The DOI matches its Crossref record; 69 of the 71 references it cites were found in a registry or an index.
Oligomeric and Fibrillar Species of Amyloid-β Peptides Differentially Affect Neuronal Viability
Open accessAbstract
Genetic evidence predicts a causative role for amyloid-beta (A beta) in Alzheimer's disease. Recent debate has focused on whether fibrils (amyloid) or soluble oligomers of A beta are the active species that contribute to neurodegeneration and dementia. We developed two aggregation protocols for the consistent production of stable oligomeric or fibrillar preparations of A beta-(1-42). Here we report that oligomers inhibit neuronal viability 10-fold more than fibrils and approximately 40-fold more than unaggregated peptide, with oligomeric A beta-(1-42)-induced inhibition significant at 10 nm. Under A beta-(1-42) oligomer- and fibril-forming conditions, A beta-(1-40) remains predominantly as unassembled monomer and had significantly less effect on neuronal viability than preparations of A beta-(1-42). We applied the aggregation protocols developed for wild type A beta-(1-42) to A beta-(1-42) with the Dutch (E22Q) or Arctic (E22G) mutations. Oligomeric preparations of the mutations exhibited extensive protofibril and fibril formation, respectively, but were not consistently different from wild type A beta-(1-42) in terms of inhibition of neuronal viability. However, fibrillar preparations of the mutants appeared larger and induced significantly more inhibition of neuronal viability than wild type A beta-(1-42) fibril preparations. These data demonstrate that protocols developed to produce oligomeric and fibrillar A beta-(1-42) are useful in distinguishing the structural and functional differences between A beta-(1-42) and A beta-(1-40) and genetic mutations of A beta-(1-42).
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In addition, the MOAB-2-based oA42 ELISA detects oligomeric but not monomeric A42 using synthetic preparations characterized previously by our laboratory (data not shown) (47,48).”
From APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease (2012) · cites this paper as [47]
In the citing paper
“The 48 h total incubation leads to mature Aβ42 fibrils, as observed by TEM (Figure 10, panel a) while the Western blot shows the presence of higher order Aβ42 oligomers (Figure 10, lane a), likely due to an assembly-disassembly equilibrium that is established for mature Aβ fibrils.89–91”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [90]
In the citing paper
“However, this approach may not be optimal for the Aβ42 peptide, given the increased toxicity observed for the soluble Aβ42 oligomers.90”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [90]
In the citing paper
“Finally, in neurons, PCSK9 overexpression led to a worsening of neurotoxicity induced by different aggregation forms of Aβ, which have previously been demonstrated to have toxic effects in these cells [31,52].”
From PCSK9 affects astrocyte cholesterol metabolism and reduces neuron cholesterol supplying in vitro: potential implications in Alzheimer’s disease (2022) · cites this paper as [52]
In the citing paper
“All A preparations used were similar to those characterized previously (24) in that they contain monomers and oligomers of A but do not contain fibrils (see supplemental Fig. 1, A and B).”
From Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E (2007) · cites this paper as [24]
Citations
Cites
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
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
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
Self-citationNeurotrophic 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
Saudou, F., Finkbeiner, S. M., Devys, D., & Greenberg, M. E. (1998) · Cell · doi:10.1016/s0092-8674(00)81782-1 · Cited by 1,598
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
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
Flagged first, then by citations
2 of the 71 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–200 of 1,002
Epidermal growth factor receptor is a preferred target for treating Amyloid-β–induced memory loss
Wang, L., Chiang, H.-C., Wu, W., Liang, B., Xie, Z., Yao, X., Ma, W., Du, S., & Zhong, Y. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208011109 · Cited by 190
Alberdi, E. M., Wyssenbach, A., Alberdi, M., Sánchez‐Gómez, M. V., Cavaliere, F., Rodriguez, J. J., Verkhratsky, A., & Matute, C. (2013) · Aging Cell · doi:10.1111/acel.12054 · Cited by 197
Kim, J., Dh, K., Jh, K., Lee, D., Hb, J., Sj, K., Kim, S., Yj, Y., Eh, L., Sj, C., et al. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.140 · Cited by 190
Methylene Blue Inhibits Amyloid Aβ Oligomerization by Promoting Fibrillization
Necula, M., Breydo, L., Milton, S., Kayed, R., van der Veer, W. E., Tone, P., & Glabe, C. G. (2007) · Biochemistry · doi:10.1021/bi700411k · Cited by 213
Effects of Grape Seed-derived Polyphenols on Amyloid β-Protein Self-assembly and Cytotoxicity*
Ono, K., Condron, M. M., Ho, L., Wang, J., Zhao, W., Pasinetti, G. M., & Teplow, D. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806154200 · Cited by 190
Glabe, C. C. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_8 · Cited by 193
S100 Proteins in Alzheimer’s Disease
Cristóvão, J. S., & Gomes, C. M. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00463 · Cited by 188
HIV-1 Tat inhibits neprilysin and elevates amyloid β
Rempel, H. C., & Pulliam, L. (2005) · AIDS · doi:10.1097/00002030-200501280-00004 · Cited by 186
Fradinger, E. A., Monien, B. H., Urbanc, B., Lomakin, A., Tan, M., Li, H., Spring, S. M., Condron, M. M., Cruz, L., Xie, C.-W., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807163105 · Cited by 189
The Oxidative Stress Metabolite 4-Hydroxynonenal Promotes Alzheimer Protofibril Formation
Siegel, S. J., Bieschke, J., Powers, E. T., & Kelly, J. W. (2007) · Biochemistry · doi:10.1021/bi061853s · Cited by 186
Ferreira, I. L., Bajouco, M., Mota, S. I., Auberson, Y. P., Oliveira, C. R., & Rego, A. C. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.11.008 · Cited by 196
Knowles, J. K., Rajadas, J., Nguyen, T.-V. V., Yang, T., LeMieux, M. C., Vander Griend, L., Ishikawa, C., Massa, S. M., Wyss-Coray, T., & Longo, F. M. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.0620-09.2009 · Cited by 184
Solution State Characterization of Amyloid β-Derived Diffusible Ligands
Hepler, R. W., Grimm, K. M., Nahas, D. D., Breese, R., Chen-Dodson, E., Acton, P. J., Keller, P. M., Yeager, M. D., Wang, H., Shughrue, P. J., et al. (2006) · Biochemistry · doi:10.1021/bi061850f · Cited by 182
Garzon, D. J., & Fahnestock, M. L. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.5053-06.2007 · Cited by 182
Oligomeric amyloid-β peptide disrupts phosphatidylinositol-4,5-bisphosphate metabolism
Berman, D. E., Dall'Armi, C., Voronov, S. V., McIntire, L. B. J., Zhang, H., Moore, A. Z., Staniszewski, A., Arancio, O., Kim, T.-W., & Di Paolo, G. (2008) · Nature Neuroscience · doi:10.1038/nn.2100 · Cited by 199
Oliveira, T. G., Chan, R., Tian, H., Laredo, M., Shui, G., Staniszewski, A., Zhang, H., Wang, L., Kim, T., Duff, K., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3317-10.2010 · Cited by 179
Interactions between the amyloid and cholinergic mechanisms in Alzheimer's disease
Pákáski, M., & Kalman, J. L. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.06.005 · Cited by 191
Walker, D. G., Link, J., Lue, L., Dalsing-Hernandez, J. E., & Boyes, B. E. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.0705377 · Cited by 183
Gu, Z., Liu, W., & Yan, Z. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806508200 · Cited by 185
Rolleston, H. D. (2009) · Cambridge University Press eBooks · doi:10.1017/cbo9780511693632.005 · Cited by 179
Increased Neurogenesis in Young Transgenic Mice Overexpressing Human APPSw,Ind
López-Toledano, M. A., & Shelanski, M. L. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-12304 · Cited by 179
Activation of PERK Signaling Attenuates Aβ-Mediated ER Stress
Lee, D. Y., Lee, K., Lee, H. J., Kim, D. H., Noh, Y. H., Yu, K., Jung, H. Y., Lee, S. H., Lee, J., Youn, Y. C., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010489 · Cited by 175
Udan, M. L. D., Ajit, D., Crouse, N. R., & Nichols, M. R. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05001.x · Cited by 179
A dual role for apolipoprotein e in neuroinflammation: anti- and pro-inflammatory activity
Guo, L., LaDu, M. J., & Van Eldik, L. J. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:23:3:205 · Cited by 175
Amyloid beta mediates memory formationPreprint
García‐Osta, A., & Alberini, C. M. (2009) · Learning & Memory · doi:10.1101/lm.1310209 · Cited by 185
Matsuzaki, K. (2014) · Accounts of Chemical Research · doi:10.1021/ar500127z · Cited by 173
Insight into Amyloid Structure Using Chemical Probes
Reinke, A. A., & Gestwicki, J. E. (2011) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2011.01110.x · Cited by 173
Hu, Y., Xu, P., Pigino, G. F., Brady, S. T., Larson, J., & Lazarov, O. (2010) · The FASEB Journal · doi:10.1096/fj.09-136945 · Cited by 176
Wan, W., Cao, L., Liu, L., Zhang, C., Kalionis, B., Tai, X., Li, Y., & Xia, S. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13122 · Cited by 169
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 166
Bode, D. C., Freeley, M., Nield, J., Palma, M., & Viles, J. H. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ac118.007195 · Cited by 166
Conformation‐Dependent Anti‐Amyloid Oligomer Antibodies
Kayed, R., & Glabe, C. G. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)13017-7 · Cited by 167
Li, Q., Zhao, H., Zhang, Z. F., Liu, Z. G., Pei, X., Wang, J. B., & Li, Y. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.07.014 · Cited by 165
Tai, L. M., Bilousova, T., Jungbauer, L., Roeske, S. K., Youmans, K. L., Yu, C., Poon, W. W., Cornwell, L. B., Miller, C. A., Vinters, H. V., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442103 · Cited by 165
Self-citationNielsen, H. M., Mulder, S. D., Beliën, J. A. M., Musters, R. J. P., Eikelenboom, P., & Veerhuis, R. (2010) · Glia · doi:10.1002/glia.21004 · Cited by 170
Chong, Y. H., Shin, Y. J., Lee, E. O., Kayed, R., Glabe, C. G., & Tenner, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601016200 · Cited by 165
Intraneuronal Aβ detection in 5xFAD mice by a new Aβ-specific antibody
Youmans, K. L., Tai, L. M., Kanekiyo, T., Stine Jr, W. B., Michon, S.-C., Nwabuisi-Heath, E., Manelli, A. M., Fu, Y., Riordan, S., Eimer, W. A., et al. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-8 · Cited by 164
Self-citationAlzheimers Disease and Retinal Neurodegeneration
Guo, L., Duggan, J., & Cordeiro, M. F. (2010) · Current Alzheimer Research · doi:10.2174/156720510790274491 · Cited by 164
A Molecular Switch in Amyloid Assembly: Met35and Amyloid β-Protein Oligomerization
Bitan, G., Tarus, B., Vollers, S. S., Lashuel, H. A., Condron, M. M., Straub, J. E., & Teplow, D. B. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0349296 · Cited by 158
Mizuno, T., Doi, Y., Mizoguchi, H., Jin, S., Noda, M., Sonobe, Y., Takeuchi, H., & Suzumura, A. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2011.06.011 · Cited by 159
CCL11 enhances excitotoxic neuronal death by producing reactive oxygen species in microglia
Parajuli, B., Horiuchi, H., Mizuno, T., Takeuchi, H., & Suzumura, A. (2015) · Glia · doi:10.1002/glia.22892 · Cited by 163
Grimm, M. O. W., Mett, J., Stahlmann, C. P., Haupenthal, V. J., Zimmer, V. C., & Hartmann, T. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00098 · Cited by 170
Differences in β-strand Populations of Monomeric Aβ40 and Aβ42
Ball, K. A., Phillips, A. H., Wemmer, D. E., & Head-Gordon, T. L. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.04.056 · Cited by 157
Modarresi, F., Faghihi, M. A., Patel, N. S., Sahagan, B. G., Wahlestedt, C., & López-Toledano, M. A. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/929042 · Cited by 154
Rangachari, V., Moore, B. D., Reed, D. K., Sonoda, L. K., Bridges, A. W., Conboy, E. E., Hartigan, D., & Rosenberry, T. L. (2007) · Biochemistry · doi:10.1021/bi701213s · Cited by 156
Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins
Murphy, R. M. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.12.014 · Cited by 157
Liu, R. T., Gao, J., Cao, S., Sandhu, N., Cui, J. Z., Chou, C. L., Fang, E., & Matsubara, J. A. (2013) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.12-10849 · Cited by 152
He, N., Jin, W.-L., Lok, K.-H., Wang, Y., Yin, M., & Wang, Z.-J. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.437 · Cited by 151
The PI3K-Akt-mTOR pathway regulates Aβ oligomer induced neuronal cell cycle events
Bhaskar, K., Miller, M., Chludzinski, A., Herrup, K., Zagorski, M., & Lamb, B. T. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-14 · Cited by 177
Bana, L., Minniti, S., Salvati, E., Sesana, S., Zambelli, V., Cagnotto, A., Orlando, A., Cazzaniga, E., Zwart, R., Scheper, W., et al. (2013) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2013.12.001 · Cited by 153
Alzheimer’s disease: How metal ions define β-amyloid function
Kepp, K. P. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.05.007 · Cited by 154
Liu, X., Hao, W., Qin, Y., Decker, Y., Wang, X., Burkart, M., Schötz, K., Menger, M. D., Fassbender, K., & Liu, Y. (2015) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2015.01.011 · Cited by 149
Aβ43 is more frequent than Aβ40 in amyloid plaque cores from Alzheimer disease brains
Welander, H., Frånberg, J., Graff, C., Sundström, E., Winblad, B. G., & Tjernberg, L. O. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06170.x · Cited by 150
Rat, D., Schmitt, U., Tippmann, F., Dewachter, I., Theunis, C., Wieczerzak, E., Postina, R., LEUVEN, F. V., Fahrenholz, F., & Kojro, E. (2011) · The FASEB Journal · doi:10.1096/fj.10-180133 · Cited by 155
Long-term neprilysin inhibition — implications for ARNIs
Campbell, D. J. (2016) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2016.200 · Cited by 152
Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's β‐amyloid
Kanapathipillai, M., Lentzen, G., Sierks, M. R., & Park, C. B. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.07.057 · Cited by 148
Aβ aggregation and possible implications in Alzheimer's disease pathogenesis
Bharadwaj, P. R., Dubey, A. K., Masters, C. L., Martins, R. N., & Macreadie, I. G. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00609.x · Cited by 155
Structure-based design of conformation- and sequence-specific antibodies against amyloid β
Perchiacca, J. M., Ladiwala, A. R. A., Bhattacharya, M., & Tessier, P. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111232108 · Cited by 147
Benilova, I., Gallardo, R. U., Ungureanu, A.-A., Cano, V. C., Snellinx, A., Ramakers, M., Bartic, C., Rousseau, F., Schymkowitz, J. W. H., & Strooper, B. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.599027 · Cited by 151
IL-4-Induced Selective Clearance of Oligomeric β-Amyloid Peptide1–42 by Rat Primary Type 2 Microglia
Shimizu, E., Kawahara, K., Kajizono, M., Sawada, M., & Nakayama, H. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.9.6503 · Cited by 143
Smilansky, A., Dangoor, L., Nakdimon, I., Ben-Hail, D., Mizrachi, D., & Shoshan-Barmatz, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691493 · Cited by 143
Amyloid Protofibrils of Lysozyme Nucleate and Grow Via Oligomer Fusion
Hill, S. E., Robinson, J., Matthews, G., & Muschol, M. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.01.044 · Cited by 145
ER stress is involved in Aβ‐induced GSK‐3β activation and tau phosphorylation
Resende, R., Ferreiro, E. B., Pereira, C., & Oliveira, C. R. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21648 · Cited by 142
Formation and physicochemical properties of amyloid fibrils from soy protein
Wang, Y., Shen, Y., Qi, G., Li, Y., Sun, X. S., Qiu, D., & Li, Y. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.01.258 · Cited by 141
Fine structure study of Aβ 1–42 fibrillogenesis with atomic force microscopy
Arimon, M., Díez‐Pérez, I., Kogan, M. J., Durany, N., Giralt, E., Sanz, F., & Fernàndez‐Busquets, X. (2005) · The FASEB Journal · doi:10.1096/fj.04-3137fje · Cited by 141
Branched KLVFF Tetramers Strongly Potentiate Inhibition of β‐Amyloid Aggregation
Chafekar, S. M., Malda, H., Merkx, M., Meijer, E. W., Viertl, D., Lashuel, H. A., Baas, F., & Scheper, W. (2007) · ChemBioChem · doi:10.1002/cbic.200700338 · Cited by 145
Lee, M., Yu, W., Shih, Y., Chen, C., Guo, Z., Huang, S., Chan, J. C. C., & Chen, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-23122-x · Cited by 141
Wu, L., Ahmadvand, D., Su, J., Hall, A., Tan, X., Farhangrazi, Z. S., & Moghimi, S. M. (2019) · Nature Communications · doi:10.1038/s41467-019-12554-2 · Cited by 145
Amino-Terminally Truncated Aβ Peptide Species Are the Main Component of Cotton Wool Plaques
Miravalle, L., Calero, M., Takao, M., Roher, A. E., Ghetti, B. F., & Vidal, R. (2005) · Biochemistry · doi:10.1021/bi0508237 · Cited by 140
Garcia, P., Youssef, I., Utvik, J. K., Florent-Béchard, S., Barthélémy, V., Malaplate-Armand, C., Kriem, B., Stenger, C., Koziel, V., Olivier, J.-L., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4182-09.2010 · Cited by 139
Ren, X., Zhao, Y., Xue, F., Zheng, Y., Huang, H., Wang, W., Chang, Y., Yang, H., & Zhang, J. (2019) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.07.008 · Cited by 143
Aggressive amyloidosis in mice expressing human amyloid peptides with the Arctic mutation
Cheng, I. H.-J., Palop, J. J., Esposito, L., Bien‐Ly, N., Yan, F., & Mucke, L. (2004) · Nature Medicine · doi:10.1038/nm1123 · Cited by 134
Strategies for the Inhibition of Protein Aggregation in Human Diseases
Bartolini, M., & Andrisano, V. (2010) · ChemBioChem · doi:10.1002/cbic.200900666 · Cited by 140
Chloride intracellular channel 1 (CLIC1): Sensor and effector during oxidative stress
Averaimo, S., Milton, R. H., Duchen, M. R., & Mazzanti, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.073 · Cited by 134
Doi, Y., Mizuno, T., Maki, Y., Jin, S., Mizoguchi, H., Ikeyama, M., Doi, M., Michikawa, M., Takeuchi, H., & Suzumura, A. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.090418 · Cited by 135
The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity
Sharma, A. K., Pavlova, S. T., Kim, J., Kim, J., & Mirica, L. M. (2013) · Metallomics · doi:10.1039/c3mt00161j · Cited by 135
Silibinin: A novel inhibitor of Aβ aggregation
Yin, F., Liu, J., Ji, X., Wang, Y., Zidichouski, J. A., & Zhang, J. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.12.017 · Cited by 134
Comparison of force fields for Alzheimer's A: A case study for intrinsically disordered proteins
Carballo‐Pacheco, M., & Strodel, B. (2016) · Protein Science · doi:10.1002/pro.3064 · Cited by 132
LRP in Amyloid‐β Production and Metabolism
Bu, G., Cam, J. A., & Zerbinatti, C. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1377.005 · Cited by 141
Baumketner, A., & Shea, J. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.015 · Cited by 133
Jung, K., Astarita, G., Yaşar, S., Vasilevko, V., Cribbs, D. H., Head, E., Cotman, C. W., & Piomelli, D. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.03.012 · Cited by 136
Zerbinatti, C. V., Wozniak, D. F., Cirrito, J., Cam, J. A., Osaka, H., Bales, K. R., Zhuo, M., Paul, S. M., Holtzman, D. M., & Bu, G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305803101 · Cited by 133
RETRACTED: Cognitive effects of cell-derived and synthetically derived Aβ oligomers
Reed, M. N., Hofmeister, J. J., Jungbauer, L. M., Welzel, A. T., Yu, C., Sherman, M. A., Lesné, S., LaDu, M. J., Walsh, D. M., Ashe, K. H., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.11.007 · Cited by 135
RetractedMaloney, M. T., Minamide, L. S., Kinley, A. W., Boyle, J. A., & Bamburg, J. R. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3711-05.2005 · Cited by 140
Plasma lipidome is dysregulated in Alzheimer’s disease and is associated with disease risk genes
Liu, Y., Thalamuthu, A., Mather, K. A., Crawford, J. D., Ulanova, M., Wong, M. W. K., Pickford, R., Sachdev, P. S., & Braidy, N. (2021) · Translational Psychiatry · doi:10.1038/s41398-021-01362-2 · Cited by 140
Itkin, A., Duprès, V., Dufrêne, Y. F., Bechinger, B., Ruysschaert, J., & Raussens, V. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018250 · Cited by 131
Clementi, M. E., Marini, S., Coletta, M., Orsini, F., Giardina, B., & Misiti, F. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.04.041 · Cited by 131
Decreased pH in the aging brain and Alzheimer's disease
Decker, Y., Németh, E., Schomburg, R., Chemla, A., Fülöp, L., Menger, M. D., Liu, Y., & Fassbender, K. C. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.12.007 · Cited by 129
Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization
Murray, M. M., Bernstein, S. L., Nyugen, V., Condron, M. M., Teplow, D. B., & Bowers, M. T. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8092604 · Cited by 128
The pleiotropic effects of omega-3 docosahexaenoic acid on the hallmarks of Alzheimer's disease
Belkouch, M., Hachem, M., Elgot, A., Van, A. L., Picq, M., Guichardant, M., Lagarde, M., & Bernoud‐Hubac, N. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.03.002 · Cited by 131
Yap, J. K. Y., Pickard, B. S., Chan, E. W. L., & Gan, S. Y. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1638-7 · Cited by 130
Reactivity of Apolipoprotein E4 and Amyloid β Peptide
Ji, Z.-S., Müllendorff, K., Cheng, I. H., Miranda, R. D., Huang, Y., & Mahley, R. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m506646200 · Cited by 127
Soluble Amyloid-beta Aggregates from Human Alzheimer’s Disease Brains
Esparza, T. J., Wildburger, N. C., Jiang, H., Gangolli, M., Cairns, N. J., Bateman, R. J., & Brody, D. L. (2016) · Scientific Reports · doi:10.1038/srep38187 · Cited by 127
Signal transduction during amyloid-β-peptide neurotoxicity: role in Alzheimer disease
Fuentealba, R. A., Farı́as, G. G., Scheu, J., Bronfman, M., Marzolo, M., & Inestrosa, N. C. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2004.07.018 · Cited by 126
Gan, L., Ye, S., Chu, A., Anton, K., Yi, S.-L., Vincent, V. A. M., von Schack, D., Chin, D. J., Murray, J. C., Lohr, S., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306183200 · Cited by 130
Mechanism mediating oligomeric Aβ clearance by naïve primary microglia
Yang, C.-N., Shiao, Y.-J., Shie, F.-S., Guo, B.-S., Chen, P.-H., Cho, C.-Y., Chen, Y.-J., Huang, F.-L., & Tsay, H.-J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.005 · Cited by 117
Alzheimer disease: Amyloidogenesis, the presenilins and animal models
Newman, M., Musgrave, I., & Lardelli, M. T. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.12.001 · Cited by 129
Amyloid-beta-induced neurotoxicity is reduced by inhibition of glycogen synthase kinase-3
Koh, S., Noh, M., & Kim, S. H. (2007) · Brain Research · doi:10.1016/j.brainres.2007.10.064 · Cited by 126
Marzolo, M.-P., & Bu, G. (2009) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2008.10.005 · Cited by 122
Askanas (2006) · doi:10.1212/01.wnl.0000192128.13875.1e · Cited by 168
Metadata
- Authors
- Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J.
- Affiliations
- Northwestern University (US)
- Corresponding author
- LaDu, Mary Jo
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-08
- Volume
- 277
- Issue
- 35
- Pages
- 32046-32053
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2168025729
- Cited by
- 1,452
- References
- 71
- Citations by year
- 2026: 25 · 2025: 33 · 2024: 40 · 2023: 46 · 2022: 45 · 2021: 47 · 2020: 49 · 2019: 55 · 2018: 65 · 2017: 58 · 2016: 61 · 2015: 70 · 2014: 78 · 2013: 86 · 2012: 86
- FWCI
- 22.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, amyloid-beta oligomers, amyloid fibrils, Alzheimer's disease, neuronal viability, peptide aggregation, protofibrils, neurotoxicity
- MeSH terms
- Alzheimer Disease, Cell Survival, Humans, Neuroblastoma, Neurons, Peptide Fragments, Tumor Cells, Cultured, Amyloid beta-Peptides, Microscopy, Atomic Force
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review