Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing

Clinical diagnosis of Alzheimer's disease: Report of the NINCDS‐ADRDA Work Group* under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease

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

Characterization and Chromosomal Localization of a cDNA Encoding Brain Amyloid of Alzheimer's Disease

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

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

Leukoencephalopathy-related cerebral amyloid angiopathy with cystatin C deposition.

Shimode, K., Kobayashi, S., Imaoka, K., Umegae, N., & Nagai, A. (1996) · Stroke · doi:10.1161/01.str.27.8.1417 · Cited by 22

Alterations of GABA B receptors in the APP/PS1 mouse model of Alzheimer's disease

Salazar, A., Osse, A. M. L., Ortiz, A. A., Murtishaw, A. S., & Kinney, J. W. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.10.013 · Cited by 26

Challenges in Designing Therapeutic Agents for Treating Alzheimer’s Disease-from Serendipity to Rationality

Rashid, U., & Ansari, F. L. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803959-5.50002-7 · Cited by 23

Biomarkers for Evaluation of Clinical Efficacy of Multipotential Neuroprotective Drugs for Alzheimer's and Parkinson's Diseases

Halperin, I. J. Y., Morelli, M., Korczyn, A. D., Youdim, M. B. H., & Mandel, S. A. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.10.033 · Cited by 22

Zinc binding agonist effect on the recognition of the β-amyloid (4–10) epitope by anti-β-amyloid antibodies

Zirah, S., Ştefănescu, R., Manea, M., Tian, X., Cecal, R., Kozin, S. A., Debey, P., Rebuffat, S., & Przybylski, M. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.150 · Cited by 22

Nimodipine selectively stimulates β-amyloid 1–42 secretion by a mechanism independent of calcium influx blockage

Facchinetti, F., Fasolato, C., DELGIUDICE, E., Burgo, A., Furegato, S., Fusco, M., Basso, E., Seraglia, R., D'Arrigo, A. M., & Leon, A.-S. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.02.006 · Cited by 23

Widespread γ-secretase activity in the cell, but do we need it at the mitochondria?

Teng, F. Y. H., & Tang, B. L. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.131 · Cited by 21

The role of probiotics, prebiotics, and postbiotics: cellular and molecular pathways activated on glial cells in Alzheimer’s disease

Patricio-Martínez, A., Patricio, F., Macuil-Chapuli, E., Martínez-Juárez, E. Á., Flores-Díaz, S., Cedillo-Ramirez, M. L., & Limón, I. D. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1598011 · Cited by 23

Mechanism of oxidative stress and neurotoxicity associated with heme and copper–Aβ relevant to Alzheimer's disease

Dey, C., Roy, M., Pal, P., Ghosh, R., & Dey, S. G. (2025) · Chemical Society Reviews · doi:10.1039/d5cs00544b · Cited by 22

Redox Imbalance in Neurological Disorders in Adults and Children

Rey, F., Berardo, C., Maghraby, E., Mauri, A., Messa, L., Esposito, L., Casili, G., Ottolenghi, S., Bonaventura, E., Cuzzocrea, S., et al. (2023) · Antioxidants · doi:10.3390/antiox12040965 · Cited by 23

Endocytic pathways of pathogenic protein aggregates in neurodegenerative diseases

Hivare, P., Mujmer, K., Swarup, G., Gupta, S. K., & Bhatia, D. D. (2023) · Traffic · doi:10.1111/tra.12906 · Cited by 24

Solution and solid state study of copper(II) ternary complexes containing amino acids of interest for brain biochemistry – 1: Aspartic or glutamic acids with methionine or cysteine

Pinto, L. D., Puppin, P. A. L., Behring, V. M., Flinker, D. H., Mercê, A. L. R., Mangrich, A. S., Rey, N. A., & Felcman, J. (2010) · Inorganica Chimica Acta · doi:10.1016/j.ica.2010.04.036 · Cited by 20

Loss of thioredoxin function in retinas of mice overexpressing amyloid β

Lamoke, F., Ripandelli, G., Webster, S. J., Montemari, A. L., Maraschi, A., Martin, P. M., Marcus, D. M., Liou, G. I., & Bartoli, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.04.010 · Cited by 20

Ameliorative effects of a non-competitive BACE1 inhibitor TAK-070 on Aβ peptide levels and impaired learning behavior in aged rats

Takahashi, H., Fukumoto, H., Maeda, R., Terauchi, J., Kato, K., & Miyamoto, M. (2010) · Brain Research · doi:10.1016/j.brainres.2010.09.032 · Cited by 21

Guinea-pig primary cell cultures provide a model to study expression and amyloidogenic processing of endogenous amyloid precursor protein

Beck, M., Brückner, M. K., Holzer, M., Kaap, S., Pannicke, T., Arendt, T., & Bigl, V. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00390-5 · Cited by 21

The significance of the Swedish APP670/671 mutation for the development of Alzheimer's disease amyloidosis

Johnston, J. A., O’Neill, C., Lannfelt, L., Winblad, B. G., & Cowburn, R. F. (1994) · Neurochemistry International · doi:10.1016/0197-0186(94)90056-6 · Cited by 23

Accumulation of proteolytic fragments of mutant presenilin 1 and accelerated amyloid deposition are co-regulated in transgenic mice

Borchelt, D., Lee, M. K., Gonzales, V., Slunt, H. H., Ratovitski, T., Jenkins, N. A., Copeland, N. G., Price, D. L., & Sisodia, S. S. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00280-9 · Cited by 21

β-Amyloid peptides inhibit acetylcholine release from cholinergic presynaptic nerve endings isolated from an electric ray

Satoh, Y., Hirakura, Y., Shibayama, S., Hirashima, N., Suzuki, T., & Kirino, Y. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01665-2 · Cited by 21

Ca 2+ Interacts with Glu-22 of Aβ(1–42) and Phospholipid Bilayers to Accelerate the Aβ(1–42) Aggregation Below the Critical Micelle Concentration

Yi, X., Zhang, Y., Gong, M., Yu, X., Darabedian, N., Zheng, J., & Zhou, F. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00719 · Cited by 21

[30] Design and testing of inhibitors of fibril formation

Findeis, M. A., & Molineaux, S. M. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)09032-1 · Cited by 21

A Novel Metalloprotease in Rat Brain Cleaves the Amyloid Precursor Protein of Alzheimer's Disease Generating Amyloidogenic Fragments

Mok, S. S., Evin, G. M., Li, Q., Smith, A. I., Beyreuther, K. T., Masters, C. L., & Small, D. H. (1997) · Biochemistry · doi:10.1021/bi961848w · Cited by 21

Potentially amyloidogenic fragment of 50 kDa and intracellular processing of amyloid precursor protein in cells cultured under leupeptin

Tsuzuki, K., Fukatsu, R., Takamaru, Y., Fujii, N., & Takahata, N. (1994) · Brain Research · doi:10.1016/0006-8993(94)90881-8 · Cited by 21

β-Amyloid precursor protein gene in squirrel monkeys with cerebral amyloid angiopathy

Levy, E., Amorim, A., Frangione, B., & Walker, L. C. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00090-2 · Cited by 21

Amyloid β protein and transthyretin, sequestrating protein colocalize in normal human kidney

Tsuzuki, K., Fukatsu, R., Hayashi, Y., Yoshida, T., Sasaki, N., Takamaru, Y., Yamaguchi, H., Tateno, M., Fujii, N., & Takahata, N. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)13369-9 · Cited by 20

Is Brain Copper Deficiency in Alzheimer's, Lewy Body, and Creutzfeldt Jakob Diseases the Common Key for a Free Radical Mechanism and Oxidative Stress-Induced Damage?

Deloncle, R., & Guillard, O. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140765 · Cited by 20

Sodium azide and 2-deoxy-D-glucose-induced cellular stress affects phosphorylation-dependent AβPP processing

Henriques, A. G., Domingues, S. C., Fardilha, M., Silva, E. F. D. C. E., & Silva, O. A. B. D. C. E. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-7302 · Cited by 20

Specific inhibitory effect of amyloid-β on presynaptic muscarinic receptor subtypes modulating neurotransmitter release in the rat nucleus accumbens

Grilli, M., Lagomarsino, F., Zappettini, S., Preda, S., Mura, E., Govoni, S. M., & Marchi, M. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.01.058 · Cited by 20

The molecular significance of amyloid β-peptide for Alzheimer's disease

Haass, C. (1996) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/bf02189111 · Cited by 20

The Amyloid .BETA. Protein Precursor Mutations Linked to Familial Alzheimer's Disease Alter Processing in a Way That Fosters Amyloid Deposition.

Younkin, S. G. (1994) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.174.217 · Cited by 20

Secretory cleavage site of Alzheimer amyloid precursor protein is heterogeneous in Down's syndrome brain

Kametania, F., Tanaka, K., Tokuda, T., & Ikeda, S. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00851-5 · Cited by 20

Solubilization of full‐length amyloid precursor proteins from PC12 cell membranes

Ripellino, J. A., Vassilacopoulou, D., & Robakis, N. K. R. K. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490390211 · Cited by 20

Differential diagnosis of neurodegenerative diseases with special emphasis on Creutzfeldt-Jakob disease

Otto, M., & Wiltfang, J. (2003) · Restorative Neurology and Neuroscience · doi:10.3233/rnn-2003-00238 · Cited by 20

Glutamate, beta-amyloid precursor proteins, and calcium mediated neurofibrillary degeneration

Smith‐Swintosky, V. L., & Mattson, M. P. (1994) · Springer eBooks · doi:10.1007/978-3-7091-9350-1_3 · Cited by 20

Familial Alzheimer's Disease Cells Abnormally Accumulate β‐Amyloid‐Harbouring Peptides Preferentially in Cytosol but not in Extracellular Fluid

Matsumoto, A., & Matsumoto, R. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.1055b.x · Cited by 20

Novel Effects of FCCP [Carbonyl Cyanide p‐(Trifluoromethoxy)phenylhydrazone] on Amyloid Precursor Protein Processing

Connop, B. P., Thies, R. L., Beyreuther, K., Ida, N., & Reiner, P. B. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.721457.x · Cited by 19

Supramolecular Structures of Amyloid-Related Peptides in an Ambient Water Nanofilm

Ye, M., Zhang, Y., Li, H., Xie, M., & Hu, J. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp105501x · Cited by 19

Refining the amyloid β peptide and oligomer fingerprint ambiguities in Alzheimer’s disease: Mass spectrometric molecular characterization in brain, cerebrospinal fluid, blood, and plasma

Michno, W., Blennow, K., Zetterberg, H., & Brinkmalm, G. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15466 · Cited by 18

Specific Neuromodulatory Actions of Amyloid-β on Dopamine Release in Rat Nucleus Accumbens and Caudate Putamen

Mura, E., Preda, S., Govoni, S. M., Lanni, C., Trabace, L., Grilli, M., Lagomarsino, F., Pittaluga, A., & Marchi, M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1299 · Cited by 19

Platelet Microparticles as Carriers of Soluble Alzheimer's Amyloid β (sAβ)

Matsubara, E., Shoji, M., Murakami, T., Abe, K., Frangione, B., & Ghiso, J. A. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb04836.x · Cited by 19

Pharmacological modulation of dietary lipid-induced cerebral capillary dysfunction: Considerations for reducing risk for Alzheimer’s disease

Pallebage‐Gamarallage, M. M., Takechi, R., Lam, V., Elahy, M., & Mamo, J. C. L. (2015) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408363.2015.1115820 · Cited by 20

γ-secretase processing of APLP1 leads to the production of a p3-like peptide that does not aggregate and is not toxic to neurons

Minogue, A. M., Stubbs, A. K., Frigerio, C. S., Boland, B., Fadeeva, J. V., Tang, J., Selkoe, D. J., & Walsh, D. M. (2009) · Brain Research · doi:10.1016/j.brainres.2009.01.008 · Cited by 20

Schwann Cell‐Axon Interactions in Charcot‐Marie‐Tooth Disease

Griffin, J. W., & Sheikh, K. A. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb08571.x · Cited by 19

The Rationale for Insulin Therapy in Alzheimer’s Disease

Ribarič, S. (2016) · Molecules · doi:10.3390/molecules21060689 · Cited by 20

Assessing the Effects of Acute Amyloid β Oligomer Exposure in the Rat

Wong, R., Cechetto, D. F., & Whitehead, S. N. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17091390 · Cited by 19

Recent Understanding of the Molecular Mechanisms of Alzheimer?s Disease

Grimm, M. O. W., & Hartmann, T. (2011) · Journal of Addiction Research & Therapy · doi:10.4172/2155-6105.s5-004 · Cited by 20

Interaction of synthetic Alzheimerβ-protein-derived analogs with aqueous aluminum: A low-field27Al NMR investigation

Vyas, S. B., & Duffy, L. K. (1995) · Journal of Protein Chemistry · doi:10.1007/bf01886902 · Cited by 19

Fimbria–Fornix Lesion Does Not Affect APP Levels and Amyloid Deposition in the Hippocampus of APP+PS1 Double Transgenic Mice

Liu, L., Ikonen, S., Tapiola, T., Tanila, H., & van Groen, T. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.8015 · Cited by 19

Caloric Intake, Dietary Lifestyles, Macronutrient Composition, and Alzheimer′ Disease Dementia

Pasinetti, G. M., Wang, J., Porter, S., & Ho, L. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/806293 · Cited by 19

A meta-analysis of the relationship between sleep and β-Amyloid biomarkers in Alzheimer’s disease

Harenbrock, J., Holling, H., Reid, G., & Koychev, I. G. (2023) · Biomarkers in Neuropsychiatry · doi:10.1016/j.bionps.2023.100068 · Cited by 20

Introduction to Alzheimer's Disease

Allsop, D. (2003) · Humana Press eBooks · doi:10.1385/1-59259-195-7:1 · Cited by 17

PI3K activation prevents Aβ42-induced synapse loss and favors insoluble amyloid deposit formation

Arnés, M., Romero, N., Casas‐Tintó, S., Acebes, Á., & Ferrús, A. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-05-0303 · Cited by 16

Neuroinflammation and Alteration of the Blood-Brain Barrier in Alzheimer´s Disease

Soto-Rojas, L. O., de la Cruz‐López, F., Ontiveros‐Torres, M. Á., Viramontes‐Pintos, A., Cárdenas‐Aguayo, M. D. C., Meraz‐Ríos, M. A., Salinas‐Lara, C., Florán, B., & Luna‐Muñoz, J. (2015) · InTech eBooks · doi:10.5772/60024 · Cited by 21

Is pharmacological prevention of Alzheimer's a realistic goal?

Anthony, J. C., Breitner, J. C. S., & Zandi, P. P. (2002) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.3.4.365 · Cited by 18

Human neutrophil phagocytic granules contain a truncated soluble form of the Alzheimer beta/A4 amyloid precursor protein (APP)

Nordstedt, C., Näslund, J., Thyberg, J., Messamore, E., Gandy, S., & Terenius, L. Y. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36954-5 · Cited by 18

Automated synthesis of fluorogenic protease substrates: design of probes for alzheimer's disease-associated proteases

Wang, G. T., & Krafft, G. A. (1992) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(00)80452-7 · Cited by 18

Proteolytic Degradation of the Amyloid β-Protein: The Forgotten Side of Alzheimers Disease

Leissring, M. A. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025206 · Cited by 17

Amyloidogenesis in familial British dementia is associated with a genetic defect on chromosome 13

GHISO, J., VIDAL, R., ROSTAGNO, A., MIRAVALLE, L., HOLTON, J. L., MEAD, S., RÉVÉSZ, T., PLANT, G., & FRANGIONE, B. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06908.x · Cited by 12

Evidence that glypican is a receptor mediating β-amyloid neurotoxicity in PC12 cells

Schulz, J. G., Megow, D., Reszka, R. C., Villringer, A., Einhäupl, K. M., & Dirnagl, U. (1998) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1998.00220.x · Cited by 18

Probing modifications of the neuronal cytoskeleton

Doering, L. C. (1993) · Molecular Neurobiology · doi:10.1007/bf02769179 · Cited by 18

Early onset Alzheimer's disease in a South American pedigree from Argentina

Mangone, C. A., Castaño, E. M., Levy, E., Abiusi, G., Wisniewski, T., Marques, M. R., Faccio, E., Gorelick, P. B., Frangione, B., & Sica, R. E. P. (1995) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.1995.tb05835.x · Cited by 10

Alzheimer's presenilin 1 gene expression in platelets and megakaryocytes

Vidal, R., Ghiso, J. A., Wısnıewskı, T., & Frangione, B. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00845-9 · Cited by 19

Modulation of amyloid precursor protein processing by compounds with various mechanisms of action: detection by liquid phase electrochemiluminescent system

Khorkova, O., Patel, K., Heroux, J. A., & Sahasrabudhe, S. R. (1998) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(98)00053-3 · Cited by 17

Peptide p3 may play a neuroprotective role in the brain

Han, W., Ji, T., Mei, B., & Su, J. (2011) · Medical Hypotheses · doi:10.1016/j.mehy.2010.12.013 · Cited by 17

The Genetics of Alzheimer’s Disease and Parkinson’s Disease

Bekris, L. M., Yu, C., Bird, T. D., & Tsuang, D. W. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-7104-3_21 · Cited by 16

Intracellular and cell-surface distribution of amyloid precursor protein in cortical astrocytes

Young, M. J., Lee, R. K. K., Jhaveri, S., & Wurtman, R. J. (1999) · Brain Research Bulletin · doi:10.1016/s0361-9230(99)00084-2 · Cited by 17

Talsaclidine (WAL 2014 FU), a muscarinic M1 receptor agonist for the treatment of Alzheimer's disease

Wienrich, M., Ceci, A., Ensinger, H. A., Gaida, W., Mendla, K. D., Osugi, T., Raschig, A., & Weiser, T. W. (2002) · Drug Development Research · doi:10.1002/ddr.10085 · Cited by 17

Stretching Single-Stranded DNA on a Surface

Michalet, X. (2001) · Nano Letters · doi:10.1021/nl010035c · Cited by 17

Brain cathepsin B but not metalloendopeptidases degrade rAPP751 with production of amyloidogenic fragments

Marks, N., Berg, M. J., Sapirstein, V. S., Durrie, R., Swistok, J., MAKOFSKE, R. C., & Danho, W. (1995) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1995.tb00602.x · Cited by 17

Editor's note for debate Sporadic dementia of Alzheimer type: Role of amyloid in etiology is challenged

Hoyer, S. (1993) · Journal of Neural Transmission - Parkinsons Disease and Dementia Section · doi:10.1007/bf02260918 · Cited by 17

The Amyloid β Protein

Lazo, N. D., Maji, S. K., Fradinger, E. A., Bitan, G., & Teplow, D. B. (2005) · Wiley eBooks · doi:10.1002/9783527619344.ch17 · Cited by 18

In Vivo Sub-chronic Treatment with Dichlorvos in Young Rats Promotes Synaptic Plasticity and Learning by a Mechanism that Involves Acylpeptide Hydrolase Instead of Acetylcholinesterase Inhibition. Correlation with Endogenous β-Amyloid Levels

García‐Rojo, G., Gámiz, F., Ampuero, E., Rojas-Espina, D., Sandoval, R., Rozas, C., Morales, B., Wyneken, Ú., & Pancetti, F. C. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00483 · Cited by 16

O-GlcNAcylation of Amyloid-β Protein Precursor by Insulin Signaling Reduces Amyloid-β Production

Kwon, O.-H., Cho, Y. Y., Kim, T., & Chung, S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190060 · Cited by 16

Isoform Specific Amyloid-β Protein Precursor Metabolism

Henriques, A. G., Vieira, S. I., Rebelo, S., Domingues, S. C., Silva, E. F. D. C. E., & Silva, O. A. B. D. C. E. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11112 · Cited by 16

Visualization of β-secretase cleavage in living cells using a genetically encoded surface-displayed FRET probe

Lu, J., Zhang, Z., Yang, J., Chu, J., Li, P., Zeng, S., & Luo, Q. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.07.145 · Cited by 16

Transient reduction of spontaneous neuronal network activity by sublethal amyloid β (1–42) peptide concentrations

Görtz, P., Opatz, J., Siebler, M., Funke, S. A., Willbold, D., & Lange‐Asschenfeldt, C. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0188-y · Cited by 16

Chronic psychosocial stress exposes Alzheimer s disease phenotype in a novel at-risk model

Karim, A. A. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/371 · Cited by 18

Fe–oxy adducts of heme–Aβ and heme–hIAPP complexes: intermediates in ROS generation

Seal, M., Mukherjee, S., & Dey, S. G. (2016) · Metallomics · doi:10.1039/c6mt00214e · Cited by 16

The APP and PS1/2 Mutations Linked to Early Onset Familial Alzheimer’s Disease Increase the Extracellular Concentration of Aβ1–42(43)

Younkin, S. G. (1998) · Springer eBooks · doi:10.1007/978-3-642-72103-8_4 · Cited by 16

The βA4 Amyloid Protein Precursor in Human Circulationa

Bush, A. I., Beyreuther, K. T., & Masters, C. L. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb23048.x · Cited by 16

A capillary electrophoresis method for evaluation of Aβ proteolysis in vitro

Alper, B. J., & Schmidt, W. K. (2008) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2008.11.010 · Cited by 16

Amyloid β protein in rat soleus muscle in chloroquine-induced myopathy using end-specific antibodies for Aβ40 and Aβ42: immunohistochemical evidence for amyloid β protein

Tsuzuki, K., Fukatsu, R., Takamaru, Y., Yoshida, T., Hayashi, Y., Yamaguchi, H., Fujii, N., & Takahata, N. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)12205-2 · Cited by 16

Serum ?1-antitrypsin and ?2-macroglobulin in Alzheimer's and Binswanger's disease

Wetterling, T., & Tegtmeyer, K. F. (1994) · Journal of Molecular Medicine · doi:10.1007/bf00189310 · Cited by 16

A novel serine proteinase-like sequence from human brain

Dihanich, M., & Spiess, M. (1994) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(94)90018-3 · Cited by 16

Major Issues in Geriatrics over the Last Five Years

Morley, J. E., & Solomon, D. H. (1994) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.1994.tb04957.x · Cited by 16

New Insights into Alzheimer’s Disease: Novel Pathogenesis, Drug Target and Delivery

Chen, H., Xu, J., Xu, H., Luo, T., Li, Y., Jiang, K., Shentu, Y., & Tong, Z. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15041133 · Cited by 15

Secondary Structure Assignment of Amyloid-β Peptide Using Chemical Shifts

Wood, G. P. F., & Röthlisberger, U. (2011) · Journal of Chemical Theory and Computation · doi:10.1021/ct200156e · Cited by 15

Inhibitory Effect of Piperlonguminine/Dihydropiperlonguminine on the Production of Amyloid β and APP in SK-N-SH Cells

Qi, H.-S. (2009) · The Chinese Journal of Physiology · doi:10.4077/cjp.2009.amh062 · Cited by 17

Acceleration of amyloidogenesis and memory impairment by estrogen deficiency through NF-κB dependent beta-secretase activation in presenilin 2 mutant mice

Hwang, C. J., Park, M. H., Choi, M. K., Choi, J. S., Oh, K. W., Hwang, D. Y., Han, S., & Hong, J. T. (2015) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2015.11.013 · Cited by 15

Microtubule-Tau Interaction as a Therapeutic Target for Alzheimer’s Disease

Ivashko‐Pachima, Y., Zhou, L.-Y., Lei, P., & Gozes, I. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0715-x · Cited by 15

Alpha-linolenic acid regulates amyloid precursor protein processing by mitogen-activated protein kinase pathway and neuronal apoptosis in amyloid beta-induced SH-SY5Y neuronal cells

Lee, A. Y., Lee, M.-H., Lee, S., & Cho, E. J. (2017) · Applied Biological Chemistry · doi:10.1007/s13765-017-0334-4 · Cited by 15

Glutamate Receptors in Aging and Alzheimer's Disease

Mishizen-Eberz, A. J., Ikonomović, M. D., & Armstrong, D. M. (2001) · Elsevier eBooks · doi:10.1016/b978-012351830-9/50022-6 · Cited by 18

Aβ Upregulates and Colocalizes with LGI3 in Cultured Rat Astrocytes

Kimura, N., Ishii, Y., Suzaki, S., Negishi, T., Kyuwa, S., & Yoshikawa, Y. (2007) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-006-9127-8 · Cited by 16

Modulation of amyloid β protein precursor processing as a means of retarding progression of Alzheimer’s disease

Wagner, S. L., & Muñoz, B. (1999) · Journal of Clinical Investigation · doi:10.1172/jci8729 · Cited by 15

Expression of β-amyloid precursor protein in the developing human spinal cord

Arai, H., Higuchi, S., Matsushita, S., Yuzuriha, T., Trojanowski, J. Q., & Lee, V. M. ‐. (1994) · Brain Research · doi:10.1016/0006-8993(94)90914-8 · Cited by 15

Effect of ionophores on the processing of theβ-amyloid precursor protein in different cell lines

Lahiri, D. K. (1994) · Cellular and Molecular Neurobiology · doi:10.1007/bf02088713 · Cited by 15

Apolipoprotein E, Aβ‐Amyloid, and the Molecular Pathology of Alzheimer's Disease Therapeutic Implicationsa

KAPLITT, M., GOURAS, G. K., MAKIMURA, H., JOVANOVIC, J., SWEENEY, D., GREENGARD, P., RELKIN, N. R., & GANDY, S. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb32597.x · Cited by 12

A new brain metalloendopeptidase which degrades the Alzheimer ß-amyloid 1-40 peptide producing soluble fragments without neurotoxic effects

Carvalho, K. M., França, M. S. F., Camarão, G. C., & Ruchon, A. F. (1997) · Brazilian Journal of Medical and Biological Research · doi:10.1590/s0100-879x1997001000002 · Cited by 11

Untitled work

Cole (2000) · doi:10.1002/1097-0029(20000815)50:4

Untitled work

Ard (1996) · doi:10.1002/(sici)1097-4547(19960115)43:2

Untitled work

(1999) · doi:10.1002/1531-8249(199904)45:4

Production of Amyloid β Protein from Normal Amyloid β‐Protein Precursor (βAPP) and the Mutated βAPPS Linked to Familial Alzheimer's Diseasea

Golde, T. E., Cai, X.-D., Shoji, M., & Younkin, S. G. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb23036.x · Cited by 35

Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor

Cai, X.-D., Golde, T. E., & Younkin, S. G. (1993) · Science · doi:10.1126/science.8424174 · Cited by 913

Normal Cellular Processing of the β‐Amyloid Precursor Protein Results in the Secretion of the Amyloid β Peptide and Related Moleculesa

Haass, C., Hung, A. Y., Schlossmacher, M. G., Oltersdorf, T., Teplow, D. B., & Selkoe, D. J. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb23037.x · Cited by 123

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

Production of the Alzheimer's β‐amyloid peptide by C6 glioma cells

Morato, E., & Mayor, F. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80819-g · Cited by 10