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RNA Biology|April 19, 2023
Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase PAnna Perederina, Igor Berezin, Andrey S KrasilnikovNucleic Acids Research|May 4, 2018
In vitro reconstitution and analysis of eukaryotic RNase P RNPsAnna Perederina, Igor Berezin, Andrey S KrasilnikovNucleic Acids Research|May 24, 2013
Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrateOlga Esakova, Anna Perederina, Igor Berezin, et al.RNA (New York, N.Y.)|July 3, 2015
Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA componentsRobert D Fagerlund, Anna Perederina, Igor Berezin, et al.RNA (New York, N.Y.)|December 22, 2010
Substrate recognition by ribonucleoprotein ribonuclease MRPOlga Esakova, Anna Perederina, Chao Quan, et al.RNA (New York, N.Y.)|February 15, 2012
Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactionsElena Khanova, Olga Esakova, Anna Perederina, et al.RNA (New York, N.Y.)|September 1, 2011
Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRPAnna Perederina, Elena Khanova, Chao Quan, et al.RNA Biology|June 5, 2010
The P3 domain of eukaryotic RNases P/MRP: making a protein-rich RNA-based enzymeAnna Perederina, Andrey S KrasilnikovMethods in Molecular Biology (Clifton, N.J.)|June 28, 2012
Crystallization of RNA-protein complexes: from synthesis and purification of individual components to crystalsAnna Perederina, Andrey S KrasilnikovNature Communications|July 12, 2020
Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRPAnna Perederina, Di Li, Hyunwook Lee, et al.Pageof 4