Cargando…
Insights into the structure and activity of prototype foamy virus RNase H
BACKGROUND: RNase H is an endonuclease that hydrolyzes the RNA strand in RNA/DNA hybrids. Retroviral reverse transcriptases harbor a C-terminal RNase H domain whose activity is essential for viral replication. The RNase H degrades the viral genomic RNA after the first DNA strand is synthesized. Here...
Autores principales: | Leo, Berit, Hartl, Maximilian J, Schweimer, Kristian, Mayr, Florian, Wöhrl, Birgitta M |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3305377/ https://www.ncbi.nlm.nih.gov/pubmed/22325739 http://dx.doi.org/10.1186/1742-4690-9-14 |
Ejemplares similares
-
The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding
por: Leo, Berit, et al.
Publicado: (2012) -
Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases
por: Hartl, Maximilian J, et al.
Publicado: (2010) -
Impact of human immunodeficiency virus type 1 ribonuclease H inhibitors on the polymerase and RNase H function of foamy virus reverse transcriptase
por: Corona, Angela, et al.
Publicado: (2013) -
The prototype foamy virus protease is active independently of the integrase domain
por: Spannaus, Ralf, et al.
Publicado: (2012) -
Regulation of foamy virus protease activity by viral RNA
por: Hartl, Maximilian J, et al.
Publicado: (2011)