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Secretion of β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid peptide
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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
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
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
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
Self-citationIsolation 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
Self-citationMullan, 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
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
Chartier-Harlin, M.-C., Crawford, F., Houlden, H., Warren, A., Hughes, D., Fidani, L., Goate, A., Rossor, M., Roques, P., Hardy, J., et al. (1991) · Nature · doi:10.1038/353844a0 · Cited by 1,214
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Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
Self-citationPurification and cloning of amyloid precursor protein β-secretase from human brain
Sinha, S., Anderson, J. P., Barbour, R., Basi, G. S., Caccavello, R., Davis, D., Doan, M., Dovey, H. F., Frigon, N., Hong, J., et al. (1999) · Nature · doi:10.1038/990114 · Cited by 1,612
Self-citationCitron, M., Westaway, D., Xia, W., Carlson, G., Diehl, T., Levesque, G., Johnson-wood, K., Lee, M., Seubert, P., Davis, A., et al. (1997) · Nature Medicine · doi:10.1038/nm0197-67 · Cited by 1,271
Self-citationTranslating cell biology into therapeutic advances in Alzheimer's disease
Selkoe, D. J. (1999) · Nature · doi:10.1038/399a023 · Cited by 1,166
The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease
Selkoe, D. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01363-4 · Cited by 862
The secretases: enzymes with therapeutic potential in Alzheimer disease
De Strooper, B., Vassar, R., & Golde, T. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2009.218 · Cited by 799
Roberds, S. L. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.12.1317 · Cited by 705
Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
Haass, C., & Selkoe, D. J. (1993) · Cell · doi:10.1016/0092-8674(93)90312-e · Cited by 686
Mattson, M. P., Cheng, B., Culwell, A. R., Esch, F. S., Lieberburg, I., & Rydel, R. E. (1993) · Neuron · doi:10.1016/0896-6273(93)90315-i · Cited by 656
Self-citationThe Alzheimer's disease Beta-secretase enzyme, BACE1
Cole, S. L., & Vassar, R. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-22 · Cited by 550
(1997) · doi:10.1073/pnas.94.4.1550 · Cited by 535
Exosomes: Vehicles for the Transfer of Toxic Proteins Associated with Neurodegenerative Diseases?
Bellingham, S. A., Guo, B. B., Coleman, B. M., & Hill, A. F. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00124 · Cited by 412
The molecular bases of Alzheimer’s disease and other neurodegenerative disorders
Maccioni, R. B., Muñoz, J. P., & Barbeito, L. (2001) · Archives of Medical Research · doi:10.1016/s0188-4409(01)00316-2 · Cited by 474
Liao, Y.-F., Wang, B.-J., Cheng, H.-T., Kuo, L.-H., & Wolfe, M. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402034200 · Cited by 389
Gabuzda, D., Busciglio, J., Chen, L. B., Matsudaira, P., & Yankner, B. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36875-8 · Cited by 373
Cholesterol Modulates α-Secretase Cleavage of Amyloid Precursor Protein
Bodovitz, S., & Klein, W. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4436 · Cited by 359
Kurochkin, I. V., & Goto, S. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00387-4 · Cited by 340
Expression Analysis of BACE2 in Brain and Peripheral Tissues
Bennett, B. D., Babu-Khan, S., Loeloff, R., Louis, J.-C., Curran, E., Citron, M., & Vassar, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002688200 · Cited by 317
Ghiso, J., Matsubara, E., Koudinov, A., Choi-Miura, N. H., Tomita, M., Wisniewski, T., & Frangione, B. (1993) · Biochemical Journal · doi:10.1042/bj2930027 · Cited by 304
Velliquette, R. A., O'Connor, T., & Vassar, R. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2350-05.2005 · Cited by 254
Golde, T. E., Eckman, C. B., & Younkin, S. G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00043-0 · Cited by 244
Wertkin, A. M., Turner, R. S., Pleasure, S. J., Golde, T. E., Younkin, S. G., Trojanowski, J. Q., & Lee, V. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9513 · Cited by 231
Ling, Y., Morgan, K., & Kalsheker, N. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00133-x · Cited by 224
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Sahni, J. K., Doggui, S., Ali, J., Baboota, S., Dao, L., & Ramassamy, C. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2010.11.033 · Cited by 219
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Nitsch, R. M., Deng, M., Growdon, J. H., & Wurtman, R. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4188 · Cited by 219
Implications of the serine protease HtrA1 in amyloid precursor protein processing
Grau, S., Baldi, A., Bussani, R., Tian, X., Stefanescu, R., Przybylski, M., Richards, P., Jones, S. A., Shridhar, V., Clausen, T., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501823102 · Cited by 215
Coleman, B. M., & Hill, A. F. (2015) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.02.007 · Cited by 208
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SELKOE, D. J., YAMAZAKI, T., CITRON, M., PODLISNY, M. B., KOO, E. H., TEPLOW, D. B., & HAASS, C. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34401.x · Cited by 205
MATTSON, M. P. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb44401.x · Cited by 166
Turner, R. S., Suzuki, N., Chyung, A. S. C., Younkin, S. G., & Lee, V. M.-Y. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8966 · Cited by 161
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Pedrini, S., Carter, T. L., Prendergast, G., Petanceska, S., Ehrlich, M. E., & Gandy, S. (2005) · PLoS Medicine · doi:10.1371/journal.pmed.0020018 · Cited by 154
Reaume, A. G., Howland, D. S., Trusko, S. P., Savage, M. J., Lang, D. M., Greenberg, B. D., Siman, R., & Scott, R. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23380 · Cited by 150
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(2008) · Handbook of Clinical Neurology · doi:10.1016/s0072-9752(07)01223-7 · Cited by 137
Avila-Muñoz, E., & Arias, C. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.07.004 · Cited by 114
Nitsch, R. M., Rebeck, G. W., Deng, M., Richardson, U. I., Tennis, M., Schenk, D. B., Vigo‐Pelfrey, C., Lieberburg, I., Wurtman, R. J., Hyman, B. T., et al. (1995) · Annals of Neurology · doi:10.1002/ana.410370414 · Cited by 113
Self-citationMURAKAMI, N., YAMAKI, T., IWAMOTO, Y., SAKAKIBARA, T., KOBORI, N., FUSHIKI, S., & UEDA, S. (1998) · Journal of Neurotrauma · doi:10.1089/neu.1998.15.993 · Cited by 100
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Fluhrer, R., Capell, A., Westmeyer, G., Willem, M., Hartung, B., Condron, M. M., Teplow, D. B., Haass, C., & Walter, J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00908.x · Cited by 95
Felsenstein, K. M., Hunihan, L. W., & Roberts, S. B. (1994) · Nature Genetics · doi:10.1038/ng0394-251 · Cited by 90
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Hoe, H.-S., & Rebeck, G. W. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.02.013 · Cited by 85
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Vassar, R., & Cole, S. (2007) · Current Genomics · doi:10.2174/138920207783769512 · Cited by 84
Zhao, J., Paganini, L., Mucke, L., Gordon, M., Refolo, L., Carman, M., Sinha, S., Oltersdorf, T., Lieberburg, I., & McConlogue, L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31407 · Cited by 84
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Bodendorf, U., Fischer, F., Bodian, D., Multhaup, G., & Paganetti, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008861200 · Cited by 58
Expression of the Anti-amyloidogenic Secretase ADAM10 Is Suppressed by Its 5′-Untranslated Region
Lammich, S., Buell, D., Zilow, S., Ludwig, A.-K., Nuscher, B., Lichtenthaler, S. F., Prinzen, C., Fahrenholz, F., & Haass, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110742 · Cited by 48
Motonaga, K., Itoh, M., Becker, L. E., Goto, Y.-I., & Takashima, S. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00287-2 · Cited by 45
Savage, M. J., Iqbal, M., Loh, T., Trusko, S. P., Scott, R., & Siman, R. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90490-1 · Cited by 42
MASUMURA, M., HATA, R., URAMOTO, H., MURAYAMA, N., OHNO, T., & SAWADA, T. (2000) · Journal of Neurotrauma · doi:10.1089/neu.2000.17.123 · Cited by 34
Dodart, J.-C., Bales, K. R., Johnstone, E. M., Little, S. P., & Paul, S. M. (2002) · Brain Research · doi:10.1016/s0006-8993(02)03437-6 · Cited by 30
Connop, B. P., Thies, R. L., Beyreuther, K., Ida, N., & Reiner, P. B. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.721457.x · Cited by 19
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KAPLITT, M., GOURAS, G. K., MAKIMURA, H., JOVANOVIC, J., SWEENEY, D., GREENGARD, P., RELKIN, N. R., & GANDY, S. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb32597.x · Cited by 12
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SINHA, S., ANDERSON, J., JOHN, V., McCONLOGUE, L., BASI, G., THORSETT, E., & SCHENK, D. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06923.x · Cited by 12
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Metadata
- Authors
- Seubert, P., Oltersdorf, T., Lee, M. G., Barbour, R., Blomquist, C., Davis, D. L., Bryant, K., Fritz, L. C., Galasko, D., Thal, L. J., Lieberburg, I., & Schenk, D. B.
- Venue
- Nature
- Published
- 1993-01
- Volume
- 361
- Issue
- 6409
- Pages
- 260-263
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1980433009
- Cited by
- 552
- References
- 8
- FWCI
- 36.20
- Type
- journal article
- Language
- en
- Open access
- closed
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