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Andrey S Krasilnikov

Showing results (11-20 of 24) with videos related to

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Nucleic 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.)|January 21, 2010
Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein componentsQiaosheng Lu, Sara Wierzbicki, Andrey S Krasilnikov, et al.
RNA (New York, N.Y.)|December 22, 2010
Substrate recognition by ribonucleoprotein ribonuclease MRPOlga Esakova, Anna Perederina, Chao Quan, et al.
The EMBO Journal|January 16, 2010
Eukaryotic ribonucleases P/MRP: the crystal structure of the P3 domainAnna Perederina, Olga Esakova, 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.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|January 9, 2010
Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast ribonuclease MRP in a complex with RNase P/MRP protein components Pop6 and Pop7Anna Perederina, Olga Esakova, Chao Quan, et al.
RNA (New York, N.Y.)|June 27, 2008
Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymesOlga Esakova, Anna Perederina, Chao Quan, et al.
RNA (New York, N.Y.)|August 25, 2007
Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAsAnna Perederina, Olga Esakova, Hasan Koc, et al.
Nature|August 23, 2005
Crystal structure of the RNA component of bacterial ribonuclease PAlfredo Torres-Larios, Kerren K Swinger, Andrey S Krasilnikov, et al.
Pageof 3

Showing results (11-20 of 24) with videos related to

Sort By:
Pageof 3
Nucleic 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.)|January 21, 2010
Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein componentsQiaosheng Lu, Sara Wierzbicki, Andrey S Krasilnikov, et al.
RNA (New York, N.Y.)|December 22, 2010
Substrate recognition by ribonucleoprotein ribonuclease MRPOlga Esakova, Anna Perederina, Chao Quan, et al.
The EMBO Journal|January 16, 2010
Eukaryotic ribonucleases P/MRP: the crystal structure of the P3 domainAnna Perederina, Olga Esakova, 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.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|January 9, 2010
Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast ribonuclease MRP in a complex with RNase P/MRP protein components Pop6 and Pop7Anna Perederina, Olga Esakova, Chao Quan, et al.
RNA (New York, N.Y.)|June 27, 2008
Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymesOlga Esakova, Anna Perederina, Chao Quan, et al.
RNA (New York, N.Y.)|August 25, 2007
Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAsAnna Perederina, Olga Esakova, Hasan Koc, et al.
Nature|August 23, 2005
Crystal structure of the RNA component of bacterial ribonuclease PAlfredo Torres-Larios, Kerren K Swinger, Andrey S Krasilnikov, et al.
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