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Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12128/17172
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dc.contributor.authorMarzec, Marek-
dc.date.accessioned2020-11-19T11:56:05Z-
dc.date.available2020-11-19T11:56:05Z-
dc.date.issued2020-
dc.identifier.citation"PLOS Genetics" iss. 11 (2020), art. no. e1009058pl_PL
dc.identifier.issn1553-7390-
dc.identifier.issn1553-7404-
dc.identifier.urihttp://hdl.handle.net/20.500.12128/17172-
dc.description.abstractUncovering the mechanisms that recognise a microRNA (miRNA) target is 1 of the biggest challenges because the Ago–miRNA complex is able to overcome different derogations of complementarity when binding targets. However, the recently solved crystallographic structure of Argonaute2 (Ago2) and a high-throughput analysis that used repurposed sequencing techniques has brought us closer to achieving this goal.pl_PL
dc.language.isoenpl_PL
dc.rightsUznanie autorstwa 3.0 Polska*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/pl/*
dc.subjectMicroRNAspl_PL
dc.subjectCrystallization seedingpl_PL
dc.subjectNucleotidespl_PL
dc.subjectNucleotide sequencingpl_PL
dc.subjectBinding analysispl_PL
dc.subjectCrystal structurepl_PL
dc.subjectMessenger RNApl_PL
dc.subjectRNA structurepl_PL
dc.titleNew insights into the function of mammalian Argonaute2pl_PL
dc.typeinfo:eu-repo/semantics/articlepl_PL
dc.identifier.doi10.1371/journal.pgen.1009058-
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