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The role of presenilin cofactors in the γ-secretase complex
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Deficiency 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
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
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
Cited by
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
Amyloid Precursor Protein Processing and Alzheimer's Disease
O'Brien, R. J., & Wong, P. C. (2011) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-061010-113613 · Cited by 2,061
Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965
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
Alzheimer’s Disease: The Challenge of the Second Century
Holtzman, D. M., Morris, J. C., & Goate, A. M. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002369 · Cited by 1,424
Review Article: Genetics of Alzheimer Disease
Bekris, L. M., Yu, C.-E., Bird, T. D., & Tsuang, D. W. (2010) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/0891988710383571 · Cited by 1,029
APP processing in Alzheimer’s disease.
Zhang, Y.-W., Thompson, R., Zhang, H., & Xu, H. (2011) · Molecular Brain · doi:10.1186/1756-6606-4-3 · Cited by 983
Aph-1, Pen-2, and Nicastrin with Presenilin Generate an Active γ-Secretase Complex
De Strooper, B. (2003) · Neuron · doi:10.1016/s0896-6273(03)00205-8 · Cited by 965
Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future
Zhang, Y., Chen, H., Li, R., Sterling, K., & Song, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01484-7 · Cited by 988
Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases
Selkoe, D. J. (2004) · Nature Cell Biology · doi:10.1038/ncb1104-1054 · Cited by 863
Reconsideration of Amyloid Hypothesis and Tau Hypothesis in Alzheimer's Disease
Kametani, F., & Hasegawa, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00025 · Cited by 836
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
Animal models of Alzheimer's disease and frontotemporal dementia
Götz, J., & Ittner, L. M. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2420 · Cited by 676
NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ42 in vivo
Eriksen, J. L., Sagi, S. A., Smith, T. E., Weggen, S., Das, P., McLendon, D. C., Ozols, V. V., Jessing, K. W., Zavitz, K. H., Koo, E. H., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18162 · Cited by 634
The 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
Laird, F. M., Cai, H., Savonenko, A. V., Farah, M. H., He, K., Melnikova, T., Wen, H., Chiang, H.-C., Xu, G., Koliatsos, V. E., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2766-05.2005 · Cited by 521
Proteases and Proteolysis in Alzheimer Disease: A Multifactorial View on the Disease Process
De Strooper, B. (2010) · Physiological Reviews · doi:10.1152/physrev.00023.2009 · Cited by 455
Iijima, K., Liu, H.-P., Chiang, A.-S., Hearn, S. A., Konsolaki, M., & Zhong, Y. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400895101 · Cited by 440
Association of γ-Secretase with Lipid Rafts in Post-Golgi and Endosome Membranes
Vetrivel, K. S., Cheng, H., Lin, W., Sakurai, T., Li, T., Nukina, N., Wong, P. C., Xu, H., & Thinakaran, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407986200 · Cited by 413
Self-citationLiao, 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
Lichtenthaler, S. F., Lemberg, M. K., & Fluhrer, R. (2018) · The EMBO Journal · doi:10.15252/embj.201899456 · Cited by 323
Recognition of the amyloid precursor protein by human γ-secretase
Zhou, R., Yang, G., Guo, X., Zhou, Q., Lei, J., & Shi, Y. (2019) · Science · doi:10.1126/science.aaw0930 · Cited by 304
Sannerud, R., Esselens, C., Ejsmont, P., Mattera, R., Rochin, L., Tharkeshwar, A. K., De Baets, G., De Wever, V., Habets, R., Baert, V., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.020 · Cited by 299
Neurotherapeutic applications of nanoparticles in Alzheimer’s disease
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
Mouse Models of Alzheimer’s Disease
Yokoyama, M., Kobayashi, H., Tatsumi, L., & Tomita, T. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.912995 · Cited by 213
Self-citationLichtenthaler, S. F., Haass, C., & Steiner, H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07248.x · Cited by 205
The potential role of amyloid in the pathogenesis of age-related macular degeneration
Yoshida, T. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24635 · Cited by 202
Neuronal Cell Death in Alzheimers Disease and a Neuroprotective Factor, Humanin
Niikura, T., Tajima, H., & Kita, Y. (2006) · Current Neuropharmacology · doi:10.2174/157015906776359577 · Cited by 184
BACE1 activity is modulated by cell-associated sphingosine-1-phosphate
Takasugi, N., Sasaki, T., Suzuki, K., Osawa, S., Isshiki, H., Hori, Y., Shimada, N., Higo, T., Yokoshima, S., Fukuyama, T., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6467-10.2011 · Cited by 181
Self-citationSubcellular Topography of Neuronal Aβ Peptide in APPxPS1 Transgenic Mice
Langui, D., Girardot, N., El Hachimi, K. H., Allinquant, B., Blanchard, V., Pradier, L., & Duyckaerts, C. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63405-0 · Cited by 165
The physiology of the β‐amyloid precursor protein intracellular domain AICD
Pardossi‐Piquard, R., & Checler, F. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07475.x · Cited by 159
Bolduc, D. M., Montagna, D. R., Gu, Y., Selkoe, D. J., & Wolfe, M. S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512952113 · Cited by 144
Wu, Y., Du, S., Johnson, J. L., Tung, H.-Y., Landers, C. T., Liu, Y., Seman, B. G., Wheeler, R. T., Costa-Mattioli, M., Kheradmand, F., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-07991-4 · Cited by 143
Abolhassani, N., Leon, J., Sheng, Z., Oka, S., Hamasaki, H., Iwaki, T., & Nakabeppu, Y. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.05.005 · Cited by 140
Wakabayashi, T., Craessaerts, K., Bammens, L., Bentahir, M., Borgions, F., Herdewijn, P., Staes, A., Timmerman, E., Vandekerckhove, J., Rubinstein, E., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1978 · Cited by 135
Making the final cut: Pathogenic amyloid-β peptide generation by γ-secretase
Steiner, H., Fukumori, A., Tagami, S., & Okochi, M. (2018) · Cell Stress · doi:10.15698/cst2018.11.162 · Cited by 133
Genome instability in Alzheimer disease
Hou, Y., Song, H., Croteau, D. L., Akbari, M., & Bohr, V. A. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.04.005 · Cited by 120
Araki, Y., Tomita, S., Yamaguchi, H., Miyagi, N., Sumioka, A., Kirino, Y., & Suzuki, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306024200 · Cited by 122
Zhang, X., Garbett, K., Veeraraghavalu, K., Wilburn, B., Gilmore, R., Mirnics, K., & Sisodia, S. S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0556-12.2012 · Cited by 122
Quintero-Monzon, O., Martin, M. M., Fernandez, M. A., Cappello, C. A., Krzysiak, A. J., Osenkowski, P., & Wolfe, M. S. (2011) · Biochemistry · doi:10.1021/bi2007146 · Cited by 118
Potential Contribution of Exosomes to the Prion-Like Propagation of Lesions in Alzheimer’s Disease
Vingtdeux, V., Sergeant, N., & Buée, L. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00229 · Cited by 116
Axonal transport of APP and the spatial regulation of APP cleavage and function in neuronal cells
Brunholz, S., Sisodia, S., Lorenzo, A., Deyts, C., Kins, S., & Morfini, G. (2012) · Experimental Brain Research · doi:10.1007/s00221-011-2870-1 · Cited by 92
FTY720/fingolimod, a sphingosine analogue, reduces amyloid-β production in neurons
Takasugi, N., Sasaki, T., Ebinuma, I., Osawa, S., Isshiki, H., Takeo, K., Tomita, T., & Iwatsubo, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064050 · Cited by 85
Self-citationThe Basic Biology of BACE1: A Key Therapeutic Target for Alzheimers Disease
Vassar, R., & Cole, S. (2007) · Current Genomics · doi:10.2174/138920207783769512 · Cited by 84
TREM2‐dependent effects on microglia in Alzheimer's disease
Zhou, Y., Ulland, T. K., & Colonna, M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00202 · Cited by 82
APOE and other loci affect age‐at‐onset in Alzheimer's disease families with PS2 mutation
Wijsman, E. M., Daw, E. W., Yu, X., Steinbart, E. J., Nochlin, D., Bird, T. D., & Schellenberg, G. D. (2005) · American Journal of Medical Genetics Part B: Neuropsychiatric Genetics · doi:10.1002/ajmg.b.30087 · Cited by 79
Modeling the complex pathology of Alzheimer's disease in Drosophila
Fernandez-Funez, P., de Mena, L., & Rincon-Limas, D. E. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.05.013 · Cited by 69
Massey, L. K., Mah, A. L., & Monteiro, M. J. (2005) · Biochemical Journal · doi:10.1042/bj20050491 · Cited by 66
A presenilin-1 mutation causes Alzheimer disease without affecting Notch signaling
Zhang, S., Cai, F., Wu, Y., Bozorgmehr, T., Wang, Z., Zhang, S., Huang, D., Guo, J., Shen, L., Rankin, C., et al. (2020) · Molecular Psychiatry · doi:10.1038/s41380-018-0101-x · Cited by 66
Alexander, C., Li, T., Hattori, Y., Chiu, D., Frost, G. R., Jonas, L., Liu, C., Anderson, C. J., Wong, E., Park, L., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01676-7 · Cited by 64
A cellular complex of BACE1 and γ-secretase sequentially generates Aβ from its full-length precursor
Liu, L., Ding, L., Rovere, M., Wolfe, M. S., & Selkoe, D. J. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201806205 · Cited by 64
Toh, W. H., & Gleeson, P. A. (2016) · Biochemical Journal · doi:10.1042/bcj20160147 · Cited by 62
Turning the tide on Alzheimer’s disease: modulation of γ-secretase
Luo, J. E., & Li, Y.-M. (2022) · Cell & Bioscience · doi:10.1186/s13578-021-00738-7 · Cited by 59
Molecular mechanism of intramembrane proteolysis by γ-secretase
Tomita, T. (2014) · The Journal of Biochemistry · doi:10.1093/jb/mvu049 · Cited by 58
Self-citationThomas, R. S., Henson, A., Gerrish, A., Jones, L., Williams, J., & Kidd, E. J. (2016) · BMC Neuroscience · doi:10.1186/s12868-016-0288-1 · Cited by 55
Expression of BC1 Impairs Spatial Learning and Memory in Alzheimer’s Disease Via APP Translation
Zhang, T., Pang, P., Fang, Z., Guo, Y., Li, H., Li, X., Tian, T., Yang, X., Chen, W., Shu, S., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0820-z · Cited by 52
γ-Secretase and its modulators: Twenty years and beyond
Xia, W. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.02.011 · Cited by 54
László, Z. I., & Lele, Z. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.972059 · Cited by 49
Tate, B. A., & Mathews, P. M. (2006) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2006.10.re2 · Cited by 48
Kaneko, H., Kakita, A., Kasuga, K., Nozaki, H., Ishikawa, A., Miyashita, A., Kuwano, R., Ito, G., Iwatsubo, T., Takahashi, H., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4244-07.2007 · Cited by 44
Self-citationDe Strooper, B., & Karran, E. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00057-w · Cited by 36
A non-human primate model of familial Alzheimer’s disease
Sato, K., Sasaguri, H., Kumita, W., Inoue, T., Kurotaki, Y., Nagata, K., Mihira, N., Sato, K., Sakuma, T., Yamamoto, T., et al. (2020) · doi:10.1101/2020.08.24.264259 · Cited by 29
γ-Secretase fanning the fire of innate immunity
Liu, C., Nikain, C., & Li, Y.-M. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221445 · Cited by 4
The roles of GxxxG motif and gamma-secretase components in APP processing
Kim, J. (2009) · Interdisciplinary Bio Central · doi:10.4051/ibc.2009.4.0015 · Cited by 3
Metadata
- Authors
- Takasugi, N., Tomita, T., Hayashi, I., Tsuruoka, M., Niimura, M., Takahashi, Y., Thinakaran, G., & Iwatsubo, T.
- Venue
- Nature
- Published
- 2003-03
- Volume
- 422
- Issue
- 6930
- Pages
- 438-441
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2075829521
- Cited by
- 867
- References
- 3
- FWCI
- 42.70
- Type
- journal article
- Language
- en
- Open access
- closed
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