ReviewFrontiers in neuroscience2016
Multifaceted Role of Sialylation in Prion Diseases.
Review in Frontiers in neuroscience, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 53 citations in OpenAlex.
- Biological function of sialic acid and sialylation in human health and disease.Cell death discovery · 2024Review
- Post-translational modifications in prion diseases.Frontiers in molecular neuroscience · 2024Review
- Multiple steps of prion strain adaptation to a new host.Frontiers in neuroscience · 2024Article
- Reactive astrocytes associated with prion disease impair the blood brain barrier.Neurobiology of disease · 2023Article
- Reactive astrocytes associated with prion disease impair the blood brain barrier.bioRxiv : the preprint server for biology · 2023Article
- Deficiency in ST6GAL1, one of the two α2,6-sialyltransferases, has only a minor effect on the pathogenesis of prion disease.Frontiers in molecular biosciences · 2022Article
- Review
- Article
- Non-cell autonomous astrocyte-mediated neuronal toxicity in prion diseases.Acta neuropathologica communications · 2021Article
- From Posttranslational Modifications to Disease Phenotype: A Substrate Selection Hypothesis in Neurodegenerative Diseases.International journal of molecular sciences · 2021Review
- Posttranslational modifications define course of prion strain adaptation and disease phenotype.The Journal of clinical investigation · 2020Article
- Region-specific glial homeostatic signature in prion diseases is replaced by a uniform neuroinflammation signature, common for brain regions and prion strains with different cell tropism.Neurobiology of disease · 2020Article
- Sialylated N-glycan profile during acute and chronic infections with Toxoplasma gondii in mice.Scientific reports · 2020Article
- Production of Artificially Doubly Glycosylated,The Journal of organic chemistry · 2020Article
- Region-Specific Sialylation Pattern of Prion Strains Provides Novel Insight into Prion Neurotropism.International journal of molecular sciences · 2020Article
- Modeling PrPFrontiers in bioengineering and biotechnology · 2020Article
- Article
- Review
- Full atomistic model of prion structure and conversion.PLoS pathogens · 2019Article
- Identification of serum N-glycoproteins as a biological correlate underlying chronic stress response in mice.Molecular biology reports · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Mammalian prion or PrP(Sc) is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycoprotein called the prion protein, or PrP(C). Sialylation of the prion protein N-linked glycans was discovered more than 30 years ago, yet the role of sialylation in prion pathogenesis remains poorly understood. Recent years have witnessed extraordinary growth in interest in sialylation and established a critical role for sialic acids in host invasion and host-pathogen interactions. This review article summarizes current knowledge on the role of sialylation of the prion protein in prion diseases. First, we discuss the correlation between sialylation of PrP(Sc) glycans and prion infectivity and describe the factors that control sialylation of PrP(Sc). Second, we explain how glycan sialylation contributes to the prion replication barrier, defines strain-specific glycoform ratios, and imposes constraints for PrP(Sc) structure. Third, several topics, including a possible role for sialylation in animal-to-human prion transmission, prion lymphotropism, toxicity, strain interference, and normal function of PrP(C), are critically reviewed. Finally, a metabolic hypothesis on the role of sialylation in the etiology of sporadic prion diseases is proposed.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.