Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor

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 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

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484

Alzheimer's Disease: Genes, Proteins, and Therapy

Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063

The molecular pathology of Alzheimer's disease

Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708

Amyloid deposition as the central event in the aetiology of Alzheimer’s disease

Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538

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

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

Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757

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

Alzheimer's disease: Targeting the Cholinergic System

H. Ferreira-Vieira, T., M. Guimaraes, I., R. Silva, F., & M. Ribeiro, F. (2016) · Current Neuropharmacology · doi:10.2174/1570159x13666150716165726 · Cited by 1,551

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

Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state

Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417

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

Trafficking and Proteolytic Processing of APP

Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075

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

Constitutive and regulated α-secretase cleavage of Alzheimer’s amyloid precursor protein by a disintegrin metalloprotease

Lammich, S., Kojro, E., Postina, R., Gilbert, S., Pfeiffer, R., Jasionowski, M., Haass, C., & Fahrenholz, F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3922 · Cited by 975

Arrest of -Amyloid Fibril Formation by a Pentapeptide Ligand

Tjernberg, L. O., Näslund, J., Lindqvist, F., Johansson, J., Karlström, A. R., Thyberg, J., Terenius, L., & Nordstedt, C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8545 · Cited by 963

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

Release of Alzheimer Amyloid Precursor Derivatives Stimulated by Activation of Muscarinic Acetylcholine Receptors

Nitsch, R. M., Slack, B. E., Wurtman, R. J., & Growdon, J. H. (1992) · Science · doi:10.1126/science.1411529 · Cited by 898

The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease

Selkoe, D. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01363-4 · Cited by 862

Evidence that production and release of amyloid beta-protein involves the endocytic pathway

Koo, E. H., & Squazzo, S. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32449-3 · Cited by 829

Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10

Kojro, E., Gimpl, G., Lammich, S., März, W., & Fahrenholz, F. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081612998 · Cited by 804

Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease.

Roher, A. E., Lowenson, J. D., Clarke, S., Wolkow, C., Wang, R., Cotter, R. J., Reardon, I. M., Zürcher-Neely, H. A., Heinrikson, R. L., & Ball, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53661-9 · Cited by 799

Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide

Haass, C., & Selkoe, D. J. (1993) · Cell · doi:10.1016/0092-8674(93)90312-e · Cited by 686

Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein

Mattson, M. P., Cheng, B., Culwell, A. R., Esch, F. S., Lieberburg, I., & Rydel, R. E. (1993) · Neuron · doi:10.1016/0896-6273(93)90315-i · Cited by 656

A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model

Postina, R., Schroeder, A., Dewachter, I., Bohl, J., Schmitt, U., Kojro, E., Prinzen, C., Endres, K., Hiemke, C., Blessing, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20864 · Cited by 638

Nose-to-brain drug delivery: An update on clinical challenges and progress towards approval of anti-Alzheimer drugs

Agrawal, M., Saraf, S., Saraf, S., Antimisiaris, S. G., Chougule, M. B., Shoyele, S. A., & Alexander, A. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.05.011 · Cited by 630

ADAM10 is the physiologically relevant, constitutive α‐secretase of the amyloid precursor protein in primary neurons

Kuhn, P., Wang, H., Dislich, B., Colombo, A., Zeitschel, U., Ellwart, J. W., Kremmer, E., Roßner, S., & Lichtenthaler, S. F. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.167 · Cited by 621

Brain-Derived Neurotrophic Factor in Alzheimer’s Disease and Its Pharmaceutical Potential

Gao, L., Zhang, Y., Sterling, K., & Song, W. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00279-0 · Cited by 606

The Swedish mutation causes early-onset Alzheimer's disease by β-secretase cleavage within the secretory pathway

Haass, C., Lemere, C. A., Capell, A., Citron, M., Seubert, P., Schenk, D., Lannfelt, L., & Selkoe, D. J. (1995) · Nature Medicine · doi:10.1038/nm1295-1291 · Cited by 592

Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells.

Busciglio, J., Gabuzda, D. H., Matsudaira, P., & Yankner, B. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.2092 · Cited by 569

Untitled work

(1997) · doi:10.1073/pnas.94.4.1550 · Cited by 535

γ-Secretase, notch, Aβ and alzheimer's disease: Where do the presenilins fit in?

Sisodia, S. S., & St George-Hyslop, P. H. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn785 · Cited by 512

A Portrait of Alzheimer Secretases--New Features and Familiar Faces

Esler, W. P., & Wolfe, M. S. (2001) · Science · doi:10.1126/science.1064638 · Cited by 493

Interleukin‐6 and α‐2‐macroglobulin indicate an acute‐phase state in Alzheimer's disease cortices

Bauer, J., Strauss, S., Schreiter-Gasser, U., Ganter, U., Schlegel, P., Witt, I., Yolk, B., & Berger, M. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80737-n · Cited by 483

Progress in studies of huperzine A, a natural cholinesterase inhibitor from Chinese herbal medicine1

WANG, R., YAN, H., & TANG, X.-C. (2006) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2006.00255.x · Cited by 470

Relative Abundance of Alzheimer A Beta Amyloid Peptide Variants in Alzheimer Disease and normal Aging

Näslund, J., Schierhorn, A., Hellman, U., Lannfelt, L., Roses, A. D., Tjernberg, L. O., Silberring, J., Gandy, S. E., Winblad, B., & Greengard, P. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8378 · Cited by 468

A Hundred Years of Alzheimer's Disease Research

Hardy, J. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.016 · Cited by 467

The physiological roles of tau and Aβ: implications for Alzheimer’s disease pathology and therapeutics

Kent, S. A., Spires-Jones, T. L., & Durrant, C. S. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02196-w · Cited by 446

ALZHEIMER'S DISEASE: Genetic Studies and Transgenic Models

Price, D. L., Tanzi, R. E., Borchelt, D. R., & Sisodia, S. S. (1998) · Annual Review of Genetics · doi:10.1146/annurev.genet.32.1.461 · Cited by 406

LDL receptor-related protein, a multifunctional ApoE receptor, binds secreted β-amyloid precursor protein and mediates its degradation

Kounnas, M. Z., Moir, R. D., Rebeck, G. W., Bush, A. I., Argraves, W. S., Tanzi, R. E., Hyman, B. T., & Strickland, D. K. (1995) · Cell · doi:10.1016/0092-8674(95)90320-8 · Cited by 401

Lipopolysaccharide-induced-neuroinflammation increases intracellular accumulation of amyloid precursor protein and amyloid β peptide in APPswe transgenic mice

Sheng, J. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00069-x · Cited by 388

Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative

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

Excessive production of amyloid beta-protein by peripheral cells of symptomatic and presymptomatic patients carrying the Swedish familial Alzheimer disease mutation.

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

Cholesterol Modulates α-Secretase Cleavage of Amyloid Precursor Protein

Bodovitz, S., & Klein, W. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4436 · Cited by 359

BACE2, a β-secretase homolog, cleaves at the β site and within the amyloid-β region of the amyloid-β precursor protein

Farzan, M., Schnitzler, C. E., Vasilieva, N., Leung, D., & Choe, H. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160115697 · Cited by 357

Mass spectrometric characterization of brain amyloid beta isoform signatures in familial and sporadic Alzheimer’s disease

Portelius, E., Bogdanovic, N., Gustavsson, M. K., Volkmann, I., Brinkmalm, G., Zetterberg, H., Winblad, B., & Blennow, K. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0690-1 · Cited by 348

Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-β peptide (1–40).

Backstrom, J. R., Lim, G. P., Cullen, M. J., & Tökés, Z. A. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-24-07910.1996 · Cited by 331

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

Recognition of the amyloid precursor protein by human γ-secretase

Zhou, R., Yang, G., Guo, X., Zhou, Q., Lei, J., & Shi, Y. (2019) · Science · doi:10.1126/science.aaw0930 · Cited by 304

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

The cerebrospinal-fluid soluble form of Alzheimer's amyloid β is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex

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

Amino-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

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

Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer’s disease.

Zhang, Z., Song, M., Liu, X., Su Kang, S., Duong, D. M., Seyfried, N. T., Cao, X., Cheng, L., Sun, Y. E., Ping Yu, S., et al. (2015) · Nature Communications · doi:10.1038/ncomms9762 · Cited by 277

Release of amyloid beta-protein precursor derivatives by electrical depolarization of rat hippocampal slices

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

Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein.

Knauer, M. F., Soreghan, B., Burdick, D., Kosmoski, J., & Glabe, C. G. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7437 · Cited by 233

Amyloid Precursor Protein (APP) and ΒZA4 Amyloid in the Etiology of Alzheimer's Disease: Precursor‐Product Relationships in the Derangement of Neuronal Function

Beyreuther, K., & Masters, C. L. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00667.x · Cited by 221

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

Implications of the serine protease HtrA1 in amyloid precursor protein processing

Grau, S., Baldi, A., Bussani, R., Tian, X., Stefanescu, R., Przybylski, M., Richards, P., Jones, S. A., Shridhar, V., Clausen, T., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501823102 · Cited by 215

Secreted APP regulates the function of full-length APP in neurite outgrowth through interaction with integrin beta1

Young-Pearse, T. L., Chen, A. C., Chang, R., Marquez, C., & Selkoe, D. J. (2008) · Neural Development · doi:10.1186/1749-8104-3-15 · Cited by 210

Regulated intramembrane proteolysis - lessons from amyloid precursor protein processing: Regulated intramembrane proteolysis and APP processing

Lichtenthaler, S. F., Haass, C., & Steiner, H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07248.x · Cited by 205

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

Maturation and Pro-peptide Cleavage of β-Secretase

Capell, A., Steiner, H., Willem, M., Kaiser, H., Meyer, C., Walter, J., Lammich, S., Multhaup, G., & Haass, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003202200 · Cited by 205

Role of microglia in senile plaque formation

Mackenzie, I. R. A., Hao, C., & Munoz, D. G. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00092-s · Cited by 183

A β 42 and A β 40: similarities and differences

Qiu, T., Liu, Q., Chen, Y., Zhao, Y., & Li, Y. (2015) · Journal of Peptide Science · doi:10.1002/psc.2789 · Cited by 180

β-Secretase Processing in the Trans-Golgi Network Preferentially Generates Truncated Amyloid Species That Accumulate in Alzheimer’s Disease Brain

Huse, J. T., Liu, K., Pijak, D. S., Carlin, D., Lee, V. M.-Y., & Doms, R. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111141200 · Cited by 176

Neuroprotective effects of huperzine A: New therapeutic targets for neurodegenerative disease

Zhang, H. Y., & Tang, X. C. (2006) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2006.10.004 · Cited by 174

Synaptic pathology and glial responses to neuronal injury precede the formation of senile plaques and amyloid deposits in the aging cerebral cortex.

(1994) · PubMed Central · Cited by 169

Senile plaques in temporal lobe epilepsy

Mackenzie, I. R. A., & Miller, L. A. (1994) · Acta Neuropathologica · doi:10.1007/bf00294177 · Cited by 168

Calcium and Neuronal Injury in Alzheimer's Disease: Contributions of β‐Amyloid Precursor Protein Mismetabolism, Free Radicals, and Metabolic Compromisea

MATTSON, M. P. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb44401.x · Cited by 166

Amyloids and Are Generated Intracellularly in Cultured Human Neurons and Their Secretion Increases with Maturation

Turner, R. S., Suzuki, N., Chyung, A. S. C., Younkin, S. G., & Lee, V. M.-Y. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8966 · Cited by 161

Intramembrane proteolysis by presenilins

Steiner, H., & Haass, C. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043065 · Cited by 161

Enhanced Amyloidogenic Processing of the β-Amyloid Precursor Protein in Gene-targeted Mice Bearing the Swedish Familial Alzheimer's Disease Mutations and a “Humanized” Aβ Sequence

Reaume, A. G., Howland, D. S., Trusko, S. P., Savage, M. J., Lang, D. M., Greenberg, B. D., Siman, R., & Scott, R. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23380 · Cited by 150

β‐Amyloid Precursor Protein Isoforms in Various Rat Brain Regions and During Brain Development

Löffler, J., & Huber, G. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb08443.x · Cited by 150

Endo‐lysosomal and autophagic dysfunction: a driving factor in Alzheimer's disease?

Whyte, L. S., Lau, A. A., Hemsley, K. M., Hopwood, J. J., & Sargeant, T. J. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13935 · Cited by 150

Biology of Aβ Amyloid in Alzheimer's Disease

Wisniewski, T., Ghiso, J., & Frangione, B. (1997) · Neurobiology of Disease · doi:10.1006/nbdi.1997.0147 · Cited by 134

Amyloidogenic processing of the human amyloid precursor protein in primary cultures of rat hippocampal neurons.

Simons, M., de Strooper, B., Multhaup, G., Tienari, P., Dotti, C., & Beyreuther, K. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-03-00899.1996 · Cited by 131

Blood-brain barrier leakage in Alzheimer’s disease: From discovery to clinical relevance

Nehra, G., Bauer, B., & Hartz, A. M. S. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108119 · Cited by 127

Disease modifying therapy for AD?1

Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117

pH‐Dependent Binding of Synthetic β‐Amyloid Peptides to Glycosaminoglycans

Brunden, K. R., Richter‐Cook, N. J., Chaturvedi, N., & Frederickson, R. C. A. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07453.x · Cited by 117

The γ Secretase-generated Carboxyl-terminal Domain of the Amyloid Precursor Protein Induces Apoptosis via Tip60 in H4 Cells

Kinoshita, A., Whelan, C. M., Berezovska, O., & Hyman, B. T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203372200 · Cited by 109

Anti-Amyloid Therapies for Alzheimer’s Disease and the Amyloid Cascade Hypothesis

Fedele, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914499 · Cited by 102

Aged Non‐Human Primates: An Animal Model of Age‐Associated Neurodegenerative Disease

Price, D. L., Martin, L. J., Sisodia, S. S., Wagster, M. V., Koo, E. H., Walker, L. C., Koliatsos, V. E., & Cork, L. C. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00672.x · Cited by 100

Experimental brain injury induces expression of amyloid precursor protein, which may be related to neuronal loss in the hippocampus

MURAKAMI, N., YAMAKI, T., IWAMOTO, Y., SAKAKIBARA, T., KOBORI, N., FUSHIKI, S., & UEDA, S. (1998) · Journal of Neurotrauma · doi:10.1089/neu.1998.15.993 · Cited by 100

Cathepsin D is involved in the clearance of Alzheimer's β‐amyloid protein

Hamazaki, H. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)01087-3 · Cited by 92

Altered cleavage and secretion of a recombinant β–APP bearing the Swedish familial Alzheimer's disease mutation

Felsenstein, K. M., Hunihan, L. W., & Roberts, S. B. (1994) · Nature Genetics · doi:10.1038/ng0394-251 · Cited by 90

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

Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site

Schönherr, C., Bien, J., Isbert, S., Wichert, R., Prox, J., Altmeppen, H., Kumar, S., Walter, J., Lichtenthaler, S. F., Weggen, S., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0084-5 · Cited by 76

Emerging Roles of Endothelial Nitric Oxide in Preservation of Cognitive Health

Katusic, Z. S., d’Uscio, L. V., & He, T. (2023) · Stroke · doi:10.1161/strokeaha.122.041444 · Cited by 73

β-Amyloid precursor protein gene is differentially expressed in axotomized sensory and motor systems

Scott, J. N., Parhad, I. M., & Clark, A. W. (1991) · Molecular Brain Research · doi:10.1016/0169-328x(91)90090-k · Cited by 68

Intracellular Itinerary of Internalised β‐Secretase, BACE1, and Its Potential Impact on β‐Amyloid Peptide Biogenesis

Chia, P. Z. C., Toh, W. H., Sharples, R., Gasnereau, I., Hill, A. F., & Gleeson, P. A. (2013) · Traffic · doi:10.1111/tra.12088 · Cited by 67

Metabolic syndrome as a risk factor for Alzheimer's disease: Is Aβ a crucial factor in both pathologies?

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