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The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases
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Mechanisms of helicases
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Structural basis for RNA unwinding by the DEAD-box protein Drosophila vasa
T Sengoku et al.
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A DEAD-box protein alone promotes group II intron splicing and reverse splicing by acting as an RNA chaperone
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Repositioning of the reaction intermediate within the catalytic center of the spliceosome
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YxiN is a modular protein combining a DExD/H core and a specific RNA-binding domain
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ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1
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The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function
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Studies on three E-coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases
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The carboxy-terminal domain of the DExD/H protein YxiN is sufficient to confer specificity for 23 S rRNA
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A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
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Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA
KJ Polach et al.
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Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA
CM Diges et al.
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The Escherichia coli DEAD protein DbpA recognizes a small RNA hairpin in 23S rRNA
CA Tsu et al.
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Further characterization of the helicase activity of eIF4A - Substrate specificity
GW Rogers et al.
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Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD box splicing factor
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