H
Hanna Kratzat
Researcher at Center for Integrated Protein Science Munich
Publications - 13
Citations - 1040
Hanna Kratzat is an academic researcher from Center for Integrated Protein Science Munich. The author has contributed to research in topics: Ribosome & Translation (biology). The author has an hindex of 5, co-authored 10 publications receiving 431 citations. Previous affiliations of Hanna Kratzat include Ludwig Maximilian University of Munich.
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Journal ArticleDOI
Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2.
Matthias Thoms,Robert Buschauer,Michael Ameismeier,Lennart Koepke,Timo Denk,Maximilian Hirschenberger,Hanna Kratzat,Manuel Hayn,Timur Mackens-Kiani,Jingdong Cheng,Jan Hendrik Straub,Christina M. Stürzel,Thomas Fröhlich,Otto Berninghausen,Thomas Becker,Frank Kirchhoff,Konstantin M. J. Sparrer,Roland Beckmann +17 more
TL;DR: Structural characterization of the inhibitory mechanism of Nsp1 may aid structure-based drug design against SARS-CoV-2 and effectively blocks retinoic acid–inducible gene I–dependent innate immune responses that would otherwise facilitate clearance of the infection.
Posted ContentDOI
Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2
Matthias Thoms,Robert Buschauer,Michael Ameismeier,Lennart Koepke,Timo Denk,Maximilian Hirschenberger,Hanna Kratzat,Manuel Hayn,Timur Mackens-Kiani,Jingdong Cheng,Christina M. Stürzel,Thomas Fröhlich,Otto Berninghausen,Thomas Becker,Frank Kirchhoff,Konstantin M. J. Sparrer,Roland Beckmann +16 more
TL;DR: It is shown that Nsp1 from SARS-CoV-2 binds to 40S and 80S ribosomes, resulting in shutdown of capped mRNA translation both in vitro and in cells, which effectively blocks RIG-I-dependent innate immune responses that would otherwise facilitate clearance of the infection.
Journal ArticleDOI
Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes.
Jennifer N. Wells,Robert Buschauer,Timur Mackens-Kiani,Katharina Best,Hanna Kratzat,Otto Berninghausen,Thomas Becker,Wendy V. Gilbert,Jingdong Cheng,Roland Beckmann +9 more
TL;DR: A model in which Lso2 facilitates rapid translation reactivation by stabilizing the recycling-competent state of inactive ribosomes is proposed, which allows accommodation of the duplication of multilocus region 34 protein (Dom34)-dependent ribosome recycling system.
Posted ContentDOI
Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes
Jennifer N. Wells,Robert Buschauer,Timur Mackens-Kiani,Katharina Best,Hanna Kratzat,Otto Berninghausen,Thomas Becker,Wendy V. Gilbert,Jingdong Cheng,Roland Beckmann +9 more
TL;DR: A model in which Lso2 facilitates rapid translation reactivation by stabilizing the recycling-competent state of inactive ribosomes is proposed, which allows accommodation of the Dom34-dependent ribosome recycling system.
Journal ArticleDOI
Ribosome collisions induce mRNA cleavage and ribosome rescue in bacteria
Kazuki Saito,Hanna Kratzat,Annabelle Campbell,Robert Buschauer,A. Maxwell Burroughs,Otto Berninghausen,L. Aravind,Rachel Green,Roland Beckmann,Allen R. Buskirk +9 more
TL;DR: In this paper , the authors used a genetic screen in Escherichia coli and discovered a new rescue factor that has endonuclease activity, called SmrB, which cleaves mRNAs upstream of stalled ribosomes.