Role of the β‐amyloid protein in Alzheimer's disease
Abstract
A major histopathological hallmark of Alzheimer's disease (AD) is the presence of amyloid deposits in the parenchyma of the amygdala, hippocampus, and neocortex. The principal component of amyloid is the beta-amyloid protein (A beta), a 39-43 amino acid peptide composed of a portion of the transmembrane domain and the extracellular domain of the amyloid precursor protein (APP). APP occurs as several A beta-containing isoforms of 695, 751, and 770 amino acids, with the latter two APP containing a domain that shares structural and functional homologies with Kunitz serine protease inhibitors. In cultured cells, APP mature through the constitutive secretory pathway, and some cell surface-bound APP are cleaved by an enzyme, designated as alpha-secretase, within the A beta domain, an event that precludes A beta amyloidogenesis. Several studies have delineated two additional pathways of APP processing: first, an endosomal/lysosomal pathway generates a complex set of APP-related membrane-bound fragments, some of which contain the entire A beta sequence; and, second, by mechanisms which are not fully understood, A beta 1-40 is secreted into the conditioned medium in vitro and is present in cerebrospinal fluid in vivo. The intracellular sites of enzymes responsible for proteolytic cleavage at the NH2 and COOH termini of A beta, termed gamma- and beta-secretase, respectively, have not been identified. Finally, recent molecular genetic investigations have identified a variety of mutation…
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Proteolysis by β- and γ-secretase is thought to occur within endosomal compartments.
“Proteolysis by the β- and γ-secretase is thought to occur within the endosomal compartments (Sisodia and Price, 1995).”
From LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking (2011) · cites this paper as Sisodia and Price, 1995
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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 · see citing works
Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345 · see citing works
Iwata, N., Tsubuki, S., Takaki, Y., Watanabe, K., Sekiguchi, M., Hosoki, E., Kawashima-Morishima, M., Lee, H.-J., Hama, E., Sekine-Aizawa, Y., et al. (2000) · Nature Medicine · doi:10.1038/72237 · Cited by 867 · see citing works
Gervais, F. G., Xu, D., Robertson, G. S., Vaillancourt, J. P., Zhu, Y., Huang, J., LeBlanc, A. C., Smith, D., Rigby, M., Shearman, M. S., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80748-5 · Cited by 784 · see citing works
Molecular mechanisms of neurodegeneration in Alzheimer's disease
Crews, L., & Masliah, E. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq160 · Cited by 772 · see citing works
Scavenger receptor-mediated adhesion of microglia to β-amyloid fibrils
Khoury, J. E., Hickman, S. E., Thomas, C. A., Cao, L., Silverstein, S. C., & Loike, J. D. (1996) · Nature · doi:10.1038/382716a0 · Cited by 727 · see citing works
Koronyo-Hamaoui, M., Koronyo, Y., Ljubimov, A. V., Miller, C. A., Ko, M. K., Black, K. L., Schwartz, M., & Farkas, D. L. (2011) · NeuroImage · doi:10.1016/j.neuroimage.2010.06.020 · Cited by 672 · see citing works
Microglia, neuroinflammation, and beta-amyloid protein in Alzheimer’s disease
Cai, Z., Hussain, M. D., & Yan, L.-J. (2014) · International Journal of Neuroscience · doi:10.3109/00207454.2013.833510 · Cited by 583 · see citing works
Izumi, Y., Hirata, M., Hasuwa, H., Iwamoto, R., Umata, T., Miyado, K., Tamai, Y., Kurisaki, T., Sehara‐Fujisawa, A., Ohno, S., et al. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7260 · Cited by 521 · see citing works
Alzheimer's disease and oxidative stress: implications for novel therapeutic approaches
Behl, C. (1999) · Progress in Neurobiology · doi:10.1016/s0301-0082(98)00055-0 · Cited by 444 · see citing works
Abnormal accumulation of NACP/alpha-synuclein in neurodegenerative disorders.
Takeda, A., Mallory, M. E., Sundsmo, M. P., Honer, W. G., Hansen, L. A., & Masliah, E. (1998) · Europe PMC (PubMed Central) · Cited by 404 · see citing works
Arribas, J., Coodly, L. R., Vollmer, P., Kishimoto, T., Rose‐John, S., & Massagué, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11376 · Cited by 391 · see citing works
Pitschke, M., Prior, R., Haupt, M., & Riesner, D. (1998) · Nature Medicine · doi:10.1038/nm0798-832 · Cited by 326 · see citing works
Jiang, Y., Mullaney, K. A., Peterhoff, C. M., Che, S., Schmidt, S. D., Boyer‐Boiteau, A., Ginsberg, S. D., Cataldo, A. M., Mathews, P. M., & Nixon, R. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908953107 · Cited by 288 · see citing works
Tsigelny, I. F., Crews, L., Desplats, P., Shaked, G. M., Sharikov, Y., Mizuno, H., Spencer, B., Rockenstein, E., Trejo, M., Platoshyn, O., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003135 · Cited by 281 · see citing works
RetractedOxidative stress and β-amyloid protein in Alzheimer’s disease
Cai, Z., Zhao, B., & Ratka, A. (2011) · NeuroMolecular Medicine · doi:10.1007/s12017-011-8155-9 · Cited by 279 · see citing works
Engineered nanoparticles for biomolecular imaging
Mahmoudi, M., Serpooshan, V., & Laurent, S. (2011) · Nanoscale · doi:10.1039/c1nr10326a · Cited by 262 · see citing works
Alpha‐synuclein in Lewy Body Disease and Alzheimer's Disease
Hashimoto, M., & Masliah, E. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00552.x · Cited by 251 · see citing works
Shin, J. Y., Park, H. J., Kim, H. N., Oh, S. H., Bae, J.-S., Ha, H.-J., & Lee, P. H. (2014) · Autophagy · doi:10.4161/auto.26508 · Cited by 243 · see citing works
Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease
Overk, C. R., & Masliah, E. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.015 · Cited by 242 · see citing works
Extracellular tau is toxic to neuronal cells
Gómez-Ramos, A., Díaz-Hernández, M., Cuadros, R., Hernández, F., & Avila, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.07.078 · Cited by 241 · see citing works
Immune reactive cells in senile plaques and cognitive decline in Alzheimer’s disease
Vehmas, A. K., Kawas, C. H., Stewart, W. F., & Troncoso, J. C. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00090-8 · Cited by 230 · see citing works
Tian, Y., Bustos, V., Flajolet, M., & Greengard, P. (2011) · The FASEB Journal · doi:10.1096/fj.10-175158 · Cited by 223 · see citing works
Pham, E., Crews, L. A., Ubhi, K. K., Hansen, L. A., Adame, A., Cartier, A. E., Salmon, D. P., Galasko, D. R., Michael, S., Savas, J. N., et al. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07719.x · Cited by 218 · see citing works
Choo, L.-P., Wetzel, D. L., HALLIDAY, W. C., Jackson, M., LeVine, S. M., & Mantsch, H. H. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79411-0 · Cited by 220 · see citing works
Neuroprotective properties of resveratrol and derivatives
Richard, T., Pawlus, A. D., Iglésias, M., Pédrot, E., Waffo‐Téguo, P., Mérillon, J., & Monti, J. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05865.x · Cited by 210 · see citing works
Heart Failure and Protein Quality Control
Wang, X., & Robbins, J. M. (2006) · Circulation Research · doi:10.1161/01.res.0000252342.61447.a2 · Cited by 208 · see citing works
Torroja, L., Chu, H., Kotovsky, I., & White, K. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80215-2 · Cited by 203 · see citing works
Amyloid β Protein-(1–42) Forms Calcium-permeable, Zn2+-sensitive Channel
Rhee, S. K., Quist, A. P., & Lal, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13379 · Cited by 194 · see citing works
Roles of AMP-activated Protein Kinase in Alzheimer’s Disease
Cai, Z., Yan, L., Li, K., Quazi, S. H., & Zhao, B. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8173-2 · Cited by 191 · see citing works
Shimura, H., Hattori, N., Kubo, S., Yoshikawa, M., Kitada, T., Matsumine, H., Asakawa, S., Minoshima, S., Yamamura, Y., Shimizu, N., et al. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199905)45:5 · Cited by 282 · see citing works
Liu, B., Rasool, S., Yang, Z., Glabe, C. G., Schreiber, S. S., Ge, J., & Tan, Z. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.090159 · Cited by 182 · see citing works
Actin dynamics and cofilin‐actin rods in alzheimer disease
Bamburg, J. R., & Bernstein, B. W. (2016) · Cytoskeleton · doi:10.1002/cm.21282 · Cited by 181 · see citing works
Sousa, M. M., Yan, S. D., Stern, D. M., & Saraiva, M. J. (2000) · Laboratory Investigation · doi:10.1038/labinvest.3780116 · Cited by 176 · see citing works
Cytoskeletal pathologies of Alzheimer disease
Bamburg, J. R., & Bloom, G. S. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20388 · Cited by 168 · see citing works
Ng, L. F., Gruber, J., Cheah, I. K.-M., Goo, C. K., Cheong, W. F., Shui, G., Sit, K. P., Wenk, M. R., & Halliwell, B. B. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.003 · Cited by 170 · see citing works
Distribution of Cystine/Glutamate Exchange Transporter, System xc−, in the Mouse Brain
Sato, H., Tamba, M., Okuno, S., Sato, K., Keino‐Masu, K., Masu, M., & Bannai, S. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-18-08028.2002 · Cited by 167 · see citing works
Green tea catechins as a BACE1 (β-Secretase) inhibitor
Jeon, S.-Y., Bae, K., Seong, Y.-H., & Song, K. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2003.09.018 · Cited by 168 · see citing works
Gong, N.-J., Dibb, R., Bulk, M., van der Weerd, L., & Liu, C. (2019) · NeuroImage · doi:10.1016/j.neuroimage.2019.02.019 · Cited by 162 · see citing works
Disrupting β-Amyloid Aggregation for Alzheimer Disease Treatment
Estrada, L. D., & Soto, C. A. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802607779318262 · Cited by 162 · see citing works
Chronic Intermittent Hypoxia/Reoxygenation Facilitate Amyloid-β Generation in Mice
Shiota, S., Takekawa, H., Matsumoto, S., Takeda, K., Nurwidya, F., Yoshioka, Y., Takahashi, F., Hattori, N., Tabira, T., Mochizuki, H., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130419 · Cited by 155 · see citing works
Microglia, Scavenger Receptors, and the Pathogenesis of Alzheimer’s Disease
Khoury, J. B. E., Hickman, S., Thomas, C. A., Loike, J. D., & Silverstein, S. C. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00036-0 · Cited by 157 · see citing works
Lin, H., Zhu, Y. J., & Lal, R. (1999) · Biochemistry · doi:10.1021/bi982997c · Cited by 156 · see citing works
Oh, S. H., Kim, H. N., Park, H.-J., Shin, J. Y., & Lee, P. H. (2014) · Cell Transplantation · doi:10.3727/096368914x679237 · Cited by 153 · see citing works
Roles of Glycogen Synthase Kinase 3 in Alzheimer’s Disease
Cai, Z., Zhao, Y. C., & Zhao, B. (2012) · Current Alzheimer Research · doi:10.2174/156720512802455386 · Cited by 146 · see citing works
Obaid, R. J., Naeem, N., Mughal, E. U., Al‐Rooqi, M. M., Sadiq, A., Jassas, R. S., Moussa, Z., & Ahmed, S. A. (2022) · RSC Advances · doi:10.1039/d2ra03081k · Cited by 147 · see citing works
Alzheimer’s Disease as Proteolytic Disorders: Anabolism and Catabolism of β-Amyloid
Saido, T. C. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00033-5 · Cited by 140 · see citing works
Abnormal Glutamate Transport Function in Mutant Amyloid Precursor Protein Transgenic Mice
Masliah, E., Alford, M. F., Mallory, M. E., Rockenstein, E. M., Moechars, D., & LEUVEN, F. V. (2000) · Experimental Neurology · doi:10.1006/exnr.2000.7386 · Cited by 145 · see citing works
Diffuse Plaques Contain C-terminal Aβ42and not Aβ40: Evidence From Cats and Dogs
Cummings, B. J., Satou, T., Head, E., Milgram, N. W., Cole, G. M., Savage, M. J., Podlisny, M. B., Selkoe, D. J., Siman, R. G., Greenberg, B., et al. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(96)00062-0 · Cited by 140 · see citing works
Characterization of Alternative Isoforms and Inclusion Body of the TAR DNA-binding Protein-43
Nishimoto, Y., Ito, D., Yagi, T., Nihei, Y., Tsunoda, Y., & Suzuki, N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022012 · Cited by 138 · see citing works
Pinnix, I., Musunuru, U., Tun, H. W., Sridharan, A., Golde, T. E., Eckman, C. B., Ziani‐Cherif, C., Onstead, L., & Sambamurti, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005968200 · Cited by 138 · see citing works
Cai, Z.-Y., Zhao, B., Li, K.-S., Zhang, L.-Q., Li, C., Quazi, S. H., & Tan, Y. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23011 · Cited by 129 · see citing works
Maloney, 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 131 · see citing works
Paris, D., Humphrey, J., Quadros, A., Patel, N., Crescentini, R., Crawford, F., & Mullan, M. (2003) · Neurological Research · doi:10.1179/016164103101201940 · Cited by 127 · see citing works
Cholinergic activity and amyloid precursor protein metabolism
Roberson, M. R. (1997) · Brain Research Reviews · doi:10.1016/s0165-0173(97)00016-7 · Cited by 127 · see citing works
Nuclear receptors as therapeutic targets for Alzheimer's disease
Mandrekar-Colucci, S., & Landreth, G. E. (2011) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2011.594043 · Cited by 126 · see citing works
Chiang, M., Cheng, Y., Chen, S., Yen, C., & Huang, R. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.08.013 · Cited by 123 · see citing works
Telomere Shortening and Alzheimer’s Disease
Cai, Z., Yan, L., & Ratka, A. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8207-9 · Cited by 120 · see citing works
Role of ERAB/l-3-Hydroxyacyl-coenzyme A Dehydrogenase Type II Activity in Aβ-induced Cytotoxicity
Yan, S. D., Shi, Y., Zhu, A., Fu, J., Zhu, H., Zhu, Y., Gibson, L., Stern, E., Collison, K. S., Al-Mohanna, F. A., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2145 · Cited by 121 · see citing works
Synapses and Dendritic Spines as Pathogenic Targets in Alzheimer’s Disease
Yu, W., & Lu, B. (2012) · Neural Plasticity · doi:10.1155/2012/247150 · Cited by 119 · see citing works
Amyloid Precursor Protein Is Trafficked and Secreted via Synaptic Vesicles
Groemer, T. W., Thiel, C. S., Holt, M. G., Riedel, D., Hua, Y., Hüve, J., Wilhelm, B. G., & Klingauf, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018754 · Cited by 109 · see citing works
β-Secretase(BACE1) inhibitors from pomegranate (Punica granatum) husk
Kwak, H.-M., Jeon, S.-Y., Sohng, B.-H., Kim, J.-G., Lee, J.-M., Lee, K., Jeong, H.-H., Hur, J.-M., Kang, Y., & Song, K. (2005) · Archives of Pharmacal Research · doi:10.1007/bf02977896 · Cited by 107 · see citing works
Choucair, A., Chakrapani, M., Chakravarthy, B., Katsaras, J., & Johnston, L. J. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.005 · Cited by 105 · see citing works
Advances in development of fluorescent probes for detecting amyloid-β aggregates
Xu, M., Ren, W., Tang, X.-C., Hu, Y., & Zhang, H. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2015.155 · Cited by 101 · see citing works
Davis, R. C., Marsden, I. T., Maloney, M. T., Minamide, L. S., Podlisny, M. B., Selkoe, D. J., & Bamburg, J. R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-10 · Cited by 97 · see citing works
Satpute‐Krishnan, P., DeGiorgis, J. A., & Bearer, E. L. (2003) · Aging Cell · doi:10.1046/j.1474-9728.2003.00069.x · Cited by 96 · see citing works
Zhiyou, C., Yong, Y., Shanquan, S., Jun, Z., Liangguo, H., Ling, Y., & Li, J. (2009) · Neurochemical Research · doi:10.1007/s11064-008-9899-y · Cited by 96 · see citing works
Mamikonyan, G., Necula, M., Mkrtichyan, M., Ghochikyan, A., Petrushina, I., Movsesyan, N., Mina, E. W., Kiyatkin, A. B., Glabe, C. G., Cribbs, D. H., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700088200 · Cited by 93 · see citing works
Pietrzik, C. U., Hoffmann, J., Stoeber, K., Chen, C., Bauer, C. R., Otero, D. A. C., Roch, J., & Herzog, V. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1770 · Cited by 90 · see citing works
New polyphenols active on β-amyloid aggregation
Rivière, C., Richard, T., Vitrac, X., Mérillon, J., Valls, J., & Monti, J. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.11.028 · Cited by 88 · see citing works
Alzheimer's and prion diseases: distinct pathologies, common proteolytic denominators
Checler, F., & Vincent, B. (2002) · Trends in Neurosciences · doi:10.1016/s0166-2236(02)02263-4 · Cited by 87 · see citing works
Role of Synucleins in Alzheimer’s Disease
Crews, L. A., Tsigelny, I. F., Hashimoto, M., & Masliah, E. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9073-6 · Cited by 84 · see citing works
Baweja, L., Balamurugan, K., Subramanian, V., & Dhawan, A. (2015) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2015.07.007 · Cited by 83 · see citing works
Ikin, A. F., Annaert, W. G., Takei, K., Camilli, P. V. D., Jahn, R., Greengard, P., & Buxbaum, J. D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.50.31783 · Cited by 83 · see citing works
A damaged microcirculation contributes to neuronal cell death in Alzheimer’s disease☆
Grammas, P. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00102-0 · Cited by 81 · see citing works
β-secretase (BACE1)-inhibiting stilbenoids from Smilax Rhizoma
Jeon, S. Y., Kwon, S.-H., Seong, Y. H., Bae, K., Hur, J.-M., Lee, Y.-Y., Suh, D., & Song, K. S. (2006) · Phytomedicine · doi:10.1016/j.phymed.2006.09.003 · Cited by 81 · see citing works
Opioid System and Alzheimer’s Disease
Cai, Z., & Ratka, A. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8180-3 · Cited by 80 · see citing works
Hoffmann, J., Twiesselmann, C., Kummer, M. P., Romagnoli, P., & Herzog, V. (2000) · European Journal of Cell Biology · doi:10.1078/0171-9335-00117 · Cited by 79 · see citing works
Grabrucker, A. M., Schmeißer, M. J., Udvardi, P. T., Arons, M. H., Schoen, M., Woodling, N. S., Andreasson, K. I., Hof, P. R., Buxbaum, J. D., Garner, C. C., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-65 · Cited by 77 · see citing works
Association between the TNFα‐308 A/G polymorphism and the onset‐age of Alzheimer disease
Álvarez, V., Mata, I. F., González, P., Lahoz, C., Martínez, C., Peña, J., Guisasola, L. M., & Coto, E. (2002) · American Journal of Medical Genetics · doi:10.1002/ajmg.10515 · Cited by 75 · see citing works
Alzheimer's Disease: Recent Advances and Future Perspectives
Ubhi, K. K., & Masliah, E. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129028 · Cited by 76 · see citing works
Cho, H. J., Jin, S. M., Youn, H., Huh, K., & Mook‐Jung, I. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00360.x · Cited by 71 · see citing works
Papassotiropoulos, A., Bagli, M., Feder, O., Jessen, F., Maier, W., Rao, M. L., Ludwig, M. Z., Schwab, S. G., & Heun, R. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00071-3 · Cited by 74 · see citing works
Jaberi, S., & Fahnestock, M. L. (2023) · Biomolecules · doi:10.3390/biom13111577 · Cited by 74 · see citing works
Harkany, T., Mulder, J., Sasvári, M., Ábrahám, I. M., Kónya, C., Zarándi, M., Penke, B., Luiten, P. G. M., & Nyakas, C. J. (1999) · Neurobiology of Disease · doi:10.1006/nbdi.1998.0230 · Cited by 73 · see citing works
Role of Ionizing Radiation in Neurodegenerative Diseases
Sharma, N., Sharma, R., Mathur, D., Sharad, S., Minhas, G., Bhatia, K., Anand, A., & Ghosh, S. P. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00134 · Cited by 68 · see citing works
Jackson, H. M., Soto, I., Graham, L. C., Carter, G. W., & Howell, G. R. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-831 · Cited by 66 · see citing works
Masliah, E. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3117 · Cited by 66 · see citing works
Soluble β-amyloid peptides mediate vasoactivity via activation of a pro-inflammatory pathway
Paris, D., Town, T., Mori, T., Parker, T. A., Humphrey, J., & MULLAN, M. J. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00111-6 · Cited by 64 · see citing works
Bachmeier, C. J., Beaulieu‐Abdelahad, D., MULLAN, M. J., & Paris, D. (2011) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2011.03.048 · Cited by 61 · see citing works
Activation of Phospholipase A2 by Amyloid β-Peptides in Vitro
Lehtonen, J. Y. A., Holopainen, J. M., & Kinnunen, P. K. J. (1996) · Biochemistry · doi:10.1021/bi960148o · Cited by 61 · see citing works
Permanne, B., Pérez, C. A., Soto, C., Frangione, B., & Wisniewski, T. (1997) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1006/bbrc.1997.7727 · Cited by 62 · see citing works
Cerebrovascular endothelial dysfunction mediated by β-amyloid
Thomas, T., McLendon, C., Sutton, E. T., & Thomas, G. (1997) · Neuroreport · doi:10.1097/00001756-199704140-00014 · Cited by 59 · see citing works
Maltese, W. A., Wilson, S. E., Tan, Y., Suomensaari, S., Sinha, S., Barbour, R., & McConlogue, L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007238200 · Cited by 60 · see citing works
Wegrzyn, J., Bark, S. J., Funkelstein, L., Mosier, C., Yap, A., Kazemi‐Esfarjani, P., Spada, A. R. L., Sigurdson, C. J., O’Connor, D. T., & HOOK, V. Y. H. (2010) · Journal of Proteome Research · doi:10.1021/pr1003104 · Cited by 57 · see citing works
Forman, M. S., Cook, D. G., Leight, S., Doms, R. W., & Lee, V. M. ‐. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32247 · Cited by 57 · see citing works
Cellular cofactors potentiating induction of stress and cytotoxicity by amyloid β-peptide
Yan, S. D., Roher, A. E., Chaney, M., Zloković, B. V., Schmidt, A. M., & Stern, D. M. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00041-7 · Cited by 58 · see citing works
β-secretase (BACE1) inhibitors from Perilla frutescens var. acuta
Choi, S.-H., Hur, J.-M., Yang, E. J., Jun, M., Park, H., Lee, K., Moon, E., & Song, K. (2008) · Archives of Pharmacal Research · doi:10.1007/s12272-001-1139-9 · Cited by 57 · see citing works
Zga, N., Papastamoulis, Y., Toribio, A., Richard, T., Delaunay, J.-C., Jeandet, P., Renault, J., Monti, J., Mérillon, J., & Waffo‐Téguo, P. (2009) · Journal of Chromatography B · doi:10.1016/j.jchromb.2009.02.026 · Cited by 55 · see citing works
Autophagy-lysosome dysfunction is involved in Aβ deposition in STZ-induced diabetic rats
Ma, L., Lv, Y.-L., Huo, K., Liu, J., Shang, S., Fei, Y., Li, Y., Zhao, B., Wei, M., Deng, Y., et al. (2016) · Behavioural Brain Research · doi:10.1016/j.bbr.2016.10.031 · Cited by 55 · see citing works
- Authors
- Sisodia, S. S., & Price, D. L.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Sisodia, Sangram S.
- ORCID
- Sisodia, Sangram S.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 1995-03
- Volume
- 9
- Issue
- 5
- Pages
- 366-370
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W1955730586
- Cited by
- 262
- References
- 0
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 7 · 2023: 8 · 2022: 5 · 2021: 4 · 2020: 6 · 2019: 4 · 2018: 8 · 2017: 2 · 2016: 9 · 2015: 5 · 2014: 4 · 2013: 15 · 2012: 13
- FWCI
- 9.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r35ag007914-03)
- National Institute on Aging (AG07914, P50AG005146, AG 05146)
- National Institute of Neurological Disorders and Stroke (NS-20471)
- Topics
- Health Sciences › Medicine › Physiology › 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
- Alzheimer's disease, amyloid-beta, amyloid precursor protein, APP processing, alpha-secretase, gamma-secretase, beta-secretase, APP mutations, familial Alzheimer's disease, cerebrospinal fluid, amyloid plaques
- MeSH terms
- Prion Proteins, Alzheimer Disease, Amyloid, Humans, Prions, Protein Precursors, Amyloid beta-Peptides
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.
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