Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Maximilian J. Hartl"'
Autor:
Jonas Schubert, Maximilian J. Hartl, Christian Goldhahn, Lucas P. Kreuzer, Max J. Männel, Munish Chanana
Publikováno v:
ACS Catalysis. 7:1664-1672
In this work, we show that different enzymes, such as horseradish peroxidase (HRP), glucose oxidase, laccase, and catalase, can be directly immobilized onto plasmonic gold nanoparticles (NPs) and superparamagnetic iron oxide NPs simply via unspecific
Autor:
Kristian Schweimer, Christian Seutter von Loetzen, Olivia Hartl-Spiegelhauer, Wilfried Schwab, Paul Rösch, Thomas Hoffmann, Maximilian J. Hartl
Publikováno v:
Biochemical Journal. 457:379-390
The major birch pollen allergen Bet v 1 is the main elicitor of airborne type I allergies and belongs to the PR-10 family (pathogenesis-related proteins 10). Bet v 1 is the most extensively studied allergen, and is well characterized at a biochemical
Autor:
Jessica Schmitt, Berit Leo, Daniel Peter, Anna Schneider, Franziska Richter, Birgitta M. Wöhrl, Maximilian J. Hartl, Paul Rösch
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 82:375-385
Reverse transcriptases (RTs) are pivotal in the life cycle of retroviruses and convert the genomic viral RNA into double-stranded DNA. The RT polymerase domain is subdivided into fingers, palm, thumb, and the connection subdomain, which links the pol
Autor:
Anne Frohn, Axel Rethwilm, Maximilian J. Hartl, Ali Nowrouzi, Benedikt Kretzschmar, Birgitta M. Wöhrl
Publikováno v:
Nucleic Acids Research
Azidothymidine (AZT, zidovudine) is one of the few nucleoside inhibitors known to inhibit foamy virus replication. We have shown previously that up to four mutations in the reverse transcriptase gene of simian foamy virus from macaque (SFVmac) are ne
Publikováno v:
Journal of Virology. 87:7774-7776
In contrast to orthoretroviruses, processing of foamy viral p71 Gag is limited to a single cleavage site. Nevertheless, Gag maturation is essential for infectivity, but deletion of p3 results in a modest drop in infectivity. Here, we show that Gag pr
Autor:
Stefan Vieths, Hanna Berkner, Lothar Vogel, Felix Husslik, Andreas Reuter, Dirk Schiller, Jonas Lidholm, Christian Seutter von Loetzen, Stefanie Randow, Paul Rösch, Maximilian J. Hartl, Michaela Gubesch, Barbara Ballmer-Weber
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 10, p e111691 (2014)
PLoS ONE, Vol 9, Iss 10, p e111691 (2014)
Background: Birch pollen-allergic subjects produce polyclonal cross-reactive IgE antibodies that mediate pollen-associated food allergies. The major allergen Bet v 1 and its homologs in plant foods bind IgE in their native protein conformation. Infor
Autor:
Felix Husslik, Andreas Reuter, Christian Seutter von Loetzen, Jörg Kleine-Tebbe, Regina Treudler, Lothar Vogel, Michaela Gubesch, Barbara Ballmer-Weber, Diana Mittag, Thomas Holzhauser, Maximilian J. Hartl, Jan-Christoph Simon, Paul Rösch, Kay-Martin Hanschmann, Dirk Schiller, Stefan Vieths
Publikováno v:
Clinical and Translational Allergy
Individuals with birch pollinosis may show allergic reactions after consumption of soybean-containing food. This is caused by cross-reaction of IgE directed against the major birch pollen allergen Bet v 1 with the structurally homologous allergen Gly
Publikováno v:
Biomolecular NMR Assignments. 1:175-177
The backbone and side chain assignments of the retroviral aspartate protease from Simian Foamy Virus from macaques (SFVmac) have been determined by triple resonance NMR techniques.
Autor:
Anna, Schneider, Daniel, Peter, Jessica, Schmitt, Berit, Leo, Franziska, Richter, Paul, Rösch, Birgitta M, Wöhrl, Maximilian J, Hartl
Publikováno v:
Proteins. 82(3)
Reverse transcriptases (RTs) are pivotal in the life cycle of retroviruses and convert the genomic viral RNA into double-stranded DNA. The RT polymerase domain is subdivided into fingers, palm, thumb, and the connection subdomain, which links the pol
Publikováno v:
Retrovirology, Vol 9, Iss 1, p 14 (2012)
Retrovirology
Retrovirology
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 RN