M
Markus T. Bohnsack
Researcher at University of Göttingen
Publications - 85
Citations - 7397
Markus T. Bohnsack is an academic researcher from University of Göttingen. The author has contributed to research in topics: Ribosome & RNA. The author has an hindex of 38, co-authored 72 publications receiving 5646 citations. Previous affiliations of Markus T. Bohnsack include Heidelberg University & University of Edinburgh.
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Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates nuclear export of pre-miRNAs
TL;DR: Nuclear export of pre-miRNAs is studied and it is shown that the process is saturable and thus carrier-mediated, and that exportin 5 interacts with double-stranded RNA in a sequence-independent manner.
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Tuning the ribosome: The influence of rRNA modification on eukaryotic ribosome biogenesis and function
Katherine E. Sloan,Ahmed S. Warda,Sunny Sharma,Karl-Dieter Entian,Denis L. J. Lafontaine,Markus T. Bohnsack +5 more
TL;DR: Changes in the rRNA modification pattern have been observed in response to environmental changes, during development, and in disease, which suggests that rRNA modifications may contribute to the translational control of gene expression.
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Human METTL16 is a N6‐methyladenosine (m6A) methyltransferase that targets pre‐mRNAs and various non‐coding RNAs
Ahmed S. Warda,Jens Kretschmer,Philipp Hackert,Christof Lenz,Christof Lenz,Henning Urlaub,Henning Urlaub,Claudia Höbartner,Katherine E. Sloan,Markus T. Bohnsack +9 more
TL;DR: It is demonstrated that METTL16 is responsible for N6‐methylation of A43 of the U6 snRNA and the early U6 biogenesis factors La, LARP7 and the methylphosphate capping enzyme MEPCE asMETTL16 interaction partners.
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The box C/D and H/ACA snoRNPs: key players in the modification, processing and the dynamic folding of ribosomal RNA.
TL;DR: High resolution structures of the archaeal C/D and H/ACA sRNPs have not only provided a detailed understanding of the molecular architecture of these complexes but also produced key insights into substrate binding and product release.
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The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112.
Nhan van Tran,Felix G.M. Ernst,Ben R Hawley,Christiane Zorbas,Nathalie Ulryck,Philipp Hackert,Katherine E. Bohnsack,Markus T. Bohnsack,Samie R. Jaffrey,Marc Graille,Denis L. J. Lafontaine +10 more
TL;DR: It is proposed that METTL5–TRMT112 acts by extruding the adenosine to be modified from a double-stranded nucleic acid, supporting that its RNA-binding mode differs distinctly from that of other m6A RNA methyltransferases.