The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1742-4690
- 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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The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding ; volume:9 ; number:1 ; day:10 ; month:9 ; year:2012 ; pages:1-11 ; date:12.2012
Retrovirology ; 9, Heft 1 (10.9.2012), 1-11, 12.2012
- Creator
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Leo, Berit
- Contributor
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Schweimer, Kristian
Rösch, Paul
Hartl, Maximilian J.
Wöhrl, Birgitta M.
SpringerLink (Online service)
- DOI
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10.1186/1742-4690-9-73
- URN
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urn:nbn:de:1111-2016080721597
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:44 AM CEST
Data provider
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Associated
- Leo, Berit
- Schweimer, Kristian
- Rösch, Paul
- Hartl, Maximilian J.
- Wöhrl, Birgitta M.
- SpringerLink (Online service)
Other Objects (12)
Insights into the structure and activity of prototype foamy virus RNase H
Foamy Virus RNase H - Aktivität, Struktur und Funktion
The prototype foamy virus protease is active independently of the integrase domain
The prototype foamy virus protease is active independently of the integrase domain
PREB inhibits the replication of prototype foamy virus by affecting its transcription
Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases
Prototype foamy virus elicits complete autophagy involving the ER stress-related UPR pathway
Antiviral role of IFITM3 in prototype foamy virus infection
A nuclear export signal within the structural Gag protein is required for prototype foamy virus replication
Prototype foamy virus gag nuclear localization and glycine-arginine box functions revised
The Regulation of Prototype Foamy Virus 5′Long Terminal Repeats and Internal Promoter by Endogenous Transcription Factors
The cooperative function of arginine residues in the Prototype Foamy Virus Gag C-terminus mediates viral and cellular RNA encapsidation
Insights into the structure and activity of prototype foamy virus RNase H
Foamy Virus RNase H - Aktivität, Struktur und Funktion
The prototype foamy virus protease is active independently of the integrase domain
The prototype foamy virus protease is active independently of the integrase domain
PREB inhibits the replication of prototype foamy virus by affecting its transcription
Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases
Prototype foamy virus elicits complete autophagy involving the ER stress-related UPR pathway
Antiviral role of IFITM3 in prototype foamy virus infection
A nuclear export signal within the structural Gag protein is required for prototype foamy virus replication
Prototype foamy virus gag nuclear localization and glycine-arginine box functions revised
The Regulation of Prototype Foamy Virus 5′Long Terminal Repeats and Internal Promoter by Endogenous Transcription Factors
The cooperative function of arginine residues in the Prototype Foamy Virus Gag C-terminus mediates viral and cellular RNA encapsidation
Insights into the structure and activity of prototype foamy virus RNase H
Foamy Virus RNase H - Aktivität, Struktur und Funktion
The prototype foamy virus protease is active independently of the integrase domain
The prototype foamy virus protease is active independently of the integrase domain
PREB inhibits the replication of prototype foamy virus by affecting its transcription
Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases
Prototype foamy virus elicits complete autophagy involving the ER stress-related UPR pathway
Antiviral role of IFITM3 in prototype foamy virus infection
A nuclear export signal within the structural Gag protein is required for prototype foamy virus replication
Prototype foamy virus gag nuclear localization and glycine-arginine box functions revised
The Regulation of Prototype Foamy Virus 5′Long Terminal Repeats and Internal Promoter by Endogenous Transcription Factors