| SUMOylation modulates the function of DDX19 in mRNA export. | SUMOylation modulates the function of DDX19 in mRNA export.
Banerjee P, Markande S, Kalarikkal M, Joseph J. | 03/12/2022 |
| Translation mediated by the nuclear cap-binding complex is confined to the perinuclear region via a CTIF-DDX19B interaction. | Translation mediated by the nuclear cap-binding complex is confined to the perinuclear region via a CTIF-DDX19B interaction.
Park Y, Park J, Hwang HJ, Kim L, Jeong K, Song HK, Rufener SC, Mühlemann O, Kim YK., Free PMC Article | 10/9/2021 |
| Emerging molecular functions and novel roles for the DEAD-box protein Dbp5/DDX19 in gene expression. | Emerging molecular functions and novel roles for the DEAD-box protein Dbp5/DDX19 in gene expression.
Arul Nambi Rajan A, Montpetit B., Free PMC Article | 04/3/2021 |
| Dbp5/DDX19 between Translational Readthrough and Nonsense Mediated Decay. | Dbp5/DDX19 between Translational Readthrough and Nonsense Mediated Decay.
Beißel C, Grosse S, Krebber H., Free PMC Article | 11/21/2020 |
| Results found that Nup159 did not accelerate ADP release, while Gle1 actually slowed it independently of Mg(2+) which is not consistent with Nup159 acting as a nucleotide exchange factor to promote ADP release and Dbp5 ATPase cycling. Instead, in the presence of Nup159, the interaction between Gle1 and ADP-bound Dbp5 was found more reduced, suggesting that Nup159 alters the Dbp5-Gle1 to aid Gle1 release from Dbp5. | Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP Release.
Wong EV, Gray S, Cao W, Montpetit R, Montpetit B, De La Cruz EM., Free PMC Article | 06/22/2019 |
| These results imply that DBP5, GLE1 and IP6 have a conserved and individual function in the cytoplasmic mRNA expression. Variations in phenotype are due to the difference in each function of DBP5, GLE1 and IPPK in intracellular mRNA metabolism. | Depletion of mRNA export regulator DBP5/DDX19, GLE1 or IPPK that is a key enzyme for the production of IP6, resulting in differentially altered cytoplasmic mRNA expression and specific cell defect.
Okamura M, Yamanaka Y, Shigemoto M, Kitadani Y, Kobayashi Y, Kambe T, Nagao M, Kobayashi I, Okumura K, Masuda S., Free PMC Article | 08/4/2018 |
| DDX19 interacts with pre-termination complexes (preTCs) in a nucleotide-dependent manner. Furthermore, DDX19 increases the efficiency of termination complex (TC) formation and the peptide release in the presence of eukaryotic release factors. DDX19 also stabilizes ribosome complexes with translation elongation factors eEF1 and eEF2. | RNA helicase DDX19 stabilizes ribosomal elongation and termination complexes.
Mikhailova T, Shuvalova E, Ivanov A, Susorov D, Shuvalov A, Kolosov PM, Alkalaeva E., Free PMC Article | 10/7/2017 |
| Ddx19 is an RNA export factor required for nuclear import of the SRF coactivator MKL1 | RNA export factor Ddx19 is required for nuclear import of the SRF coactivator MKL1.
Rajakylä EK, Viita T, Kyheröinen S, Huet G, Treisman R, Vartiainen MK., Free PMC Article | 02/13/2016 |
| Dbp5, Gle1-IP6 and Nup159: a working model for mRNP export. | Dbp5, Gle1-IP6 and Nup159: a working model for mRNP export.
Folkmann AW, Noble KN, Cole CN, Wente SR., Free PMC Article | 05/26/2012 |
| Results describe the crystal structures of human DDX19, a DEXD/H-box protein, in its open and closed cleft conformations. | The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch.
Collins R, Karlberg T, Lehtiö L, Schütz P, van den Berg S, Dahlgren LG, Hammarström M, Weigelt J, Schüler H., Free PMC Article | 01/21/2010 |
| Using in vitro assays, the authors demonstrate that NUP214 decreases both the RNA binding and ATPase activities of DBP5. | The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner.
von Moeller H, Basquin C, Conti E. | 01/21/2010 |
| identification and characterization of a gene coding a novel isoform | Identification and characterization of a gene coding a novel isoform of DEAD-box protein.
Yin L, Li J, Zhu H, Lin M, Cheng L, Wang Y, Zhou Z, Sha J. | 01/21/2010 |