Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1471-2164
- 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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Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes ; volume:21 ; number:1 ; day:8 ; month:1 ; year:2020 ; pages:1-18 ; date:12.2020
BMC genomics ; 21, Heft 1 (8.1.2020), 1-18, 12.2020
- Creator
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Cascarina, Sean M.
Ross, Eric D.
- Contributor
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SpringerLink (Online service)
- DOI
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10.1186/s12864-019-6425-3
- URN
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urn:nbn:de:101:1-2020041404214515127561
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:45 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
- Cascarina, Sean M.
- Ross, Eric D.
- SpringerLink (Online service)
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Studies on pathogenic mechanisms of prion diseases and evaluation of prion strains properties
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Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior
Immune cell proteomes
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Frameworks for Large Scale Annotation of Proteins, Proteomes and Meta-proteomes
PrionScan: an online database of predicted prion domains in complete proteomes
Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains
Prion-like Domains in Eukaryotic Viruses
A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes
Studies on pathogenic mechanisms of prion diseases and evaluation of prion strains properties
Studies on pathogenic mechanisms of prion diseases and evaluation of prion strains properties
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Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior
Immune cell proteomes
Nε-Carboxymethyl Modification of Lysine Residues in Pathogenic Prion Isoforms
The role of prion-like domains in plant temperatur sensing