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Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2016, v. 72, n. 2, p. 112, doi. 10.1107/S2053230X15024498
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Structural insights into the mechanism of the DEAH-box RNA helicase Prp43.
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- eLife, 2017, p. 1, doi. 10.7554/eLife.21510
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The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP- intron interaction.
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- eLife, 2016, p. 1, doi. 10.7554/eLife.15564
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Regulation of Prp43-mediated disassembly of spliceosomes by its cofactors Ntr1 and Ntr2.
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- Nucleic Acids Research, 2017, v. 45, n. 7, p. 4068, doi. 10.1093/nar/gkw1225
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Combined in silico and experimental identification of the Pyrococcus abyssi H/ACA sRNAs and their target sites in ribosomal RNAs.
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- Nucleic Acids Research, 2008, v. 36, n. 8, p. 2459, doi. 10.1093/nar/gkn077
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- Article
Identification of determinants in the protein partners aCBF5 and aNOP10 necessary for the tRNA:Ψ55-synthase and RNA-guided RNA:Ψ-synthase activities.
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- Nucleic Acids Research, 2007, v. 35, n. 16, p. 5610, doi. 10.1093/nar/gkm606
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Comparative Study of Two Box H/ACA Ribonucleoprotein Pseudouridine-Synthases: Relation between Conformational Dynamics of the Guide RNA, Enzyme Assembly and Activity.
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- PLoS ONE, 2013, v. 8, n. 7, p. 1, doi. 10.1371/journal.pone.0070313
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Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5–aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity.
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- Nucleic Acids Research, 2006, v. 34, n. 3, p. 826, doi. 10.1093/nar/gkj482
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- Article