Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
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Aβ1-42 forms insoluble amyloid fibrils more rapidly than Aβ1-40.
“A{31-42 has been shown to form insoluble amyloid fibrils more rapidly than A{31-40 (10)(11)(12)(13).”
From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [12]
Cites
Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757 · see citing works
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731 · see citing works
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447 · see citing works
Some Speculations about Prions, Amyloid, and Alzheimer's Disease
Prusiner, S. B. (1984) · New England Journal of Medicine · doi:10.1056/nejm198403083101021 · Cited by 213 · see citing works
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The amyloid hypothesis of Alzheimer's disease at 25 years
Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164 · see citing works
Jack, C. R., Knopman, D. S., Jagust, W. J., Petersen, R. C., Weiner, M. W., Aisen, P. S., Shaw, L. M., Vemuri, P., Wiste, H. J., Weigand, S. D., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70291-0 · Cited by 4,396 · see citing works
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599 · see citing works
Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y. (1994) · Neuron · doi:10.1016/0896-6273(94)90458-8 · Cited by 1,774 · see citing works
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663 · see citing works
Jankowsky, J. L., Fadale, D. J., Anderson, J., Xu, G. M., Gonzales, V., Jenkins, N. A., Copeland, N. G., Lee, M. K., Younkin, L. H., Wagner, S. L., et al. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh019 · Cited by 1,575 · see citing works
Borchelt, D. R., Thinakaran, G., Eckman, C. B., Lee, M. K., Davenport, F., Ratovitsky, T., Prada, C.-M., Kim, G., Seekins, S., Yager, D., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80230-5 · Cited by 1,478 · see citing works
Scherzinger, E., Lurz, R., Turmaine, M., Mangiarini, L., Hollenbach, B., Hasenbank, R., Bates, G. P., Davies, S. W., Lehrach, H., & Wanker, E. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80514-0 · Cited by 1,291 · see citing works
Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline
Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268 · see citing works
Curcumin has potent anti‐amyloidogenic effects for Alzheimer's β‐amyloid fibrils in vitro
Ono, K., Hasegawa, K., Naiki, H., & Yamada, M. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20025 · Cited by 1,254 · see citing works
Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases
Soto, C., & Pritzkow, S. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0235-9 · Cited by 1,180 · see citing works
Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-Synuclein
Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105343200 · Cited by 1,103 · see citing works
Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer’s disease
Meyer-Luehmann, M., Spires-Jones, T. L., Prada, C., Garcia-Alloza, M., de Calignon, A., Rozkalne, A., Koenigsknecht-Talboo, J., Holtzman, D. M., Bacskai, B. J., & Hyman, B. T. (2008) · Nature · doi:10.1038/nature06616 · Cited by 987 · see citing works
The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870 · see citing works
Insulin-degrading Enzyme Regulates Extracellular Levels of Amyloid β-Protein by Degradation
Qiu, W. Q., Walsh, D. M., Ye, Z., Vekrellis, K., Zhang, J., Podlisny, M. B., Rosner, M. R., Safavi, A., Hersh, L. B., & Selkoe, D. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32730 · Cited by 812 · see citing works
Advanced glycation end products contribute to amyloidosis in Alzheimer disease
Vitek, M. P., Bhattacharya, K., Glendening, J. M., Stopa, E., Vlassara, H., Bucala, R., Manogue, K., & Cerami, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4766 · Cited by 806 · see citing works
Review: Alzheimer's Amyloid β-Peptide-Associated Free Radical Oxidative Stress and Neurotoxicity
Varadarajan, S., Yatin, S., Aksenova, M., & Butterfield, D. A. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4274 · Cited by 735 · see citing works
Yankner, B. A., Lu, T., & Loerch, P. (2008) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.2.010506.092044 · Cited by 677 · see citing works
Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain
Gravina, S. A., Ho, L., Eckman, C. B., Long, K. E., Otvos, L., Younkin, L. H., Suzuki, N., & Younkin, S. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7013 · Cited by 676 · see citing works
Folding funnels, binding funnels, and protein function
Tsai, C., Kumar, S., Ma, B., & Nussinov, R. (1999) · Protein Science · doi:10.1110/ps.8.6.1181 · Cited by 648 · see citing works
Saido, T. C., Iwatsubo, T., Mann, D. M. A., Shimada, H., Ihara, Y., & Kawashima, S. (1995) · Neuron · doi:10.1016/0896-6273(95)90301-1 · Cited by 587 · see citing works
Folding funnels and binding mechanisms
Ma, B., Kumar, S., Tsai, C.-J., & Nussinov, R. (1999) · Protein Engineering, Design and Selection · doi:10.1093/protein/12.9.713 · Cited by 594 · see citing works
Haass, C., Lemere, C. A., Capell, A., Citron, M., Seubert, P., Schenk, D., Lannfelt, L., & Selkoe, D. J. (1995) · Nature Medicine · doi:10.1038/nm1295-1291 · Cited by 592 · see citing works
Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice
McGowan, E., Pickford, F., Kim, J., Onstead, L., Eriksen, J., Yu, C., Skipper, L., Murphy, M. P., Beard, J., Das, P., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.030 · Cited by 565 · see citing works
Kuperstein, I., Broersen, K., Benilova, I., Rozenski, J., Jonckheere, W., Debulpaep, M., Vandersteen, A., Segers‐Nolten, I., Van Der Werf, K., Subramaniam, V., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.211 · Cited by 532 · see citing works
γ-Secretase, notch, Aβ and alzheimer's disease: Where do the presenilins fit in?
Sisodia, S. S., & St George-Hyslop, P. H. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn785 · Cited by 512 · see citing works
Näslund, J., Schierhorn, A., Hellman, U., Lannfelt, L., Roses, A. D., Tjernberg, L. O., Silberring, J., Gandy, S. E., Winblad, B., & Greengard, P. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8378 · Cited by 468 · see citing works
Snyder, S. W., Ladror, U. S., Wade, W. S., Wang, G. T., Barrett, L. W., Matayoshi, E. D., Huffaker, H. J., Krafft, G. A., & Holzman, T. F. (1994) · Biophysical Journal · doi:10.1016/s0006-3495(94)80591-0 · Cited by 381 · see citing works
Uryu, K., Laurer, H., McIntosh, T., Praticò, D., Martinez, D., Leight, S., Lee, V. M.-Y., & Trojanowski, J. Q. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-02-00446.2002 · Cited by 337 · see citing works
Amyloid β-Peptide Is Transported on Lipoproteins and Albumin in Human Plasma
Biere, A. L., Ostaszewski, B., Stimson, E. R., Hyman, B. T., Maggio, J. E., & Selkoe, D. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.51.32916 · Cited by 331 · see citing works
Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade
Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313 · see citing works
Jan, A., Gokce, O., Luthi-Carter, R., & Lashuel, H. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803159200 · Cited by 291 · see citing works
Skovronsky, D. M., Doms, R. W., & Lee, V. M.-Y. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.4.1031 · Cited by 290 · see citing works
A Dynamic Relationship between Intracellular and Extracellular Pools of Aβ
Oddo, S., Caccamo, A., Smith, I. F., Green, K. N., & LaFerla, F. M. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.050593 · Cited by 261 · see citing works
Lord, A., Kalimo, H., Eckman, C., Zhang, X.-Q., Lannfelt, L., & Nilsson, L. N. G. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.12.007 · Cited by 260 · see citing works
Misfolded protein aggregates: Mechanisms, structures and potential for disease transmission
Moreno-Gonzalez, I., & Soto, C. (2011) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2011.04.002 · Cited by 252 · see citing works
New Insights on How Metals Disrupt Amyloid β-Aggregation and Their Effects on Amyloid-β Cytotoxicity
Yoshiike, Y., Tanemura, K., Murayama, O., Akagi, T., Murayama, M., Sato, S., Sun, X., Tanaka, N., & Takashima, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010706200 · Cited by 244 · see citing works
Mackic, J. B., Stins, M., McComb, J. G., Calero, M., Ghiso, J., Kim, K. S., Yan, S. D., Stern, D., Schmidt, A. M., Frangione, B., et al. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2029 · Cited by 242 · see citing works
Yamada, K., Tanaka, T., Han, D., Senzaki, K., Kameyama, T., & Nabeshima, T. (1999) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1999.00408.x · Cited by 238 · see citing works
Takeuchi, A., Irizarry, M. C., Duff, K., Saido, T. C., Hsiao Ashe, K., Hasegawa, M., Mann, D. M. A., Hyman, B. T., & Iwatsubo, T. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64544-0 · Cited by 229 · see citing works
Age-Dependent Effects of apoE Reduction Using Antisense Oligonucleotides in a Model of β-amyloidosis
Huynh, T.-P. V., Liao, F., Francis, C. M., Robinson, G. O., Serrano, J. R., Jiang, H., Roh, J., Finn, M. B., Sullivan, P. M., Esparza, T. J., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.11.014 · Cited by 209 · see citing works
Huynh, T.-P. V., Davis, A. A., Ulrich, J. D., & Holtzman, D. M. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075481 · Cited by 210 · see citing works
Clearance of amyloid β-peptide from brain: transport or metabolism?
Zlokovic, B. V., Yamada, S., Holtzman, D., Ghiso, J., & Frangione, B. (2000) · Nature Medicine · doi:10.1038/77397 · Cited by 186 · see citing works
Wilson, M. R., Yerbury, J. J., & Poon, S. (2007) · Molecular BioSystems · doi:10.1039/b712728f · Cited by 142 · see citing works
Haass, C., & Selkoe, D. (2022) · PLOS Biology · doi:10.1371/journal.pbio.3001694 · Cited by 145 · see citing works
β-Amyloid (Aβ) Deposition in the Brains of Aged Orangutans
Gearing, M., Tigges, J., Mori, H., & Mirra, S. S. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00012-2 · Cited by 130 · see citing works
Lamb, B. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.9.1535 · Cited by 128 · see citing works
Burke, K. A., Yates, E. A., & Legleiter, J. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00017 · Cited by 127 · see citing works
Rodent Aβ Modulates the Solubility and Distribution of Amyloid Deposits in Transgenic Mice
Jankowsky, J. L., Younkin, L. H., Gonzales, V., Fadale, D. J., Slunt, H. H., Lester, H. A., Younkin, S. G., & Borchelt, D. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611050200 · Cited by 122 · see citing works
Disease modifying therapy for AD?<sup>1</sup>
Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117 · see citing works
Microglia and Astrocytes in Alzheimer’s Disease: Significance and Summary of Recent Advances
Deng, Q., Wu, C., Parker, E., Liu, T. C.-Y., Duan, R., & Yang, L. (2023) · Aging and disease · doi:10.14336/ad.2023.0907 · Cited by 102 · see citing works
The Proteasome and Oxidative Stress in Alzheimer's Disease
Bonet-Costa, V., Pomatto, L. C.-D., & Davies, K. J. A. (2016) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6802 · Cited by 99 · see citing works
Uhlmann, R. E., Rother, C., Rasmussen, J., Schelle, J., Bergmann, C., Ullrich Gavilanes, E. M., Fritschi, S. K., Buehler, A., Baumann, F., Skodras, A., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-00737-w · Cited by 87 · see citing works
Grant, J. L., Ghosn, E. E. B., Axtell, R. C., Herges, K., Kuipers, H. F., Woodling, N. S., Andreasson, K., Herzenberg, L. A., Herzenberg, L. A., & Steinman, L. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3004145 · Cited by 92 · see citing works
“In the context of AD, Ab42 has a well-characterized role in neurodegeneration and has been implicated in various cytotoxic pathologies including excitotoxicity and oxidative stress on neurons (46).”
BackgroundLiu, S., Hossinger, A., Heumüller, S.-E., Hornberger, A., Buravlova, O., Konstantoulea, K., Müller, S. A., Paulsen, L., Rousseau, F., Schymkowitz, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25855-2 · Cited by 72 · see citing works
Cross Currents in Protein Misfolding Disorders: Interactions and Therapy
Morales, R., Green, K., & Soto, C. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709789541998 · Cited by 72 · see citing works
In vivo imaging reveals sigmoidal growth kinetic of β-amyloid plaques
Burgold, S., Filser, S., Dorostkar, M. M., Schmidt, B., & Herms, J. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-30 · Cited by 59 · see citing works
Hirohata, M., Ono, K., Takasaki, J.-I., Takahashi, R., Ikeda, T., Morinaga, A., & Yamada, M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.05.006 · Cited by 43 · see citing works
A new neuronal target for beta-amyloid peptide in the rat hippocampus
Villette, V., Poindessous-Jazat, F., Bellessort, B., Roullot, E., Peterschmitt, Y., Epelbaum, J., Stéphan, A., & Dutar, P. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.024 · Cited by 37 · see citing works
Haugabook, S. J., Yager, D. M., Eckman, E. A., Golde, T. E., Younkin, S. G., & Eckman, C. B. (2001) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(01)00388-0 · Cited by 39 · see citing works
Studies on the first described Alzheimer's disease amyloid β mutant, the Dutch variant
Levy, E., Prelli, F., & Frangione, B. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-9s337 · Cited by 24 · see citing works
Illouz, T., Nicola, R., Ben-Shushan, L., Madar, R., Biragyn, A., & Okun, E. (2021) · Communications Biology · doi:10.1038/s42003-021-01851-6 · Cited by 21 · see citing works
- Authors
- Jarrett, J. T., & Lansbury, P. T.
- Affiliations
- Massachusetts Institute of Technology (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1993-06
- Volume
- 73
- Issue
- 6
- Pages
- 1055-1058
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2059804089
- Cited by
- 2,178
- References
- 4
- Citations by year
- 2026: 19 · 2025: 30 · 2024: 36 · 2023: 47 · 2022: 58 · 2021: 59 · 2020: 61 · 2019: 58 · 2018: 71 · 2017: 83 · 2016: 68 · 2015: 77 · 2014: 79 · 2013: 82 · 2012: 93
- FWCI
- 8.44
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, scrapie, amyloid fibril formation, protein aggregation, prion protein, amyloid plaques, Creutzfeldt-Jakob disease, prion disease, pathophysiological mechanisms, neurodegeneration, protein crystallization, microtubule formation, rate-determining step
- MeSH terms
- Alzheimer Disease, Amyloid, Animals, Humans, Scrapie
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