DED1 Antibody

1. Ded1p affects translation initiation by controlling the use of near-cognate initiation codons that are proximal to mRNA structure in 5' untranslated regions PMID: 29950728
2. Oligomerization represents a previously unappreciated level of regulation for Ded1p DEAD-box helicase activities. PMID: 26212457
3. Individual members of the Ded1/DDX3 subfamily perform multiple functions in RNA metabolism in both nucleus and cytoplasm. [review] PMID: 25039764
4. The authors conclude that Ded1 is an mRNP cofactor of the cap complex that may function to remodel the different mRNPs and thereby regulate the expression of the mRNAs. PMID: 25013175
5. DEAD-box helicase Ded1p forms exceptionally long-lived complexes with RNA PMID: 24367975
6. Ded1p and glyceraldehyde-3-phosphate dehydrogenase enhance tombusvirus (+)-strand synthesis PMID: 22359508
7. Ded1 is a translation initiation factor that assembles and remodels an intermediate complex in translation initiation. PMID: 21925384
8. motif III and the binding energy of gamma-PO(4) of ATP are used to coordinate motifs I, II, and VI and the two RecA-like domains to create a high-affinity single-stranded RNA binding site PMID: 20026132
9. DED1 establishes an ATP-dependent steady state between unwinding & annealing, which enables the enzyme to modulate balance between the 2 opposing activities through ATP & ADP levels, by facilitating not only disruption but also formation of RNA duplexes. PMID: 16216083
10. In vitro measurements of DED1 disassembly of model ribonucleoproteins were made. PMID: 16556937
11. Ded1 uses the single-stranded region to gain access to the duplex, strand separation is directly initiated from the duplex region and no covalent connection between the single strand and the duplex region is required. PMID: 17072313
12. Ded1p is a bifunctional protein that can affect both translation initiation and P-body formation. PMID: 18162578
13. Intragenic suppressors of the F405L mutation in Ded1 mapped close to regions of the protein involved in ATP or RNA binding in DEAD-box crystal structures, which implicated a defect at this level. PMID: 18332124

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KEGG: sce:YOR204W

STRING: 4932.YOR204W