Cited by 1,921Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Amyloid β-peptide is produced by cultured cells during normal metabolism

Haass, Christian, Schlossmacher, Michael G., Hung, Albert Y., Vigo-Pelfrey, Carmen, Mellon, Angela, Ostaszewski, Beth L., Lieberburg, Ivan, Koo, Edward H., Schenk, Dale, Teplow, David B., Selkoe, Dennis J.·1992·Nature

DOI 10.1038/359322a0

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Abstract

Alzheimer's disease is characterized by the extracellular deposition in the brain and its blood vessels of insoluble aggregates of the amyloid beta-peptide (A beta), a fragment, of about 40 amino acids in length, of the integral membrane protein beta-amyloid precursor protein (beta-APP). The mechanism of extracellular accumulation of A beta in brain is unknown and no simple in vitro or in vivo model systems that produce extracellular A beta have been described. We report here the unexpected identification of the 4K (M(r) 4,000) A beta and a truncated form of A beta (approximately 3K) in media from cultures of primary cells and untransfected and beta-APP-transfected cell lines grown under normal conditions. These peptides were immunoprecipitated readily from culture medium by A beta-specific antibodies and their identities confirmed by sequencing. The concept that pathological processes are responsible for the production of A beta must not be reassessed in light of the observation that A beta is produced in soluble form in vitro and in vivo during normal cellular metabolism. Further, these findings provide the basis for using simple cell culture systems to identify drugs that block the formation or release of A beta, the primary protein constituent of the senile plaques of Alzheimer's disease.

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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
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
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
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
Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments
Haass, C., Koo, E. H., Mellon, A., Hung, A. Y., & Selkoe, D. J. (1992) · Nature · doi:10.1038/357500a0 · Cited by 919
Self-citation
Evidence that β-Amyloid Protein in Alzheimer's Disease Is Not Derived by Normal Processing
Sisodia, S. S., Koo, E. H., Beyreuther, K. T., Unterbeck, A., & Price, D. L. (1990) · Science · doi:10.1126/science.1691865 · Cited by 894
Self-citation
Processing of the Amyloid Protein Precursor to Potentially Amyloidogenic Derivatives
Golde, T. E., Estus, S., Younkin, L. H., Selkoe, D. J., & Younkin, S. G. (1992) · Science · doi:10.1126/science.1738847 · Cited by 737
Self-citation
Beta-amyloid precursor protein of Alzheimer disease occurs as 110- to 135-kilodalton membrane-associated proteins in neural and nonneural tissues.
Selkoe, D. J., Podlisny, M. B., Joachim, C. L., Vickers, E., Lee, G. S., Fritz, L. C., & Oltersdorf, T. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.19.7341 · Cited by 579
Self-citation
Mass spectrometry of purified amyloid beta protein in Alzheimer's disease.
Mori, H., Takio, K., OGAWARA, M., & Selkoe, D. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41896-0 · Cited by 486
Self-citation
Amyloid β-protein deposition in tissues other than brain in Alzheimer's disease
Joachim, C. L., Mori, H., & Selkoe, D. J. (1989) · Nature · doi:10.1038/341226a0 · Cited by 462
Self-citation

Flagged first, then by citations

Show all 17 references

Research works printed but not linked: 4

Greenberg, S. M., Rosenthal, D. S., Greeley, T. A., Tantravahi, R. & Handin, R. I. Blood 72, 1968–1977 (1988). · DOI
Podlisny, M. B., Tolan, D. & Selkoe, D. J. Am. J. Path. 139, 1423–1435 (1991).
Gabuzda, D. H., Busciglio, J. & Yankner, B. A. Neurology (abstr.) 42, 304 (1992).
Anderson, J. P., Chen, Y., Kim, K. S. & Robakis, N. K. J. Neurochem. (in the press).

Sorted by citations

Items 501–600 of 1,009

Examining the zinc binding site of the amyloid‐β peptide
Yang, D., McLaurin, J., Qin, K., Westaway, D. A., & Fraser, P. E. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01767.x · Cited by 113
A non‐amyloidogenic function of BACE‐2 in the secretory pathway
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
Self-citation
Alzheimer's Disease, β-Amyloid Protein and Zinc
Huang, X., Cuajungco, M. P., Atwood, C., Moir, R. D., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Nutrition · doi:10.1093/jn/130.5.1488s · Cited by 114
BACE1 in Alzheimer's disease
Sathya, M., Palanisamy, P., Chennakesavan, K., Ponnusamy, M., Jayachandran, K. S., & Anusuyadevi, M. (2012) · Clinica Chimica Acta · doi:10.1016/j.cca.2012.08.013 · Cited by 113
Regulation of β-amyloid precursor protein isoform mRNAs by transforming growth factor-β1 and interleukin-1β in astrocytes
Gray, C. W., & Patel, A. J. (1993) · Molecular Brain Research · doi:10.1016/0169-328x(93)90037-p · Cited by 117
Cerebrospinal fluid levels of amyloid β‐protein in alzheimer's disease: Inverse correlation with severity of dementia and effect of apolipoprotein e genotype
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-citation
Passage of human amyloid β-protein 1–40 across the murine blood-brain barrier
Maness, L. M., Banks, W. A., Podlisny, M. B., Selkoe, D. J., & Kastin, A. J. (1994) · Life Sciences · doi:10.1016/0024-3205(94)00331-9 · Cited by 97
Self-citation
Extracellular deposition of beta-amyloid upon p53-dependent neuronal cell death in transgenic mice.
LaFerla, F. M., Hall, C. K., Ngo, L. T., & Jay, G. D. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118957 · Cited by 112
Influence of fluorinated and hydrogenated nanoparticles on the structure and fibrillogenesis of amyloid beta-peptide
Rocha, S., Thünemann, A. F., Pereira, M. D. C., Coelho, M. A. N., Möhwald, H., & Brezesinski, G. (2008) · Biophysical Chemistry · doi:10.1016/j.bpc.2008.06.010 · Cited by 112
Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Aβ1–42, in differentiated PC12 cells
Burdick, D., Kosmoski, J., Knauer, M. F., & Glabe, C. G. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01262-0 · Cited by 102
The neuronal endosomal-lysosomal system in Alzheimer's disease
Nixon, R. A., Mathews, P. M., & Cataldo, A. M. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3114 · Cited by 114
Architecture of the Alzheimer?s A�P Ion Channel Pore
Arispe, N. J. (2004) · The Journal of Membrane Biology · doi:10.1007/s00232-003-0638-7 · Cited by 117
Alzheimer's disease and soluble Aβ
Wısnıewskı, T., Ghiso, J. A., & Frangione, B. (1994) · Neurobiology of Aging · doi:10.1016/0197-4580(94)90105-8 · Cited by 112
Apolipoprotein E, transthyretin and actin in the CSF of Alzheimer's patients: relation with the senile plaques and cytoskeleton biochemistry
Merched, A. J., Sérot, J., Visvikis‐Siest, S., Aguillon, D., Faure, G. C., & Siest, G. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00234-8 · Cited by 111
Omega-3 fatty acids, lipids, and apoE lipidation in Alzheimer's disease: a rationale for multi-nutrient dementia prevention
Grimm, M. O. W., Michaelson, D. M., & Hartmann, T. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r076331 · Cited by 114
In vitro stimulation of tissue-type plasminogen activator by Alzheimer amyloid β-peptide analogues
Kingston, I. B., Castro, M. J. M., & Anderson, S. (1995) · Nature Medicine · doi:10.1038/nm0295-138 · Cited by 110
Cognitive changes and modified processing of amyloid precursor protein in the cortical and hippocampal system after cholinergic synapse loss and muscarinic receptor activation
Lin, L., Georgievska, B., Mattsson, A., & Ole Isacson, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.21.12108 · Cited by 110
A Reductionist View of Alzheimer's Disease
Lansbury, P. T. (1996) · Accounts of Chemical Research · doi:10.1021/ar950159u · Cited by 109
Intracellular Accumulation of Insoluble, Newly Synthesized Aβn-42 in Amyloid Precursor Protein-transfected Cells That Have Been Treated with Aβ1–42
Yang, A. J., Chandswangbhuvana, D., Shu, T., Henschen, A., & Glabe, C. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20650 · Cited by 108
Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity
Cappai, R., & Barnham, K. J. (2008) · Neurochemical Research · doi:10.1007/s11064-007-9469-8 · Cited by 108
Synaptic Dysfunction in Alzheimer’s Disease
Marcello, E. E., Epis, R., Saraceno, C., & Luca, M. D. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-3-7091-0932-8_25 · Cited by 115
β‐Amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH
Klug, G. M., Lošić, D., Supundi, Subasinghe, S., Aguilar, M., Martin, L. L., & Small, D. H. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03815.x · Cited by 109
Amyloid precursor protein and alpha synuclein translation, implications for iron and inflammation in neurodegenerative diseases
Cahill, C. M., Lahiri, D. K., Huang, X., & Rogers, J. T. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.12.001 · Cited by 108
Huperzine A Activates Wnt/β-Catenin Signaling and Enhances the Nonamyloidogenic Pathway in an Alzheimer Transgenic Mouse Model
Wang, C., Zheng, W. H., Wang, T., Xie, J., Wang, S., Zhao, B., Teng, W., & Wang, Z. (2011) · Neuropsychopharmacology · doi:10.1038/npp.2010.245 · Cited by 108
Conformational mimicry in Alzheimer's disease. Role of apolipoproteins in amyloidogenesis.
Wısnıewskı, T., Golabek, A. A., Kida, E., Wisniewski, K. E., & Frangione, B. (1995) · Europe PMC (PubMed Central) · Cited by 107
The Cell-Selective Neurotoxicity of the Alzheimer's Aβ Peptide Is Determined by Surface Phosphatidylserine and Cytosolic ATP Levels. Membrane Binding Is Required for Aβ Toxicity
Šimáková, O., & Arispe, N. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3006-07.2007 · Cited by 106
Polyunsaturated Fatty Acids Induce α-Synuclein-Related Pathogenic Changes in Neuronal Cells
Assayag, K., Yakunin, E., Loeb, V., Selkoe, D. J., & Sharon, R. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070373 · Cited by 109
Self-citation
β-Amyloid-induced calcium influx induces apoptosis in culture by oxidative stress rather than tau phosphorylation
Ekinci, F. J., Linsley, M.-D., & Shea, T. B. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00025-5 · Cited by 106
Cell‐free assays for γ‐secretase activity
McLendon, C., Xin, T. A., Ziani‐Cherif, C., Murphy, M. P., Findlay, K. A., Lewis, P. A., Pinnix, I., Sambamurti, K., Wang, R., Fauq, A. H., et al. (2000) · The FASEB Journal · doi:10.1096/fj.00-0286fje · Cited by 106
Generation of βA4 from the amyloid protein precursor and fragments thereof
Dyrks, T., Dyrks, E., Mönning, U., Urmoneit, B., Turner, J. D., & Beyreuther, K. T. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80446-2 · Cited by 105
Behavioral Disturbances without Amyloid Deposits in Mice Overexpressing Human Amyloid Precursor Protein with Flemish (A692G) or Dutch (E693Q) Mutation
Kumar‐Singh, S., Dewachter, I., Moechars, D., Lübke, U., Jonghe, C. D., Ceuterick, C., Checler, F., Naidu, A., Cordell, B., Cras, P. P., et al. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0272 · Cited by 106
Accumulation of intercellular adhesion molecule-1 in senile plaques in brain tissue of patients with Alzheimer's disease.
(1994) · PubMed Central · Cited by 105
How Can Insulin Resistance Cause Alzheimer’s Disease?
Yoon, J. H., Hwang, J., Son, S. U., Choi, J., You, S.-W., Park, H., Cha, S.-Y., & Maeng, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043506 · Cited by 106
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
Engineered Polymer Nanoparticles Containing Hydrophobic Dipeptide for Inhibition of Amyloid-β Fibrillation
Skaat, H., Chen, R., Grinberg, I., & Margel, S. (2012) · Biomacromolecules · doi:10.1021/bm3011177 · Cited by 104
The involvement of mitogen‐activated protein (MAP) kinase in the regulation of amyloid precursor protein processing by novel cholinesterase inhibitors derived from rasagiline
Yogev‐Falach, M., Amit, T., Bar‐Am, O., Weinstock, M., & Youdim, M. B. H. (2002) · The FASEB Journal · doi:10.1096/fj.02-0198fje · Cited by 104
Intracellular Accumulation of β-Amyloid in Cells Expressing the Swedish Mutant Amyloid Precursor Protein
Martin, B. L., Schrader‐Fischer, G., Busciglio, J. A., Duke, M., Paganetti, P., & Yankner, B. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26727 · Cited by 104
Amyloid Precursor Protein Is Synthesized by Retinal Ganglion Cells, Rapidly Transported to the Optic Nerve Plasma Membrane and Nerve Terminals, and Metabolized
Morin, P. J., Abraham, C. R., Amaratunga, A., Johnson, R. J., Huber, G., Sandell, J. H., & Fine, R. E. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb02147.x · Cited by 105
β-Amyloid(Phe(SO3H)24)25–35 in rat nucleus basalis induces behavioral dysfunctions, impairs learning and memory and disrupts cortical cholinergic innervation
Harkany, T., O’Mahony, S. M., Kelly, J. P., Soós, K., Törõ, I., Penke, B., Luiten, P. G. M., Nyakas, C. J., Gulya, K., & Leonard, B. E. (1998) · Behavioural Brain Research · doi:10.1016/s0166-4328(97)00091-0 · Cited by 107
The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils.
Nordstedt, C., Näslund, J., Tjernberg, L. O., Karlström, A. R., Thyberg, J., & Terenius, L. Y. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47347-4 · Cited by 103
Review: Model Peptides and the Physicochemical Approach to β-Amyloids
Lynn, D. G., & Meredith, S. C. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4287 · Cited by 105
The Blood–Brain Barrier in Alzheimer's Disease
Sharma, H. S., Castellani, R. J., Smith, M. A., & Sharma, A. (2012) · International review of neurobiology · doi:10.1016/b978-0-12-386986-9.00003-x · Cited by 105
A “Protease Activation Cascade” in the Pathogenesis of Alzheimer's Disease
Nixon, R. A. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05570.x · Cited by 102
Neuronal and glial β‐secretase (BACE) protein expression in transgenic Tg2576 mice with amyloid plaque pathology
Roßner, S., Apelt, J., Schliebs, R., Perez-Polo, J. R., & Bigl, V. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1095 · Cited by 102
Stress and glucocorticoid footprints in the brain—The path from depression to Alzheimer's disease
Sotiropoulos, I., Cerqueira, J., Catania, C., Takashima, A., Sousa, N., & Almeida, O. F. X. (2008) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2008.05.007 · Cited by 105
Caspase-3-Mediated Cleavage of Amyloid Precursor Protein and Formation of Amyloid β Peptide in Traumatic Axonal Injury
Stone, J. R., Okonkwo, D. O., Singleton, R. H., Mutlu, L. K., Helm, G. A., & Povlishock, J. T. (2002) · Journal of Neurotrauma · doi:10.1089/089771502753754073 · Cited by 101
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Frozza, R. L., Horn, A. P., Hoppe, J. B., Simão, F., Gerhardt, D., Comiran, R. A., & Salbego, C. G. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9776-8 · Cited by 108
Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells
Yang, L., He, H. Y., & Zhang, X. (2002) · Neuroscience Research · doi:10.1016/s0168-0102(02)00005-6 · Cited by 101
APP Peptides Stimulate Lymphocyte Proliferation in Normals, But Not in Patients With Alzheimer's Disease
Trieb, K., Ransmayr, G. N., Sgonc, R., Lassmann, H., & Grubeck-Loebenstein, B. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(96)00068-1 · Cited by 101
Amyloid β protein levels in cerebrospinal fluid are elevated in early‐onset Alzheimer's disease
Nakamura, T., Shoji, M., Harigaya, Y., 渡辺, 光., Hosoda, K., Cheung, T. T., Shaffer, L. M., Golde, T. E., Younkin, L. H., Younkin, S. G., et al. (1994) · Annals of Neurology · doi:10.1002/ana.410360616 · Cited by 103
Copper mediated neurological disorder: Visions into amyotrophic lateral sclerosis, Alzheimer and Menkes disease
Ahuja, A., Dev, K., Tanwar, R. S., Selwal, K. K., & Tyagi, P. K. (2014) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2014.05.003 · Cited by 103
The Basic Biology of BACE1: A Key Therapeutic Target for Alzheimers Disease
Vassar, R. J., & Cole, S. (2007) · Current Genomics · doi:10.2174/138920207783769512 · Cited by 108
Structures of the Amyloid β-Peptides Aβ1–40 and Aβ1–42 as Influenced by pH and a d -Peptide
Olubiyi, O. O., & Strodel, B. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp2076337 · Cited by 100
Molecular Genetics of Alzheimer's Disease
Clark, R. F., & Goate, A. (1993) · Archives of Neurology · doi:10.1001/archneur.1993.00540110044004 · Cited by 100
Amyloid β peptide as a physiological modulator of neuronal ‘A’-type K+ current
Plant, L. D., Webster, N. J., Boyle, J. P., Ramsden, M., Freir, D. B., Peers, C., & Pearson, H. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.038 · Cited by 98
Structures of β-Amyloid Peptide 1−40, 1−42, and 1−55—the 672−726 Fragment of APP—in a Membrane Environment with Implications for Interactions with γ-Secretase
Miyashita, N., Straub, J. E., & Thirumalai, D. (2009) · Journal of the American Chemical Society · doi:10.1021/ja905457d · Cited by 98
Degradation of Amyloid β-Protein by a Serine Protease-α2-Macroglobulin Complex
Qiu, W. Q., Borth, W., Ye, Z., Haass, C., Teplow, D. B., & Selkoe, D. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.14.8443 · Cited by 98
Self-citation
Role of neurotransmission in the regulation of amyloid β-protein precursor processing
Nitsch, R. M., & Growdon, J. H. (1994) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)90325-5 · Cited by 99
Secreted Amyloid β-Proteins in a Cell Culture Model Include N-Terminally Extended Peptides That Impair Synaptic Plasticity
Welzel, A. T., Maggio, J. E., Shankar, G. M., Walker, D., Ostaszewski, B. L., Li, S., Klyubin, I. V., Rowan, M. J., Seubert, P. A., Walsh, D. M., et al. (2014) · Biochemistry · doi:10.1021/bi5003053 · Cited by 102
Self-citation
Modulation of Disordered Proteins with a Focus on Neurodegenerative Diseases and Other Pathologies
Martinelli, A. H. S., Lopes, F. C., John, E. B. D. O., Carlini, C. R., & Ligabue‐Braun, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061322 · Cited by 99
The amyloid‐β peptide and its role in Alzheimer's disease
Clippingdale, A. B., Wade, J. D., & Barrow, C. J. (2001) · Journal of Peptide Science · doi:10.1002/psc.324 · Cited by 103
Binding of Gelsolin, a Secretory Protein, to Amyloid β-Protein
Chauhan, V. P. S., Ray, I., Chauhan, A., & Wı́sniewski, H. M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0623 · Cited by 98
BACE1 inhibition reduces endogenous Abeta and alters APP processing in wild‐type mice2
Nishitomi, K., Sakaguchi, G., Horikoshi, Y., Gray, A. J., Maeda, M., Hirata‐Fukae, C., Becker, A. G., Hosono, M., Sakaguchi, I., Minami, S., et al. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04178.x · Cited by 97
Cholesterol decreases secretion of the secreted form of amyloid precursor protein by interfering with glycosylation in the protein secretory pathway
Galbete, J. L., Martin, T. R., PERESSINI, E., Modena, P., Bianchi, R., & Forloni, G. (2000) · Biochemical Journal · doi:10.1042/bj3480307 · Cited by 98
β-Secretase Processing of the β-Amyloid Precursor Protein in Transgenic Mice Is Efficient in Neurons but Inefficient in Astrocytes
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
Self-citation
Neuroprotective approaches in experimental models of β-Amyloid neurotoxicity: Relevance to Alzheimer's disease
Harkany, T., Hortobágyi, T., Sasvári, M., Kónya, C., Penke, B., Luiten, P. G. M., & Nyakas, C. J. (1999) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/s0278-5846(99)00058-5 · Cited by 97
Multiple cellular and molecular mechanisms Are involved in human Aβ clearance by transplanted adult astrocytes
Pihlaja, R., Koistinaho, J., Kauppinen, R., Sandholm, J., Tanila, H., & Koistinaho, M. (2011) · Glia · doi:10.1002/glia.21212 · Cited by 96
Amyloid β-Protein (Aβ) 1–40 But Not Aβ1–42 Contributes to the Experimental Formation of Alzheimer Disease Amyloid Fibrils in Rat Brain
Shin, R., Ogino, K., Kondo, A., Saido, T. C., Trojanowski, J. Q., Kitamoto, T., & Tateishi, J. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-21-08187.1997 · Cited by 96
BACE1 Structure and Function in Health and Alzheimers Disease
Cole, S., & Vassar, R. (2008) · Current Alzheimer Research · doi:10.2174/156720508783954758 · Cited by 98
Glutamine synthetase, hemoglobin α-chain, and macrophage migration inhibitory factor binding to amyloid β-protein: their identification in rat brain by a novel affinity chromatography and in Alzheimer’s disease brain by immunoprecipitation
Oyama, R., Yamamoto, H., & Titani, K. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00057-1 · Cited by 96
Aging, Amyloid, and Alzheimer's Disease: A Perspective in Honor of Carl Cotman
Selkoe, D. J. (2003) · Neurochemical Research · doi:10.1023/a:1026065122854 · Cited by 98
Self-citation
Amyloid β-protein precursor: new clues to the genesis of Alzheimer's disease
Selkoe, D. J. (1994) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(94)90014-0 · Cited by 96
Self-citation
Presenilin 1 Regulates Pharmacologically Distinct γ-Secretase Activities
Murphy, M. P., Uljon, S., Fraser, P. E., Fauq, A. H., Lookingbill, H. A., Findlay, K. A., Smith, T. E., Lewis, P. A., McLendon, D. C., Wang, R., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002812200 · Cited by 96
β-Amyloid Precursor Protein
Tischer, E., & Cordell, B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.21914 · Cited by 96
Extracellular Vesicles in Alzheimer’s Disease: Friends or Foes? Focus on Aβ-Vesicle Interaction
Joshi, P., Benussi, L., Furlan, R., Ghidoni, R., & Verderio, C. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16034800 · Cited by 99
Amyloid β‐peptide induces nitric oxide production in rat hippocampus: association with cholinergic dysfunction and amelioration by inducible nitric oxide synthase inhibitors
Tran, M. H., Yamada, K., Olariu, A., Mizuno, M., Ren, X. H., & Nabeshima, T. (2001) · The FASEB Journal · doi:10.1096/fj.00-0719fje · Cited by 95
Role of the β-amyloid precursor protein in Alzheimer's disease
Ashall, F., & Goate, A. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90173-2 · Cited by 95
Regulation by phorbol esters of amyloid precursor protein release from Swiss 3T3 fibroblasts overexpressing protein kinase C alpha.
Slack, B. E., Nitsch, R. M., Livneh, E., Kunz, G. M., Breu, J. J., Eldar-Finkelman, H., & Wurtman, R. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36898-x · Cited by 95
Redox proteomics analysis of brains from subjects with amnestic mild cognitive impairment compared to brains from subjects with preclinical Alzheimer’s disease: Insights into memory loss in MCI
Aluise, C. D., Robinson, R. A. S., Cai, J., Pierce, W. M., Markesbery, W. R., & Butterfield, D. A. (2011) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-101083 · Cited by 94
Partial BACE1 reduction in a Down syndrome mouse model blocks Alzheimer-related endosomal anomalies and cholinergic neurodegeneration: role of APP-CTF
Jiang, Y., Rigoglioso, A., Peterhoff, C. M., Pawlik, M., Sato, Y., Bleiwas, C., Stavrides, P., Smiley, J. F., Ginsberg, S. D., Mathews, P. M., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.11.013 · Cited by 97
Understanding the roles of mutations in the amyloid precursor protein in Alzheimer disease
Hunter, S., & Brayne, C. (2018) · Molecular Psychiatry · doi:10.1038/mp.2017.218 · Cited by 94
NMDA receptor regulation by amyloid-β does not account for its inhibition of LTP in rat hippocampus
Raymond, C. R., Ireland, D. R., & Abraham, W. C. (2003) · Brain Research · doi:10.1016/s0006-8993(03)02269-8 · Cited by 94
Polarized secretion of beta-amyloid precursor proteinand amyloid beta-peptide in MDCK cells.
Haass, C., Koo, E. H., Teplow, D. B., & Selkoe, D. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.4.1564 · Cited by 94
Self-citation
Alternative Selection of β-Site APP-Cleaving Enzyme 1 (BACE1) Cleavage Sites in Amyloid β-Protein Precursor (APP) Harboring Protective and Pathogenic Mutations within the Aβ Sequence
Kimura, A., Hata, S., & Suzuki, T. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.744722 · Cited by 95
Multi-faced neuroprotective effects of geniposide depending on the RAGE-mediated signaling in an Alzheimer mouse model
Lv, C., Wang, L., Liu, X., Yan, S., Yan, S. S., Wang, Y., & Zhang, W. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.09.019 · Cited by 94
The Vacuolar H+-ATPase Inhibitor Bafilomycin A1 Differentially Affects Proteolytic Processing of Mutant and Wild-type β-Amyloid Precursor Protein
Haass, C., Capell, A., Citron, M., Teplow, D. B., & Selkoe, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.11.6186 · Cited by 98
Self-citation
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
Infectious origin of Alzheimer’s disease: Amyloid beta as a component of brain antimicrobial immunity
Vojtechova, I., Machacek, T., Kristofikova, Z., Stuchlik, A., & Petrasek, T. (2022) · PLOS Pathogens · doi:10.1371/journal.ppat.1010929 · Cited by 92
Reversal of Paralysis and Reduced Inflammation from Peripheral Administration of β-Amyloid in T H 1 and T H 17 Versions of Experimental Autoimmune Encephalomyelitis
Grant, J. L., Ghosn, E. E. B., Axtell, R. C., Herges, K., Kuipers, H. F., Woodling, N. S., Andreasson, K., Herzenberg, L. A., Herzenberg, L. A., & Steinman, L. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3004145 · Cited by 92
“Under normal physiological conditions, Ab40 is present at 10-fold higher concentration levels compared to Ab42 in the central nervous system (CNS) (14).”
Background
Reductions in β-amyloid concentrations in vivo by the γ-secretase inhibitors BMS-289948 and BMS-299897
Anderson, J. J., Holtz, G., Baskin, P. P., Turner, M., Rowe, B. A., Wang, B., Kounnas, M. Z., Lamb, B. T., Barten, D. M., Felsenstein, K. M., et al. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.11.015 · Cited by 93
Current concepts in therapeutic strategies targeting cognitive decline and disease modification in Alzheimer’s disease
Jacobsen, J. S., Reinhart, P. H., & Pangalos, M. N. (2005) · NeuroRx · doi:10.1602/neurorx.2.4.612 · Cited by 94
Synthesis of fluorescent-maghemite nanoparticles as multimodal imaging agents for amyloid-β fibrils detection and removal by a magnetic field
Skaat, H., & Margel, S. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.06.110 · Cited by 92
Omega-3 polyunsaturated fatty acids in the brain: metabolism and neuroprotection
Zhang, W. (2011) · Frontiers in bioscience · doi:10.2741/3878 · Cited by 94
Plasma Levels of amyloid β proteins Aβ1–40 and Aβ1–42(43) are elevated in Down's syndrome
Tokuda, T., Fukushima, T., Ikeda, S., Sekijima, Y., Shoji, S., Yanagisawa, N., & Tamaoka, A. (1997) · Annals of Neurology · doi:10.1002/ana.410410220 · Cited by 92
AßT Amyloidogenesis: Unique, or Variation on a Systemic Theme
Kisilevsky, R., Fraser, P. E., & Benson, M. D. (1997) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239709082674 · Cited by 92
Ibuprofen Decreases Cytokine-Induced Amyloid Beta Production in Neuronal Cells
Blasko, I., Apochal, A., Boeck, G., Hartmann, T., Grubeck‐Loebenstein, B., & Ransmayr, G. N. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0451 · Cited by 92
Effects of SEL-12 presenilin on LIN-12 localization and function in Caenorhabditis elegans
Levitan, D. J., & Greenwald, I. (1998) · Development · doi:10.1242/dev.125.18.3599 · Cited by 92
Inhibitors of free radical formation fail to attenuate direct β‐amyloid25–35 peptide‐mediated neurotoxicity in rat hippocampal cultures
Lockhart, B. P., Bénicourt, C., Junien, J., & Privat, A. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490390416 · Cited by 92
Diminished Parkin Solubility and Co-Localization with Intraneuronal Amyloid-β are Associated with Autophagic Defects in Alzheimer's Disease
Lonskaya, I., Shekoyan, A. R., Hebron, M. L., Desforges, N. M., Algarzae, N. K., & Moussa, C. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121141 · Cited by 93
The release of Alzheimer's disease beta amyloid peptide is reduced by phorbol treatment.
Jacobsen, J. S., Spruyt, M. A., Brown, A. M., Sahasrabudhe, S. R., Blume, A. J., Vitek, M. P., Muenkel, H. A., & Sonnenberg‐Reines, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37204-6 · Cited by 91

Authors: 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., & Selkoe, D. J.
Affiliations: Harvard University (US)
Brigham and Women's Hospital (US)
ORCID: Haass, Christian
Schlossmacher, Michael G.
Hung, Albert Y.
Koo, Edward H.
Teplow, David B.
Selkoe, Dennis J.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1992-09
Volume: 359
Issue: 6393
Pages: 322-325
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/359322a0
OpenAlex: W1979543098
Cited by: 1,921
References: 17
Citations by year: 2026: 12 · 2025: 14 · 2024: 22 · 2023: 15 · 2022: 19 · 2021: 28 · 2020: 31 · 2019: 25 · 2018: 29 · 2017: 35 · 2016: 43 · 2015: 46 · 2014: 51 · 2013: 43 · 2012: 67
FWCI: 80.93
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: amyloid-beta, Alzheimer's disease, amyloid precursor protein, amyloid plaques, cell culture model, drug screening
MeSH terms: Antibodies, Epitopes, Cell Line, DNA, Humans, Kidney, Methionine, Molecular Weight, Recombinant Proteins, Transfection, Amyloid beta-Peptides, Amyloid beta-Protein Precursor

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Amyloid β-peptide is produced by cultured cells during normal metabolism

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