Cited by 103Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.

Additive Effects of PS1 and APP Mutations on Secretion of the 42-Residue Amyloid β-Protein

Open access

Citron, Martin, Eckman, Christopher B., Diehl, Thekla S., Corcoran, Chris, Ostaszewski, Beth L., Xia, Weiming, Levesque, Georges, St. George Hyslop, Peter, Younkin, Steven G., Selkoe, Dennis J.·1998·Neurobiology of Disease

DOI 10.1006/nbdi.1998.0183

Open this paper in CoChat — free account

Abstract

Humans harboring missense mutations in the presenilin 1 (PS1) gene undergo progressive cerebral deposition of the 42-residue amyloid beta-protein (A beta 42) at an early age and develop severe Alzheimer's disease. A beta 42 is selectively elevated in the conditioned media of cells expressing mutant but not wild-type PS1, indicating that presenilin mutations alter APP processing. Here we analyze the effects of various PS1 mutant constructs on the cellular production of A beta 42. A construct expressing only the PS1 N-terminal endoproteolytic fragment with the mutation Y115H causes no significant increase in A beta 42, whereas a full-length PS1 construct with the same mutation does. This result suggests that the pathogenic effect of mutant presenilins is produced by the full-length molecule even though only a minor proportion of total PS1 occurs as holoprotein in tissues and cell lines. We demonstrate that the effects of two different PS1 mutations are additive when engineered into the same PS1 molecule. Therefore, two mutations alter gamma-secretase processing of APP more than one and the PS1 mutations described to date do not cause the maximum possible PS1-mediated rise in A beta 42. When a PS1 mutation was expressed in cells carrying the APPV717I mutation, A beta 42 rose dramatically to become the predominant secreted A beta species, an observation of interest for transgenic modeling of AD. Our results are consistent with the hypothesis that presenilin is a major regulator of the proteolytic processing of APP by gamma-secretases.

Integrity signals

Registry

Crossref · 10.1006/nbdi.1998.0183

Cites

29 of 29 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
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
Self-citation
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
Self-citation
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 1,486
Self-citation
Familial Alzheimer's Disease–Linked Presenilin 1 Variants Elevate Aβ1–42/1–40 Ratio In Vitro and In Vivo
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
Self-citation
An Increased Percentage of Long Amyloid β Protein Secreted by Familial Amyloid β Protein Precursor (βApp 717 ) Mutants
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471
Self-citation
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
Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice
Citron, 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-citation
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 1,025
Accelerated Amyloid Deposition in the Brains of Transgenic Mice Coexpressing Mutant Presenilin 1 and Amyloid Precursor Proteins
Borchelt, D. R., Ratovitski, T., van Lare, J., Lee, M. K., Gonzales, V., Jenkins, N. A., Copeland, N. G., Price, D. L., & Sisodia, S. S. (1997) · Neuron · doi:10.1016/s0896-6273(00)80974-5 · Cited by 1,023

Show all 28 references

Research works printed but not linked: 1

Zhang, 1997, Subcellular distribution of presenilin in transfected cells, Soc. Neurosci. Abstr.

Sorted by citations

Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530
“…the reports that intramolecular combination of FAD mutations in either APP or PS1 act additively to increase A 42 generation (Eckman et al., 1997; Citron et al., 1998), we established transgenic mouse lines that co-overexpress human APP695 with the Swedish (K670N, M671L), Florida (I716V), and…”
Background
Early-onset Amyloid Deposition and Cognitive Deficits in Transgenic Mice Expressing a Double Mutant Form of Amyloid Precursor Protein 695
Chishti, M. A., Yang, D.-S., Janus, C., Phinney, A. L., Horne, P., Pearson, J., Strome, R., Zuker, N., Loukides, J., French, J., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100710200 · Cited by 955
Self-citation
Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
Yu, G., Nishimura, M., Arawaka, S., Levitan, D. J., Zhang, L., Tandon, A., Song, Y., Rogaeva, E. A., Chen, F., Kawarai, T., et al. (2000) · Nature · doi:10.1038/35024009 · Cited by 929
Exosome reduction in vivo is associated with lower amyloid plaque load in the 5XFAD mouse model of Alzheimer's disease
Dinkins, M. B., Dasgupta, S., Wang, G., Zhu, G., & Bieberich, E. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.02.012 · Cited by 494
Neuron loss in the 5XFAD mouse model of Alzheimer’s disease correlates with intraneuronal Aβ42 accumulation and Caspase-3 activation
Eimer, W. A., & Vassar, R. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-2 · Cited by 425
“In the case of the 5XFAD model, the mouse overexpresses APP with K670N/M671L (Swedish mutation [12]), I716V (Florida mutation [13]), and V717I (London mutation [14]), and PS1 with M146L and L286V mutations [15].”
Background
Presenilin 1 Controls γ-Secretase Processing of Amyloid Precursor Protein in Pre-Golgi Compartments of Hippocampal Neurons
Annaert, W. G., Lévesque, L., Craessaerts, K., Dierinck, I., Snellings, G., Westaway, D. A., George‐Hyslop, P. S., Cordell, B., Fraser, P., & Strooper, B. D. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.2.277 · Cited by 316
Update on hypertension and Alzheimer's disease
Skoog, I. G., & Gustafson, D. (2006) · Neurological Research · doi:10.1179/016164106x130506 · Cited by 295
BACE1 gene deletion prevents neuron loss and memory deficits in 5XFAD APP/PS1 transgenic mice
Ohno, M., Cole, S. L., Yasvoina, M., Zhao, J., Citron, M., Berry, R., Disterhoft, J. F., & Vassar, R. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.12.008 · Cited by 290
Self-citation
Molecular genetics of Alzheimer's disease: An update
Brouwers, N., Sleegers, K., & Broeckhoven, C. V. (2008) · Annals of Medicine · doi:10.1080/07853890802186905 · Cited by 213
Expression of Alzheimer’s Disease-associated Presenilin-1 Is Controlled by Proteolytic Degradation and Complex Formation
Steiner, H., Capell, A., Pesold, B., Citron, M., Kloetzel, P. M., Selkoe, D. J., Romig, H., Mendla, K. D., & Haass, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.32322 · Cited by 198
Self-citation
Behavioural and psychological symptoms of dementia in mouse models of Alzheimer’s disease-related pathology
Kosel, F., Pelley, J. M. S., & Franklin, T. B. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.02.012 · Cited by 173
Presenilins and Alzheimer’s disease: biological functions and pathogenic mechanisms
Czech, C., Tremp, G. L., & Pradier, L. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(99)00033-7 · Cited by 160
The Genetics of Adult-Onset Neuropsychiatric Disease: Complexities and Conundra?
Kennedy, J. L., Farrer, L. A., Andreasen, N. C., Mayeux, R. P., & George‐Hyslop, P. S. (2003) · Science · doi:10.1126/science.1092132 · Cited by 149
Presenilin function and γ‐secretase activity
Brunkan, A. L., & Goate, A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03099.x · Cited by 149
Potential Link between Amyloid β-Protein 42 and C-terminal Fragment γ 49–99 of β-Amyloid Precursor Protein
Sato, T., Dohmae, N., Qi, Y. A., Kakuda, N., Misonou, H., Mitsumori, R., Maruyama, H., Koo, E. H., Haass, C., Takio, K., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211161200 · Cited by 150
Activation and intrinsic γ-secretase activity of presenilin 1
Ahn, K., Shelton, C. C., Tian, Y., Zhang, X., Gilchrist, M. L., Sisodia, S. S., & Li, Y. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013246107 · Cited by 139
Intramembrane proteolysis by presenilins
Steiner, H., & Haass, C. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043065 · Cited by 161
Protein misfolding in Alzheimer’s and Parkinson’s disease: genetics and molecular mechanisms
Forloni, G., Terreni, L., Bertani, I., Fogliarino, S., Invernizzi, R. W., Assini, A., Ribizzi, G., Negro, A., Calabrese, E., & Volonté, M. A. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00076-3 · Cited by 132
C Terminus of Presenilin Is Required for Overproduction of Amyloidogenic Aβ42 through Stabilization and Endoproteolysis of Presenilin
Tomita, T., Takikawa, R., Koyama, A., Morohashi, Y., Takasugi, N., Saido, T. C., Maruyama, K., & Iwatsubo, T. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-24-10627.1999 · Cited by 106
Increased fragmentation of sleep–wake cycles in the 5XFAD mouse model of Alzheimer’s disease
Sethi, M., Joshi, S., Webb, R. L., Beckett, T. L., Donohue, K. D., Murphy, M. P., O’Hara, B. F., & Duncan, M. J. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.01.035 · Cited by 109
Aging Increased Amyloid Peptide and Caused Amyloid Plaques in Brain of Old APP/V717I Transgenic Mice by a Different Mechanism than Mutant Presenilin1
Dewachter, I., Dorpe, J. V., Smeijers, L., Gilis, M., Kuipéri, C., Laenen, I., Caluwaerts, N., Moechars, D., Checler, F., Vanderstichele, H., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-17-06452.2000 · Cited by 108
Aging sensitizes toward ROS formation and lipid peroxidation in PS1M146L transgenic mice
Schüssel, K., Frey, C., Jourdan, C., Keil, U., Weber, C. C., Müller-Spahn, F., Müller, W. E., & Eckert, A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.041 · Cited by 94
Removing Protein Aggregates: The Role of Proteolysis in Neurodegeneration
Nijholt, D. A. T., Kimpe, L. D., Elfrink, H. L., Hoozemans, J. J. M., & Scheper, W. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711795843236 · Cited by 96
The First Proline of PALP Motif at the C Terminus of Presenilins Is Obligatory for Stabilization, Complex Formation, and γ-Secretase Activities of Presenilins
Tomita, T., Watabiki, T., Takikawa, R., Morohashi, Y., Takasugi, N., Kopan, R., Strooper, B. D., & Iwatsubo, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011152200 · Cited by 92
Sex‐biased hippocampal pathology in the 5XFAD mouse model of Alzheimer's disease: A multi‐omic analysis
Bundy, J. L., Vied, C., Badger, C., & Nowakowski, R. S. (2019) · Journal of Comparative Neurology · doi:10.1002/cne.24551 · Cited by 90
Impact of Insulin Degrading Enzyme and Neprilysin in Alzheimer’s Disease Biology: Characterization of Putative Cognates for Therapeutic Applications
Jha, N. K., Jha, S. K., Kumar, D., Kejriwal, N., Sharma, R., Ambasta, R. K., & Kumar, P. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150379 · Cited by 90
Myelin changes at the early stage of 5XFAD mice
Gu, L., Wu, D., Tang, X., Qi, X., Li, X., Bai, F., Chen, X., Ren, Q., & Zhang, Z. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.12.013 · Cited by 87
PS1 N- and C-terminal fragments form a complex that functions in APP processing and Notch signaling
Levitan, D. J., Lee, J., Song, L., Manning, R., Wong, G., Parker, E. M., & Zhang, L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211321898 · Cited by 85
A Pathogenic Presenilin-1 Deletion Causes Abberrant Aβ42 Production in the Absence of Congophilic Amyloid Plaques
Steiner, H., Révész, T., Neumann, M., Romig, H., Grim, M. G., Pesold, B., Kretzschmar, H. A., Hardy, J., Holton, J. L., Baumeister, R., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007183200 · Cited by 89
Separation of presenilin function in amyloid β-peptide generation and endoproteolysis of Notch
Kulic, L., Walter, J., Multhaup, G., Teplow, D. B., Baumeister, R., Romig, H., Capell, A., Steiner, H., & Haass, C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100049897 · Cited by 85
Utilizing Structures of CYP2D6 and BACE1 Complexes To Reduce Risk of Drug–Drug Interactions with a Novel Series of Centrally Efficacious BACE1 Inhibitors
Brodney, M. A., Beck, E. M., Butler, C. R., Barreiro, G., Johnson, E. F., Riddell, D. R., Parris, K. D., Nolan, C. E., Fan, Y., Atchison, K. P., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00191 · Cited by 83
Alzheimer's Disease-Linked Mutations in Presenilin-1 Result in a Drastic Loss of Activity in Purified γ-Secretase Complexes
Cacquevel, M., Aeschbach, L., Houacine, J., & Fraering, P. C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035133 · Cited by 75
Evidence That Intramolecular Associations between Presenilin Domains Are Obligatory for Endoproteolytic Processing
Saura, C. A., Tomita, T., Davenport, F., Harris, C. L., Iwatsubo, T., & Thinakaran, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.13818 · Cited by 75
Pro‐apoptotic function of calsenilin/DREAM/KChIP3
Jo, D., Kim, M., Choi, Y., Kim, I., Song, Y.-H., Woo, H., Chung, C., & Jung, Y. (2001) · The FASEB Journal · doi:10.1096/fj.00-0541fje · Cited by 73
Aβ42-induced Increase in Neprilysin Is Associated with Prevention of Amyloid Plaque Formation in Vivo
Mohajeri, M. H., Wollmer, M. A., & Nitsch, R. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202899200 · Cited by 66
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
Self-citation
PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2
Pellegrini, L., Passer, B. J., Cañelles, M., Lefterov, I. M., Ganjei, J. K., Fowlkes, B. J., Koonin, E. V., & D'adamio, L. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3203 · Cited by 65
The Role of Astrocytes in Synapse Loss in Alzheimer's Disease: A Systematic Review
Hulshof, L. A., van Nuijs, D., Hol, E. M., & Middeldorp, J. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.899251 · Cited by 66
Reduced antioxidant enzyme activity in brains of mice transgenic for human presenilin-1 with single or multiple mutations
Leutner, S., Czech, C., Schindowski, K., Touchet, N., Eckert, A., & Müller, W. E. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01449-x · Cited by 60
Passive Immunization against β-Amyloid Peptide Protects Central Nervous System (CNS) Neurons from Increased Vulnerability Associated with an Alzheimer’s Disease-causing Mutation
Mohajeri, M. H., Saini, K., Schultz, J. G., Wollmer, M. A., Höck, C., & Nitsch, R. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203193200 · Cited by 62
The β-amyloid-related proteins presenilin 1 and BACE1 are axonally transported to nerve terminals in the brain
Sheng, J. G., Price, D. L., & Koliatsos, V. E. (2003) · Experimental Neurology · doi:10.1016/j.expneurol.2003.08.018 · Cited by 56
ER stress is not elevated in the 5XFAD mouse model of Alzheimer's disease
Sadleir, K. R., Popović, J., & Vassar, R. J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005769 · Cited by 61
Alzheimer's Disease-like Alterations in Peripheral Cells from Presenilin-1 Transgenic Mice
Eckert, A., Schindowski, K., Leutner, S., Luckhaus, C., Touchet, N., Czech, C., & Müller, W. E. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0378 · Cited by 55
Identification of the Aβ37/42 peptide ratio in CSF as an improved Aβ biomarker for Alzheimer's disease
Liu, L., Lauro, B. M., He, A., Lee, H., Bhattarai, S., Wolfe, M. S., Bennett, D. A., Karch, C. M. M., Young‐Pearse, T. L., Dominantly Inherited Alzheimer Network (DIAN), et al. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12646 · Cited by 45
Self-citation
Distribution of β-amyloid and amyloid precursor protein in the brain of spawning (senescent) salmon: a natural, brain-aging model
Maldonado, T. A., Jones, R. E., & Norris, D. O. (2000) · Brain Research · doi:10.1016/s0006-8993(99)02328-8 · Cited by 46
Homodimerization of presenilin N‐terminal fragments is affected by mutations linked to Alzheimer's disease
Cervantes, S., Gonzàlez‐Duarte, R., & Marfany, G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02785-5 · Cited by 48
Apolipoprotein E structural requirements for the formation of SDS-stable complexes with β-amyloid-(1–40): the role of salt bridges
Bentley, N. M., LaDu, M. J., Rajan, C., Getz, G. S., & Reardon, C. A. (2002) · Biochemical Journal · doi:10.1042/bj20020207 · Cited by 43
Evidence That Aβ42 Plasma Levels in Presenilin-1 Mutation Carriers Do not Allow for Prediction of Their Clinical Phenotype
Jonghe, C. D., Cras, P. P., Vanderstichele, H., Cruts, M., Vanderhoeven, I., Smouts, I., Vanmechelen, E., Martin, J.-J., Hendriks, L., & Broeckhoven, C. V. (1999) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0247 · Cited by 45
Linkage Between the Proteasome Pathway and Neurodegenerative Diseases and Aging
Vigouroux, S., Briand, M., & Briand, Y. (2004) · Molecular Neurobiology · doi:10.1385/mn:30:2:201 · Cited by 43
Design and Synthesis of Clinical Candidate PF-06751979: A Potent, Brain Penetrant, β-Site Amyloid Precursor Protein Cleaving Enzyme 1 (BACE1) Inhibitor Lacking Hypopigmentation
O’Neill, B. T., Beck, E. M., Butler, C. R., Nolan, C. E., Gonzales, C., Zhang, L., Doran, S. D., Lapham, K., Buzon, L. M., Dutra, J. K., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00246 · Cited by 43
Anti‐amyloid activity of neprilysin in plaque‐bearing mouse models of Alzheimer's disease
Mohajeri, M. H., Kuehnle, K., Li, H., Poirier, R., Tracy, J., & Nitsch, R. M. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00169-3 · Cited by 42
Presenilin-1 interacts directly with the β-site amyloid protein precursor cleaving enzyme (BACE1)
Hébert, S. S., Bourdages, V., Godin, C., Ferland, M., Carreau, M., & Lévesque, G. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00035-4 · Cited by 39
Notch signaling proteins HES-1 and Hey-1 bind to insulin degrading enzyme (IDE) proximal promoter and repress its transcription and activity: Implications for cellular Aβ metabolism
Leal, M. C., Surace, E., Holgado, M., Ferrari, C., Tarelli, R., Pitossi, F., Wisniewski, T., Castaño, E., & Morelli, L. (2011) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamcr.2011.09.014 · Cited by 41
Ube3a deficiency inhibits amyloid plaque formation in APPswe/PS1δE9 mouse model of Alzheimer’s disease
Singh, B. K., Vatsa, N., Kumar, V., Shekhar, S., Sharma, A., & Jana, N. R. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx295 · Cited by 38
A Loss of Function Mutant of the Presenilin Homologue SEL-12 Undergoes Aberrant Endoproteolysis in Caenorhabditis elegans and Increases Aβ42 Generation in Human Cells
Okochi, M., Eimer, S., Böttcher, A., Baumeister, R., Romig, H., Walter, J., Capell, A., Steiner, H., & Haass, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005254200 · Cited by 37
Discovery of AM-6494: A Potent and Orally Efficacious β-Site Amyloid Precursor Protein Cleaving Enzyme 1 (BACE1) Inhibitor with in Vivo Selectivity over BACE2
Pettus, L. H., Bourbeau, M. P., Bradley, J., Bartberger, M. D., Chen, K., Hickman, D., Johnson, M., Liu, Q., Manning, J. R., Nañez, A., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01034 · Cited by 36
The Functions of the Amyloid Precursor Protein Gene
Panegyres, P. K. (2001) · Reviews in the Neurosciences · doi:10.1515/revneuro.2001.12.1.1 · Cited by 36
The Role of Proteolysis in Alzheimer’s Disease
Hooper, N. M., Trew, A. J., Parkin, E. T., & Turner, A. J. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-46826-3_39 · Cited by 34
Timing of neurodegeneration and beta-amyloid (Abeta) peptide deposition in the brain of aging kokanee salmon.
Maldonado, T. A., Jones, R. E., & Norris, D. O. (2002) · Journal of Neurobiology · doi:10.1002/neu.10090 · Cited by 38
Motor impairment and aberrant production of neurochemicals in human α-synuclein A30P+A53T transgenic mice with α-synuclein pathology
Ikeda, M., Kawarabayashi, T., Harigaya, Y., Sasaki, A., Yamada, S., Matsubara, E., Murakami, T., Tanaka, Y., Kurata, T., Wuhua, X., et al. (2008) · Brain Research · doi:10.1016/j.brainres.2008.10.011 · Cited by 34
What Can Rodent Models Tell Us About Cognitive Decline in Alzheimer's Disease?
Davis, S., & Laroche, S. (2003) · Molecular Neurobiology · doi:10.1385/mn:27:3:249 · Cited by 32
Modelling APOE ɛ3/4 allele-associated sporadic Alzheimer’s disease in an induced neuron
Kim, H., Yoo, J., Shin, J., Chang, Y., Jung, J., Jo, D., Kim, J., Jang, W., Lengner, C. J., Kim, B., et al. (2017) · Brain · doi:10.1093/brain/awx144 · Cited by 30
Pathological Hallmarks, Clinical Parallels, and Value for Drug Testing in Alzheimer's Disease of the APP[V717I] London Transgenic Mouse Model
Tanghe, A., Termont, A., Merchiers, P., Schilling, S., Demuth, H., Scrocchi, L. A., LEUVEN, F. V., Griffioen, G., & Dooren, T. V. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/417314 · Cited by 31
DNA microarray profiling of developing PS1-deficient mouse brain reveals complex and coregulated expression changes
Mirnics, Z. K., Mirnics, K., Terrano, D. T., Lewis, D. A., Sisodia, S. S., & Schor, N. F. (2003) · Molecular Psychiatry · doi:10.1038/sj.mp.4001389 · Cited by 30
P75 neurotrophin receptor regulates expression of neural cell adhesion molecule 1
Korade, Ž., Yan, C., Portugal, C. F., Kim, T.-W., Saragovi, H. U., Sisodia, S. S., Mirnics, K., & Schor, N. F. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.06.004 · Cited by 30
Mutational Analysis of Intrinsic Regions of Presenilin 2 That Determine Its Endoproteolytic Cleavage and Pathological Function
Shirotani, K., Takahashi, K., Araki, W., Maruyama, K., & Tabira, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3681 · Cited by 27
Notch signaling in the pathologic adult brain
Mathieu, P., Adami, P. V. M., & Morelli, L. (2013) · BioMolecular Concepts · doi:10.1515/bmc-2013-0006 · Cited by 27
Early Detection of Aβ Deposition in the 5xFAD Mouse by Amyloid PET
Oh, S. J., Lee, H., Kang, K. J., Han, S. J., Lee, Y. J., Lee, K. C., Lim, S. M., Yoon, D., Kim, K. M., Park, J. A., et al. (2018) · Contrast Media & Molecular Imaging · doi:10.1155/2018/5272014 · Cited by 23
Post‐translational processing of beta‐secretase in Alzheimer's disease
Sidera, C., Parsons, R. B., & Austen, B. (2005) · PROTEOMICS · doi:10.1002/pmic.200401185 · Cited by 24
Regulation of distinct pools of amyloid β-protein by multiple cellular proteases
Leissring, M. A., & Turner, A. J. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt194 · Cited by 20
Sodium–calcium exchanger isoform-3 targeted Withania somnifera (L.) Dunal therapeutic intervention ameliorates cognition in the 5xFAD mouse model of Alzheimer’s disease
Afewerky, H. K., Li, H., Zhang, T., Li, X., Mahaman, Y. A. R., Duan, L., Qin, P., Zheng, J., Pei, L., & Lu, Y. (2022) · Scientific Reports · doi:10.1038/s41598-022-05568-2 · Cited by 18
The GSM BPN-15606 as a Potential Candidate for Preventative Therapy in Alzheimer’s Disease
Prikhodko, O., Rynearson, K. D., Sekhon, T., Mante, M., Nguyen, P. D., Rissman, R. A., Tanzi, R. E., & Wagner, S. L. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-190442 · Cited by 18
Aβ Infusion and Related Models of Alzheimer Dementia
Lawlor, P. A., & Young, D. (2010) · Neuromethods · doi:10.1007/978-1-60761-898-0_17 · Cited by 19
Genetic testing for Alzheimerʼs disease: how close is reality?
Blennow, K., & Skoog, I. G. (1999) · Current Opinion in Psychiatry · doi:10.1097/00001504-199907000-00019 · Cited by 15
Chapter 4. Secretase inhibitors as therapeutics for Alzheimer's disease
Olson, R. E., & Thompson, L. A. (2000) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(00)35005-9 · Cited by 14
Effects of presenilin N-terminal fragments on production of amyloid β peptide and accumulation of endogenous presenilins
Shirotani, K., Takahashi, K., & Tabira, T. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00037-3 · Cited by 11
Decanoic Acid Rescues Differences in AMPA-Mediated Calcium Rises in Hippocampal CA1 Astrocytes and Neurons in the 5xFAD Mouse Model of Alzheimer’s Disease
Abghari, M., Vu, J. T. C. M., Eckberg, N., Aldana, B. I., & Kohlmeier, K. A. (2023) · Biomolecules · doi:10.3390/biom13101461 · Cited by 12
3,4-Methylenedioxymethamphetamine (MDMA), but not morphine, alters APP processing in the rat brain
Kalman, J. L., Bjelik, A., Hugyecz, M., Tímár, J., Gyarmati, Z., Zana, M., Fürst, Z., Janka, Z., Rakonczay, Z., Horváth, Z., et al. (2006) · The International Journal of Neuropsychopharmacology · doi:10.1017/s146114570600650x · Cited by 9
A clathrin mediated endocytosis scaffolding protein, Intersectin 1, changes in an isoform, brain region, and sex specific manner in Alzheimer’s disease
Jaye, S., Sandau, U. S., McFarland, T. J., Woltjer, R. L., & Saugstad, J. A. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1426180 · Cited by 5
Silencing of Amyloid Precursor Protein Expression Using a New Engineered Delta Ribozyme
Aissa, M. B., April, M.-C., Bergeron, L. J., Perreault, J., & Lévesque, G. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/947147 · Cited by 5
The functions of the amyloid precursor protein gene.
Panegyres, P., & Atkins, E. (2011) · Reviews in the Neurosciences · doi:10.4236/nm.2011.22018 · Cited by 28
Generation of Amyloid‐β Peptides by γ‐Secretase
Aguayo‐Ortiz, R., & Domı́nguez, L. (2016) · Israel Journal of Chemistry · doi:10.1002/ijch.201600073 · Cited by 4
Presenilin Proteins and Their Function During Embryonic Development and Alzheimer’s Disease
Haass, C. (2000) · Springer eBooks · doi:10.1007/978-3-662-04264-9_4 · Cited by 4
Novel presenilin 1 mutation (p.Thr-Pro116-117Ser-Thr) in a Spanish family with early-onset Alzheimer's disease
Garrote, J. A. B., Alonso, A., Blanco, J., Rojo, E., Orriols, J. J. T., Torres, M. Á., & Uribe, F. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.05.012 · Cited by 2
Role of caspases, apoptosis and additional factors in pathology of Alzheimer's disease
Gupta, A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820122-0.00001-7 · Cited by 2
Etiology, Genetics, and Pathogenesis of Alzheimer's Disease
McKeon‐O'Malley, C., & Tanzi, R. E. (2001) · Elsevier eBooks · doi:10.1016/b978-012351830-9/50024-x · Cited by 3
Utilizing CYP2D6 and BACE1 Structure Complexes to Reduce Risk of Drug-Drug Interactions with a Novel Series of Centrally Efficacious BACE1 Inhibitors
Brodney, M. A., Beck, E. M., Butler, C. R., Barreiro, G., Johnson, E. F., Riddell, D. R., Parris, K. D., Fan, Y., Atchison, K. P., Gonzales, C., et al. (2015) · Cited by 1
Purification of Full-Length β-Secretase Involved in Alzheimer’s Disease, and Proteomic Identification of Binding Partners
Ly, L., Parsons, R. B., & Austen, B. (2020) · Journal of Biomedical Science and Engineering · doi:10.4236/jbise.2020.131001 · Cited by 1
Antibody-based therapeutics
Tachibana, T., & Kuwabara, T. (2019) · Drug Metabolism and Pharmacokinetics · doi:10.1016/j.dmpk.2019.01.006 · Cited by 1
Recombinant AAV gene therapy and delivery for Alzheimer's disease
Carty, N. (2009)
Neurobiologic Basis of Age-Related Dementing Disorders
Hof, P. R., Bussière, T., Buxbaum, J. D., & Morrison, J. H. (2006) · Springer eBooks · doi:10.1007/0-387-22621-4_76
Characterization of a novel interaction between presenilin-1 and monoamine oxidase-A
Gabriel, G. G. (2008) · University Library - University of Saskatchewan (University of Saskatchewan)
Signaltransduktion des humanen Neuropeptidrezeptors SorLA - γ-Secretase-abhängige Freisetzung der Intrazellulärdomäne des
Böhm, C. (2005)
SLEEP ALTERATIONS IN MOUSE GENETIC MODELS OF HUMAN DISEASE
Sethi, M. (2016) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2016.522
Analyse structurale et fonctionnelle de la préséniline-1 humaine : implications dans la maladie d'Alzheimer
Hébert, S. S. (2003) · Corpus Université Laval (Université Laval)
Amelioration of Memory Deficits in a Transgenic Mouse Model of Alzheimer’s Disease by Manipulation of the Histone Acetyltransferase p300/CBP Associated Factor (PCAF)
Creighton, S. D. (2019) · The Atrium (University of Guelph)
Recombinant AAV Gene Therapy and Delivery
Carty, N. (2009) · Digital Commons - University of South Florida (University of South Florida)
Appearance of Amyloid-β Early in Life Initiates Neuronal Hyper-excitability, Mitochondrial Decay, and Loss of Dendritic Complexity in the Hippocampal CA1 Region of 5xFAD MicePreprint
Kelley, A., Sackinger, E. D., Frischman, M., Thomas, N. O., Kim, K., Scuderi, G., Labut, E. M., MacMurchy, D., Ikea-Mario, T., Rauenhorst, J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.04.703883
Pre-plaque glutamatergic hyperexcitability, mitochondrial dysfunction, and dendritic remodeling in the hippocampus of one-month-old 5xFAD mice
Kelley, A., Sackinger, E. D., Frischman, M., Thomas, N. O., Kim, K., Scuderi, G., Labut, E. M., MacMurchy, D., Ikea-Mario, T., Rauenhorst, J., et al. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1804332
Differential Genotypic Effects of HSV-1 Infection on Cognitive Function and Pathology in the 5xFAD Mouse Model
Lin, K., Gu, E., Ackerman, S., Wang, X., Huener, A. F., Abou-Seada, I., Li, A., Magnusson, K. R., & Jin, L. (2026) · Cells · doi:10.3390/cells15201841

Authors: Citron, M., Eckman, C. B., Diehl, T. S., Corcoran, C., Ostaszewski, B. L., Xia, W., Levesque, G., St. George Hyslop, P., Younkin, S. G., & Selkoe, D. J.
Affiliations: Amgen (United States) (US)
Mayo Clinic (US)
Harvard University (US)
ORCID: Citron, Martin
Corcoran, Chris
Xia, Weiming
Selkoe, Dennis J.
Venue: Neurobiology of Disease
Publisher: Elsevier BV
Published: 1998-08
Volume: 5
Issue: 2
Pages: 107-116
ISSN: 0969-9961 (ISSN-L)
DOI: 10.1006/nbdi.1998.0183
OpenAlex: W2012968591
Cited by: 101
References: 28
Citations by year: 2026: 3 · 2024: 1 · 2023: 1 · 2022: 3 · 2021: 1 · 2020: 3 · 2019: 5 · 2018: 4 · 2017: 3 · 2016: 2 · 2015: 4 · 2014: 1 · 2013: 3 · 2012: 2
FWCI: 5.67
Type: journal article
Language: en
Open access: green
doaj.org
Licence: cc-by-sa
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Neurobiology of Disease (publishedVersion)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: National Institutes of Health
National Institute on Aging (AG 12749, AG-06173, R01AG012749)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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: presenilin 1, APP mutations, amyloid-beta 42, gamma-secretase, APP processing, Alzheimer's disease, conditioned medium, transgenic mouse model
MeSH terms: Alzheimer Disease, Cell Line, Gene Expression Regulation, Humans, Leucine, Membrane Proteins, Methionine, Peptide Fragments, Valine, Amyloid beta-Peptides, Mutagenesis, Site-Directed, Amyloid beta-Protein Precursor, Age of Onset, Amino Acid Substitution, Presenilin-1

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.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Additive Effects of PS1 and APP Mutations on Secretion of the 42-Residue Amyloid β-Protein

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks