The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Abstract
The 4-kilodalton (39 to 43 amino acids) amyloid β protein (βAP), which is deposited as amyloid in the brains of patients with Alzheimer's disease, is derived from a large protein, the amyloid β protein precursor (βAPP). Human mononuclear leukemic (K562) cells expressing a βAP-bearing, carboxyl-terminal βAPP derivative released significant amounts of a soluble 4-kilodalton βAPP derivative essentially identical to the βAP deposited in Alzheimer's disease. Human neuroblastoma (M17) cells transfected with constructs expressing full-length βAPP and M17 cells expressing only endogenous βAPP also released soluble 4-kilodalton βAP, and a similar, if not identical, fragment was readily detected in cerebrospinal fluid from individuals with Alzheimer's disease and normal individuals. Thus cells normally produce and release soluble 4-kilodalton βAP that is essentially identical to the 4-kilodalton βAP deposited as insoluble amyloid fibrils in Alzheimer's disease.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Recently, we and others have shown that normal processing of the large amyloid f3 protein precursor ({3-APP) secretes 4-kDa A(3 that is readily detected in human cerebrospinal fluid and in medium conditioned by cultured cells (3)(4)(5)(6).”
From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [5]
Citations
Cites
McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91209-9 · Cited by 1,693
Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus
Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611
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
Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U., & Gajdusek, D. C. (1987) · Science · doi:10.1126/science.3810169 · Cited by 1,359
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
Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014
Haass, C., Koo, E. H., Mellon, A., Hung, A. Y., & Selkoe, D. J. (1992) · Nature · doi:10.1038/357500a0 · Cited by 919
Flagged first, then by citations
Research works printed but not linked: 5
- Cole, G. M., Molecular Biology and Genetics of Alzheimer's Disease: 113 (1990).
- FRUCHT, S. J., JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY 51: 369 (1992).
- GLENNER, G, BRANBURY REPORT 15: 137 (1983).
- KIM, K.S., NEUROSCIENCE RESEARCH COMMUNICATIONS 2: 121 (1988).
- TERRY, R.D., BRAIN 311: 528 (1963).
Cited by
Sorted by citations
Items 101–200 of 1,002
Snyder, S. W., Ladror, U. S., Wade, W. S., Wang, G. T., Barrett, L. W., Matayoshi, E. D., Huffaker, H. J., Krafft, G. A., & Holzman, T. F. (1994) · Biophysical Journal · doi:10.1016/s0006-3495(94)80591-0 · Cited by 381
β‐Amyloid efflux mediated by p‐glycoprotein
Lam, F. C., Liu, R., Lu, P., Shapiro, A. B., Renoir, J., Sharom, F. J., & Reiner, P. B. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00113.x · Cited by 379
Cataldo, A. M., Barnett, J. L., Berman, S. A., Li, J., Quarless, S., Bursztajn, S., Lippa, C., & Nixon, R. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90324-0 · Cited by 379
A potential role for apoptosis in neurodegeneration and Alzheimer's disease
Cotman, C. W., & Anderson, A. J. (1995) · Molecular Neurobiology · doi:10.1007/bf02740836 · Cited by 378
Alzheimer's DiseasePreprint
Selkoe, D. J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004457 · Cited by 384
Copper Mediates Dityrosine Cross-Linking of Alzheimer's Amyloid-β
Atwood, C., Perry, G. L., Zeng, H., Kato, Y., Jones, W. D., Ling, K.-Q., Huang, X., Moir, R. D., Wang, D., Sayre, L. M., et al. (2003) · Biochemistry · doi:10.1021/bi0358824 · Cited by 371
Gabuzda, D., Busciglio, J., Chen, L. B., Matsudaira, P., & Yankner, B. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36875-8 · Cited by 373
Podlisny, M. B., Ostaszewski, B. L., Squazzo, S. L., Koo, E. H., Rydel, R. E., Teplow, D. B., & Selkoe, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.16.9564 · Cited by 369
Dawson, G. R., Seabrook, G. R., Zheng, H., Smith, D. W., Graham, S. J., O'Dowd, G., Bowery, B. J., Boyce, S., Trumbauer, M. E., Chen, H. Y., et al. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00410-2 · Cited by 394
Estrogen regulates metabolism of Alzheimer amyloid beta precursor protein.
Jaffe, A. B., Toran‐Allerand, C. D., Greengard, P., & Gandy, S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36796-0 · Cited by 363
Interactions between β-amyloid and central cholinergic neurons: implications for Alzheimer’s disease
Kar, S., Slowikowski, S. P. M., Westaway, D. A., & Mount, H. T. J. (2004) · Journal of Psychiatry and Neuroscience · doi:10.1139/jpn.0442 · Cited by 366
Therapeutic approaches to Alzheimer's disease
Klafki, H., Staufenbiel, M., Kornhuber, J., & Wiltfang, J. (2006) · Brain · doi:10.1093/brain/awl280 · Cited by 362
Melatonin Prevents Death of Neuroblastoma Cells Exposed to the Alzheimer Amyloid Peptide
Pappolla, M. A., Sos, M., Omar, R. A., Bick, R. J., Hickson-Bick, D. L. M., Reiter, R. J., Efthimiopoulos, S., & Robakis, N. K. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-05-01683.1997 · Cited by 359
Reddy, P. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03530.x · Cited by 367
Sherriff, F. E., Bridges, L., & Sivaloganathan, S. (1994) · Acta Neuropathologica · doi:10.1007/bf00386254 · Cited by 357
Metallostasis in Alzheimer's disease
Ayton, S., Lei, P., & Bush, A. I. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.558 · Cited by 359
Zhao, W.-Q., & Townsend, M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.014 · Cited by 291
Weldon, D. T., Rogers, S. D., Ghilardi, J. R., Finke, M. P., Cleary, J. P., O’Hare, E., Esler, W. P., Maggio, J. E., & Mantyh, P. W. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-06-02161.1998 · Cited by 348
Bartolini, M., Bertucci, C., Bolognesi, M. L., Cavalli, A., Melchiorre, C., & Andrisano, V. (2007) · ChemBioChem · doi:10.1002/cbic.200700427 · Cited by 355
Slunt, H. H., Thinakaran, G., von Koch, C., Lo, A., Tanzi, R. E., & Sisodia, S. S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41992-2 · Cited by 346
Kanai, M., Matsubara, E., Isoe, K., Urakami, K., Nakashima, K., Arai, H., Sasaki, H., Abe, K., Iwatsubo, T., Kosaka, T., et al. (1998) · Annals of Neurology · doi:10.1002/ana.410440108 · Cited by 340
Self-citationCopper(II)-induced self-oligomerization of α-synuclein
Paik, S. R., Shin, H.-J., Lee, J., Chang, C., & Kim, J. (1999) · Biochemical Journal · doi:10.1042/bj3400821 · Cited by 340
Inhibition of Alzheimer β-Fibrillogenesis by Melatonin
Pappolla, M. A., Bozner, P., Soto, C. A., Shao, H., Robakis, N. K., Zagorski, M. G., Frangione, B., & Ghiso, J. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7185 · Cited by 340
Self-citationWang, J., Ho, L., Chen, L., Zhao, Z., Zhao, W., Qian, X., Humala, N., Seror, I., Bartholomew, S. R., Rosendorff, C., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31547 · Cited by 333
Nalbantoglu, J. N., Santiago, G. T., Lahsaïni, A., Poirier, J., Goncalves, O., Verge, G. M., Momoli, F., Welner, S. A., Massicotte, G., Julien, J., et al. (1997) · Nature · doi:10.1038/387500a0 · Cited by 342
Evidence that Aβ42 is the real culprit in alzheimer's disease
Younkin, S. G. (1995) · Annals of Neurology · doi:10.1002/ana.410370303 · Cited by 331
Self-citationCook, D. G., Leverenz, J. B., McMillan, P. J., Kulstad, J. J., Ericksen, S., Roth, R. A., Schellenberg, G. D., Jin, L., Kovacina, K. S., & Craft, S. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63822-9 · Cited by 329
On the nucleation of amyloid β‐protein monomer folding
Lazo, N. D., Grant, M. A., Condron, M. M., Rigby, A. C., & Teplow, D. B. (2005) · Protein Science · doi:10.1110/ps.041292205 · Cited by 333
Modulation of A beta adhesiveness and secretase site cleavage by zinc.
Bush, A. I., Pettingell, W. H., Paradis, M. D., & Tanzi, R. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32694-7 · Cited by 331
Sorting through the Cell Biology of Alzheimer's Disease: Intracellular Pathways to Pathogenesis
Small, S. A., & Gandy, S. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.001 · Cited by 328
Soto, C. A., Castaño, E. M., Frangione, B., & Inestrosa, N. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.3063 · Cited by 321
Self-citationHaass, C., Hung, A. Y., Selkoe, D. J., & Teplow, D. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32503-6 · Cited by 319
Metabolism of the “Swedish” Amyloid Precursor Protein Variant in Neuro2a (N2a) Cells
Thinakaran, G., Teplow, D. B., Siman, R., Greenberg, B., & Sisodia, S. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9390 · Cited by 317
Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide.
Solomon, B., Koppel, R., Hanan, E., & Katzav-Gozansky, T. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.452 · Cited by 314
Zinc-induced Alzheimer's Aβ1–40 Aggregation Is Mediated by Conformational Factors
Huang, X., Atwood, C., Moir, R. D., Hartshorn, M. A., Vonsattel, J., Tanzi, R. E., & Bush, A. I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26464 · Cited by 317
Introduction and expression of the 400 kilobase precursor amyloid protein gene in transgenic mice
Lamb, B. T., Sisodia, S. S., Lawler, A. M., Slunt, H. H., Kitt, C. A., Kearns, W. G., Pearson, P. L., Price, D. L., & Gearhart, J. D. (1993) · Nature Genetics · doi:10.1038/ng0993-22 · Cited by 311
Mattson, M. P., & Scheff, S. W. (1994) · Journal of Neurotrauma · doi:10.1089/neu.1994.11.3 · Cited by 308
Ghiso, J., Matsubara, E., Koudinov, A., Choi-Miura, N. H., Tomita, M., Wisniewski, T., & Frangione, B. (1993) · Biochemical Journal · doi:10.1042/bj2930027 · Cited by 304
Self-citationGolde, T. E., Eckman, C. B., & Younkin, S. G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00043-0 · Cited by 244
Self-citationAmino-terminal Deletions Enhance Aggregation of β-Amyloid Peptides in Vitro
Pike, C. J., Overman, M. J., & Cotman, C. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.23895 · Cited by 302
Rebeck, G. W., Harr, S. D., Hyman, B. T., & Strickland, D. K. (1995) · Annals of Neurology · doi:10.1002/ana.410370212 · Cited by 232
Inhibition of Amyloid β Protein Aggregation and Neurotoxicity by Rifampicin
Tomiyama, T., Shoji, A., Kataoka, K.-I., Suwa, Y., Asano, S., Kaneko, H., & Endo, N. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.6839 · Cited by 295
Genetics and molecular pathogenesis of sporadic and hereditary cerebral amyloid angiopathies
Révész, T., Holton, J. L., Lashley, T., Plant, G. T., Frangione, B., Rostagno, A. A., & Ghiso, J. A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0501-8 · Cited by 300
Self-citationMolecular pathology of neurodegenerative diseases by cryo-EM of amyloids
Scheres, S. H. W., Falcon, B., & Goedert, M. (2023) · Nature · doi:10.1038/s41586-023-06437-2 · Cited by 308
The Profile of Soluble Amyloid β Protein in Cultured Cell Media
Wang, R., Sweeney, D. A., Gandy, S., & Sisodia, S. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.50.31894 · Cited by 293
Atwood, C., Obrenovich, M. E., Liu, T., Chan, H., Perry, G. L., Smith, M. A., & Martins, R. N. (2003) · Brain Research Reviews · doi:10.1016/s0165-0173(03)00174-7 · Cited by 297
Jan, A., Gokce, O., Luthi-Carter, R., & Lashuel, H. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803159200 · Cited by 291
Monoaminergic neuropathology in Alzheimer’s disease
Šimić, G., Leko, M. B., Wray, S., Harrington, C. R., Delalle, I., Milošević, N. J., Bažadona, D., Buée, L., de Silva, R., Giovanni, G. D., et al. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.04.001 · Cited by 297
Skovronsky, D. M., Doms, R. W., & Lee, V. M.-Y. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.4.1031 · Cited by 290
Citron, M., Diehl, T. S., Gordon, G., Biere, A. L., Seubert, P. A., & Selkoe, D. J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.13170 · Cited by 287
The Origins of Alzheimer Disease
Selkoe, D. J. (2000) · JAMA · doi:10.1001/jama.283.12.1615 · Cited by 285
Citron, M., Vigo-Pelfrey, C., Teplow, D. B., Miller, C., Schenk, D., Johnston, J., Winblad, B., Venizelos, N., Lannfelt, L., & Selkoe, D. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.11993 · Cited by 366
The genetic architecture of Alzheimer's disease: beyond APP, PSENs and APOE
Guerreiro, R. J., Gustafson, D. R., & Hardy, J. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.03.025 · Cited by 285
Sisodia, S., Koo, E., Hoffman, P., Perry, G. L., & Price, D. (1993) · Journal of Neuroscience · doi:10.1523/jneurosci.13-07-03136.1993 · Cited by 284
Xu, H., Sweeney, D. A., Wang, R., Thinakaran, G., Lo, A., Sisodia, S. S., Greengard, P., & Gandy, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3748 · Cited by 281
The role of Aβ42 in Alzheimer's disease
Younkin, S. G. (1998) · Journal of Physiology-Paris · doi:10.1016/s0928-4257(98)80035-1 · Cited by 282
Self-citationMolecular genetics of Alzheimer’s disease
George‐Hyslop, P. S. (2000) · Biological Psychiatry · doi:10.1016/s0006-3223(99)00301-7 · Cited by 281
Protein phosphorylation inhibits production of Alzheimer amyloid beta/A4 peptide.
Buxbaum, J. D., Koo, E. H., & Greengard, P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.19.9195 · Cited by 276
TOKUDA, T., CALERO, M., MATSUBARA, E., VIDAL, R., KUMAR, A., PERMANNE, B., ZLOKOVIC, B., SMITH, J. D., LADU, M. J., ROSTAGNO, A., et al. (2000) · Biochemical Journal · doi:10.1042/bj3480359 · Cited by 272
Self-citationγ-Secretase inhibitors and modulators
Golde, T. E., Koo, E. H., Felsenstein, K. M., Osborne, B. A., & Miele, L. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.06.005 · Cited by 275
Self-citationWiltfang, J., Esselmann, H., Bibl, M., Av, S., Otto, M., Paul, S., Schmidt, B., Klafki, H., Maler, M., Dyrks, T., et al. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00818.x · Cited by 274
Synaptotrophic effects of human amyloid β protein precursors in the cortex of transgenic mice
Mucke, L., Masliah, E., Johnson, W. B., Ruppe, M. D., Alford, M. F., Rockenstein, E. M., Forss‐Petter, S., Pietropaolo, M., Mallory, M. E., & Abraham, C. R. (1994) · Brain Research · doi:10.1016/0006-8993(94)90767-6 · Cited by 270
Fibrillogenesis in Alzheimer's disease of amyloid β peptides and apolipoprotein E
Castano, E. M., Prelli, F., Wisniewski, T., Golabek, A., Kumar, R. A., Soto, C., & Frangione, B. (1995) · Biochemical Journal · doi:10.1042/bj3060599 · Cited by 267
Self-citationGeneration of amyloid β protein from its precursor is sequence specific
Citron, M., Teplow, D. B., & Selkoe, D. J. (1995) · Neuron · doi:10.1016/0896-6273(95)90323-2 · Cited by 263
Therapeutic strategies for human amyloid diseases
Sacchettini, J. C., & Kelly, J. W. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd769 · Cited by 259
Gender, sex steroid hormones, and Alzheimer’s disease
Vest, R. S., & Pike, C. J. (2013) · Hormones and Behavior · doi:10.1016/j.yhbeh.2012.04.006 · Cited by 260
Jan, A., Hartley, D. M., & Lashuel, H. A. (2010) · Nature Protocols · doi:10.1038/nprot.2010.72 · Cited by 263
Role of metabolism in neurodegenerative disorders
Procaccini, C., Santopaolo, M., Faicchia, D., Colamatteo, A., Formisano, L., de Candia, P., Galgani, M., De Rosa, V., & Matarese, G. (2016) · Metabolism · doi:10.1016/j.metabol.2016.05.018 · Cited by 258
The cause of neuronal degeneration in Alzheimer’s disease
Vickers, J. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(99)00023-4 · Cited by 254
Sharples, R. A., Vella, L. J., Nisbet, R. M., Naylor, R., Perez, K. A., Barnham, K. J., Masters, C. L., & Hill, A. F. (2008) · The FASEB Journal · doi:10.1096/fj.07-9357com · Cited by 253
Amyloid-β as a Modulator of Synaptic Plasticity
Parihar, M. S., & Brewer, G. J. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101020 · Cited by 264
The Role of APP Processing and Trafficking Pathways in the Formation of Amyloid β‐Proteina
SELKOE, D. J., YAMAZAKI, T., CITRON, M., PODLISNY, M. B., KOO, E. H., TEPLOW, D. B., & HAASS, C. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34401.x · Cited by 205
ISHIZUKA, K., KIMURA, T., IGATA‐YI, R., KATSURAGI, S., TAKAMATSU, J., & MIYAKAWA, T. (1997) · Psychiatry and Clinical Neurosciences · doi:10.1111/j.1440-1819.1997.tb02375.x · Cited by 245
Calcium Ionophore Increases Amyloid .beta. Peptide Production by Cultured Cells
Querfurth, H. W., & Selkoe, D. J. (1994) · Biochemistry · doi:10.1021/bi00181a016 · Cited by 247
Nitsch, R. M., Farber, S. A., Growdon, J. H., & Wurtman, R. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5191 · Cited by 244
Mackic, J. B., Stins, M., McComb, J. G., Calero, M., Ghiso, J., Kim, K. S., Yan, S. D., Stern, D., Schmidt, A. M., Frangione, B., et al. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2029 · Cited by 242
Self-citationSenile plaques stimulate microglia to release a neurotoxin found in Alzheimer brain
Giulian, D., Haverkamp, L. J., Li, J., Karshin, W. L., Yu, J., Tom, D., Li, X., & Kirkpatrick, J. B. (1995) · Neurochemistry International · doi:10.1016/0197-0186(95)00067-i · Cited by 242
Non-A.beta. Component of Alzheimer's Disease Amyloid (NAC) is Amyloidogenic
Iwai, A., Yoshimoto, M., Masliah, E., & Saitoh, T. (1995) · Biochemistry · doi:10.1021/bi00032a006 · Cited by 237
Ermekova, K. S., Zambrano, N., Linn, H., Minopoli, G., Gertler, F. B., Russo, T., & Sudol, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.32869 · Cited by 239
Reduced levels of amyloid β-peptide antibody in Alzheimer disease
Du, Y., Dodel, R. C., Hampel, H. J., Büerger, K., Lin, S., Eastwood, B. J., Bales, K. R., Gao, F., Moeller, H. –., Oertel, W. H., et al. (2001) · Neurology · doi:10.1212/wnl.57.5.801 · Cited by 236
Serpinopathies and the conformational dementias
Lomas, D. A., & Carrell, R. W. (2002) · Nature Reviews Genetics · doi:10.1038/nrg907 · Cited by 231
Lichtenthaler, S. F., Wang, R., Grimm, H. S., Uljon, S., Masters, C. L., & Beyreuther, K. T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3053 · Cited by 231
Yao, M., Nguyen, T. V., & Pike, C. J. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4736-04.2005 · Cited by 233
Amyloid β-Protein Inhibits Ubiquitin-dependent Protein Degradation in Vitro
Gregori, L. L., Fuchs, C., Figueiredo‐Pereira, M. E., Nostrand, W. E. V., & Goldgaber, D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.34.19702 · Cited by 239
Mancuso, C., & Santangelo, R. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2017.12.009 · Cited by 232
Wertkin, A. M., Turner, R. S., Pleasure, S. J., Golde, T. E., Younkin, S. G., Trojanowski, J. Q., & Lee, V. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9513 · Cited by 231
Self-citationReactive oxygen species and Alzheimer's disease
Multhaup, G., Ruppert, T., Schlicksupp, A., Hesse, L., Beher, D., Masters, C. L., & Beyreuther, K. (1997) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00062-2 · Cited by 228
Ling, Y., Morgan, K., & Kalsheker, N. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00133-x · Cited by 224
Gowing, E., Roher, A. E., Woods, A. S., Cotter, R. J., Chaney, M., Little, S. P., & Ball, M. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78080-6 · Cited by 223
Kowalik‐Jankowska, T., Ruta, M., Wiśniewska, K., & Łankiewicz, L. (2003) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(03)00128-4 · Cited by 222
Daigle, I., & Li, C. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.24.12045 · Cited by 228
Combination assay of CSF Tau, Aβ1-40 and Aβ1-42(43) as a biochemical marker of Alzheimer's disease
Shoji, M., Matsubara, E., Kanai, M., Watanabe, M., Nakamura, T., Tomidokoro, Y., Shizuka, M., Wakabayashi, K., Igeta, Y., Ikeda, Y., et al. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00122-1 · Cited by 221
Self-citationRegulation of Amyloid Precursor Protein Cleavage
Mills, J., & Reiner, P. B. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0720443.x · Cited by 222
Serotonin 5-HT2a and 5-HT2c Receptors Stimulate Amyloid Precursor Protein Ectodomain Secretion
Nitsch, R. M., Deng, M., Growdon, J. H., & Wurtman, R. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4188 · Cited by 219
Eide, P. K., & Ringstad, G. (2015) · Acta Radiologica Open · doi:10.1177/2058460115609635 · Cited by 218
Suzuki, T., Oishi, M., Marshak, D. R., Czernik, A. J., Nairn, A. C., & Greengard, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06360.x · Cited by 216
α 2 -macroglobulin associates with β-amyloid peptide and prevents fibril formation
Hughes, S. R., Khorkova, O., Goyal, S., Knäblein, J., Heroux, J. A., Riedel, N. G., & Sahasrabudhe, S. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3275 · Cited by 212
Weidemann, A., Paliga, K., Dürrwang, U., Czech, C., Evin, G. M., Masters, C. L., & Beyreuther, K. T. (1997) · Nature Medicine · doi:10.1038/nm0397-328 · Cited by 214
Turnover of Amyloid β-Protein in Mouse Brain and Acute Reduction of Its Level by Phorbol Ester
Savage, M. J., Trusko, S. P., Howland, D. S., Pinsker, L. R., Mistretta, S., Reaume, A. G., Greenberg, B. D., Siman, R., & Scott, R. W. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-05-01743.1998 · Cited by 213
Hyman, B. T., West, H. L., Rebeck, G. W., Buldyrev, S. V., Mantegna, R. N., Ukleja, M., Havlin, S., & Stanley, H. E. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.8.3586 · Cited by 212
Metadata
- Authors
- 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., & Younkin, S. G.
- Affiliations
- Gunma University (JP)
- Case Western Reserve University (US)
- NYU Langone Health (US)
- Washington University in St. Louis (US)
- The University of Texas Southwestern Medical Center (US)
- Venue
- Science
- Published
- 1992-10-02
- Volume
- 258
- Issue
- 5079
- Pages
- 126-129
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2033382511
- Cited by
- 1,447
- References
- 32
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 16 · 2023: 13 · 2022: 13 · 2021: 18 · 2020: 23 · 2019: 16 · 2018: 18 · 2017: 15 · 2016: 37 · 2015: 26 · 2014: 28 · 2013: 38 · 2012: 37
- FWCI
- 80.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG06656, R01AG006656, AG05891)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR02594)
- 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, proteolytic processing, soluble amyloid-beta, amyloid fibrils, cerebrospinal fluid, K562 cells, neuroblastoma cells, transfection, protein secretion
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Base Sequence, Cell Line, Leukemia, Myeloid, Molecular Sequence Data, Neuroblastoma, Transfection, Immunoblotting, Amyloid beta-Peptides, Amyloid beta-Protein Precursor
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