Peter J. Lukavsky
Central European Institute of Technology
6 Papers
13 Citations
Peter J. Lukavsky is an academic researcher from Central European Institute of Technology. The author has contributed to research in topics: RNA & Biology. The author has an hindex of 5, co-authored 6 publications.
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Papers
Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
Peter J. Lukavsky,Dalia Daujotyte,Dalia Daujotyte,James R. Tollervey,James R. Tollervey,Jernej Ule,Jernej Ule,Cristiana Stuani,Emanuele Buratti,Francisco E. Baralle,Fred F. Damberger,Frédéric H.-T. Allain +11 more
TL;DR: This work solved the solution structure of the TDP-43 RRMs in complex with UG-rich RNA and revealed not only how T DP-43 recognizes UG repeats but also how RNA binding–dependent inter-RRM interactions are crucial for TDP
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Strategy for automated NMR resonance assignment of RNA: application to 48-nucleotide K10
TL;DR: The automated analysis of the APSY data led to highly accurate and precise 3- to 4-dimensional peak lists which provided a reliable basis for the subsequent sequence-specific resonance assignment with the algorithm FLYA and resulted in the fully automated resonance assignment of more than 80 % of the resonances of the 13C–1H moieties.
Efficient large-scale preparation and purification of short single-stranded RNA oligonucleotides
TL;DR: A fast and robust method for large-scale preparation and purification of short ssRNA oligonucleotides for biochemical, biophysical, and structural studies and for high-resolution NMR structure determination of RNA-protein complexes is presented.
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Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition
Deepak Kumar Yadav,Dagmar Zigáčková,Maria Zlobina,Tomáš Klumpler,Christelle Beaumont,Monika Kubíčková,Štěpánka Vaňáčová,Peter J. Lukavsky +7 more
TL;DR: The structure of the ARF1 SBS–STAU1 complex uncovers target recognition by ST AU1 and reveals how STAU1 recognizes minor groove features in dsRNA relevant for target selection.
NMR solution structure determination of large RNA-protein complexes.
TL;DR: Approaches for the design of RNA-protein complexes for NMR structural studies, established and emerging isotope and segmental labeling schemes suitable for large RNPs and how to gain distance restraints from NOEs, PREs and EPR and orientational information from RDCs and SAXS/SANS in such systems are discussed.