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Unlocking the Sugar Code: Implications and Consequences of Glycosylation in Alzheimer’s Disease and Other Tauopathies
Andrei-Cristian Bondar, Marius P. Iordache, Mirela Coroescu, Anca Buliman, Elena Emanuela Rusu, Magdalena Budișteanu, Cristiana Tănase. Biomedicines, 2025-11-26
Topic: Amyloid, tau and blood-test diagnosis
Alzheimer’s disease (AD) is the most prevalent cause of dementia, characterized by progressive cognitive decline, amyloid-β (Aβ) plaques, and neurofibrillary tangles composed of hyperphosphorylated tau protein. Other tauopathies, including frontotemporal lobar degeneration (FTLD), progressive supranuclear palsy (PSP), and corticobasal degeneration (CBD) share pathological hallmarks centered on abnormal tau biology. Increasing evidence highlights the role of post-translational modifications in modulating these pathogenic processes. Among these, glycosylation, the enzymatic attachment of glycans to proteins or lipids, has emerged as a critical regulator of protein folding, trafficking, aggregation, and clearance. Both N-linked glycosylation (N-glycosylation) and O-linked glycosylation (O-glycosylation) influence tau stability, Aβ processing, receptor signaling, synaptic integrity, and neuroinflammation. Dysregulated glycosylation patterns have been documented in brains and cerebrospinal fluid (CSF) of AD patients, suggesting biomarker potential and novel therapeutic targets. Moreover, glycosyltransferases and glycosidases show altered expression in neurodegeneration, linking metabolic and inflammatory pathways to tauopathy progression. This review synthesizes current evidence on the implications and consequences of glycosylation in AD and other tauopathies, integrating mechanistic, pathological, and clinical findings. We also discuss advances in glycoproteomics, the interplay between glycosylation and phosphorylation, and the translational potential of targeting glycosylation pathways for diagnosis and therapy.
Key findings
- Both N-linked glycosylation (N-glycosylation) and O-linked glycosylation (O-glycosylation) influence tau stability, Aβ processing, receptor signaling, synaptic integrity, and neuroinflammation.
- Dysregulated glycosylation patterns have been documented in brains and cerebrospinal fluid (CSF) of AD patients, suggesting biomarker potential and novel therapeutic targets.
- Moreover, glycosyltransferases and glycosidases show altered expression in neurodegeneration, linking metabolic and inflammatory pathways to tauopathy progression.
- This review synthesizes current evidence on the implications and consequences of glycosylation in AD and other tauopathies, integrating mechanistic, pathological, and clinical findings.
- We also discuss advances in glycoproteomics, the interplay between glycosylation and phosphorylation, and the translational potential of targeting glycosylation pathways for diagnosis and therapy.
Why it matters
This review describes how glycosylation, the attachment of glycans to proteins or lipids, influences tau stability, Aβ processing, synaptic integrity, and neuroinflammation. It notes that dysregulated glycosylation patterns in brains and cerebrospinal fluid of Alzheimer's patients suggest biomarker potential and novel therapeutic targets.
Study details
- Evidence strengthLow
How this study scored 38/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Biomedicines) |
| Journal's citation record | 1 / 4 | Biomedicines: journal h-index 133 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 4 / 5 | 2025 — within 3 year(s) of the newest study here |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 2 / 7 | Cited 6 times (OpenAlex, 2026-10-10) |
| Citations per year | 1 / 5 | 2.0 citations a year over 3 year(s) since 2025 |
| Impact for its field and year | 3 / 6 | Cited 3.3× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 0 / 6 | No other study in this library cites it |
| Still being cited | 1 / 4 | Cited 6 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Cristiana Tănase: h-index 33 (OpenAlex, whole career) |
| Institution's track record | 0 / 3 | Institutul National Victor Babes: institution h-index 132 (OpenAlex) |
| Multi-centre collaboration | 2 / 3 | OpenAlex lists 4 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 41462898) |
| Free to read | 2 / 2 | Free to read |
| Total | 38 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
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Cite this study APA, Vancouver, BibTeX · download .bib or .ris
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. The record names 7 authors; APA and Vancouver show the first six, BibTeX and the downloads carry all of them. Check the citation against the original before you use it.
APA 7th
Bondar, A.-C., Iordache, M. P., Coroescu, M., Buliman, A., Rusu, E. E., Budișteanu, M., et al. (2025). Unlocking the Sugar Code: Implications and Consequences of Glycosylation in Alzheimer’s Disease and Other Tauopathies. Biomedicines. https://doi.org/10.3390/biomedicines13122884
Vancouver
Bondar A.-C, Iordache MP, Coroescu M, Buliman A, Rusu EE, Budișteanu M, et al. Unlocking the Sugar Code: Implications and Consequences of Glycosylation in Alzheimer’s Disease and Other Tauopathies. Biomedicines. 2025. doi:10.3390/biomedicines13122884. PMID: 41462898.
BibTeX
@article{bondar2025-41462898,
author = {Bondar, Andrei-Cristian and Iordache, Marius P. and Coroescu, Mirela and Buliman, Anca and Rusu, Elena Emanuela and Budișteanu, Magdalena and Tănase, Cristiana},
title = {{Unlocking the Sugar Code: Implications and Consequences of Glycosylation in Alzheimer’s Disease and Other Tauopathies}},
journal = {Biomedicines},
year = {2025},
doi = {10.3390/biomedicines13122884},
pmid = {41462898},
url = {https://doi.org/10.3390/biomedicines13122884}
}
Studies this one cites
Referenced by this study and also in the alzhub library, so you can read them here.