:10.1002/cbic.201600243 · Cited by 38

In vitroOligomerization and Fibrillogenesis of Amyloid-beta Peptides

Benseny‐Cases, N., Klementieva, O., & Cladera, J. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5416-4_3 · Cited by 39

CDK5 Is Essential for Soluble Amyloid β-Induced Degradation of GKAP and Remodeling of the Synaptic Actin Cytoskeleton

Roselli, F., Livrea, P., & Almeida, O. F. X. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023097 · Cited by 38

Overcoming synthetic Aβ peptide aging: a new approach to an age-old problem

Manzoni, C., Colombo, L., Messa, M., Cagnotto, A., Cantú, L., Favero, E. D., & Salmona, M. (2009) · Amyloid · doi:10.1080/13506120902879848 · Cited by 37

Lynx1 and Aβ1–42 bind competitively to multiple nicotinic acetylcholine receptor subtypes

Thomsen, M. S., Arvaniti, M., Jensen, M. M., Shulepko, M. A., Dolgikh, D. A., Pinborg, L. H., Härtig, W., Lyukmanova, E. N., & Mikkelsen, J. D. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.06.009 · Cited by 37

Size-Dependent Interaction of Amyloid β Oligomers with Brain Total Lipid Extract Bilayer─Fibrillation Versus Membrane Destruction

Mrđenović, D., Majewska, M., Pieta, I. S., Bernatowicz, P., Nowakowski, R., Kutner, W., Lipkowski, J., & Pięta, P. (2019) · Langmuir · doi:10.1021/acs.langmuir.9b01645 · Cited by 39

A Brain-Targeting Bispecific-Multivalent Antibody Clears Soluble Amyloid-Beta Aggregates in Alzheimer's Disease Mice

Rofo, F., Meier, S. R., Metzendorf, N. G., Morrison, J. I., Petrovic, A., Syvänen, S., Sehlin, D., & Hultqvist, G. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01283-y · Cited by 41

Use of surface plasmon resonance to study the elongation kinetics and the binding properties of the highly amyloidogenic Aβ1–42 peptide, synthesized by depsi-peptide technique

Stravalaci, M., Beeg, M., Salmona, M., & Gobbi, M. (2010) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2010.10.038 · Cited by 36

‘O-Acyl isopeptide method’ for the efficient preparation of amyloid β peptide 1–42 mutants

Sohma, Y., Chiyomori, Y., Kimura, M., Fukao, F., Taniguchi, A., Hayashi, Y., Kimura, T., & Kiso, Y. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.06.037 · Cited by 38

Effects of Amyloid β-Peptides on the Lysis Tension of Lipid Bilayer Vesicles Containing Oxysterols

Kim, D. H., & Frangos, J. A. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.114983 · Cited by 37

LPYFDa Neutralizes Amyloid-β-Induced Memory Impairment and Toxicity

Granic, I., Masman, M. F., Mulder, C. K., Nijholt, I. M., Naudé, P., de Haan, A., Borbély, E., Penke, B., Luiten, P. G. M., & Eisel, U. L. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1297 · Cited by 37

Effect of agitation on the peptide fibrillization: Alzheimer's amyloid‐β peptide 1‐42 but not amylin and insulin fibrils can grow under quiescent conditions

Tiiman, A., Noormägi, A., Friedemann, M., Krishtal, J., Palumaa, P., & Tõugu, V. (2013) · Journal of Peptide Science · doi:10.1002/psc.2513 · Cited by 36

Calpain inhibition prevents amyloid-β-induced neurodegeneration and associated behavioral dysfunction in rats

Granic, I., Nyakas, C. J., Luiten, P. G. M., Eisel, U. L. M., Halmy, L. G., Groß, G., Schoemaker, H., Möller, A., & Nimmrich, V. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.07.013 · Cited by 36

An integrated strategy to correlate aggregation state, structure and toxicity of Aß 1–42 oligomers

Bisceglia, F., Natalello, A., Serafini, M. M., Colombo, R., Verga, L., Lanni, C., & Lorenzi, E. D. (2018) · Talanta · doi:10.1016/j.talanta.2018.05.062 · Cited by 37

Immunosenescence as a convergence pathway in neurodegeneration

Mohapatra, L., Mishra, D. K., Tripathi, A. S., & Parida, S. K. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110521 · Cited by 38

Deficits in the miRNA-34a-regulated endogenous TREM2 phagocytosis sensor-receptor in Alzheimer’s disease (AD); an update

Bhattacharjee, S., Zhao, Y., & Lukiw, W. J. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00116 · Cited by 34

H2O2 and PAF mediate Aβ1-42-induced Ca2+ dyshomeostasis that is blocked by EGb761

Shi, C., Wu, F., & Xu, J. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.03.016 · Cited by 35

Switchable electrochemical aptasensor for amyloid-β oligomers detection based on triple helix switch coupling with AuNPs@CuMOF labeled signaling displaced-probe

Wang, X., Li, L., Gu, X., Yu, B., & Jiang, M. (2021) · Microchimica Acta · doi:10.1007/s00604-021-04704-5 · Cited by 35

Biological and methodological complexities of beta‐amyloid peptide: Implications for Alzheimer’s disease research

Matuszyk, M. M., Garwood, C. J., Ferraiuolo, L., Simpson, J. E., Staniforth, R. A., & Wharton, S. B. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15538 · Cited by 37

Hexafluoroisopropanol induces self‐assembly of β‐amyloid peptides into highly ordered nanostructures

Pachahara, S. K., Chaudhary, N., Subbalakshmi, C., & Nagaraj, R. (2012) · Journal of Peptide Science · doi:10.1002/psc.2391 · Cited by 33

Uncoupling of M1 muscarinic receptor/G-protein interaction by amyloid β1–42

Janíčková, H., Rudajev, V., Zimčík, P., Jakubík, J., Tanila, H., El‐Fakahany, E. E., & Doležal, V. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2012.11.014 · Cited by 37

Randomization of Amyloid‐β‐Peptide(1‐42) Conformation by Sulfonated and Sulfated Nanoparticles Reduces Aggregation and Cytotoxicity

Saraiva, A. M., Cardoso, I., Saraiva, M. J., Tauer, K., Pereira, M. D. C., Coelho, M. A. N., Möhwald, H., & Brezesinski, G. (2010) · Macromolecular Bioscience · doi:10.1002/mabi.200900448 · Cited by 36

Circular dichroism and aggregation studies of amyloid beta (11-8) fragment and its variants.

Juszczyk, P., Kołodziejczyk, A. S., & Grzonka, Z. (2005) · Acta Biochimica Polonica · doi:10.18388/abp.2005_3455 · Cited by 40

Correction: Metabolic changes and inflammation in cultured astrocytes from the 5xFAD mouse model of Alzheimer's disease: Alleviation by pantethine

van Gijsel‐Bonnello, M., Baranger, K., Benech, P., Rivera, S., Khrestchatisky, M., Reggi, M. L. D., & Gharib, B. (2018) · PLoS ONE · doi:10.1371/journal.pone.0194586 · Cited by 35

High-affinity Anticalins with aggregation-blocking activity directed against the Alzheimer β-amyloid peptide

Rauth, S., Hinz, D., Borger, M. A., Uhrig, M., Mayhaus, M., Riemenschneider, M. J., & Skerra, A. (2016) · Biochemical Journal · doi:10.1042/bcj20160114 · Cited by 35

Detection of amyloid β oligomers toward early diagnosis of Alzheimer's disease

Hwang, S., Chan, H. K., Sorci, M., Deventer, J. A. V., Wittrup, K. D., Belfort, G., & Walt, D. R. (2018) · Analytical Biochemistry · doi:10.1016/j.ab.2018.09.011 · Cited by 36

SAR228810: an antibody for protofibrillar amyloid β peptide designed to reduce the risk of amyloid-related imaging abnormalities (ARIA)

Pradier, L., Blanchard-Brégeon, V., Bohme, A., Debeir, T., Ménager, J., Benoit, P., Barnéoud, P., Taupin, V., Bertrand, P., Dugay, P., et al. (2018) · Alzheimer s Research & Therapy · doi:10.1186/s13195-018-0447-y · Cited by 37

Co-activation of selective nicotinic acetylcholine receptors is required to reverse beta amyloid–induced Ca2+ hyperexcitation

Sun, J. L., Stokoe, S. A., Roberts, J. P., Sathler, M. F., Nip, K., Shou, J., Ko, K. H., Tsunoda, S., & Kim, S. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.09.005 · Cited by 36

Effects of Aβ-derived peptide fragments on fibrillogenesis of Aβ

Abedin, F., Kandel, N., & Tatulian, S. A. (2021) · Scientific Reports · doi:10.1038/s41598-021-98644-y · Cited by 34

Kinetic studies of inhibition of the amyloid beta (1–42) aggregation using a ferrocene-tagged β-sheet breaker peptide

Zhang, L., Yagnik, G. B., Peng, Y., Wang, J., Xu, H. H., Hao, Y., Liu, Y., & Zhou, F. (2012) · Analytical Biochemistry · doi:10.1016/j.ab.2012.11.025 · Cited by 34

Toxicity in Rat Primary Neurons through the Cellular Oxidative Stress Induced by the Turn Formation at Positions 22 and 23 of Aβ42

Izuo, N., Kume, T., Sato, M., Murakami, K., Irie, K., Izumi, Y., & Akaike, A. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300033k · Cited by 34

Myelin Basic Protein Binds to and Inhibits the Fibrillar Assembly of Aβ42 in Vitro

Hoos, M. D., Ahmed, M., Smith, S. O., & Nostrand, W. E. V. (2009) · Biochemistry · doi:10.1021/bi900037s · Cited by 37

Resting microglia react to Aβ42 fibrils but do not detect oligomers or oligomer-induced neuronal damage

Ferrera, D., Mazzaro, N., Canale, C., & Gasparini, L. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.05.023 · Cited by 33

Inhibition of poly(ADP-ribose) polymerase-1 alters expression of mitochondria-related genes in PC12 cells: relevance to mitochondrial homeostasis in neurodegenerative disorders

Czapski, G. A., Cieślik, M., Wencel, P. L., Wójtowicz, S., Strosznajder, R. P., & Strosznajder, J. B. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.11.003 · Cited by 33

Opposite Effects of Low and High Doses of Aβ42 on Electrical Network and Neuronal Excitability in the Rat Prefrontal Cortex

Wang, Y., Zhang, G., Zhou, H., Barakat, A., & Querfurth, H. W. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008366 · Cited by 34

Interaction between Prion Protein and Aβ Amyloid Fibrils Revisited

Nieznański, K., Surewicz, K. A., Chen, S., Nieznańska, H., & Surewicz, W. K. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500019c · Cited by 33

Proteolytic Antibody Light Chains Alter β-Amyloid Aggregation and Prevent Cytotoxicity

Liu, R., McAllister, C., Lyubchenko, Y. L., & Sierks, M. R. (2004) · Biochemistry · doi:10.1021/bi0492354 · Cited by 34

Turn Nucleation Perturbs Amyloid β Self-Assembly and Cytotoxicity

Doran, T. M., Anderson, E. A., Latchney, S. E., Opanashuk, L. A., & Nilsson, B. L. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.055 · Cited by 32

The role of caffeine as an inhibitor in the aggregation of amyloid forming peptides: a unified molecular dynamics simulation and experimental study

Sharma, B., Kalita, S., Paul, A., Mandal, B., & Paul, S. (2016) · RSC Advances · doi:10.1039/c6ra17602j · Cited by 32

Lipid microdomain modification sustains neuronal viability in models of Alzheimer’s disease

Herzer, S., Meldner, S., Rehder, K. F., Gröne, H., & Nordström, V. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0354-z · Cited by 33

An acute functional screen identifies an effective antibody targeting amyloid-β oligomers based on calcium imaging

Wang, X., Kastanenka, K. V., Arbel‐Ornath, M., Commins, C., Kuzuya, A., Lariviere, A., Krafft, G. A., Hefti, F. F., Jerecìć, J., & Bacskai, B. J. (2018) · Scientific Reports · doi:10.1038/s41598-018-22979-2 · Cited by 32

Keto form of curcumin derivatives strongly binds to Aβ oligomers but not fibrils

Yanagisawa, D., Kato, T., Taguchi, H., Shirai, N., Hirao, K., Sogabe, T., Tomiyama, T., Gamo, K., Hirahara, Y., Kitada, M., et al. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.120686 · Cited by 32

A New Method to Measure Cellular Toxicity of Non-Fibrillar and Fibrillar Alzheimer's Aβ Using Yeast

Bharadwaj, P., Waddington, L. J., Varghese, J. N., & Macreadie, I. G. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-13204 · Cited by 34

Hematopoietic MyD88-adaptor Protein Acts as a Natural Defense Mechanism for Cognitive Deficits in Alzheimer’s Disease

Michaud, J.-P., Richard, K. L., & Rivest, S. (2012) · Stem Cell Reviews and Reports · doi:10.1007/s12015-012-9356-9 · Cited by 32

TrkA pathway activation induced by amyloid-beta (Abeta)

Bulbarelli, A., Lonati, E., Cazzaniga, E., Re, F., Sesana, S., Barisani, D., Sancini, G., Mutoh, T., & Masserini, M. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.12.006 · Cited by 32

Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis

Shigemitsu, Y., & Hiroaki, H. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvx056 · Cited by 34

Overview on Rodent Models of Alzheimer's Disease

Dodart, J., & May, P. C. (2005) · Current Protocols in Neuroscience · doi:10.1002/0471142301.ns0922s33 · Cited by 32

The CCAAT/enhancer binding protein (C/EBP) δ is differently regulated by fibrillar and oligomeric forms of the Alzheimer amyloid-β peptide

Ramberg, V., Tracy, L. M., Samuelsson, M., Nilsson, L. N. G., & Iverfeldt, K. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-34 · Cited by 33

Aβ Inhibition of Ionic Conductance in Mouse Basal Forebrain Neurons Is Dependent upon the Cellular Prion Protein PrPC

Alier, K. A., Ma, L., Yang, J., Westaway, D. A., & Jhamandas, J. H. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4367-11.2011 · Cited by 30

Laser-Induced Liquid Bead Ion Desorption Mass Spectrometry: An Approach to Precisely Monitor the Oligomerization of the β-Amyloid Peptide

Cernescu, M., Stark, T., Kalden, E., Kurz, C., Leuner, K., Deller, T., Göbel, M., Eckert, G. P., & Brutschy, B. (2012) · Analytical Chemistry · doi:10.1021/ac300258m · Cited by 30

Structural conformation and self‐assembly process of p31‐43 gliadin peptide in aqueous solution. Implications for celiac disease

Herrera, M. G., Castro, M. F. G., Prieto, E. D., Barrera, E., Dodero, V. I., Pantano, S., & Chirdo, F. G. (2019) · FEBS Journal · doi:10.1111/febs.15109 · Cited by 31

Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: Application to Aβ(1‐40) fibrillogenesis

Qi, W., Zhang, A., Patel, D. A., Lee, S., Harrington, J. L., Zhao, L., Schaefer, D., Good, T. A., & Fernández, E. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.21846 · Cited by 31

Amyloid-β fibril formation is not necessarily required for microglial activation by the peptides

Hashioka, S., Monji, A., Ueda, T., Kanba, S., & Nakanishi, H. (2005) · Neurochemistry International · doi:10.1016/j.neuint.2005.05.001 · Cited by 30

IMM-H004, a novel coumarin derivative compound, protects against amyloid beta-induced neurotoxicity through a mitochondrial-dependent pathway

Song, X., Hu, J., Sun, M., Li, Z. P., Wu, D. H., Ji, H.-L., Yuan, Y., Zhu, Z., Han, N., Liu, G., et al. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.02.049 · Cited by 30

Controlled aggregation of peptide–DNA hybrids into amyloid-like fibrils

Abraham, J. N., Gour, N., Bolisetty, S., Mezzenga, R., & Nardin, C. (2015) · European Polymer Journal · doi:10.1016/j.eurpolymj.2015.02.009 · Cited by 30

Ex Situ Atomic Force Microscopy Analysis of β-Amyloid Self-Assembly and Deposition on a Synthetic Template

Ha, C., & Park, C. B. (2006) · Langmuir · doi:10.1021/la0601511 · Cited by 30

Hierarchical and ultra-sensitive amyloid beta oligomer sensor for practical applications

Qin, J., Kim, S., Cho, M., & Lee, Y. (2020) · Chemical Engineering Journal · doi:10.1016/j.cej.2020.126055 · Cited by 31

Beta-Amyloid Instigates Dysfunction of Mitochondria in Cardiac Cells

Jang, S., Chapa‐Dubocq, X. R., Parodi‐Rullán, R. M., Fossati, S., & Javadov, S. A. (2022) · Cells · doi:10.3390/cells11030373 · Cited by 30

Amyloid beta1-42 peptide regulates microtubule stability independently of tau

Pianu, B., Lefort, R., Thuiliere, L., Tabourier, E., & Bartolini, F. (2014) · Journal of Cell Science · doi:10.1242/jcs.143750 · Cited by 30

Quantifying Prefibrillar Amyloids in vitro by Using a “Thioflavin‐Like” Spectroscopic Method

Reinke, A. A., Abulwerdi, G. A., & Gestwicki, J. E. (2010) · ChemBioChem · doi:10.1002/cbic.201000358 · Cited by 30

Dopamine release in prefrontal cortex in response to β-amyloid activation of α7∗ nicotinic receptors

Wu, J., Khan, G. M., & Nichols, R. A. (2007) · Brain Research · doi:10.1016/j.brainres.2007.08.079 · Cited by 30

Involvement of Intracellular and Mitochondrial Aβ in the Ameliorative Effects of Huperzine A against Oligomeric Aβ42-Induced Injury in Primary Rat Neurons

Lei, Y., Yang, L., Ye, C. Y., Qin, M. Y., Yang, H. Y., Jiang, H. L., Tang, X. C., & Zhang, H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128366 · Cited by 30

Probing Amyloid-Beta Fibril Stability by Increasing Ionic Strengths

Zidar, J., & Merzel, F. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp109025b · Cited by 30

Inhibition of Familial Cerebral Amyloid Angiopathy Mutant Amyloid β-Protein Fibril Assembly by Myelin Basic Protein

Hoos, M. D., Ahmed, M., Smith, S. O., & Nostrand, W. E. V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m603494200 · Cited by 30

Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability

Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452

Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils

Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111

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

The Alzheimer's Amyloid-β(1–42) Peptide Forms Off-Pathway Oligomers and Fibrils That Are Distinguished Structurally by Intermolecular Organization

Tay, W. M., Huang, D., Rosenberry, T. L., & Paravastu, A. K. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.04.003 · Cited by 111

Conformational Differences between Two Amyloid β Oligomers of Similar Size and Dissimilar Toxicity

Ladiwala, A. R. A., Litt, J., Kane, R. S., Aucoin, D., Smith, S. O., Ranjan, S., Davis, J., Nostrand, W. E. V., & Tessier, P. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.329763 · Cited by 228