Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains.

Diagnosis of Alzheimer's Disease

Khachaturian, Z. S. (1985) · Archives of Neurology · doi:10.1001/archneur.1985.04060100083029 · Cited by 2,499

Amyloid Deposits and Amyloidosis

Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006053022305 · Cited by 1,780

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780

Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.

Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,491

Phosphorylation affects the ability of tau protein to promote microtubule assembly.

Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901

Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis.

Hershko, A., Ciechanover, A. J., Heller, H., Haas, A. L., & Rose, I. A. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.4.1783 · Cited by 769

Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)

Wood, J. G., Mirra, S. S., Pollock, N. J., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4040 · Cited by 763

Mechanisms of Intracellular Protein Breakdown

Hershko, A., & Ciechanover, A. J. (1982) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.51.070182.002003 · Cited by 650

Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85

Ciechanover, A. J., Finley, D. J., & Varshavsky, A. J. (1984) · Cell · doi:10.1016/0092-8674(84)90300-3 · Cited by 532

Amyloid Deposits and Amyloidosis

Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006123022403 · Cited by 515

The molecular pathology of Alzheimer's disease

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

beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity

Mattson, M. P., Cheng, B., Davis, D. G., Bryant, K., Lieberburg, I. M., & Rydel, R. E. (1992) · Journal of Neuroscience · doi:10.1523/jneurosci.12-02-00376.1992 · Cited by 1,633

Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134

Tau in Alzheimer Disease and Related Tauopathies

Iqbal, K., Liu, F., Gong, C., & Grundke, I. (2010) · Current Alzheimer Research · doi:10.2174/156720510793611592 · Cited by 1,163

Tau-targeting therapies for Alzheimer disease

Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113

Tau pathology in Alzheimer disease and other tauopathies

Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037

Classification and basic pathology of Alzheimer disease

Duyckaerts, C., Delatour, B., & Potier, M.-C. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0532-1 · Cited by 1,031

Degradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies

Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898

Neuropathology of Alzheimer's Disease

Perl, D. P. (2010) · Mount Sinai Journal of Medicine: A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20157 · Cited by 825

Tau and neurodegenerative disease: the story so far

Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806

Accumulation of abnormally phosphorylated τ precedes the formation of neurofibrillary tangles in Alzheimer's disease

Bancher, C., Brunner, C., Lassmann, H., Budka, H., Jellinger, K., Wiche, G., Seitelberger, F., Grundke-Iqbal, I., Iqbal, K., & Wisniewski, H. M. (1989) · Brain Research · doi:10.1016/0006-8993(89)91396-6 · Cited by 818

tau protein in cerebrospinal fluid: A biochemical marker for axonal degeneration in Alzheimer disease?

Blennow, K., Wallin, A., Ågren, H., Spenger, C., Siegfried, J., & Vanmechelen, E. (1995) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815140 · Cited by 789

Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779

Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the β–amyloid precursor protein gene

Hendriks, L., van Duijn, C. M., Cras, P. P., Cruts, M., Hul, W. V., van Harskamp, F., Warren, A., McInnis, M. G., Antonarakis, S. E., Martin, J., et al. (1992) · Nature Genetics · doi:10.1038/ng0692-218 · Cited by 741

The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis

Finley, D. J., Bartel, B., & Varshavsky, A. J. (1989) · Nature · doi:10.1038/338394a0 · Cited by 720

Tau protein and the neurofibrillary pathology of Alzheimer's disease

Goedert, M. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90078-z · Cited by 721

Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies

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) · Biomolecules · doi:10.3390/biom6010006 · Cited by 730

Post-translational modifications of tau protein: Implications for Alzheimer's disease

Martin, L., Latypova, X., & Terro, F. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2010.12.023 · Cited by 683

Mechanisms of tau-induced neurodegeneration

Iqbal, K., Liu, F., Gong, C.-X., Alonso, A. D. C., & Grundke-Iqbal, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0486-3 · Cited by 628

The Unfolded Protein Response Is Activated in Pretangle Neurons in Alzheimer's Disease Hippocampus

Hoozemans, J. J. M., van Haastert, E. S., Nijholt, D. A. T., Rozemuller, A. J. M., Eikelenboom, P., & Scheper, W. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080814 · Cited by 600

Half a century of amyloids: past, present and future

Ke, P. C., Zhou, R., Serpell, L. C., Riek, R., Knowles, T. P. J., Lashuel, H. A., Gazit, E., Hamley, I. W., Davis, T. P., Fändrich, M., et al. (2020) · Chemical Society Reviews · doi:10.1039/c9cs00199a · Cited by 577

Proline-directed and non-proline-directed phosphorylation of PHF-tau

Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Yoshida, H., Titani, K., & Ihara, Y. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.823 · Cited by 557

Abnormal Hyperphosphorylation of Tau: Sites, Regulation, and Molecular Mechanism of Neurofibrillary Degeneration

Wang, J., Xia, Y., Grundke, I., & Iqbal, K. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129031 · Cited by 547

The role of tau in neurodegeneration

Gendron, T. F., & Petrucelli, L. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-13 · Cited by 478

Cerebrospinal fluid protein biomarkers for Alzheimer’s disease

Blennow, K. (2004) · Neurotherapeutics · doi:10.1602/neurorx.1.2.213 · Cited by 500

The ubiquitin‐proteasome pathway and proteasome inhibitors

Myung, J., Kim, K. B., & Crews, C. M. (2001) · Medicinal Research Reviews · doi:10.1002/med.1009 · Cited by 453

Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease

Lowe, J., Blanchard, A., Morrell, K., Lennox, G., Reynolds, L., Billett, M., Landon, M., & Mayer, R. J. (1988) · The Journal of Pathology · doi:10.1002/path.1711550105 · Cited by 539

Alzheimer’s disease: insights into pathology, molecular mechanisms, and therapy

Zheng, Q., & Wang, X. (2024) · Protein & Cell · doi:10.1093/procel/pwae026 · Cited by 483

Heme oxygenase-1 is associated with the neurofibrillary pathology of Alzheimer's disease.

Smith, M. A., Kutty, R. K., Richey, P. L., Yan, S. D., Stern, D., Chader, G. J., Wiggert, B. O., Petersen, R. B., & Perry, G. L. (1994) · PubMed Central · Cited by 425

The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease.

Snow, A. D., Mar, H., Nochlin, D., Kimata, K., Kato, M., Suzuki, S., Hassell, J., & Wight, T. N. (1988) · PubMed Central · Cited by 418

Microtubule-associated protein tau in development, degeneration and protection of neurons

Wang, J., & Liu, F. (2008) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2008.03.002 · Cited by 405

Tau protein kinase I is essential for amyloid beta-protein-induced neurotoxicity.

Takashima, A., Noguchi, K., Sato, K., Hoshino, T., & Imahori, K. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7789 · Cited by 385

Oxidative stress, neurodegeneration, and the balance of protein degradation and protein synthesis

Dasuri, K., Zhang, L., & Keller, J. N. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.016 · Cited by 371

Phosphorylated tau interactome in the human Alzheimer's disease brain

Drummond, E., Pires, G., MacMurray, C., Askenazi, M., Nayak, S., Bourdon, M., Safar, J., Ueberheide, B., & Wisniewski, T. (2020) · Brain · doi:10.1093/brain/awaa223 · Cited by 357

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367

Tau-targeting therapies for Alzheimer disease: Current status and future directions

Congdon, E. E., Ji, C., Tetlow, A. M., Jiang, Y., & Sigurdsson, E. M. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00883-2 · Cited by 371

Ubiquitin carboxyl‐terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases

Lowe, J. S., McDermott, H., Landon, M., Mayer, R. J., & Wilkinson, K. D. (1990) · The Journal of Pathology · doi:10.1002/path.1711610210 · Cited by 359

Global changes in DNA methylation and hydroxymethylation in Alzheimer's disease human brain

Coppieters, N., Dieriks, B. V., Lill, C. L., Faull, R. L. M., Curtis, M. A., & Dragunow, M. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.11.031 · Cited by 360

Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies

Kuusisto, E., Salminen, A., & Alafuzoff, I. I. (2001) · Neuroreport · doi:10.1097/00001756-200107200-00009 · Cited by 341

Expression of β-amyloid precursor protein in reactive astrocytes following neuronal damage

Siman, R. G., Card, J. P., Nelson, R. B., & Davis, L. G. (1989) · Neuron · doi:10.1016/0896-6273(89)90252-3 · Cited by 344

HDAC6 as a target for neurodegenerative diseases: what makes it different from the other HDACs?

Simões-Pires, C., Zwick, V., Nurisso, A., Schenker, E., Carrupt, P.-A., & Cuendet, M. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-7 · Cited by 341

Causes of oxidative stress in Alzheimer disease

Zhu, X., Su, B., Wang, X., Smith, M. A., & Perry, G. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7218-4 · Cited by 336

Visualization of neurofibrillary tangle maturity in Alzheimer's disease: A clinicopathologic perspective for biomarker research

Moloney, C. M., Lowe, V. J., & Murray, M. E. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12321 · Cited by 358

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

Amyloid-Beta Protein Clearance and Degradation (ABCD) Pathways and their Role in Alzheimer’s Disease

Baranello, R., Bharani, K., Padmaraju, V., Chopra, N., Lahiri, D., Greig, N., Pappolla, M., & Sambamurti, K. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666141218140953 · Cited by 331

Evidence of oxidative stress and in vivo neurotoxicity of beta-amyloid in a transgenic mouse model of Alzheimer's disease: a chronic oxidative paradigm for testing antioxidant therapies in vivo.

Pappolla, M. A., Chyan, Y., Omar, R. A., Hsiao, K., Perry, G. L., Smith, M. A., & Bozner, P. (1998) · Europe PMC (PubMed Central) · Cited by 328

Senile plaque neurites in Alzheimer disease accumulate amyloid precursor protein.

Cras, P. P., Kawai, M., Lowery, D. E., Gonzalez‐DeWhitt, P. A., Greenberg, B., & Perry, G. L. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.17.7552 · Cited by 314

Small Ubiquitin-like Modifier (SUMO) Modification of Natively Unfolded Proteins Tau and α-Synuclein

Dorval, V., & Fraser, P. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510127200 · Cited by 319

Dysregulation of Ubiquitin-Proteasome System in Neurodegenerative Diseases

Zheng, Q., Huang, T. Y., Zhang, L., Zhou, Y., Luo, H., Xu, H., & Wang, X. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00303 · Cited by 327

Is oxidative damage the fundamental pathogenic mechanism of Alzheimer’s and other neurodegenerative diseases?

Perry, G. L., Nunomura, A., Hirai, K., Zhu, X., Prez, M. D. F., Ávila, J., Castellani, R. J., Atwood, C., Aliev, G., Sayre, L. M., et al. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01113-9 · Cited by 297

Polyglutamine protein aggregates are dynamic

Kim, S., Nollen, E. A. A., Kitagawa, K., Bindokas, V. P., & Morimoto, R. I. (2002) · Nature Cell Biology · doi:10.1038/ncb863 · Cited by 296

Antigenic changes similar to those seen in neurofibrillary tangles are elicited by glutamate and Ca2+ influx in cultured hippocampal neurons.

Mattson, M. (1990) · Neuron · doi:10.1016/0896-6273(90)90447-n · Cited by 292

Ubiquitin deposits in anterior horn cells in motor neurone disease

Leigh, P. N., Anderton, B. H., Dodson, A. R., Gallo, J., Swash, M., & Power, D. M. (1988) · Neuroscience Letters · doi:10.1016/0304-3940(88)90081-x · Cited by 279

Tau Accumulation Activates the Unfolded Protein Response by Impairing Endoplasmic Reticulum-Associated Degradation

Abisambra, J. F., Jinwal, U. K., Blair, L. J., O’Leary, J. C., Li, Q., Brady, S., Wang, L., Guidi, C., Zhang, B., Nordhues, B. A., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5397-12.2013 · Cited by 275

The ubiquitin‐proteasome system in Alzheimer's disease

Oddo, S. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00276.x · Cited by 267

Tau-aggregation inhibitor therapy for Alzheimer's disease

Wischik, C. M., Harrington, C. R., & Storey, J. M. D. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.008 · Cited by 279

Alzheimer Disease, a Multifactorial Disorder Seeking Multi-therapies

Iqbal, K., & Grundke-Iqbal, I. (2010) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2010.04.006 · Cited by 231

Calcium as sculptor and destroyer of neural circuitry

Mattson, M. P. (1992) · Experimental Gerontology · doi:10.1016/0531-5565(92)90027-w · Cited by 250

Age-related macular degeneration (AMD): Alzheimer's disease in the eye?

Kaarniranta, K., Salminen, A., Haapasalo, A., Soininen, H., & Hiltunen, M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101908 · Cited by 248

Early accumulation of heparan sulfate in neurons and in the beta-amyloid protein containing lesions of Alzheimer's disease and Down's syndrome

Snow, A. D. (1990) · Neurobiology of Aging · doi:10.1016/0197-4580(90)90765-r · Cited by 247

Proteomic differences in amyloid plaques in rapidly progressive and sporadic Alzheimer’s disease

Drummond, E., Nayak, S., Faustin, A., Pires, G., Hickman, R. A., Askenazi, M., Cohen, M., Haldiman, T., Kim, C., Han, X., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1691-0 · Cited by 239

Alzheimer neurofibrillary degeneration: significance, etiopathogenesis, therapeutics and prevention

Iqbal, K., & Grundke, I. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00225.x · Cited by 243

An integrated bioinformatics platform for investigating the human E3 ubiquitin ligase-substrate interaction network

Li, Y., Xie, P., Lu, L., Wang, J., Diao, L., Liu, Z., Guo, F., He, Y., Liu, Y., Huang, Q., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00299-9 · Cited by 234

SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination

Luo, H.-B., Xia, Y.-Y., Shu, X.-J., Liu, Z.-C., Feng, Y., Liu, X.-H., Yu, G., Yin, G., Xiong, Y.-S., Zeng, K., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417548111 · Cited by 236

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

cAMP-induced phosphorylation of 26S proteasomes on Rpn6/PSMD11 enhances their activity and the degradation of misfolded proteins

Lokireddy, S., Kukushkin, N. V., & Goldberg, A. L. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522332112 · Cited by 228

A filamentous inclusion body within anterior horn neurones in motor neurone disease defined by immunocytochemical localisation of ubiquitin

Lowe, J. S., Lennox, G. G., Jefferson, D., Morrell, K., McQuire, D., Gray, T. B., Landon, M., DOHERTY, F. J., & Mayer, R. J. (1988) · Neuroscience Letters · doi:10.1016/0304-3940(88)90296-0 · Cited by 227

Spectrum of morphological appearance of amyloid deposits in Alzheimer's disease

Wisniewski, H. M., Bancher, C., Barcikowska, M., Wen, G. Y., & Currie, J. (1989) · Acta Neuropathologica · doi:10.1007/bf00688170 · Cited by 220

Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation

Kuusisto, E., Salminen, A., & Alafuzoff, I. I. (2002) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2002.00394.x · Cited by 213

Isoaspartate Formation and Neurodegeneration in Alzheimer's Disease

Shimizu, T., Watanabe, A., OGAWARA, M., Mori, H., & Shirasawa, T. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1955 · Cited by 217

β-Amyloid and the Pathogenesis of Alzheimer's Disease

Flier, J. S., Underhill, L. H., Yankner, B. A., & Mesulam, M. M. (1991) · New England Journal of Medicine · doi:10.1056/nejm199112263252605 · Cited by 208

Identification of Ubiquilin, a Novel Presenilin Interactor That Increases Presenilin Protein Accumulation

Mah, A. L., Perry, G. L., Smith, M. A., & Monteiro, M. J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.4.847 · Cited by 203

Alzheimer Disease

Smith, M. A. (1998) · International review of neurobiology · doi:10.1016/s0074-7742(08)60607-8 · Cited by 206

Ubiquitin is associated with abnormal cytoplasmic filaments characteristic of neurodegenerative diseases.

Manetto, V., Perry, G. L., Tabaton, M., Mulvihill, P., Fried, V. A., Smith, H. T., Gambetti, P., & AUTILIO‐GAMBETTI, L. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4501 · Cited by 200

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

Neurofibrillary Tangles and Alzheimer’s Disease

Brion, J. (1998) · European Neurology · doi:10.1159/000007969 · Cited by 208

Tau protein, the paired helical filament and Alzheimer's disease

Goedert, M., Klug, A., & Crowther, R. A. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s323 · Cited by 205

Microarray analysis of the astrocyte transcriptome in the aging brain: relationship to Alzheimer’s pathology and APOE genotype

Simpson, J. E., Ince, P. G., Shaw, P. J., Heath, P. R., Raman, R., Garwood, C. J., Gelsthorpe, C., Baxter, L., Forster, G., Matthews, F. E., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.04.013 · Cited by 197

Amyloid-β and τ serve antioxidant functions in the aging and Alzheimer brain

Smith, M. A., Casadesús, G., Joseph, J. A., & Perry, G. L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01021-3 · Cited by 189

Role of the ubiquitin proteasome system in Alzheimer's disease

Upadhya, S. C., & Hegde, A. N. (2007) · BMC Biochemistry · doi:10.1186/1471-2091-8-s1-s12 · Cited by 188

Abnormal phosphorylation of tau precedes ubiquitination in neurofibrillary pathology of Alzheimer disease

Bancher, C., Grundke, I., Iqbal, K., Fried, V. A., Smith, H. T., & Wisniewski, H. M. (1991) · Brain Research · doi:10.1016/0006-8993(91)90681-k · Cited by 185

Reactive Oxygen Species Mediate Cellular Damage in Alzheimer Disease

Perry, G. L., Castellani, R. J., Hirai, K., & Smith, M. A. (1998) · Journal of Alzheimer s Disease · doi:10.3233/jad-1998-1103 · Cited by 184

Diffuse Lewy body disease: correlative neuropathology using anti-ubiquitin immunocytochemistry.

Lennox, G. G., Lowe, J. S., Landon, M., Byrne, E. J., Mayer, R. J., & Godwin-Austen, R. B. (1989) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.52.11.1236 · Cited by 184

SUMO on the road to neurodegeneration

Dorval, V., & Fraser, P. E. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.03.017 · Cited by 188

Challenging the Amyloid Cascade Hypothesis: Senile Plaques and Amyloid‐β as Protective Adaptations to Alzheimer Disease

Lee, H., Casadesús, G., Zhu, X., Takeda, A., Perry, G. L., & Smith, M. A. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1297.001 · Cited by 183

Increased levels of oxidative stress markers detected in the brains of mice devoid of prion protein

Wong, B., Liu, T., Li, R., Pan, T., Petersen, R. B., Smith, M. A., Gambetti, P. L., Perry, G. L., Manson, J. C., Brown, D. R., et al. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00028.x · Cited by 174

Plasma biomarkers for mild cognitive impairment and Alzheimer's disease

Song, F., Poljak, A., Smythe, G. A., & Sachdev, P. S. (2009) · Brain Research Reviews · doi:10.1016/j.brainresrev.2009.05.003 · Cited by 181

Ubiquitin in Neurodegenerative Diseases

Lowe, J. S., Mayer, R. J., & Landon, M. (1993) · Brain Pathology · doi:10.1111/j.1750-3639.1993.tb00726.x · Cited by 170

Tau in Alzheimer neurofibrillary tangles. N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site

Brion, J., Hanger, D. P., Bruce, M. T., Couck, A. M., Flament-Durand, J., & Anderton, B. H. (1991) · Biochemical Journal · doi:10.1042/bj2730127 · Cited by 171

Essential Role of E2-25K/Hip-2 in Mediating Amyloid-β Neurotoxicity

Song, S., Kim, S., Hong, Y., Jo, D., Lee, J., Shim, S. M., Chung, C., Seo, S. J., Yoo, Y. J., Koh, J., et al. (2003) · Molecular Cell · doi:10.1016/j.molcel.2003.08.005 · Cited by 167

Degradation of tau protein by autophagy and proteasomal pathways

Wang, Y., & Mandelkow, E. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120071 · Cited by 166

Amyloidosis

Sipe, J. D., & Cohen, A. S. (1994) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408369409084679 · Cited by 166

Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae

Tobias, J. W., & Varshavsky, A. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99059-9 · Cited by 165

Subgroups of Alzheimer's disease based on cerebrospinal fluid molecular markers

Iqbal, K., Flory, M. J., Khatoon, S., Soininen, H. S., Pirttilä, T., Lehtovirta, M., Alafuzoff, I. I., Blennow, K., Andreasen, N., Vanmechelen, E., et al. (2005) · Annals of Neurology · doi:10.1002/ana.20639 · Cited by 164

Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies

Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 168

Abnormal localization of iron regulatory protein in Alzheimer’s disease

Smith, M. A., Wehr, K., Harris, P. L. R., Siedlak, S. L., Connor, J. R., & Perry, G. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00002-x · Cited by 162

Interaction of Tau Isoforms with Alzheimer's Disease Abnormally Hyperphosphorylated Tau and in VitroPhosphorylation into the Disease-like Protein

Alonso, A. D. C., Zaidi, T., Novák, M., Barra, H. S., Grundke, I., & Iqbal, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105365200 · Cited by 160

Antioxidant Therapy in Alzheimers Disease: Theory and Practice

Aliev, G., Obrenovich, M. E., Reddy, V. P., Shenk, J. C., Moreira, P. I., Nunomura, A., Zhu, X., Smith, M. A., & Perry, G. L. (2008) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/138955708786369582 · Cited by 160

Microtubular reorganization and dendritic growth response in alzheimer's disease

McKee, A. C., Kowall, N. W., & Kosik, K. S. (1989) · Annals of Neurology · doi:10.1002/ana.410260511 · Cited by 159

Relationship between amyloid-beta and the ubiquitin–proteasome system in Alzheimer’s disease

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Ubiquitin and microtubule-associated protein tau immunoreactivity each define distinct structures with differing distributions and solubility properties in Alzheimer brain.

Shaw, G., & Chau, V. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.8.2854 · Cited by 57

Ubiquitin-protein conjugates in Alzheimer's lesions

Cole, G. M., & Timiras, P. S. (1987) · Neuroscience Letters · doi:10.1016/0304-3940(87)90698-7 · Cited by 101

Ubiquitin is a component of neurofibrillary tangles in a variety of neurodegenerative diseases

Lennox, G. G., Lowe, J. S., Morrell, K., Landon, M., & Mayer, R. J. (1988) · Neuroscience Letters · doi:10.1016/0304-3940(88)90297-2 · Cited by 79

Two distinct ubiquitin immunoreactive senile plaques in Alzheimer's disease: relationship with the intellectual status in 29 cases

He, Y., Delaère, P., Duyckaerts, C. J., Wąsowicz, M., Piette, F., & Hauw, J. (1993) · Acta Neuropathologica · doi:10.1007/bf00454909 · Cited by 33

Heterogeneity of ubiquitin immunoreactivity in neurofibrillary tangles of Alzheimer's disease

Brion, J., Power, D. M., Hue, D., Couck, A. M., Anderton, B. H., & Flament-Durand, J. (1989) · Neurochemistry International · doi:10.1016/0197-0186(89)90111-3 · Cited by 20