Cited by 1,757Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

Citron, Martin, Oltersdorf, Tilman, Haass, Christian, McConlogue, Lisa, Hung, Albert Y., Seubert, Peter, Vigo-Pelfrey, Carmen, Lieberburg, Ivan, Selkoe, Dennis J.·1992·Nature

DOI 10.1038/360672a0

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Abstract

Progressive cerebral deposition of the 39-43-amino-acid amyloid beta-protein (A beta) is an invariant feature of Alzheimer's disease which precedes symptoms of dementia by years or decades. The only specific molecular defects that cause Alzheimer's disease which have been identified so far are missense mutations in the gene encoding the beta-amyloid precursor protein (beta-APP) in certain families with an autosomal dominant form of the disease (familial Alzheimer's disease, or FAD). These mutations are located within or immediately flanking the A beta region of beta-APP, but the mechanism by which they cause the pathological phenotype of early and accelerated A beta deposition is unknown. Here we report that cultured cells which express a beta-APP complementary DNA bearing a double mutation (Lys to Asn at residue 595 plus Met to Leu at position 596) found in a Swedish FAD family produce approximately 6-8-fold more A beta than cells expressing normal beta-APP. The Met 596 to Leu mutation is principally responsible for the increase. These data establish a direct link between a FAD genotype and the clinicopathological phenotype. Further, they confirm the relevance of the continuous A beta production by cultured cells for elucidating the fundamental mechanism of Alzheimer's disease.

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Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
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 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-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
A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N–terminus of β–amyloid
Mullan, 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
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
Self-citation
Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type
Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,399
Self-citation
Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
Weidemann, A., König, G., Bunke, D., Fischer, P. Q., Salbaum, J. M., Masters, C. L., & Beyreuther, K. T. (1989) · Cell · doi:10.1016/0092-8674(89)90177-3 · Cited by 1,233
Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene
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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Haass, C., Hung, A. Y., Schlossmacher, M. G. & Selkoe, D. J. J. biol. Chem. (in the press).
Seubert, P. et al. Nature (in the press).

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Items 801–900 of 1,006

Alzheimer's disease amyloid precursor protein (ApPP): proteolytic processing, secretases and βA4 amyloid production
Evin, G. M., Beyreuther, K. T., & Masters, C. L. (1994) · Amyloid · doi:10.3109/13506129409146118 · Cited by 48
Lysophosphatidylcholine modulates fibril formation of amyloid beta peptide
Sheikh, A. M., & Nagai, A. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07984.x · Cited by 47
Physiological and pathophysiological control of synaptic GluN2B-NMDA receptors by the C-terminal domain of amyloid precursor protein
Pousinha, P., Mouska, X., Raymond, E., Gwizdek, C., Dhib, G., Poupon, G., Zaragosi, L., Giudici, C., Bethus, I., Pacary, E., et al. (2017) · eLife · doi:10.7554/elife.25659 · Cited by 39
Opposite changes in APP processing and human Aβ levels in rats carrying either a protective or a pathogenic APP mutation
Tambini, M. D., Norris, K. A., & D'adamio, L. (2020) · eLife · doi:10.7554/elife.52612 · Cited by 47
Nose-to-brain drug delivery for the treatment of Alzheimer’s disease: current advancements and challenges
Prabakaran, A., Agrawal, M., Dethe, M. R., Ahmed, H., Yadav, A. K., Gupta, U. D., & Alexander, A. (2022) · Expert Opinion on Drug Delivery · doi:10.1080/17425247.2022.2029845 · Cited by 47
Degenerative and protective signaling mechanisms in the neurofibrillary pathology of AD
Mattson, M. P. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(94)00182-z · Cited by 47
Generation of Transgenic Zebrafish Expressing Green Fluorescent Protein Under Control of Zebrafish Amyloid Precursor Protein Gene Regulatory Elements
Lee, J.-A., & Cole, G. J. (2007) · Zebrafish · doi:10.1089/zeb.2007.0516 · Cited by 47
Obovatol improves cognitive functions in animal models for Alzheimer’s disease
Choi, D., Lee, J. W., Peng, J., Lee, Y. J., Han, J., Lee, Y. H., Choi, I. S., Han, S., Jung, J., Lee, W. S., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07642.x · Cited by 46
Pharmacogenetic features of cathepsin B inhibitors that improve memory deficit and reduce β-amyloid related to Alzheimer's disease
HOOK, V. Y. H., Hook, G., & Kindy, M. S. (2010) · Biological Chemistry · doi:10.1515/bc.2010.110 · Cited by 46
Proteolytic Processing of Amyloid-β Precursor Protein by Secretases Does Not Require Cell Surface Transport
Khvotchev, M. V., & Südhof, T. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408474200 · Cited by 46
Loss of presenilin function causes Alzheimer's disease‐like neurodegeneration in the mouse
Chen, Q., Nakajima, A., Choi, S. H., Xiong, X., & Tang, Y. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21601 · Cited by 47
Mechanisms of synaptic pathology in Alzheimer’s disease
Masliah, E. (1998) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-7091-6467-9_13 · Cited by 46
Calretinin-immunoreactive neurons are resistant to β-amyloid toxicity in vitro
Pike, C. J., & Cotman, C. W. (1995) · Brain Research · doi:10.1016/0006-8993(94)01354-k · Cited by 46
Secretion and Accumulation of Aβ by Brain Vascular Smooth Muscle Cells from AβPP-Swedish Transgenic Mice
Frackowiak, J., Miller, D. L., Potempska, A., Sukontasup, T., & Mazur‐Kolecka, B. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.6.685 · Cited by 49
Processing of Alzheimer Aβ-Amyloid Precursor Protein: Cell Biology, Regulation, and Role in Alzheimer Disease
Gandy, S., & Greengard, P. (1994) · International review of neurobiology · doi:10.1016/s0074-7742(08)60302-5 · Cited by 46
Distinct Secretases, a Cysteine Protease and a Serine Protease, Generate the C Termini of Amyloid β‐Proteins Aβ1‐40 and Aβ1‐42, Respectively
Figueiredo‐Pereira, M. E., Efthimiopoulos, S., Tezapsidis, N., Buku, A., Ghiso, J. A., Mehta, P. D., & Robakis, N. K. R. K. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.721417.x · Cited by 46
Morphological and Molecular Profiling of Amyloid-β Species in Alzheimer’s Pathogenesis
Almeida, Z. L., Vaz, D. C., & Brito, R. M. M. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04543-4 · Cited by 49
An effective treatment for Alzheimer's disease must consider both amyloid and tau
Lansdall, C. J. (2014) · Bioscience Horizons The International Journal of Student Research · doi:10.1093/biohorizons/hzu002 · Cited by 46
Expression of the Alzheimer’s Disease Mutations AβPP695sw and PSEN1M146I in Double-Transgenic Göttingen Minipigs
Jakobsen, J. E., Johansen, M., Schmidt, M. H., Liu, Y., Li, R., Callesen, H., Melnikova, M., Habekost, M., Matrone, C., Bouter, Y., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160408 · Cited by 45
Mouse models of Alzheimer's disease: The long and filamentous road
Phinney, A. L., Horne, P., Yang, J., Janus, C., Bergeron, C., & Westaway, D. A. (2003) · Neurological Research · doi:10.1179/016164103101202020 · Cited by 47
Activated cAMP-response Element-binding Protein Regulates Neuronal Expression of Presenilin-1
Mitsuda, N., Ohkubo, N., Tamatani, M., Lee, Y.-D., Taniguchi, M., Namikawa, K., Kiyama, H., Yamaguchi, A., Sato, N., Sakata, K., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006153200 · Cited by 46
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Lesuisse, C. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.22.2525 · Cited by 45
APP transgenesis: Approaches toward the development of animal models for Alzheimer disease neuropathology
Greenberg, B., Savage, M. J., Howland, D., Ali, S. M., Siedlak, S. L., Perry, G. L., Siman, R., & Scott, R. W. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(96)00001-2 · Cited by 45
Recent Advances in the Genetics of Alzheimer's Disease
Levy‐Lahad, E., Tsuang, D. W., & Bird, T. D. (1998) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/089198879801100202 · Cited by 46
Amyloid precursor protein drives down-regulation of mitochondrial oxidative phosphorylation independent of amyloid beta
Lopez Sanchez, M. I. G., Waugh, H. S., Tsatsanis, A., Wong, B. X., Crowston, J. G., Duce, J. A., & Trounce, I. A. (2017) · Scientific Reports · doi:10.1038/s41598-017-10233-0 · Cited by 45
Amyloid precursor protein‐mediated mitochondrial regulation and Alzheimer's disease
Lopez Sanchez, M. I. G., van Wijngaarden, P., & Trounce, I. A. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14554 · Cited by 45
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Mormino, E. C. (2014) · Neuropsychology Review · doi:10.1007/s11065-014-9267-4 · Cited by 44
N-Acetyl-Cysteine: Modulating the Cysteine Redox Proteome in Neurodegenerative Diseases
Martínez, M. (2022) · Antioxidants · doi:10.3390/antiox11020416 · Cited by 46
Total Lignans of Schisandra chinensis Ameliorates Aβ1-42-Induced Neurodegeneration with Cognitive Impairment in Mice and Primary Mouse Neuronal Cells
Zhao, X. D., Liu, C., Xu, M., Li, X., Bi, K., & Jia, Y. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152772 · Cited by 44
Emerging roles of N- and C-terminally truncated Aβ species in Alzheimer’s disease
Wirths, O., & Zampar, S. (2019) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2019.1702972 · Cited by 44
Age‐related changes of intracellular Aβ in cynomolgus monkey brains
Kimura, N., Yanagisawa, K., Terao, K., Ono, F., Sakakibara, I., Ishii, Y., Kyuwa, S., & Yoshikawa, Y. (2005) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00624.x · Cited by 44
Increased bisecting and core-fucosylated N-glycans on mutant human amyloid precursor proteins
Akasaka‐Manya, K., Manya, H., Sakurai, Y., Wójczyk, B. S., Spitalnik, S. L., & Endo, T. (2008) · Glycoconjugate Journal · doi:10.1007/s10719-008-9140-x · Cited by 45
11. Molecular genetics of Alzheimer's disease
Hardy, J., Owen, M. J., Goate, A., James, L., Haynes, A. R., Williamson, R., Roques, P. K., Rossor, M. N., & Mullan, M. J. (1989) · Biochemical Society Transactions · doi:10.1007/978-1-4613-0513-2_3 · Cited by 44
Human bleomycin hydrolase regulates the secretion of amyloid precursor protein
Lefterov, I. M., Koldamova, R. P., & Lazo, J. S. (2000) · The FASEB Journal · doi:10.1096/fj.99-0938com · Cited by 44
Potential Treatment Opportunities for Alzheimer's Disease Through Inhibition of Secretases and Aβ Immunization
Schenk, D., Games, D., & Seubert, P. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:2:259 · Cited by 44
Self-citation
Association studies using novel polymorphisms in BACE1 and BACE2
Nowotny, P., Kwon, J. M., Chakraverty, S., Nowotny, V., Morris, J. C., & Goate, A. (2001) · Neuroreport · doi:10.1097/00001756-200107030-00008 · Cited by 44
Genetic Epidemiology of Alzheimer Disease
Slooter, A. J. C., & van Duijn, C. M. (1997) · Epidemiologic Reviews · doi:10.1093/oxfordjournals.epirev.a017933 · Cited by 44
Increased Aβ 42(43)-plaque deposition in early-onset familial Alzheimer's disease brains with the deletion of exon 9 and the missense point mutation (H163R) in the PS-1 gene
Ishii, K., Ii, K., Hasegawa, T., Shoji, S., Doi, A., & Mori, H. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00347-9 · Cited by 44
An Update on the Amyloid Hypothesis
Eckman, C. B., & Eckman, E. A. (2007) · Neurologic Clinics · doi:10.1016/j.ncl.2007.03.007 · Cited by 43
Translatability scoring in drug development: eight case studies
Wendler, A., & Wehling, M. (2012) · Journal of Translational Medicine · doi:10.1186/1479-5876-10-39 · Cited by 43
beta PP and Tau interaction. A possible link between amyloid and neurofibrillary tangles in Alzheimer's disease.
Giaccone, G., Pedrotti, B., Migheli, A., Verga, L., Perez, J., Racagni, G., Smith, M. A., Perry, G. L., GIOIA, L. D., Selvaggini, C., et al. (1996) · Europe PMC (PubMed Central) · Cited by 43
Quantitation of amyloid-β peptides in biological milieu using a novel homogeneous time-resolved fluorescence (HTRF) assay
Clarke, E. E., & Shearman, M. S. (2000) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(00)00280-6 · Cited by 44
Transgenic murine cortical neurons expressing human Bcl-2 exhibit increased resistance to amyloid β-peptide neurotoxicity
Saillé, C., Marin, P., Martinou, J., Nicole, A., London, J., & Ceballos-Picot, I. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00089-5 · Cited by 43
Presenilin and γ‐secretase: structure meets function
Wolfe, M. S. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00245.x · Cited by 43
Differential Release of β-Amyloid from Dendrite- Versus Axon-Targeted APP
DeBoer, S. R., Dolios, G., Wang, R., & Sisodia, S. S. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2255-14.2014 · Cited by 42
Profiles of β-Amyloid Peptides and Key Secretases in Brain Autopsy Samples Differ with Sex and APOE ε4 Status: Impact for Risk and Progression of Alzheimer Disease
Nyarko, J. N. K., Quartey, M. O., Pennington, P. R., Heistad, R. M., Dea, D., Poirier, J., Baker, G. B., & Mousseau, D. D. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.01.005 · Cited by 48
Dysfunctional γ-Secretase in Familial Alzheimer’s Disease
Wolfe, M. S. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2511-1 · Cited by 47
Characterization of V642I‐AβPP‐induced cytotoxicity in primary neurons
Niikura, T., Yamada, M., Chiba, T., Aiso, S., Matsuoka, M., & Nishimoto, I. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20139 · Cited by 42
Cysteine protease inhibitors effectively reduce in vivo levels of brain β-amyloid related to Alzheimer's disease
HOOK, V. Y. H., Kindy, M. S., & Hook, G. (2007) · Biological Chemistry · doi:10.1515/bc.2007.027 · Cited by 42
Modeling of Tau-Mediated Synaptic and Neuronal Degeneration in Alzheimer's Disease
Jaworski, T., Kügler, S., & LEUVEN, F. V. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/573138 · Cited by 45
Concentrations of amyloid-β protein in cerebrospinal fluid increase with age in patients free from neurodegenerative disease
van Gool, W. A., Schenk, D. B., & Bolhuis, P. A. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90677-7 · Cited by 42
A Basic Amino Acid in the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein (APP) Is Essential for Cleavage of APP at the α-Site
Tomita, S., Kirino, Y., & Suzuki, T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.19304 · Cited by 42
Secretases Related to Amyloid Precursor Protein Processing
Liu, X., Liu, Y., & Ji, S. (2021) · Membranes · doi:10.3390/membranes11120983 · Cited by 41
Resveratrol Intervenes Cholesterol- and Isoprenoid-Mediated Amyloidogenic Processing of AβPP in Familial Alzheimer’s Disease
Sathya, M., Ponnusamy, M., Palanisamy, P., Kandasamy, M., Jayachandran, K. S., & Anusuyadevi, M. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161034 · Cited by 41
Low-dose intraperitoneal Freund's adjuvant: Toxicity and immunogenicity in mice using an immunogen targeting amyloid-β peptide
Oscherwitz, J., Hankenson, F. C., Yu, F., & Cease, K. B. (2005) · Vaccine · doi:10.1016/j.vaccine.2005.10.046 · Cited by 41
Age-related loss of phospholipid asymmetry in APP /APP x PS-1 /PS-1 human double mutant knock-in mice: Relevance to Alzheimer disease
Lange, M. L. B., Clair, D. K. S., Markesbery, W. R., Studzinski, C. M., Murphy, M. P., & Butterfield, D. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.01.004 · Cited by 41
The βA4 Amyloid Precursor Protein Gene and Alzheimer's Disease
Hendriks, L., & Broeckhoven, C. V. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0006n.x · Cited by 41
Facilitation of glutamate, but not GABA, release in Familial Alzheimer's APP mutant Knock‐in rats with increased β‐cleavage of APP
Tambini, M. D., Yao, W., & D'Adamio, L. (2019) · Aging Cell · doi:10.1111/acel.13033 · Cited by 40
“Alzheimer disease App‐Swedish Knock‐in rats As noted, several reports indicate that APPSw is a better β‐ secretase substrate as compared to WT APP (Citron et al., 1992, 1994; Johnston et al., 1994).”
BackgroundResultInfluential
Region-specific dendritic simplification induced by Aβ, mediated by tau via dysregulation of microtubule dynamics: a mechanistic distinct event from other neurodegenerative processes
Golovyashkina, N., Penazzi, L., Ballatore, C., Smith, A. B., Bakota, L., & Brandt, R. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0049-0 · Cited by 41
Using human induced pluripotent stem cells (hiPSCs) to investigate the mechanisms by which Apolipoprotein E (APOE) contributes to Alzheimer’s disease (AD) risk
Raman, S., Brookhouser, N., & Brafman, D. A. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104788 · Cited by 41
Antibody modified-silver nanoparticles for colorimetric immuno sensing of Aβ(1–40/1–42) based on the interaction between β-amyloid and Cu2+
Hu, T., Chen, C., Huang, G., & Yang, X. (2016) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2016.04.159 · Cited by 40
Altered protein phosphorylation as a resource for potential AD biomarkers
Henriques, A. G., Müller, T., Oliveira, J. M., Cova, M. M., Silva, C. B. D. C. E., & Silva, O. A. B. D. C. E. (2016) · Scientific Reports · doi:10.1038/srep30319 · Cited by 40
Blood markers in Alzheimer disease: Subnormal acetylcholinesterase and butyrylcholinesterase in lymphocytes and erythrocytes
Inestrosa, N. C., Alarcón, R., Arriagada, J., Donoso, A., Alvarez, J., & Campos, E. O. (1994) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(94)90044-2 · Cited by 40
Apolipoprotein E and Alzheimer's disease: the implications of progress in molecular medicine.
Mayeux, R. P., & Schupf, N. (1995) · American Journal of Public Health · doi:10.2105/ajph.85.9.1280 · Cited by 40
Mutant and native human β-amyloid precursor proteins in transgenic mouse brain
Howland, D. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00078-s · Cited by 40
Critical role of intraneuronal Aβ in Alzheimer's disease: Technical challenges in studying intracellular Aβ
Gouras, G. K., Willén, K., & Tampellini, D. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.06.004 · Cited by 39
Amyloid β-peptide in cerebrospinal fluid in individuals with the Swedish Alzheimer amyloid precursor protein mutation
Lannfelt, L., Basun, H., Vigo-Pelfrey, C., Wahlund, L.-O., Winblad, B., Lieberburg, I., & Schenk, D. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)12059-d · Cited by 39
Self-citation
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Eketjäll, S., Janson, J., Jeppsson, F., Svanhagen, A., Kolmodin, K., Gustavsson, S., Radesäter, A. ‐., Eliason, K., Briem, S., Appelkvist, P., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.1165-13.2013 · Cited by 39
Good gene, bad gene: New APP variant may be both
Fede, G. D., Catania, M., Morbin, M., Giaccone, G., Moro, M. L., Ghidoni, R., Colombo, L., Messa, M., Cagnotto, A., Romeo, M., et al. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.06.004 · Cited by 42
The human brainome: network analysis identifies HSPA2 as a novel Alzheimer’s disease target
Petyuk, V., Chang, R. R., Ramirez‐Restrepo, M., Beckmann, N. D., Henrion, M., Piehowski, P., Zhu, K., Wang, S., Clarke, J., Huentelman, M. J., et al. (2018) · Brain · doi:10.1093/brain/awy215 · Cited by 40
A Lifespan Observation of a Novel Mouse Model: In Vivo Evidence Supports Aβ Oligomer Hypothesis
Zhang, Y., Lu, L., Jia, J., Jia, L., Geula, C., Pei, J.-J., Xu, Q., Qin, W., Liu, R., Li, D., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085885 · Cited by 40
Cysteine proteases are the major β‐secretase in the regulated secretory pathway that provides most of the β‐amyloid in Alzheimer's disease: Role of BACE 1 in the constitutive secretory pathway
HOOK, V. Y. H., & Reisine, T. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10784 · Cited by 39
Amyloid β-peptide is produced by cultured cells during normal metabolism: A reprise
Selkoe, D. J. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s319 · Cited by 39
Self-citation
Altered Amyloid-β Metabolism and Deposition in Genomic-based β-Secretase Transgenic Mice
Chiocco, M. J., Kulnane, L. S., Younkin, L. H., Younkin, S., Evin, G. M., & Lamb, B. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409680200 · Cited by 39
APP processing, Aβ-amyloidogenesis, and the pathogenesis of Alzheimer's disease
Gandy, S., Caporaso, G. L., Buxbaum, J. D., Frangione, B., & Greengard, P. (1994) · Neurobiology of Aging · doi:10.1016/0197-4580(94)90125-2 · Cited by 39
Amyloid precursor protein truncated at any of the ?-secretase sites is not cleaved to ?-amyloid
Paganetti, P., Lis, M., Klafki, H.-W., & Staufenbiel, M. (1996) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19961101)46:3 · Cited by 39
Alzheimer's Disease: The apolipoprotein E connection
Utermann, G. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00081-6 · Cited by 39
Pathophysiological role of calpain in experimental demyelination
Shields, D. C., & Banik, N. L. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990301)55:5 · Cited by 64
Caspase activity sows the seeds of neuronal death
Yuan, J., & Yankner, B. A. (1999) · Nature Cell Biology · doi:10.1038/10037 · Cited by 39
Alcohol Use Disorder and Dementia: A Review
Zahr, N. M. (2024) · Alcohol research · doi:10.35946/arcr.v44.1.03 · Cited by 42
Anti-amyloid-beta to tau-based immunization: developments in immunotherapy for Alzheimer's disease
Lambracht‐Washington, D., & Rosenberg, R. N. (2013) · ImmunoTargets and Therapy · doi:10.2147/itt.s31428 · Cited by 39
Genetic Inhibition of Phosphorylation of the Translation Initiation Factor eIF2α Does Not Block Aβ-Dependent Elevation of BACE1 and APP Levels or Reduce Amyloid Pathology in a Mouse Model of Alzheimer’s Disease
Sadleir, K. R., Eimer, W. A., Kaufman, R. J., Osten, P., & Vassar, R. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101643 · Cited by 40
Interplay between α-, β-, and γ-Secretases Determines Biphasic Amyloid-β Protein Level in the Presence of a γ-Secretase Inhibitor
Ortega, F. G., Stott, J., Visser, S. A. G., & Bendtsen, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.419135 · Cited by 39
Identification of inhibitors using a cell-based assay for monitoring Golgi-resident protease activity
Coppola, J. M., Hamilton, C. A., Bhojani, M. S., Larsen, M. J., Ross, B. D., & Rehemtulla, A. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.01.013 · Cited by 38
Quantification and distribution of β-secretase alternative splice variants in the rat and human brain
Zohar, O., Cavallaro, S., D’Agata, V., & Alkon, D. L. (2003) · Molecular Brain Research · doi:10.1016/s0169-328x(03)00182-7 · Cited by 30
Monogenetic determinants of Alzheimer's disease: APP mutations
Goate, A. (1998) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050218 · Cited by 41
c‐Abl modulates AICD dependent cellular responses: Transcriptional induction and apoptosis
Vázquez, M. C., Vargas, L. M., Inestrosa, N. C., & Alvarez, A. R. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21743 · Cited by 37
Characterization of a G-Quadruplex Structure in Pre-miRNA-1229 and in Its Alzheimer’s Disease-Associated Variant rs2291418: Implications for miRNA-1229 Maturation
Imperatore, J. A., Then, M. L., McDougal, K. B., & Mihailescu, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030767 · Cited by 37
A third-generation mouse model of Alzheimer's disease shows early and increased cored plaque pathology composed of wild-type human amyloid β peptide
Sato, K., Watamura, N., Fujioka, R., Mihira, N., Sekiguchi, M., Nagata, K., Ohshima, T., Saito, T., Saido, T. C., & Sasaguri, H. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101004 · Cited by 38
Examination of the role of endopeptidase 3.4.24.15 in Aβ secretion by human transfected cells
Chevallier, N., Jiráček, J., Vincent, B., Baur, C.-P., Spillantini, M. G., Goedert, M., Dive, V., & Checler, F. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0701151 · Cited by 37
Functional Overexpression of γ-Secretase Reveals Protease-independent Trafficking Functions and a Critical Role of Lipids for Protease Activity
Wrigley, J. D. J., Schurov, I., Nunn, E. J., Martin, A. C. L., Clarke, E. E., Ellis, S., Bonnert, T. P., Shearman, M. S., & Beher, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413086200 · Cited by 37
Plant-derived acetylcholinesterase inhibitory alkaloids for the treatment of Alzheimer's disease
Dall’Acqua, S. (2013) · Botanics Targets and Therapy · doi:10.2147/btat.s17297 · Cited by 37
Human fibroblast and stem cell resource from the Dominantly Inherited Alzheimer Network
the Dominantly Inherited Alzheimer Network (DIAN), Karch, C. M. M., Hernández, D., Wang, J., Marsh, J. A., Hewitt, A. W., Hsu, S., Norton, J. B., Levitch, D., Donahue, T. A., et al. (2018) · Alzheimer s Research & Therapy · doi:10.1186/s13195-018-0400-0 · Cited by 39
Amyloid precursor protein cross‐linking stimulates beta amyloid production and pro‐inflammatory cytokine release in monocytic lineage cells
Sondag, C., & Combs, C. K. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03759.x · Cited by 37
Pathogenic theories and intrathecal analysis of the sporadic form of Alzheimer’s disease
Torreilles, F., & Touchon, J. (2002) · Progress in Neurobiology · doi:10.1016/s0301-0082(01)00030-2 · Cited by 39
Up-regulation of Bcl-xL in response to subtoxic β-amyloid: role in neuronal resistance against apoptotic and oxidative injury
Luetjens, C. M., Lankiewicz, S., Bui, N. T., Krohn, A. J., Poppe, M., & Prehn, J. H. M. (2001) · Neuroscience · doi:10.1016/s0306-4522(00)00458-9 · Cited by 37
Molecular pathology of Alzheimer's disease.
Rossor, M. N. (1993) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.56.6.583 · Cited by 37
Biochemistry of Alzheimer's disease amyloid plaques
Fraser, P. E., Lévesque, L., & McLachlan, D. R. C. (1993) · Clinical Biochemistry · doi:10.1016/0009-9120(93)90110-r · Cited by 38
Microglial APOE3 Christchurch protects neurons from Tau pathology in a human iPSC-based model of Alzheimer’s disease
Sun, G. G., Wang, C., Mazzarino, R. C., Perez-Corredor, P. A., Davtyan, H., Blurton-Jones, M., Lopera, F., Arboleda-Velasquez, J. F., & Shi, Y. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114982 · Cited by 36
Genetic of Alzheimer's Disease: A Narrative Review Article.
Khanahmadi, M., Farhud, D. D., & Malmir, M. (2015) · Europe PMC (PubMed Central) · Cited by 36

Authors: Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J.
Affiliations: Brigham and Women's Hospital (US)
ORCID: Citron, Martin
Haass, Christian
McConlogue, Lisa
Hung, Albert Y.
Selkoe, Dennis J.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1992-12
Volume: 360
Issue: 6405
Pages: 672-674
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/360672a0
OpenAlex: W2090150925
Cited by: 1,757
References: 17
Citations by year: 2026: 19 · 2025: 19 · 2024: 28 · 2023: 24 · 2022: 33 · 2021: 39 · 2020: 37 · 2019: 43 · 2018: 41 · 2017: 39 · 2016: 50 · 2015: 37 · 2014: 59 · 2013: 45 · 2012: 59
FWCI: 52.80
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
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: familial Alzheimer's disease, amyloid precursor protein, APP mutations, genotype-phenotype correlation, amyloid deposition, cultured cells, autosomal dominant inheritance
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Base Sequence, Cell Line, Humans, Kidney, Molecular Sequence Data, Mutation, Oligodeoxyribonucleotides, Sweden, Transfection, Restriction Mapping, Amyloid beta-Peptides, Amyloid beta-Protein Precursor

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Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

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