Cited by 629Alzheimer's disease research and treatmentsUbiquitin and proteasome pathwaysDementia and Cognitive Impairment Research

The DOI matches its Crossref record; 27 of the 28 references it cites were found in a registry or an index, and 1 are not checked yet.

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

Open access

Perry, G, Friedman, R, Shaw, G, Chau, V·1987·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.84.9.3033PMC PMC304795

Open this paper in CoChat — free account

Abstract

Neurofibrillary tangles (NFT) and neurites associated with senile plaques (SP) in Alzheimer disease-affected brain tissues were specifically immunostained with affinity-purified antibody preparations directed against ubiquitin. In addition, a class of neurites seen in brain regions containing NFT and SP were also specifically stained. Cross-reactivity of the ubiquitin antisera for tau protein, neurofilament proteins, and high molecular weight microtubule-associated proteins (MAPs) were ruled out by (i) the inability of the ubiquitin antisera to stain these proteins in immunoblotting experiments and (ii) the inability of tau, neurofilament, and MAP preparations, when preincubated with the ubiquitin antisera, to inhibit the selective neurofibrillar staining observed. Our results are consistent with the suggestion that ubiquitin is covalently associated with the insoluble neurofibrillary material of NFT and SP. We propose that the ubiquitin-mediated degradative pathway may be ineffective in removing these fibrillar structures in Alzheimer disease brain.

Integrity signals

Registry

Crossref · 10.1073/pnas.84.9.3033

Cites

27 of 28 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

The text we found for this paper looks like another document, so its claims and self-check weren’t run. The registry and citation checks still apply.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The text we found for this paper looks like another document, so the self-check wasn’t run.

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

Show all 27 references

Sorted by citations

Items 101–200 of 629

Resveratrol Induces Brain Resilience Against Alzheimer Neurodegeneration Through Proteostasis Enhancement
Corpas, R., Griñán‐Ferré, C., Rodrı́guez-Farré, E., Pallàs, M., & Sanfeliu, C. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1157-y · Cited by 164
Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease
Grynspan, F., Griffin, W. R., Cataldo, A. M., Katayama, S., & Nixon, R. A. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00384-3 · Cited by 156
Protein quality control in Alzheimer's disease by the ubiquitin proteasome system
de Vrij, F. M. S., Fischer, D. F., VANLEEUWEN, F., & Hol, E. M. (2004) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2004.10.001 · Cited by 155
Single-Cell RNA Sequencing of Peripheral Blood Reveals Immune Cell Signatures in Alzheimer’s Disease
Xu, H., & Jia, J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.645666 · Cited by 149
Light and electron microscopic localization of beta-amyloid protein in muscle biopsies of patients with inclusion-body myositis.
Askanas, V., Engel, W. K., & Alvarez, R. B. (1992) · PubMed Central · Cited by 148
Advanced Maillard Reaction End Products, Free Radicals, and Protein Oxidation in Alzheimer's Diseasea
Smith, M. A., Richey, P. L., Taneda, S., Kutty, R. K., Lm, S., Monnier, V. M., & Perry, G. L. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb21836.x · Cited by 146
Self-citation
Cytoplasmic argyrophilic inclusions in neurons of pontine nuclei in patients with olivopontocerebellar atrophy: immunohistochemical and ultrastructural studies
Kato, S., & Nakamura, H. (1990) · Acta Neuropathologica · doi:10.1007/bf00294235 · Cited by 145
Proteasome Involvement and Accumulation of Ubiquitinated Proteins in Cerebellar Granule Neurons Undergoing Apoptosis
Canu, N., Barbato, C., Ciotti, M. T., Serafino, A., Dus, L., & Calissano, P. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-02-00589.2000 · Cited by 144
4-Hydroxynonenal-modified amyloid-β peptide inhibits the proteasome: possible importance in Alzheimer’s disease*
Shringarpure, R., Grune, T., Sitte, N., & Davies*, K. J. A. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000660 · Cited by 140
Amyloid protein and neurofibrillary tangles coexist in the same neuron in Alzheimer disease.
Grundke, I., Iqbal, K., George, L., Tung, Y. C., Kim, K. S., & Wisniewski, H. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.8.2853 · Cited by 142
Novel Panel of Cerebrospinal Fluid Biomarkers for the Prediction of Progression to Alzheimer Dementia in Patients With Mild Cognitive Impairment
Simonsen, A. H., McGuire, J., Hansson, O., Zetterberg, H., Podust, V. N., Davies, H. A., Waldemar, G., Minthon, L., & Blennow, K. (2007) · Archives of Neurology · doi:10.1001/archneur.64.3.366 · Cited by 138
β‐Amyloid precursor epitopes in muscle fibers of inclusion body myositis
Askanas, V., Alvarez, R. B., & Engel, W. K. (1993) · Annals of Neurology · doi:10.1002/ana.410340408 · Cited by 139
Lysine-Directed Post-translational Modifications of Tau Protein in Alzheimer's Disease and Related Tauopathies
Kontaxi, C., Piccardo, P., & Gill, A. C. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00056 · Cited by 138
Blood cadmium levels and Alzheimer’s disease mortality risk in older US adults
Min, J., & Min, K. (2016) · Environmental Health · doi:10.1186/s12940-016-0155-7 · Cited by 138
Senile plaque composition and posttranslational modification of amyloid-β peptide and associated proteins
Atwood, C., Martins, R. N., Smith, M. A., & Perry, G. L. (2002) · Peptides · doi:10.1016/s0196-9781(02)00070-0 · Cited by 142
Self-citation
Ubiquitin pathways in neurodegenerative disease
Atkin, G., & Paulson, H. L. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00063 · Cited by 140
New Insights Into Drug Discovery Targeting Tau Protein
Soeda, Y., & Takashima, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.590896 · Cited by 136
Tau Oligomers Neurotoxicity
Niewiadomska, G., Niewiadomski, W., Steczkowska, M., & Gąsiorowska, A. (2021) · Life · doi:10.3390/life11010028 · Cited by 138
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
Acetylation: a new key to unlock tau’s role in neurodegeneration
Cook, C. N., Stankowski, J. N., Carlomagno, Y., Stetler, C. T., & Petrucelli, L. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt259 · Cited by 140
Traffic at the intersection of neurotrophic factor signaling and neurodegeneration
Salehi, A., Delcroix, J.-D., & Mobley, W. C. (2003) · Trends in Neurosciences · doi:10.1016/s0166-2236(02)00038-3 · Cited by 131
CELLULAR AND MOLECULAR BIOLOGY OF ALZHEIMER'S DISEASE AND ANIMAL MODELS
Price, D. L., & Sisodia, S. S. (1994) · Annual Review of Medicine · doi:10.1146/annurev.med.45.1.435 · Cited by 132
Proteasome Activation as a New Therapeutic Approach To Target Proteotoxic Disorders
Njomen, E., & Tepe, J. J. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00101 · Cited by 133
Filaments of Lewy bodies contain insoluble cytoskeletal elements.
Galloway, P. G., Mulvihill, P., & Perry, G. L. (1992) · PubMed Central · Cited by 131
Self-citation
Hsp90 regulates tau pathology through co-chaperone complexes in Alzheimer's disease
Salminen, A., Ojala, J. O., Kaarniranta, K., Hiltunen, M., & Soininen, H. S. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.10.006 · Cited by 131
Twisted tubulofilaments of inclusion body myositis muscle resemble paired helical filaments of Alzheimer brain and contain hyperphosphorylated tau.
Askanas, V., Engel, W. K., Bilak, M. M., Alvarez, R. B., & Selkoe, D. J. (1994) · PubMed Central · Cited by 127
Microtubule-associated polypeptides tau are altered in Alzheimer paired helical filaments
Grundke, I., VORBRODT, A. W., Iqbal, K., Tung, Y. C., Wang, G. P., & Wisniewski, H. M. (1988) · Molecular Brain Research · doi:10.1016/0169-328x(88)90017-4 · Cited by 128
Transgenic mice overexpressing reticulon 3 develop neuritic abnormalities
Hu, X., Shi, Q., Zhou, X., He, W., Yi, H. L., Yin, X., Gearing, M., Levey, A. I., & Yan, R. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601707 · Cited by 125
Alzheimer-specific epitopes of tau represent lipid peroxidation-induced conformations
Liu, Q., Smith, M. A., Ávila, J., DeBernardis, J. F., Kansal, M. M., Takeda, A., Zhu, X., Nunomura, A., Honda, K., Moreira, P. I., et al. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.11.005 · Cited by 129
Self-citation
Aluminum modifies the properties of Alzheimer's disease PHF tau proteins in vivo and in vitro
Shin, R. W., Lee, V., & Trojanowski, J. Q. (1994) · Journal of Neuroscience · doi:10.1523/jneurosci.14-11-07221.1994 · Cited by 126
Alzheimer disease tangles share immunological similarities with multiphosphorylation repeats in the two large neurofilament proteins.
Lee, V. M., Otvos, L. P., Schmidt, M. L., & Trojanowski, J. Q. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.19.7384 · Cited by 124
Relevance of Phosphorylation and Truncation of Tau to the Etiopathogenesis of Alzheimer’s Disease
Zhou, Y., Shi, J., Chu, D., Hu, W. H., Guan, Z., Gong, C., Iqbal, K., & Liu, F. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00027 · Cited by 130
Accumulation of NEDD8 in neuronal and glial inclusions of neurodegenerative disorders
Mori, F., Nishie, M., Piao, Y., Kito, K., Kamitani, T., Takahashi, H., & Wakabayashi, K. (2004) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00603.x · Cited by 120
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
Molecular analysis of neurofibrillary degeneration in Alzheimer's disease. An immunohistochemical study.
Bondareff, W., Wischik, C. M., Novák, M., Amos, W. B., Klug, A., & Roth, M. (1990) · Europe PMC (PubMed Central) · Cited by 121
Effects of elevated intracellular calcium levels on the cytoskeleton and tau in cultured human cortical neurons
Mattson, M. P., Engle, M. G., & Rychlik, B. (1991) · Molecular and Chemical Neuropathology · doi:10.1007/bf03159951 · Cited by 118
Brain site-specific proteome changes in aging-related dementia
Manavalan, A., Mishra, M., Feng, L., Sze, S. K., Akatsu, H., & Heese, K. (2013) · Experimental & Molecular Medicine · doi:10.1038/emm.2013.76 · Cited by 115
Alzheimer's Disease: A Description of the Structural Lesions
Probst, A., Langui, D., & ULRICH, J. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00666.x · Cited by 117
The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges
Tundo, G. R., Sbardella, D., Santoro, A. M., Coletta, A., Oddone, F., Grasso, G., Milardi, D., Lacal, P. M., Marini, S., Purrello, R., et al. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107579 · Cited by 120
Tau Protein Squired by Molecular Chaperones During Alzheimer’s Disease
Gorantla, N. V., & Chinnathambi, S. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1174-3 · Cited by 113
Relationships between Lewy bodies and pale bodies in Parkinson's disease
Dale, G. E., Probst, A., Luthert, P., Martin, J., Anderton, B. H., & Leigh, P. N. (1992) · Acta Neuropathologica · doi:10.1007/bf00310030 · Cited by 114
Alzheimer disease proteins (A68) share epitopes with tau but show distinct biochemical properties
Ksiezak‐Reding, H., Binder, L. I., & Yen, S.-H. C. (1990) · Journal of Neuroscience Research · doi:10.1002/jnr.490250320 · Cited by 113
Proteasome activation: An innovative promising approach for delaying aging and retarding age-related diseases
Chondrogianni, N., Voutetakis, K., Καπετάνου, Μ., Delitsikou, V., Papaevgeniou, N., Sakellari, M., Lefaki, M., Filippopoulou, K., & Gonos, E. S. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.12.003 · Cited by 115
The role of the ubiquitin proteasome system in Alzheimer's disease
Riederer, B. M., Leuba, G., Vernay, A., & Riederer, I. M. (2011) · Experimental Biology and Medicine · doi:10.1258/ebm.2010.010327 · Cited by 113
It Is All about (U)biquitin: Role of Altered Ubiquitin‐Proteasome System and UCHL1 in Alzheimer Disease
Tramutola, A., Domenico, F. D., Barone, E., Marzia Perluigi, A., & Butterfield, D. A. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2756068 · Cited by 109
Ubiquitination and abnormal phosphorylation of paired helical filaments in Alzheimer's disease
Iqbal, K., & Grundke, I. (1991) · Molecular Neurobiology · doi:10.1007/bf02935561 · Cited by 108
Accumulation of protein O‐GlcNAc modification inhibits proteasomes in the brain and coincides with neuronal apoptosis in brain areas with high O‐GlcNAc metabolism
Liu, K., Paterson, A. J., Zhang, F., McAndrew, J., Fukuchi, K., Wyss, J. M., Peng, L., Hu, Y., & Kudlow, J. E. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02389.x · Cited by 103
Ubiquitin immunoelectron microscopy of dystrophic neurites in cerebellar senile plaques of Alzheimer's disease
Dickson, D. W., Wertkin, A. M., Mattiace, L. A., Fier, E., Kress, Y., Davies, P., & Yen, S. H. (1990) · Acta Neuropathologica · doi:10.1007/bf00296107 · Cited by 102
Cytokines, prostaglandins and lipocortin-1 are present in the brains of scrapie-infected mice
Williams, A. E., van Dam, A., Man‐A‐Hing, W. K. H., BERKENBOSCH, F., Eikelenboom, P., & Fraser, H. (1994) · Brain Research · doi:10.1016/0006-8993(94)90480-4 · Cited by 100
Aβ40 Reduces P-Glycoprotein at the Blood–Brain Barrier through the Ubiquitin–Proteasome Pathway
Hartz, A. M. S., Zhong, Y., Wolf, A. M., LeVine, H., Miller, D. S., & Bauer, B. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0350-15.2016 · Cited by 100
Immunolocalization of ubiquitin in muscle biopsies of patients with inclusion body myositis and oculopharyngeal muscular dystrophy
Askanas, V., Serdaroglu, P., Engel, W. K., & Alvarez, R. B. (1991) · Neuroscience Letters · doi:10.1016/0304-3940(91)90230-q · Cited by 98
Role of the proteasome in Alzheimer’s disease
Checler, F., da Costa, C. A., Ancolio, K., Chevallier, N., Lopez‐Perez, E., & Marambaud, P. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00039-9 · Cited by 98
Biomarker-based dissection of neurodegenerative diseases
Olsson, B., Zetterberg, H., Hampel, H. J., & Blennow, K. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.04.006 · Cited by 102
Role of ubiquitin–proteasome-mediated proteolysis in nervous system disease
Hegde, A. N., & Upadhya, S. C. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.07.006 · Cited by 96
Parkin reverses intracellular β‐amyloid accumulation and its negative effects on proteasome function
Rosen, K. M., Moussa, C., Lee, H., Kumar, P., Kitada, T., Qin, G., Fu, Q., & Querfurth, H. W. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22178 · Cited by 97
Decreased Catalytic Activity of the Insulin-degrading Enzyme in Chromosome 10-Linked Alzheimer Disease Families
Kim, M., Hersh, L. B., Leissring, M. A., Ingelsson, M., Matsui, T., Farris, W., Lu, A., Hyman, B. T., Selkoe, D. J., Bertram, L., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609168200 · Cited by 97
THREE-DIMENSIONAL STRUCTURE OF A UBIQUITIN-CONJUGATING ENZYME (E2)
Cook, W. J., Jeffrey, L. C., Sullivan, M. L., & Vierstra, R. D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42154-0 · Cited by 94
The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer’s Disease
Sulistio, Y. A., & Heese, K. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-9063-4 · Cited by 93
Abnormal distribution of cathepsin proteinases and endogenous inhibitors (cystatins) in the hippocampus of patients with Alzheimer's disease, parkinsonism-dementia complex on Guam, and senile dementia and in the aged
Ii, K., Ito, H., Kominami, E., & Hirano, A. (1993) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf01614769 · Cited by 96
Hypothalamic neurodegeneration and adult-onset obesity in mice lacking the Ubb polyubiquitin gene
Ryu, K., Garza, J. C., Lu, X., Barsh, G. S., & Kopito, R. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800096105 · Cited by 93
Endo-lysosomal proteins and ubiquitin CSF concentrations in Alzheimer’s and Parkinson’s disease
Sjödin, S., Brinkmalm, G., Öhrfelt, A., Parnetti, L., Paciotti, S., Hansson, O., Hardy, J., Blennow, K., Zetterberg, H., & Brinkmalm, A. (2019) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0533-9 · Cited by 94
Endoplasmic Reticulum Protein Quality Control in Neurodegenerative Disease: The Good, the Bad and the Therapy
Scheper, W., & Hoozemans, J. J. M. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709787458506 · Cited by 92
SUMO and Alzheimer’s Disease
Lee, L., Sakurai, M., Matsuzaki, S., Arancio, O., & Fraser, P. E. (2013) · NeuroMolecular Medicine · doi:10.1007/s12017-013-8257-7 · Cited by 94
The monoclonal antibody, Alz 50, recognizes tau proteins in Alzheimer's disease brain
Nukina, N., Kosik, K. S., & Selkoe, D. J. (1988) · Neuroscience Letters · doi:10.1016/0304-3940(88)90455-7 · Cited by 90
Molecular pathology of amyloidogenic proteins and the role of vascular amyloidosis in Alzheimer's disease
Selkoe, D. J. (1989) · Neurobiology of Aging · doi:10.1016/0197-4580(89)90072-9 · Cited by 90
Relationship between plaques, tangles, and dystrophic processes in Alzheimer's disease
Trojanowski, J. Q., Shin, R., Schmidt, M. L., & Lee, V. M.-Y. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(94)00176-2 · Cited by 89
Brain ubiquitin is markedly elevated in Alzheimer disease
Wang, G. P., Khatoon, S., Iqbal, K., & Grundke, I. (1991) · Brain Research · doi:10.1016/0006-8993(91)91692-t · Cited by 89
New aspects of the pathology of neurodegenerative disorders as revealed by ubiquitin antibodies
Leigh, P. N., Probst, A., Dale, G. E., Power, D., Brion, J., Dodson, A. R., & Anderton, B. H. (1989) · Acta Neuropathologica · doi:10.1007/bf00308959 · Cited by 89
Immunocytochemical characterization of neurofibrillary tangles in amyotrophic lateral sclerosis and parkinsonism‐dementia of guam
Shankar, S. K., Yanagihara, R., Garruto, R. M., Grundke, I., Kosik, K. S., & Gajdusek, D. C. (1989) · Annals of Neurology · doi:10.1002/ana.410250207 · Cited by 89
Interventions for age-related diseases: Shifting the paradigm
Figueira, I., Fernandes, A. M. A., Mladenović, A., Lopez-Contreras, A. J., Henriques, C. M., Selman, C., Ferreiro, E. B., Gonos, E. S., Trejo, J. L., Misra, J., et al. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.09.009 · Cited by 92
Abnormal processing of multiple proteins in Alzheimer disease.
Zhang, H., Sternberger, N. H., Rubinstein, L. J., Herman, M. M., Binder, L. I., & Sternberger, L. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.8045 · Cited by 88
Selective presence of ubiquitin in intracellular inclusions.
Manetto, V., Abdul-Karim, F. W., Perry, G. L., Tabaton, M., AUTILIO‐GAMBETTI, L., & Gambetti, P. L. (1989) · Europe PMC (PubMed Central) · Cited by 87
Self-citation
Inverse association of Pin1 and tau accumulation in Alzheimer's disease hippocampus
Holzer, M., Gärtner, U., Stöbe, A., Härtig, W., Gruschka, H., Brückner, M. K., & Arendt, T. (2002) · Acta Neuropathologica · doi:10.1007/s00401-002-0581-1 · Cited by 86
Ubiquitin is a component of the microtubule network.
Murti, K. G., Smith, H. T., & Fried, V. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.9.3019 · Cited by 86
Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies
Silva, M. C., & Haggarty, S. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238948 · Cited by 89
Histopathological and Immunohistochemical Comparison of the Brain of Human Patients with Alzheimer’s Disease and the Brain of Aged Dogs with Cognitive Dysfunction
Yu, C.-H., Song, G. S., Yhee, J. Y., Kim, J. H., Im, K.-S., Nho, W.-G., Lee, J. H., & Sur, J. (2011) · Journal of Comparative Pathology · doi:10.1016/j.jcpa.2010.11.004 · Cited by 92
Defective proteostasis in Alzheimer’s disease
Cozachenco, D., Ribeiro, F. C., & Ferreira, S. T. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101862 · Cited by 87
Targeting mitochondrial dysfunction in neurodegenerative disease: Part II
Burchell, V., Gandhi, S., Deas, E., Wood, N. W., Abramov, A. Y., & Plun‐Favreau, H. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728221003730434 · Cited by 83
Neurofibrillary tangles in some cases of dementia pugilistica share antigens with amyloid beta-protein of Alzheimer's disease.
Allsop, D., Haga, S., Bruton, C. J., Ishii, T., & Roberts, G. W. (1990) · Europe PMC (PubMed Central) · Cited by 83
Clinically Relevant Post-Translational Modification Analyses—Maturing Workflows and Bioinformatics Tools
Pascovici, D., Wu, J. X., McKay, M. J., Joseph, C., Noor, Z., Kamath, K. S., Wu, Y., Ranganathan, S., Gupta, V., & Mirzaei, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010016 · Cited by 82
Oxygen free radicals as inducers of heat shock protein synthesis in cultured human neuroblastoma cells: Relevance to neurodegenerative disease
Omar, R., & Pappolla, M. A. (1993) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/bf02190384 · Cited by 81
The widespread alteration of neurites in Alzheimer's disease may be unrelated to amyloid deposition
Tabaton, M., Mandybur, T. I., Perry, G. L., Onorato, M., AUTILIO‐GAMBETTI, L., & Gambetti, P. L. (1989) · Annals of Neurology · doi:10.1002/ana.410260614 · Cited by 80
Self-citation
Endo-lysosomal pathway and ubiquitin-proteasome system dysfunction in Alzheimer's disease pathogenesis
Cao, J., Zhong, M. B., Toro, C. A., Zhang, L., & Cai, D. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.03.016 · Cited by 82
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
Histochemical accumulation of oxidative damage products is associated with Alzheimer-like pathology in the canine
Rofina, J., Singh, K., Skoumalova-Vesela, A., van Ederen, A. M., van Asten, A. J., Wilhelm, J., & Gruys, E. (2004) · Amyloid · doi:10.1080/13506120412331285779 · Cited by 82
Hsp70 mRNA induction is reduced in neurons of aged rat hippocampus after thermal stress
Pardue, S., Groshan, K., Raese, J. D., & Morrison‐Bogorad, M. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90088-f · Cited by 79
Amyloid cross-seeding raises new dimensions to understanding of amyloidogenesis mechanism
Chaudhuri, P., Prajapati, K. P., Anand, B. G., Dubey, K., & Kar, K. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100937 · Cited by 80
The Ubiquitin System in Alzheimer’s Disease
Harris, L. D., Jasem, S., & Licchesi, J. D. F. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_8 · Cited by 79
Neurofibrillary tangles in dementia pugilistica are ubiquitinated.
Dale, G. E., Leigh, P. N., Luthert, P. J., Anderton, B. H., & Roberts, G. W. (1991) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.54.2.116 · Cited by 78
Protein oxidation and degradation during aging: Role in skin aging and neurodegeneration
Widmer, R., Ziaja, I., & Grune, T. (2006) · Free Radical Research · doi:10.1080/10715760600911154 · Cited by 76
SUMO-1 immunoreactivity co-localizes with phospho-Tau in APP transgenic mice but not in mutant Tau transgenic mice
Takahashi, K., Ishida, M., Komano, H., & Takahashi, H. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.06.012 · Cited by 75
Deficiency of kallikrein-like enzyme activities in cerebral tissue of patients with alzheimer's disease
Aoyagi, T., Wada, T., NAGAI, M., Kojima, F., Harada, S., Takeuchi, T., Takahashi, H., Hirokawa, K., & Tsumita, T. (1990) · Cellular and Molecular Life Sciences · doi:10.1007/bf01955428 · Cited by 76
Alzheimer disease: correlation of cerebro-spinal fluid and brain ubiquitin levels
Kudo, T., Iqbal, K., Ravid, R., Swaab, D. F., & Grundke, I. (1994) · Brain Research · doi:10.1016/0006-8993(94)91757-4 · Cited by 75
Alz 50 recognizes abnormal filaments in Alzheimer's disease and progressive supranuclear palsy
Tabatonm, M., Whitehouse, P. J., Perry, G. L., Davies, P., AUTILIO‐GAMBETTI, L., & Gambetti, P. L. (1988) · Annals of Neurology · doi:10.1002/ana.410240309 · Cited by 75
Self-citation
Rodent Models of Amyloid-Beta Feature of Alzheimer’s Disease: Development and Potential Treatment Implications
Poon, C. H., Wang, Y., Fung, M., Zhang, C., & Lim, L. W. (2020) · Aging and Disease · doi:10.14336/ad.2019.1026 · Cited by 76
sAPPα antagonizes dendritic degeneration and neuron death triggered by proteasomal stress
Copanaki, E., Chang, S., Vlachos, A., Tschäpe, J., Müller, U., Kögel, D., & Deller, T. (2010) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2010.04.007 · Cited by 84
FBL2 Regulates Amyloid Precursor Protein (APP) Metabolism by Promoting Ubiquitination-Dependent APP Degradation and Inhibition of APP Endocytosis
Watanabe, T., Hikichi, Y., Willuweit, A., Shintani, Y., & Horiguchi, T. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5659-11.2012 · Cited by 76
Cellular stress response, sirtuins and UCP proteins in Alzheimer disease: role of vitagenes
Cornelius, C., Salinaro, A. T., Scuto, M. C., Fronte, V., Cambria, M. T., Pennisi, M., Bella, R., Milone, P., Graziano, A., Crupi, R., et al. (2013) · Immunity & Ageing · doi:10.1186/1742-4933-10-41 · Cited by 75
The ubiquitin–proteasome system and neurodegenerative disorders
Layfield, R., Lowe, J. S., & Bedford, L. (2005) · Essays in Biochemistry · doi:10.1042/eb0410157 · Cited by 71
Neurofilamentopathy in Neurodegenerative Diseases
Liu, Q., Xie, F., Alvarado-Diaz, A., Smith, M. A., Moreira, P. I., Zhu, X., & Perry, G. (2011) · The Open Neurology Journal · doi:10.2174/1874205x01105010058 · Cited by 72
Self-citation

Authors: Perry, G., Friedman, R., Shaw, G., & Chau, V
Affiliations: Case Western Reserve University (US)
ORCID: Perry, G
Shaw, G
Chau, V
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1987-05
Volume: 84
Issue: 9
Pages: 3033-3036
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.84.9.3033
PMC: PMC304795
OpenAlex: W2046720254
Cited by: 623
References: 27
Citations by year: 2026: 6 · 2025: 8 · 2024: 11 · 2023: 13 · 2022: 8 · 2021: 15 · 2020: 17 · 2019: 15 · 2018: 21 · 2017: 11 · 2016: 17 · 2015: 15 · 2014: 5 · 2013: 20 · 2012: 18
FWCI: 33.38
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute on Aging (AG00795)
National Institute of General Medical Sciences (GM35803)
National Institute of Neurological Disorders and Stroke (NS22695)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: ubiquitin, neurofibrillary tangles, amyloid plaques, Alzheimer's disease, neurites, protein degradation, tau protein, neurofilaments, microtubule-associated proteins, immunostaining
MeSH terms: Aged, Alzheimer Disease, Antibodies, Antigen-Antibody Complex, Axons, Brain, Humans, Immunoenzyme Techniques, Neurons, Ubiquitins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks