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• RNA unwinding activity of the hepatitis C virus NS3 helicase is modulated by the NS5B polymerase.

  2008cited by this paper
• A role for ubiquitin in the spliceosome assembly pathway

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• The long unwinding road of RNA helicases.

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• Exon ligation is proofread by the DExD/H-box ATPase Prp22p

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• Pre-mRNA splicing and retinitis pigmentosa.

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• Mutations in PRP43 that uncouple RNA-dependent NTPase activity and pre-mRNA splicing function.

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• Association of PAP-1 and Prp3p, the products of causative genes of dominant retinitis pigmentosa, in the tri-snRNP complex.

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• Mutations in HPRP3, a third member of pre-mRNA splicing factor genes, implicated in autosomal dominant retinitis pigmentosa.

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• Hierarchical, clustered protein interactions with U4/U6 snRNA: a biochemical role for U4/U6 proteins

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• The ribosomal translocase homologue Snu114p is involved in unwinding U4/U6 RNA during activation of the spliceosome

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• An RNA switch at the 5' splice site requires ATP and the DEAD box protein Prp28p.

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• RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2.

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• The DEAH‐box protein PRP22 is an ATPase that mediates ATP‐dependent mRNA release from the spliceosome and unwinds RNA duplexes

  1998cited by this paper
• Prp22, a DExH‐box RNA helicase, plays two distinct roles in yeast pre‐mRNA splicing

  1998cited by this paper
• Identification of novel genes required for yeast pre-mRNA splicing by means of cold-sensitive mutations.

  1996cited by this paper
• The HeLa 200 kDa U5 snRNP‐specific protein and its homologue in Saccharomyces cerevisiae are members of the DEXH‐box protein family of putative RNA helicases.

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• An RNA-dependent ATPase associated with U2/U6 snRNAs in pre-mRNA splicing

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• Specificity of Prp24 binding to RNA: a role for Prp24 in the dynamic interaction of U4 and U6 snRNAs.

  1995cited by this paper
• A mechanism to enhance mRNA splicing fidelity: the RNA-dependent ATPase Prp16 governs usage of a discard pathway for aberrant lariat intermediates.

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• A novel base-pairing interaction between U2 and U6 snRNAs suggests a mechanism for the catalytic activation of the spliceosome.

  1992cited by this paper
• In vitro assembly of yeast U6 snRNP: a functional assay.

  1989cited by this paper
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  1988cited by this paper
• A trans-acting suppressor restores splicing of a yeast intron with a branch point mutation.

  1987cited by this paper

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