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pro vyhledávání: '"Hartl, Maximilian J"'
Publikováno v:
In Journal of Molecular Biology 1 August 2008 381(1):141-149
Autor:
Kretzschmar, Benedikt, Nowrouzi, Ali, Hartl, Maximilian J., Gärtner, Kathleen, Wiktorowicz, Tatiana, Herchenröder, Ottmar, Kanzler, Sylvia, Rudolph, Wolfram, Mergia, Ayalew, Wöhrl, Birgitta, Rethwilm, Axel
Publikováno v:
In Virology 2008 370(1):151-157
Autor:
Hartl Maximilian J, Bodem Jochen, Jochheim Fabian, Rethwilm Axel, Rösch Paul, Wöhrl Birgitta M
Publikováno v:
Retrovirology, Vol 8, Iss Suppl 1, p A228 (2011)
Externí odkaz:
https://doaj.org/article/78693bd9c00d407cafe3ba7243ce7009
Publikováno v:
Retrovirology, Vol 9, Iss 1, p 73 (2012)
Abstract Background The ribonuclease H (RNase H) domains of retroviral reverse transcriptases play an essential role in the replication cycle of retroviruses. During reverse transcription of the viral genomic RNA, an RNA/DNA hybrid is created whose R
Externí odkaz:
https://doaj.org/article/617d873805e040d3adf699af5ecb8e8e
Publikováno v:
Retrovirology, Vol 9, Iss 1, p 41 (2012)
Abstract Background Recently, contradictory results on foamy virus protease activity were published. While our own results indicated that protease activity is regulated by the viral RNA, others suggested that the integrase is involved in the regulati
Externí odkaz:
https://doaj.org/article/6326746895df4583b81d65656527835f
Publikováno v:
Retrovirology, Vol 9, Iss 1, p 14 (2012)
Abstract 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 g
Externí odkaz:
https://doaj.org/article/7b0939a2ae374d1fb00830a3a70cfb32
Publikováno v:
Retrovirology, Vol 7, Iss 1, p 5 (2010)
Abstract Background The foamy virus Pol protein is translated independently from Gag using a separate mRNA. Thus, in contrast to orthoretroviruses no Gag-Pol precursor protein is synthesized. Only the integrase domain is cleaved off from Pol resultin
Externí odkaz:
https://doaj.org/article/a8f7c11696724c2291dc382879ca6a88
Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases.
Autor:
Hartl, Maximilian J.1, Mayr, Florian1, Rethwilm, Axel2, Wöhrl, Birgitta M.1 birgitta.woehrl@uni-bayreuth.de
Publikováno v:
Retrovirology. 2010, Vol. 7, p5-14. 10p.
Publikováno v:
Retrovirology, Vol 9, Iss 1, p 41 (2012)
Retrovirology
Retrovirology
Background Recently, contradictory results on foamy virus protease activity were published. While our own results indicated that protease activity is regulated by the viral RNA, others suggested that the integrase is involved in the regulation of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::5ec51524edf1ad6699966a93ee0099c6
https://nbn-resolving.org/urn:nbn:de:bvb:20-opus-75370
https://nbn-resolving.org/urn:nbn:de:bvb:20-opus-75370
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