{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T17:11:26Z","timestamp":1777396286733,"version":"3.51.4"},"reference-count":64,"publisher":"SAGE Publications","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JAD"],"published-print":{"date-parts":[[2020,5,5]]},"abstract":"<jats:p>Background: Frontotemporal dementia and parkinsonism-linked to chromosome-17 are a group of diseases with tau mutations leading to primary tauopathies which include progressive supranuclear palsy, corticobasal syndrome, and frontotemporal lobar degeneration. Alzheimer\u2019s disease is a non-primary tauopathy, which displays tau neuropathology of excess tangle formation and accumulation. FTDP-17 mutations are responsible for early onset of AD, which can be attributed to compromised physiological functions due to the mutations. Tau is a microtubule-binding protein that secures the integrity of polymerized microtubules in neuronal cells. It malfunctions owing to various insults and stress conditions-like mutations and post-translational modifications. Objective: In this study, we modified the wild type and tau mutants by methyl glyoxal and thus studied whether glycation can enhance the aggregation of predisposed mutant tau. Methods: Tau glycation was studied by fluorescence assays, SDS-PAGE analysis, conformational evaluation, and transmission electron microscopy. Results: Our study suggests that FTDP-17 mutant P301\u200aL leads to enhanced glycation-induced aggregation as well as advanced glycation end products formation. Glycation forms amorphous aggregates of tau and its mutants without altering its native conformation. Conclusion: The metabolic anomalies and genetic predisposition have found to accelerate tau-mediated neurodegeneration and prove detrimental for the early-onset of Alzheimer\u2019s disease.<\/jats:p>","DOI":"10.3233\/jad-191348","type":"journal-article","created":{"date-parts":[[2020,4,3]],"date-time":"2020-04-03T10:50:29Z","timestamp":1585911029000},"page":"61-71","source":"Crossref","is-referenced-by-count":13,"title":["P301 L, an FTDP-17 Mutant, Exhibits Enhanced Glycation in vitro"],"prefix":"10.1177","volume":"75","author":[{"given":"Shweta Kishor","family":"Sonawane","sequence":"first","affiliation":[{"name":"Neurobiology Group, Biochemical Sciences Division, CSIR-National Chemical Laboratory, Pune, India"},{"name":"Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Subashchandrabose","family":"Chinnathambi","sequence":"additional","affiliation":[{"name":"Neurobiology Group, Biochemical Sciences Division, CSIR-National Chemical Laboratory, Pune, India"},{"name":"Academy of Scientific and Innovative Research (AcSIR), Ghaziabad, India"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","reference":[{"key":"10.3233\/JAD-191348_ref1","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1038\/342498a0","article-title":"Organization of microtubules in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau","volume":"342","author":"Lewis","year":"1989","journal-title":"Nature"},{"key":"10.3233\/JAD-191348_ref2","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1007\/s12031-018-1111-5","article-title":"Prion-like propagation of post-translationally modified tau in Alzheimer\u2019s disease: A hypothesis","volume":"65","author":"Sonawane","year":"2018","journal-title":"J Mol Neurosci"},{"key":"10.3233\/JAD-191348_ref3","doi-asserted-by":"crossref","first-page":"3414","DOI":"10.1016\/S0021-9258(18)53710-8","article-title":"Functional organization of microtubule-associated protein tau. 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