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The DEAD-box protein DDX43 (HAGE) is a dual RNA-DNA helicase and has a K-homology domain required for full nucleic acid unwinding activity - Journal of Biological Chemistry
DEAD-Box Proteins from Escherichia coli Exhibit Multiple ATP-Independent Activities | Journal of Bacteriology
RCSB PDB - 3BER: Human DEAD-box RNA-helicase DDX47, conserved domain I in complex with AMP
Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa: Cell
Emerging molecular functions and novel roles for the DEAD-box protein Dbp5/DDX19 in gene expression | SpringerLink
ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding | PNAS
A Motif Unique to the Human Dead-Box Protein DDX3 Is Important for Nucleic Acid Binding, ATP Hydrolysis, RNA/DNA Unwinding and HIV-1 Replication
Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa: Cell
Selective targeting of the DEAD-box RNA helicase eukaryotic initiation factor (eIF) 4A by natural products - Natural Product Reports (RSC Publishing)
Modulation of RNA condensation by the DEAD-box protein eIF4A | bioRxiv
RCSB PDB - 4NHO: Structure of the spliceosomal DEAD-box protein Prp28
DEAD box - Wikipedia
IJMS | Free Full-Text | Roles of Organellar RNA-Binding Proteins in Plant Growth, Development, and Abiotic Stress Responses | HTML
Dbp9p, a Member of the DEAD Box Protein Family, Exhibits DNA Helicase Activity* - Journal of Biological Chemistry
Human DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 3, X-Linked (DDX3X) Protein (His tag), Recombinant | ABIN3092089