The DOI matches its Crossref record; 100 of the 100 references it cites were found in a registry or an index.
The role of protein glycosylation in Alzheimer disease
Abstract
Glycosylation is one of the most common, and the most complex, forms of post‐translational modification of proteins. This review serves to highlight the role of protein glycosylation in Alzheimer disease (AD), a topic that has not been thoroughly investigated, although glycosylation defects have been observed in AD patients. The major pathological hallmarks in AD are neurofibrillary tangles and amyloid plaques. Neurofibrillary tangles are composed of phosphorylated tau, and the plaques are composed of amyloid β‐peptide (Aβ), which is generated from amyloid precursor protein (APP). Defects in glycosylation of APP, tau and other proteins have been reported in AD. Another interesting observation is that the two proteases required for the generation of amyloid β‐peptide (Aβ), i.e. γ‐secretase and β‐secretase, also have roles in protein glycosylation. For instance, γ‐secretase and β‐secretase affect the extent of complex N‐glycosylation and sialylation of APP, respectively. These processes may be important in AD pathogenesis, as proper intracellular sorting, processing and export of APP are affected by how it is glycosylated. Furthermore, lack of one of the key components of γ‐secretase, presenilin, leads to defective glycosylation of many additional proteins that are related to AD pathogenesis and/or neuronal function, including nicastrin, reelin, butyrylcholinesterase, cholinesterase, neural cell adhesion molecule, v‐ATP ase, and tyrosine‐related kinase B. Improved understanding of the effects of AD on protein glycosylation, and vice versa, may therefore be important for improving the diagnosis and treatment of AD patients.
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Self-citationAn atomic structure of human γ-secretase
Bai, X.-C., Yan, C., Yang, G., Lu, P., Ma, D., Sun, L., Zhou, R., Scheres, S. H. W., & Shi, Y. (2015) · Nature · doi:10.1038/nature14892 · Cited by 498
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Metadata
- Authors
- Schedin‐Weiss, S., Winblad, B., & Tjernberg, L. O.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2013-11-26
- Volume
- 281
- Issue
- 1
- Pages
- 46-62
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2071292969
- Cited by
- 317
- References
- 100
- FWCI
- 14.28
- Type
- journal article
- Language
- en
- Open access
- closed
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