The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease
Abstract
It is a truism of modern biomedical science that the development of therapies expected to slow or arrest the progression of a disease requires as detailed an understanding of its molecular and cellular pathogenesis as possible. In turn, the cloning of novel gene products implicated in a disease often leads to new insights about fundamental features of protein structure and function. A particularly compelling example of this beneficial interplay between basic and applied cell biology arises from the exciting recent progress in deciphering Alzheimer's disease (AD). This review discusses the current understanding of the cell biology of two proteins crucial for the pathogenesis of AD, the beta-amyloid precursor protein and presenilin.
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Insulin regulates food intake, energy homeostasis, reproduction, sympathetic activity, learning and memory, as well as neuronal proliferation, apoptosis, and synaptic transmission in the central nervous system.
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Cites
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619 · see citing works
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051 · see citing works
Brown, M. S., & Goldstein, J. L. (1997) · Cell · doi:10.1016/s0092-8674(00)80213-5 · Cited by 3,834 · see citing works
A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149 · see citing works
Candidate gene for the chromosome 1 familial Alzheimer’s disease locus
Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577 · see citing works
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022 · see citing works
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921 · see citing works
Self-citationDeficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
De Strooper, B., Saftig, P., Craessaerts, K., Vanderstichele, H., Guhde, G., Annaert, W., Von Figura, K., & Van Leuven, F. (1998) · Nature · doi:10.1038/34910 · Cited by 1,818 · 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
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
Self-citationAlzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91209-9 · Cited by 1,693 · see citing works
Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
Schroeter, E. H., Kisslinger, J. A., & Kopan, R. (1998) · Nature · doi:10.1038/30756 · Cited by 1,624 · 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
Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1
Duff, K., Eckman, C., Zehr, C., Yu, X., Prada, C.-M., Pérez‐Tur, J., Hutton, M., Buée, L., Harigaya, Y., Yager, D., et al. (1996) · Nature · doi:10.1038/383710a0 · Cited by 1,465 · 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
Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor
Esch, F. S., Keim, P. S., Beattie, E. C., Blacher, R. W., Culwell, A. R., Oltersdorf, T., McClure, D., & Ward, P. J. (1990) · Science · doi:10.1126/science.2111583 · Cited by 1,403 · see citing works
Amyloid, the presenilins and Alzheimer’s disease
Hardy, J. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)01030-2 · Cited by 1,370 · see citing works
Endoproteolysis of Presenilin 1 and Accumulation of Processed Derivatives In Vivo
Thinakaran, G., Borchelt, D., Lee, M. K., Slunt, H. H., Spitzer, L., Kim, G. J., Ratovitski, T., Davenport, F., Nordstedt, C., Seeger, M., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80291-3 · Cited by 1,013 · see citing works
Evidence that production and release of amyloid beta-protein involves the endocytic pathway
Koo, E. H., & Squazzo, S. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32449-3 · Cited by 989 · see citing works
Skeletal and CNS Defects in Presenilin-1-Deficient Mice
Shen, J., Bronson, R. T., Chen, D., Xia, W., Selkoe, D. J., & Tonegawa, S. (1997) · Cell · doi:10.1016/s0092-8674(00)80244-5 · Cited by 947 · see citing works
Self-citationNitsch, R. M., Slack, B. E., Wurtman, R. J., & Growdon, J. H. (1992) · Science · doi:10.1126/science.1411529 · Cited by 898 · see citing works
Amyloid β-Protein and the Genetics of Alzheimer's Disease
Selkoe, D. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18295 · Cited by 798 · see citing works
Self-citationLevitan, D. J., & Greenwald, I. (1995) · Nature · doi:10.1038/377351a0 · Cited by 709 · see citing works
β-amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity
Zheng, H., Jiang, M., Trumbauer, M. E., SIRINATHSINGHJI, D. J. S., Hopkins, R., Smith, D. W., HEAVENS, R. P., Dawson, G. R., Boyce, S., Conner, M. W., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90073-x · Cited by 705 · 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
Secretion of β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid peptide
Seubert, P. A., Oltersdorf, T., Lee, M., Barbour, R., Blomquist, C. L., Davis, D. L., Bryant, K., Fritz, L. C., Galasko, D., Thal, L. J., et al. (1993) · Nature · doi:10.1038/361260a0 · Cited by 552 · see citing works
Miller, D. L., Papayannopoulos, I. A., Styles, J., Bobin, S. A., Lin, Y. Y., Biemann, K., & Iqbal, K. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1112 · Cited by 510 · see citing works
Activation of protein kinase C inhibits cellular production of the amyloid beta-protein.
Hung, A. Y., Haass, C., Nitsch, R. M., Qiu, W. Q., Citron, M., Wurtman, R. J., Growdon, J. H., & Selkoe, D. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49409-x · Cited by 399 · see citing works
Self-citationArribas, 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
Yu, G., Chen, F., Lévesque, G., Nishimura, M., Zhang, D., Lévesque, L., Rogaeva, E., Xu, D., Liang, Y., Duthie, M., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16470 · Cited by 367 · see citing works
Slunt, H. H., Thinakaran, G., von Koch, C., Lo, A., Tanzi, R. E., & Sisodia, S. S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41992-2 · Cited by 346 · see citing works
Capell, A., Grünberg, J., Pesold, B., Diehlmann, A., Citron, M., Nixon, R. A., Beyreuther, K. T., Selkoe, D. J., & Haass, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3205 · Cited by 322 · see citing works
Self-citationThinakaran, G., Harris, C. L., Ratovitski, T., Davenport, F., Slunt, H. H., Price, D. L., Borchelt, D., & Sisodia, S. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28415 · Cited by 314 · see citing works
Intracellular Generation and Accumulation of Amyloid β-Peptide Terminating at Amino Acid 42
Wild-Bode, C., Yamazaki, T., Capell, A., Leimer, U., Steiner, H., Ihara, Y., & Haass, C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16085 · Cited by 303 · see citing works
Platelet Coagulation Factor XI a -Inhibitor, a Form of Alzheimer Amyloid Precursor Protein
Smith, R. P., Higuchi, D. A., & Broze, G. (1990) · Science · doi:10.1126/science.2111585 · Cited by 301 · see citing works
Xia, W., Zhang, J., Kholodenko, D., Citron, M., Podlisny, M. B., Teplow, D. B., Haass, C., Seubert, P. A., Koo, E. H., & Selkoe, D. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7977 · Cited by 282 · see citing works
Self-citationPerez, R. G., Zheng, H., der Ploeg, L. H. T. V., & Koo, E. H. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-24-09407.1997 · Cited by 265 · see citing works
Yamazaki, T., Selkoe, D. J., & Koo, E. H. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.2.431 · Cited by 207 · see citing works
Self-citationQian, S., Jiang, P., Guan, X.-M., Singh, G., Trumbauer, M. E., Yu, H. H., Chen, H. Y., der Ploeg, L. H. T. V., & Zheng, H. (1998) · Neuron · doi:10.1016/s0896-6273(00)80999-x · Cited by 169 · see citing works
Klafki, H., Abramowski, D., Swoboda, R., Paganetti, P., & Staufenbiel, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.45.28655 · Cited by 159 · see citing works
Subcellular Distribution and Turnover of Presenilins in Transfected Cells
Zhang, J., Kang, D. E., Xia, W., Okochi, M., Mori, H., Selkoe, D. J., & Koo, E. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.20.12436 · Cited by 146 · see citing works
Self-citationChyung, A. S. C., Greenberg, B., Cook, D. G., Doms, R. W., & Lee, V. M. ‐. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.138.3.671 · Cited by 136 · see citing works
Yamazaki, T., Koo, E. H., & Selkoe, D. J. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.5.999 · Cited by 135 · see citing works
Self-citationDavis, J. A., Naruse, S., Chen, H., Eckman, C., Younkin, S. G., Price, D. L., Borchelt, D., Sisodia, S. S., & Wong, P. C. (1998) · Neuron · doi:10.1016/s0896-6273(00)80998-8 · Cited by 131 · see citing works
Haass, C., Koo, E. H., Capell, A., Teplow, D. B., & Selkoe, D. J. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.128.4.537 · Cited by 129 · see citing works
Self-citationSimons, M., Ikonen, E., Tienari, P. J., Cid-Arregui, Á., Mönning, U., Beyreuther, K. T., & Dotti, C. G. (1995) · Journal of Neuroscience Research · doi:10.1002/jnr.490410114 · Cited by 120 · 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
LeBlanc, A. C., Koutroumanis, M., & Goodyer, C. G. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-08-02907.1998 · Cited by 72 · see citing works
Walter, J., Grünberg, J., Schindzielorz, A., et al. (1998) · Biochemistry · doi:10.1021/bi971763a · Cited by 58 · see citing works
Ross, S. L., Martin, F. H., Simonet, L., Jacobsen, F. W., Deshpande, R. R., Vassar, R. J., Bennett, B., Luo, Y., Wooden, S. K., Hu, S., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15309 · Cited by 16 · see citing works
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Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity
Yan, R., Bienkowski, M. J., Shuck, M. E., Miao, H., Tory, M. C., Pauley, A. M., Brashler, J. R., Stratman, N. C., Mathews, W. R., Buhl, A. E., et al. (1999) · Nature · doi:10.1038/990107 · Cited by 1,438 · see citing works
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413 · see citing works
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209 · see citing works
A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60
Cao, X., & Südhof, T. C. (2001) · Science · doi:10.1126/science.1058783 · Cited by 1,202 · see citing works
Middeldorp, J., & Hol, E. M. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.01.005 · Cited by 1,080 · see citing works
Intraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991 · 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
Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
Li, Y.-M., Xu, M., Lai, M.-T., Huang, Q., Castro, J. L., DiMuzio-Mower, J., Harrison, T., Lellis, C., Nadin, A., Neduvelil, J. G., et al. (2000) · Nature · doi:10.1038/35015085 · Cited by 866 · see citing works
Neuropathology of Alzheimer's Disease
Perl, D. P. (2010) · Mount Sinai Journal of Medicine: A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20157 · Cited by 825 · see citing works
Epigenetic mechanisms in memory formation
Levenson, J. M., & Sweatt, J. D. (2005) · Nature Reviews Neuroscience · doi:10.1038/nrn1604 · Cited by 767 · see citing works
Characterization of amyloid deposition in the APPswe/PS1dE9 mouse model of Alzheimer disease
Garcia-Alloza, M., Robbins, E. M., Zhang-Nunes, S. X., Purcell, S. M., Betensky, R. A., Raju, S., Prada, C., Greenberg, S. M., Bacskai, B. J., & Frosch, M. P. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.08.017 · Cited by 744 · see citing works
Role of the Reelin Signaling Pathway in Central Nervous System Development
Rice, D. S., & Curran, T. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1005 · Cited by 667 · see citing works
Metformin: An Old But Still the Best Treatment for Type 2 Diabetes
Rojas, L. B. A., & Gomes, M. B. (2013) · Diabetology & Metabolic Syndrome · doi:10.1186/1758-5996-5-6 · Cited by 567 · 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
Dineley, K. T., Westerman, M., Bui, D., Bell, K., Ashe, K. H., & Sweatt, J. D. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-12-04125.2001 · Cited by 462 · see citing works
Zhang, Y., McLaughlin, R., Goodyer, C., & LeBlanc, A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200110119 · Cited by 418 · see citing works
Astrocytes accumulate Aβ42 and give rise to astrocytic amyloid plaques in Alzheimer disease brains
Nagele, R. G., D’Andrea, M. R., Lee, H., Venkataraman, V., & Wang, H.-Y. (2003) · Brain Research · doi:10.1016/s0006-8993(03)02361-8 · Cited by 416 · see citing works
Cabral, G. A., & Griffin-Thomas, L. (2009) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409000957 · Cited by 408 · see citing works
D'Andrea, M. R., Nagele, R. G., Wang, H., Peterson, P. A., & Lee, D. H. S. (2001) · Histopathology · doi:10.1046/j.1365-2559.2001.01082.x · Cited by 390 · see citing works
Chen, Y., Zhou, K., Wang, R., Liu, Y., Kwak, Y.-D., Ma, T., Thompson, R. C., Zhao, Y., Smith, L., Gasparini, L., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807991106 · Cited by 390 · see citing works
The role of oxidative stress in the toxicity induced by amyloid β-peptide in Alzheimer’s disease
Miranda, S., Opazo, C., Larrondo, L. F., Muñoz, F. J., Ruiz, F., Leighton, F., & Inestrosa, N. C. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(00)00015-0 · Cited by 369 · see citing works
Clearing amyloid through the blood-brain barrier
Zlokovic, B. V. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02385.x · Cited by 336 · see citing works
Matsubara, E., Bryant‐Thomas, T., Pacheco Quinto, J., Henry, T. L., Poeggeler, B., Herbert, D., Cruz‐Sanchez, F., Chyan, Y., Smith, M. A., Perry, G., et al. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01654.x · Cited by 332 · see citing works
Mourtas, S., Lazar, A. N., Markoutsa, E., Duyckaerts, C., & Antimisiaris, S. G. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.04.050 · Cited by 263 · see citing works
Ghosal, K., Vogt, D. L., Liang, M., Shen, Y., Lamb, B. T., & Pimplikar, S. W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907652106 · Cited by 245 · see citing works
Critical role of endothelial Notch1 signaling in postnatal angiogenesis
Takeshita, K., Satoh, M., Ii, M., Silver, M., Limbourg, F. P., Mukai, Y., Rikitake, Y., Radtke, F., Gridley, T., Losordo, D. W., et al. (2007) · Circulation Research · doi:10.1161/01.res.0000254788.47304.6e · Cited by 232 · see citing works
Ho, A., & Südhof, T. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308655100 · Cited by 224 · see citing works
Dineley, K. T., Xia, X., Bui, D., Sweatt, J. D., & Zheng, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200164200 · Cited by 212 · 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
Mann, D. M. A., Pickering-Brown, S. M., Takeuchi, A., & Iwatsubo, T. (2001) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64688-3 · Cited by 182 · see citing works
Amyloid-β is an antioxidant for lipoproteins in cerebrospinal fluid and plasma
Kontush, A., Berndt, C., Weber, W., Akopyan, V., Arlt, S., Schippling, S., & Beisiegel, U. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00458-5 · Cited by 180 · see citing works
Bouter, Y., Dietrich, K., Wittnam, J. L., Rezaei-Ghaleh, N., Pillot, T., Papot-Couturier, S., Lefebvre, T., Sprenger, F., Wirths, O., Zweckstetter, M., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1129-2 · Cited by 175 · see citing works
A Review of Dietary Phytochemicals and Their Relation to Oxidative Stress and Human Diseases
Guan, R., Van Le, Q., Yang, H., Zhang, D., Gu, H., Yang, Y., Sonne, C., Lam, S. S., Zhong, J., Jianguang, Z., et al. (2021) · Chemosphere · doi:10.1016/j.chemosphere.2020.129499 · Cited by 169 · see citing works
Kumar-Singh, S. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.18.2589 · Cited by 158 · see citing works
Rodríguez-Rodríguez, C., Telpoukhovskaia, M., & Orvig, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.008 · Cited by 151 · see citing works
Siman, R., Reaume, A. G., Savage, M. J., Trusko, S., Lin, Y.-G., Scott, R. W., & Flood, D. G. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-23-08717.2000 · Cited by 133 · see citing works
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 · see citing works
Shaked, G. M., Kummer, M. P., Lu, D. C., Galvan, V., Bredesen, D. E., Koo, E. H., Shaked, G. M., Kummer, M. P., Lu, D. C., Galvan, V., et al. (2006) · The FASEB Journal · doi:10.1096/fj.05-5032fje · Cited by 132 · see citing works
Morishima-Kawashima, M., Oshima, N., Ogata, H., Yamaguchi, H., Yoshimura, M., Sugihara, S., & Ihara, Y. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64847-x · Cited by 119 · see citing works
Disruption of protein–protein interactions: Towards new targets for chemotherapy
Loregian, A., & Palù, G. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20356 · Cited by 108 · see citing works
Arya, A., Chahal, R., Rao, R., Rahman, M. H., Kaushik, D., Akhtar, M. F., Saleem, A., Khalifa, S. M. A., El-Seedi, H. R., Kamel, M., et al. (2021) · Biomolecules · doi:10.3390/biom11030350 · Cited by 111 · see citing works
Amato, A., Terzo, S., & Mulè, F. (2019) · Antioxidants · doi:10.3390/antiox8120608 · Cited by 107 · see citing works
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Wirths, O., Bethge, T., Marcello, A., Harmeier, A., Jawhar, S., Lucassen, P. J., Multhaup, G., Brody, D. L., Esparza, T., Ingelsson, M., et al. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-009-0314-x · Cited by 106 · see citing works
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Wirths, O., Erck, C., Martens, H., Harmeier, A., Geumann, C., Jawhar, S., Kumar, S., Multhaup, G., Walter, J., Ingelsson, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.178707 · Cited by 103 · see citing works
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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
Wnt/β-Catenin Signaling in Alzheimer’s Disease
Ferrari, G., Avila, M., Medina, M., Perez-Palma, E., Bustos, B., & Alarcon, M. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527312666131223113900 · Cited by 95 · see citing works
Expression Profiling of Lymphocyte Plasma Membrane Proteins
Peirce, M. J., Wait, R., Begum, S., Saklatvala, J., & Cope, A. P. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m300064-mcp200 · Cited by 92 · see citing works
ERK1/2 is an endogenous negative regulator of the γsecretase activity
Kim, S., Park, H., Hong, H. S., Baik, E. J., Jung, M. W., & Mook‐Jung, I. (2006) · The FASEB Journal · doi:10.1096/fj.05-4055fje · Cited by 92 · see citing works
Function and Dysfunction of the Presenilins
Sisodia, S. S., Kim, S. H., & Thinakaran, G. (1999) · The American Journal of Human Genetics · doi:10.1086/302475 · Cited by 76 · see citing works
Zhong, P., Gu, Z., Wang, X., Jiang, H., Feng, J., & Yan, Z. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302789200 · Cited by 71 · see citing works
Modulation of β-Amyloid Fibril Formation in Alzheimer’s Disease by Microglia and Infection
Brown, M. R., Radford, S. E., & Hewitt, E. W. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.609073 · Cited by 67 · see citing works
Chen, G., Chen, P., Tan, H., Ma, D., Dou, F., Feng, J., & Yan, Z. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.04.023 · Cited by 36 · see citing works
Meißner, J. N., Bouter, Y., & Bayer, T. A. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142868 · Cited by 16 · see citing works
- Authors
- Selkoe, D.
- Affiliations
- Brigham and Women's Hospital (US)
- Corresponding author
- Selkoe, D
- ORCID
- Selkoe, D
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 1998-11-01
- Volume
- 8
- Issue
- 11
- Pages
- 447-453
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W1995650022
- Cited by
- 862
- References
- 50
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 12 · 2023: 14 · 2022: 12 · 2021: 13 · 2020: 23 · 2019: 16 · 2018: 20 · 2017: 16 · 2016: 28 · 2015: 23 · 2014: 27 · 2013: 37 · 2012: 34
- FWCI
- 39.30
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- 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 precursor protein, presenilin, amyloid-beta, cell biology, pathogenesis, gene cloning, protein structure-function relationship
- MeSH terms
- Alzheimer Disease, Animals, Biological Transport, Humans, Membrane Proteins, Neurons, Endopeptidases, Protein Processing, Post-Translational, Subcellular Fractions, Amyloid beta-Peptides, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, Presenilin-2, Amyloid Precursor Protein Secretases
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