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Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains.
Open accessAbstract
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.
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Cites
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
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
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
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
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
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Song, S., & Jung, Y. (2003) · Springer eBooks · doi:10.1007/978-1-4757-5890-0_16
Obrenovich, M. E., Raina, A. K., Ogawa, O., Atwood, C., Morelli, L., & Smith, M. A. (2007) · Springer eBooks · doi:10.1007/0-387-29390-6_6
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Anand, A., Sharma, N., Gulati, M., & Khurana, N. (2020) · IGI Global eBooks · doi:10.4018/978-1-7998-3441-0.ch001
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Chountoulesi, M., Naziris, N., Gioran, A., Papagiannopoulos, A., Steele, B. R., Micha‐Screttas, M., Stavrinides, S. G., Hanias, M. P., Chondrogianni, N., Pispas, S., et al. (2022) · Springer eBooks · doi:10.1007/978-3-319-75479-6_16-1
Upadhyay, A., Chhangani, D., Rao, N. R., Kofler, J., Vassar, R. J., Rincón-Limas, D. E., & Savas, J. N. (2023) · Figshare · doi:10.6084/m9.figshare.24144129
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Upadhyay, A., Chhangani, D., Rao, N. R., Kofler, J., Vassar, R. J., Rincón-Limas, D. E., & Savas, J. N. (2023) · Figshare · doi:10.6084/m9.figshare.24144147
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Upadhyay, A., Chhangani, D., Rao, N. R., Kofler, J., Vassar, R. J., Rincón-Limas, D. E., & Savas, J. N. (2023) · Figshare · doi:10.6084/m9.figshare.24144135
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Upadhyay, A., Chhangani, D., Rao, N. R., Kofler, J., Vassar, R. J., Rincón-Limas, D. E., & Savas, J. N. (2023) · Figshare · doi:10.6084/m9.figshare.24144141
Frameshift Mutant Ubiquitin in Alzheimer’s Disease and Other Neurodegenerative Disorders
Layfield, R. (2007) · Springer eBooks · doi:10.1007/0-387-28500-8_15
Upadhyay, A., Chhangani, D., Rao, N. R., Kofler, J., Vassar, R. J., Rincon-Limas, D. E., & Savas, J. N. (2023) · Figshare · doi:10.6084/m9.figshare.24144123
Upadhyay, A., Chhangani, D., Rao, N. R., Kofler, J., Vassar, R. J., Rincon-Limas, D. E., & Savas, J. N. (2023) · Figshare · doi:10.6084/m9.figshare.24144120
TAX1BP1 recruitment reactivates autophagy of Tau aggregates through ULK1 and TBK1Preprint
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Implication du fragment C99 dans l’avènement des phénotypes pathologiques de la maladie d’Alzheimer
Bourgeois, A. (2019) · theses.fr (ABES) · doi:10.70675/bb8ccf34zec6cz4bb6z82b4z3030b9cb28f7
The Use of Localized Proteomics to Understand the Pathogenesis of Alzheimer's Disease
Pires, G. (2021) · theses.fr (ABES) · doi:10.70675/45826fd6zd2c8z4b3dz91e0za5080544cb17
Yatoui, D. (2022) · theses.fr (ABES) · doi:10.70675/e3620ccez2ea7z43f2za0dcz257a72021b17
The Pharmacology and Dual Role of Proteostasis in Amyloidoses
Albanese, A., Natu, M. M., & Seidler, P. M. (2026) · Biophysica · doi:10.3390/biophysica6020031
The modifier matrix: emerging roles of ubiquitin-like proteins in Alzheimer’s disease
颜亭祥, Vaquer, J., Springer, W., & Fiesel, F. C. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00031-2
Endocrine and diagnostic aspects of cognitive impairment
Johansson, P. (2013) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Alzheimer%#x2019;s Disease and Genetically Engineered Animal Models
Borchelt, D., Wong, P. C., Sisodia, S. S., & Price, D. L. (1999) · Springer eBooks · doi:10.1007/978-1-4615-4887-4_9
Metadata
- Authors
- Perry, G., Friedman, R., Shaw, G., & Chau, V
- Affiliations
- Case Western Reserve University (US)
- 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
- 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
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