The DOI matches its Crossref record; 71 of the 72 references it cites were found in a registry or an index.
Analysis of microtubule-associated protein tau glycation in paired helical filaments.
Open accessAbstract
Alzheimer's disease is typified by the characteristic histopathological lesions of neurofibrillar plaques and tangles. The latter are composed of paired helical filaments (PHFs), the major components of which are modified forms of the microtubule-associated protein tau. The exact nature of these modifications remains unknown, although the presence of hyperphosphorylated tau in PHFs argues strongly that phosphorylation is one of the modifications that result in the polymerization of tau into PHFs. However, hyperphosphorylation alone is insufficient to explain the formation of PHFs. In an attempt to characterize other post-translational modifications of PHF-tau, we have analyzed its glycation. A fraction of PHF-tau seems to be glycated in vivo, whereas soluble tau from either Alzheimer's disease or non-demented human brain is not glycated at all. Purified tau from bovine brain can be efficiently glycated in vitro. Tau glycation is accompanied by a decrease in the tau binding to tubulin. These results support the view that glycation may be one of the modifications hampering the binding of tau to tubulin in Alzheimer's disease, thus facilitating tau aggregation into PHFs.
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“Glycated tau is only detected in PHF-tau isolated from AD brain samples, but not in soluble tau from AD or normal brain samples [177, 179].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [177]
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“Tau is preferentially glycated at Lys residues within the microtubule-binding domain, where advanced glycation end products are generated [177–179].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [177]
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Metadata
- Authors
- Ledesma, M. D., Bonay, P., Colaço, C., & Avila, J.
- Affiliations
- Consejo Superior de Investigaciones Científicas (ES)
- ORCID
- Ledesma, M.D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1994-08
- Volume
- 269
- Issue
- 34
- Pages
- 21614-21619
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1577069180
- Semantic Scholar
- 68928334bcb2a45f531ceaeaa8ef0e1a72308735
- Cited by
- 333
- References
- 72
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 7 · 2023: 6 · 2022: 4 · 2021: 8 · 2020: 2 · 2019: 12 · 2018: 13 · 2017: 7 · 2016: 10 · 2015: 5 · 2014: 13 · 2013: 11 · 2012: 13
- FWCI
- 11.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau protein, glycation, paired helical filaments, Alzheimer's disease, post-translational modification, tau aggregation, neurofibrillary tangles, hyperphosphorylation
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Amino Acid Sequence, Animals, Brain Chemistry, Cattle, Diabetes Mellitus, Humans, Lysine, Microtubules, Molecular Sequence Data, Protein Binding, Neurofibrillary Tangles, tau Proteins, Glycation End Products, Advanced, Diabetes Complications
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