Inflammatory response of microglia to prions is controlled by sialylation of PrPSc
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2045-2322
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Inflammatory response of microglia to prions is controlled by sialylation of PrPSc ; volume:8 ; number:1 ; day:27 ; month:7 ; year:2018 ; pages:1-15 ; date:12.2018
Scientific reports ; 8, Heft 1 (27.7.2018), 1-15, 12.2018
- Classification
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Biowissenschaften, Biologie
- Creator
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Srivastava, Saurabh
- Contributor
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Katorcha, Elizaveta
Makarava, Natallia
Barrett, James P.
Loane, David J.
Baskakov, Ilia V.
SpringerLink (Online service)
- DOI
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10.1038/s41598-018-29720-z
- URN
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urn:nbn:de:101:1-2018092521422463206515
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:22 AM CEST
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Srivastava, Saurabh
- Katorcha, Elizaveta
- Makarava, Natallia
- Barrett, James P.
- Loane, David J.
- Baskakov, Ilia V.
- SpringerLink (Online service)
Other Objects (12)
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Microglia Increase Inflammatory Responses in iPSC-Derived Human BrainSpheres
Prion protein amino acid sequence influences formation of authentic synthetic PrPSc
PrPSc spreading patterns in the brain of sheep linked to different prion types
iPSC-derived PSEN2 (N141I) astrocytes and microglia exhibit a primed inflammatory phenotype
Propagation of PrPSc in mice reveals impact of aggregate composition on prion disease pathogenesis
Cellular trafficking of the pathogenic prion protein PrPSc and phenotypic characterisation of deletion mutants in the hydrophobic domain of the normal prion protein PrPC
High Prion and PrPSc Levels but Delayed Onset of Disease in Scrapie-Inoculated Mice Heterozygous for a Disrupted PrP Gene
Microglia are not required for prion-induced retinal photoreceptor degeneration
Prion infectivity is encoded exclusively within the structure of proteinase K-resistant fragments of synthetically generated recombinant PrPSc
Retrograde Transport by Clathrin-Coated Vesicles is Involved in Intracellular Transport of PrPSc in Persistently Prion-Infected Cells
C9orf72-ALS human iPSC microglia are pro-inflammatory and toxic to co-cultured motor neurons via MMP9
Screening anti-prion compounds and diagnosing prion diseases by amplifying PrPSc in vitro
Microglia Increase Inflammatory Responses in iPSC-Derived Human BrainSpheres
Prion protein amino acid sequence influences formation of authentic synthetic PrPSc
PrPSc spreading patterns in the brain of sheep linked to different prion types
iPSC-derived PSEN2 (N141I) astrocytes and microglia exhibit a primed inflammatory phenotype
Propagation of PrPSc in mice reveals impact of aggregate composition on prion disease pathogenesis
Cellular trafficking of the pathogenic prion protein PrPSc and phenotypic characterisation of deletion mutants in the hydrophobic domain of the normal prion protein PrPC
High Prion and PrPSc Levels but Delayed Onset of Disease in Scrapie-Inoculated Mice Heterozygous for a Disrupted PrP Gene
Microglia are not required for prion-induced retinal photoreceptor degeneration
Prion infectivity is encoded exclusively within the structure of proteinase K-resistant fragments of synthetically generated recombinant PrPSc
Retrograde Transport by Clathrin-Coated Vesicles is Involved in Intracellular Transport of PrPSc in Persistently Prion-Infected Cells
C9orf72-ALS human iPSC microglia are pro-inflammatory and toxic to co-cultured motor neurons via MMP9
Screening anti-prion compounds and diagnosing prion diseases by amplifying PrPSc in vitro
Microglia Increase Inflammatory Responses in iPSC-Derived Human BrainSpheres
Prion protein amino acid sequence influences formation of authentic synthetic PrPSc
PrPSc spreading patterns in the brain of sheep linked to different prion types
iPSC-derived PSEN2 (N141I) astrocytes and microglia exhibit a primed inflammatory phenotype
Propagation of PrPSc in mice reveals impact of aggregate composition on prion disease pathogenesis
Cellular trafficking of the pathogenic prion protein PrPSc and phenotypic characterisation of deletion mutants in the hydrophobic domain of the normal prion protein PrPC
High Prion and PrPSc Levels but Delayed Onset of Disease in Scrapie-Inoculated Mice Heterozygous for a Disrupted PrP Gene
Microglia are not required for prion-induced retinal photoreceptor degeneration
Prion infectivity is encoded exclusively within the structure of proteinase K-resistant fragments of synthetically generated recombinant PrPSc
Retrograde Transport by Clathrin-Coated Vesicles is Involved in Intracellular Transport of PrPSc in Persistently Prion-Infected Cells