Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system

Molecular Cloning: A Laboratory Manual

Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589

Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures.

Hsu, S. M., Raine, L., & Fanger, H. (1981) · Journal of Histochemistry & Cytochemistry · doi:10.1177/29.4.6166661 · Cited by 14,075

Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429

The Consortium to Establish a Registry for Alzheimer's Disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease

Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659

Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue

Duve, C. D., Pressman, B. C., Gianetto, R., Wattiaux, R., & Appelmans, F. (1955) · Biochemical Journal · doi:10.1042/bj0600604 · Cited by 4,176

Apolipoprotein E: Cholesterol Transport Protein with Expanding Role in Cell Biology

Mahley, R. W. (1988) · Science · doi:10.1126/science.3283935 · Cited by 4,028

Functions of Lysosomes

de Duve, C., & Wattiaux, R. (1966) · Annual Review of Physiology · doi:10.1146/annurev.ph.28.030166.002251 · Cited by 3,033

Detection of mRNAs in sea urchin embryos by in situ hybridization using asymmetric RNA probes

Cox, K. H., DeLeon, D. V., Angerer, L. M., & Angerer, R. C. (1984) · Developmental Biology · doi:10.1016/0012-1606(84)90162-3 · Cited by 1,610

The Biogenesis of Lysosomes

Kornfeld, S. A., & Mellman, I. (1989) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.05.110189.002411 · Cited by 1,593

A Gene Network Regulating Lysosomal Biogenesis and Function

Sardiello, M., Palmieri, M., di Ronza, A., Medina, D. L., Valenza, M., Gennarino, V. A., Di Malta, C., Donaudy, F., Embrione, V., Polishchuk, R. S., et al. (2009) · Science · doi:10.1126/science.1174447 · Cited by 2,543

Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study

Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588

The inflammatory response system of brain: implications for therapy of Alzheimer and other neurodegenerative diseases

MCGEER, P., & MCGEER, E. (1995) · Brain Research Reviews · doi:10.1016/0165-0173(95)00011-9 · Cited by 1,287

Mechanisms of Neuronal Degeneration in Alzheimer's Disease

Yankner, B. A. (1996) · Neuron · doi:10.1016/s0896-6273(00)80115-4 · Cited by 953

Lysosomes as a therapeutic target

Bonam, S. R., Wang, F., & Muller, S. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0036-1 · Cited by 786

Autophagy, amyloidogenesis and Alzheimer disease

Nixon, R. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.019265 · Cited by 749

The role of protein clearance mechanisms in organismal ageing and age-related diseases

Vı́lchez, D., Sáez, I., & Dillin, A. G. (2014) · Nature Communications · doi:10.1038/ncomms6659 · Cited by 710

Cathepsin D--many functions of one aspartic protease

Benes, P., Vetvicka, V., & Fusek, M. (2008) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2008.02.008 · Cited by 572

Autophagy failure in Alzheimer's disease—locating the primary defect

Nixon, R. A., & Yang, D.-S. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.021 · Cited by 595

The autophagosomal–lysosomal compartment in programmed cell death

Bursch, W. (2001) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400852 · Cited by 620

Essential Roles of Atg5 and FADD in Autophagic Cell Death

Pyo, J.-O., Jang, M.-H., Kwon, Y., Lee, H.-J., Jun, J.-I., Woo, H., Cho, D.-H., Choi, B., Lee, H., Kim, J.-H., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413934200 · Cited by 553

Autophagy and neurodegeneration: when the cleaning crew goes on strike

Martínez‐Vicente, M., & Cuervo, A. M. (2007) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70076-5 · Cited by 495

Regulation of Autophagy by Extracellular Signal-Regulated Protein Kinases During 1-Methyl-4-Phenylpyridinium-Induced Cell Death

Zhu, J.-H., Horbinski, C., Guo, F., Watkins, S. C., Uchiyama, Y., & Chu, C. T. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.060524 · Cited by 447

Amyloid precursor protein and endosomal-lysosomal dysfunction in Alzheimer's disease: inseparable partners in a multifactorial disease

Nixon, R. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700359 · Cited by 400

Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer’s disease: Neuropathologic evidence for a mechanism of increased β-amyloidogenesis

Cataldo, A. M., Barnett, J. L., Pieroni, C., & Nixon, R. A. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-16-06142.1997 · Cited by 393

Cathepsin D Deficiency Induces Lysosomal Storage with Ceroid Lipofuscin in Mouse CNS Neurons

Koike, M., Nakanishi, H., Säftig, P., Ezaki, J., Isahara, K., Ohsawa, Y., Schulz‐Schaeffer, W., Watanabe, T., Waguri, S., Kametaka, S., et al. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-18-06898.2000 · Cited by 391

Caspase-independent programmed cell death with necrotic morphology

Kitanaka, C., & Kuchino, Y. (1999) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400526 · Cited by 378

Autophagy flux in CA1 neurons of Alzheimer hippocampus: Increased induction overburdens failing lysosomes to propel neuritic dystrophy

Bordi, M., Berg, M. J., Mohan, P. S., Peterhoff, C. M., Alldred, M. J., Che, S., Ginsberg, S. D., & Nixon, R. A. (2016) · Autophagy · doi:10.1080/15548627.2016.1239003 · Cited by 353

Huntingtin localization in brains of normal and Huntington's disease patients

Sapp, E., Schwarz, C., Chase, K. O., Bhide, P. G., Young, A. B., Penney, J. B., Vonsattel, J. P., D, N. A. M., & DiFiglia, M. (1997) · Annals of Neurology · doi:10.1002/ana.410420411 · Cited by 350

The Endosomal-Lysosomal System of Neurons in Alzheimer's Disease Pathogenesis: A Review

Nixon, R. A., Cataldo, A. M., & Mathews, P. M. (2000) · Neurochemical Research · doi:10.1023/a:1007675508413 · Cited by 320

Inflammatory changes in the substantia nigra and striatum following MPTP intoxication

onkowska, A. C., Kurkowska‐Jastrzębska, I., & onkowski, A. C. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200007)48:1 · Cited by 16

A focus on the synapse for neuroprotection in Alzheimer disease and other dementias

Coleman, P., Federoff, H., & Kurlan, R. (2004) · Neurology · doi:10.1212/01.wnl.0000140626.48118.0a · Cited by 314

Autophagic and apoptotic types of programmed cell death exhibit different fates of cytoskeletal filaments

Bursch, W., Hochegger, K., Török, L., Marian, B., Ellinger, A., & Hermann, R. S. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.7.1189 · Cited by 312

Programmed Cell Death (PCD): Apoptosis, Autophagic PCD, or Others?

Bursch, W., Ellinger, A., Gerner, C., Fröhwein, U., & Schulte‐Hermann, R. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05594.x · Cited by 311

Convergence of Multiple Autophagy and Cytoplasm to Vacuole Targeting Components to a Perivacuolar Membrane Compartment Prior tode Novo Vesicle Formation

Kim, J., Huang, W.-P., Stromhaug, P. E., & Klionsky, D. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109134200 · Cited by 272

Autophagic and lysosomal defects in human tauopathies: analysis of post-mortem brain from patients with familial Alzheimer disease, corticobasal degeneration and progressive supranuclear palsy

Piras, A., Collin, L., Grüninger, F., Graff, C., & Rönnbäck, A. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0292-9 · Cited by 271

Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression

Hamano, T., Gendron, T. F., Causevic, E., Yen, S., Lin, W., Isidoro, C., DeTure, M., & Ko, L. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06084.x · Cited by 283

Autophagy regulates the processing of amino terminal huntingtin fragments

Qin, Z. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg346 · Cited by 250

Noncaspase proteases in apoptosis

Johnson, D. (2000) · Leukemia · doi:10.1038/sj.leu.2401879 · Cited by 251

Oncogenic Ras triggers cell suicide through the activation of a caspase-independent cell death program in human cancer cells

Chi, S., Kitanaka, C., Noguchi, K., Mochizuki, T., Nagashima, Y., Shirouzu, M., Fujita, H., Yoshida, M., Chen, W., Asai, A., et al. (1999) · Oncogene · doi:10.1038/sj.onc.1202538 · Cited by 248

A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration

Tyynelä, J., Sohar, I., Sleat, D. E., Gin, R. M., Donnelly, R. J., Baumann, M., Haltia, M., & Lobel, P. (2000) · The EMBO Journal · doi:10.1093/emboj/19.12.2786 · Cited by 245

Autophagic Cell Death and Its Execution by Lysosomal Cathepsins.

UCHIYAMA, Y. (2001) · Archives of Histology and Cytology · doi:10.1679/aohc.64.233 · Cited by 243

Autophagy in neurons: a review.

Larsen, K. E., & Sulzer, D. (2002) · PubMed · doi:10.14670/hh-17.897 · Cited by 245

Degradation of Soluble Amyloid β-Peptides 1–40, 1–42, and the Dutch Variant 1–40Q by Insulin Degrading Enzyme from Alzheimer Disease and Control Brains

Pérez, A., Morelli, L., Cresto, J. C., & Castaño, E. M. (2000) · Neurochemical Research · doi:10.1023/a:1007527721160 · Cited by 240

The emerging roles of vacuolar-type ATPase-dependent Lysosomal acidification in neurodegenerative diseases

Song, Q., Meng, B., Xu, H., & Mao, Z. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00196-0 · Cited by 244

Multiple interacting cell death mechanisms in the mediation of excitotoxicity and ischemic brain damage: A challenge for neuroprotection

Puyal, J., Ginet, V., & Clarke, P. G. H. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.03.002 · Cited by 224

Autophagic Stress in Neuronal Injury and Disease

Chu, C. T. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000229233.75253.be · Cited by 211

Amyloid β-protein toxicity and oxidative stress in Alzheimer's disease

Behl, C. (1997) · Cell and Tissue Research · doi:10.1007/s004410050955 · Cited by 212

Comparative proteomics of cerebrospinal fluid in neuropathologically-confirmed Alzheimer's disease and non-demented elderly subjects

Castaño, E. M., Roher, A. E., Esh, C. L., Kokjohn, T. A., & Beach, T. G. (2006) · Neurological Research · doi:10.1179/016164106x98035 · Cited by 201

Common pathobiochemical hallmarks of progranulin-associated frontotemporal lobar degeneration and neuronal ceroid lipofuscinosis

Götzl, J. K., Mori, K., Daμμe, M., Fellerer, K., Tahirović, S., Kleinberger, G., Janssens, J., van der Zee, J., Lang, C. M., Kremmer, E., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1262-6 · Cited by 196

Mitochondrial abnormalities and oxidative imbalance in Alzheimer disease

Zhu, X., Perry, G. L., Moreira, P. I., Aliev, G., Cash, A., Hirai, K., & Smith, M. A. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9207 · Cited by 195

Lysosomal Membrane Damage in Soluble Aβ-Mediated Cell Death in Alzheimer's Disease

Ditaranto, K., Tekirian, T. L., & Yang, A. J. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0364 · Cited by 192

Degradation of Alzheimer's ß-Amyloid Protein by Human and Rat Brain Peptidases: Involvement of Insulin-Degrading Enzyme

MCDERMOTT, J. R., & GIBSON, A. M. (1997) · Neurochemical Research · doi:10.1023/a:1027325304203 · Cited by 184

Targeting microglia for the treatment of Alzheimer’s Disease

Wes, P. D., Sayed, F. A., Bard, F., & Gan, L. (2016) · Glia · doi:10.1002/glia.22988 · Cited by 185

Autophagy and Neuronal Cell Death in Neurological DisordersPreprint

Nixon, R. A., & Yang, D.-S. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008839 · Cited by 183

Increased Alzheimer's disease–like pathology in the APP/ PS1ΔE9 mouse model lacking Nrf2 through modulation of autophagy

Gururaj Joshi, A., Gan, K. A., Johnson, D. A., & Johnson, J. A. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.09.004 · Cited by 180

Altered mitochondria, energy metabolism, voltage-dependent anion channel, and lipid rafts converge to exhaust neurons in Alzheimer’s disease

Ferrer, I. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9243-5 · Cited by 172

Hippocampal plasticity during the progression of Alzheimer’s disease

Mufson, E. J., Mahady, L. J., Waters, D., Counts, S., Perez, S. E., DeKosky, S. T., Ginsberg, S. D., Ikonomović, M. D., Scheff, S. W., & Binder, L. I. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.03.006 · Cited by 184

Tau Proteolysis in the Pathogenesis of Tauopathies: Neurotoxic Fragments and Novel Biomarkers

Quinn, J. P., Corbett, N. J., Kellett, K. A. B., & Hooper, N. M. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-170959 · Cited by 170

Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99)

Jiang, Y., Sato, Y., Im, E., Berg, M., Bordi, M., Darji, S., Kumar, A., Mohan, P. S., Bandyopadhyay, U., Diaz, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0578-19.2019 · Cited by 166

Sphingolipids: Critical players in Alzheimer’s disease

van Echten‐Deckert, G., & Walter, J. (2012) · Progress in Lipid Research · doi:10.1016/j.plipres.2012.07.001 · Cited by 171

The Role of Cathepsin D in the Pathogenesis of Human Neurodegenerative Disorders

Vidoni, C., Follo, C., Savino, M., Melone, M. A. B., & Isidoro, C. (2016) · Medicinal Research Reviews · doi:10.1002/med.21394 · Cited by 164

Neuronal Apoptosis and Autophagy Cross Talk in Aging PS/APP Mice, a Model of Alzheimer's Disease

Yang, D., Kumar, A. R., Stavrides, P. H., Peterson, J. N., Peterhoff, C., Pawlik, M., Levy, E., Cataldo, A. M., & Nixon, R. A. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.071176 · Cited by 164

miR128 up-regulation correlates with impaired amyloid β(1-42) degradation in monocytes from patients with sporadic Alzheimer's disease

Tiribuzi, R., Crispoltoni, L., Porcellati, S., Di Lullo, M., Florenzano, F., Pirro, M., Bagaglia, F., Kawarai, T., Zampolini, M., Orlacchio, A., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.08.003 · Cited by 162

The insulin-like growth factor-II/mannose-6-phosphate receptor: structure, distribution and function in the central nervous system

Hawkes, C. A., & Kar, S. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2003.11.002 · Cited by 159

Dysfunction of autophagy and endosomal-lysosomal pathways: Roles in pathogenesis of Down syndrome and Alzheimer’s Disease

Colacurcio, D. J., Pensalfini, A., Jiang, Y., & Nixon, R. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.10.001 · Cited by 167

Biological and Clinical Significance of Cathepsin D in Breast Cancer Metastasis

Garcia, M., Platet, N., Liaudet‐Coopman, E., Laurent, V., Derocq, D., Brouillet, J., & Rochefort, H. (1996) · Stem Cells · doi:10.1002/stem.140642 · Cited by 158

Presenilin Mutations in Familial Alzheimer Disease and Transgenic Mouse Models Accelerate Neuronal Lysosomal Pathology

Cataldo, A. M., Peterhoff, C. M., Schmidt, S. D., Terio, N. B., Duff, K., Beard, M. E., Mathews, P. M., & Nixon, R. A. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.8.821 · Cited by 157

Lysosomal Activation Is a Compensatory Response Against Protein Accumulation and Associated Synaptopathogenesis—An Approach for Slowing Alzheimer Disease?

Bendiske, J., & Bahr, B. A. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.5.451 · Cited by 156

Role of mitochondrial homeostasis and dynamics in Alzheimer's disease

Selfridge, J. E., E, L., Lu, J., & Swerdlow, R. H. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.057 · Cited by 175

Oxidative Stress and Autophagy in the Regulation of Lysosome-Dependent Neuron Death

Pivtoraiko, V. N., Stone, S. L., Roth, K. A., & Shacka, J. J. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2263 · Cited by 154

Regulation of a novel pathway for cell death by lysosomal aspartic and cysteine proteinases

Isahara, K., Ohsawa, Y., Kanamori, S., Shibata, M., Waguri, S., Sato, N., Gotow, T., Watanabe, T., Momoi, T., Urase, K., et al. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00566-1 · Cited by 149

Lysosomal Dysfunction Promotes Cleavage and Neurotoxicity of Tau In Vivo

Khurana, V., Elson‐Schwab, I., Fulga, T. A., Sharp, K. A., Loewen, C. A., Mulkearns-Hubert, E. E., Tyynelä, J., Scherzer, C. R., & Feany, M. Β. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001026 · Cited by 152

Loss of Cathepsin B and L Leads to Lysosomal Dysfunction, NPC-Like Cholesterol Sequestration and Accumulation of the Key Alzheimer's Proteins

Čermak, S., Košiček, M., Mladenović, A., Smiljanić, K., Kanazir, S., & Hecimovic, S. K. (2016) · PLoS ONE · doi:10.1371/journal.pone.0167428 · Cited by 145

Binding of cystatin C to Alzheimer’s amyloid β inhibits in vitro amyloid fibril formation

Sastre, M., Calero, M., Pawlik, M., Mathews, P. M., Kumar, A. R., Danilov, V., Schmidt, S. D., Nixon, R. A., Frangione, B., & Levy, E. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.11.006 · Cited by 148

Autophagocytosis of Mitochondria Is Prominent in Alzheimer Disease

Moreira, P. I., Siedlak, S. L., Wang, X., Santos, M. S., Oliveira, C. R., Tabaton, M., Nunomura, A., Szweda, L. I., Aliev, G. M., Smith, M. A., et al. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000240476.73532.b0 · Cited by 145

Pathophysiology of neuropathic lysosomal storage disorders

Bellettato, C. M., & Scarpa, M. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9075-9 · Cited by 141

Autophagic dysfunction in Alzheimer’s disease: Cellular and molecular mechanistic approaches to halt Alzheimer’s pathogenesis

Uddin, M. S., Mamun, A. A., Labu, Z. K., Hidalgo‐Lanussa, O., Barreto, G. E., & Ashraf, G. M. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27588 · Cited by 141

Diffuse Plaques Contain C-terminal Aβ42and not Aβ40: Evidence From Cats and Dogs

Cummings, B. J., Satou, T., Head, E., Milgram, N. W., Cole, G. M., Savage, M. J., Podlisny, M. B., Selkoe, D. J., Siman, R. G., Greenberg, B., et al. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(96)00062-0 · Cited by 140

The endosomal-lysosomal pathway is dysregulated by APOE4 expression in vivo

Nuriel, T., Peng, K. Y., Ashok, A., Dillman, A. A., Figueroa, H. Y., Apuzzo, J., Ambat, J., Levy, E., Cookson, M. R., Mathews, P. M., et al. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00702 · Cited by 140

Cell “Self‐Eating” (Autophagy) Mechanism in Alzheimer's Disease

Funderburk, S. F., Marcellino, B. K., & Yue, Z. (2010) · Mount Sinai Journal of Medicine: A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20161 · Cited by 139

Gene Expression Profiles of Cholinergic Nucleus Basalis Neurons in Alzheimer's Disease

Mufson, E. J., Counts, S., & Ginsberg, S. D. (2002) · Neurochemical Research · doi:10.1023/a:1020952704398 · Cited by 138

Evidence for Mitochondrial UPR Gene Activation in Familial and Sporadic Alzheimer's Disease

Beck, J. S., Mufson, E. J., & Counts, S. (2016) · Current Alzheimer Research · doi:10.2174/1567205013666151221145445 · Cited by 139

The endosomal-lysosomal system of neurons: new roles

Nixon, R. A., & Cataldo, A. M. (1995) · Trends in Neurosciences · doi:10.1016/0166-2236(95)92772-i · Cited by 136

The autophagy-lysosomal degradation pathway: role in neurodegenerative disease and therapy

John, J. S. (2007) · Frontiers in bioscience · doi:10.2741/2714 · Cited by 135

Pre‐synaptic C‐terminal truncated tau is released from cortical synapses in Alzheimer's disease

Sokolow, S., Henkins, K. M., Bilousova, T., Gonzalez, B., Vinters, H. V., Miller, C. A., Cornwell, L., Poon, W. W., & Gylys, K. H. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.12991 · Cited by 133

The endocytic pathway in microglia during health, aging and Alzheimer’s disease

Solé-Domènech, S., Cruz, D. L., Capetillo-Zarate, E., & Maxfield, F. R. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.07.002 · Cited by 133

Impairment of proteostasis network in Down syndrome prior to the development of Alzheimer's disease neuropathology: Redox proteomics analysis of human brain

Domenico, F. D., Coccia, R., Cocciolo, A., Murphy, M. P., Cenini, G., Head, E., Butterfield, D. A., Giorgi, A., Schininà, M. E., Mancuso, C., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.013 · Cited by 132

Cystatin C in Alzheimer's disease

Kaur, G., & Levy, E. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00079 · Cited by 116

Ionic effects of the Alzheimer's disease β-amyloid precursor protein and its metabolic fragments

Fraser, S. P., Suh, Y.-H., & Djamgoz, M. B. A. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)10079-5 · Cited by 127

Aging, lipofuscin formation, and free radical-mediated inhibition of cellular proteolytic systems

Szweda, P. A., Camouse, M. M., Lundberg, K. C., Oberley, T. D., & Szweda, L. I. (2003) · Ageing Research Reviews · doi:10.1016/s1568-1637(03)00028-x · Cited by 123

Co-Localization of Glia Maturation Factor with NLRP3 Inflammasome and Autophagosome Markers in Human Alzheimer’s Disease Brain

Ahmed, M. E., Iyer, S. S., Thangavel, R., Kempuraj, D., Selvakumar, G. P., Raikwar, S. P., Zaheer, S. A., & Zaheer, A. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170634 · Cited by 120

Protective mechanisms by cystatin C in neurodegenerative diseases

Levy, E. (2010) · Frontiers in Bioscience-Scholar · doi:10.2741/s170 · Cited by 122

Proteolysis, free radicals, and aging1,2 1Guest Editor: Earl Stadtman 2This article is part of a series of reviews on “Oxidatively Modified Proteins in Aging and Disease.” The full list of papers may be found on the homepage of the journal.

Szweda, P. A., Friguet, B., & Szweda, L. I. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00837-7 · Cited by 120

Participation of Cathepsins B and D in Apoptosis of PC12 Cells Following Serum Deprivation

Shibata, M., Kanamori, S., Isahara, K., Ohsawa, Y., Konishi, A., Kametaka, S., Watanabe, T., Ebisu, S., Ishido, K., Kominami, E., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9422 · Cited by 118

Defective lysosomal acidification: a new prognostic marker and therapeutic target for neurodegenerative diseases

Lo, C. H., & Zeng, J. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00362-0 · Cited by 117

Elevation of Cystatin C in Susceptible Neurons in Alzheimer's Disease

Deng, A., Irizarry, M. C., Nitsch, R. M., Growdon, J. H., & Rebeck, G. W. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61781-6 · Cited by 116

Characterization of the AD7C-NTP cDNA expression in Alzheimer's disease and measurement of a 41-kD protein in cerebrospinal fluid.

de la Monte, S. M., Ghanbari, K., Frey, W. H., Beheshti, I., Averback, P., Hauser, S. L., Ghanbari, H. A., & Wands, J. R. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119864 · Cited by 114

Autophagy–lysosomal-associated neuronal death in neurodegenerative disease

Nixon, R. A. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02799-7 · Cited by 126

Gene expression changes presage neurodegeneration in a Drosophila model of Parkinson's disease

Scherzer, C. R., Jensen, R. V., Gullans, S. R., & Feany, M. Β. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg265 · Cited by 113

Up-regulation of the lysosomal system in experimental models of neuronal injury: implications for Alzheimer's disease.

Adamec, E., Mohan, P., Cataldo, A., Srinivasan, A. N., Vonsattel, J., & Nixon, R. (2000) · Neuroscience · doi:10.1016/s0306-4522(00)00281-5 · Cited by 116

Upregulation of the Endosomal-Lysosomal Pathway in the Trembler-J Neuropathy

Notterpek, L. M., Shooter, E. M., & Snipes, G. J. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-11-04190.1997 · Cited by 112

Synaptic Amyloid-β Oligomers Precede p-Tau and Differentiate High Pathology Control Cases

Bilousova, T., Miller, C. A., Poon, W. W., Vinters, H. V., Corrada, M., Kawas, C., Hayden, E. Y., Teplow, D. B., Glabe, C., Albay, R., et al. (2016) · The American Journal of Pathology · doi:10.1016/j.ajpath.2015.09.018 · Cited by 115

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

Uptake and pathogenic effects of amyloid beta peptide 1–42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists

Bi, X., Gall, C. M., Zhou, J., & Lynch, G. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00132-x · Cited by 92

Reconsider Alzheimer's disease by the ‘calpain–cathepsin hypothesis’—A perspective review

Yamashima, T. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.02.004 · Cited by 109

Interneuronal Transfer of Human Tau Between Lamprey Central Neurons in situ

Kim, W., Lee, S., Jung, C., Ahmed, A., Lee, G. S., & Hall, G. F. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1273 · Cited by 107

Protein Homeostasis, Aging and Alzheimer’s Disease

Morawe, T., Hiebel, C., Kern, A., & Behl, C. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8246-0 · Cited by 105

Degradative organelles containing mislocalized α- and β-synuclein proliferate in presenilin-1 null neurons

Wilson, C., Murphy, D. D., Giasson, B. I., Zhang, B., Trojanowski, J. Q., & Lee, V. M. ‐. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403061 · Cited by 108

Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity

Ando, K., Maruko-Otake, A., Ohtake, Y., Hayashishita, M., Sekiya, M., & Iijima, K. M. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1005917 · Cited by 105

Lysosomal cathepsin D is upregulated in Alzheimer's disease neocortex and may be a marker for neurofibrillary degeneration

Chai, Y. L., Chong, J. R., Weng, J., Howlett, D., Halsey, A., Lee, J. H., Attems, J., Aarsland, D., Francis, P. T., Chen, C. P., et al. (2019) · Brain Pathology · doi:10.1111/bpa.12631 · Cited by 73

Abnormal distribution of cathepsins in the brain of patients with Alzheimer's disease

Nakamura, Y., Takeda, M., Suzuki, H., Hattori, H., Tada, K., Hariguchi, S., Hashimoto, S., & Nishimura, T. (1991) · Neuroscience Letters · doi:10.1016/0304-3940(91)90395-a · Cited by 111

Properties of the endosomal-lysosomal system in the human central nervous system: disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease

Cataldo, A., Hamilton, D. J., Barnett, J. L., Paskevich, P. A., & Nixon, R. A. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-01-00186.1996 · Cited by 356

Up-regulation of the lysosomal system in experimental models of neuronal injury: implications for Alzheimer's disease.

Adamec, E., Mohan, P., Cataldo, A., Srinivasan, A. N., Vonsattel, J., & Nixon, R. (2000) · Neuroscience · doi:10.1016/s0306-4522(00)00281-5 · Cited by 116

Lysosomal dysfunction promotes cleavage and neurotoxicity of tau in vivo. PLoS Genet 6: e1001026

Khurana, V., Elson‐Schwab, I., Fulga, T. A., Sharp, K. A., Loewen, C. A., Mulkearns-Hubert, E. E., Tyynelä, J., Scherzer, C. R., & Feany, M. Β. (2010)