scholarly article | Q13442814 |
P819 | ADS bibcode | 2019NatCo..10.3085S |
P356 | DOI | 10.1038/S41467-019-11083-2 |
P932 | PMC publication ID | 6626043 |
P698 | PubMed publication ID | 31300642 |
P50 | author | Xinhua Ji | Q52356987 |
P2093 | author name string | He Song | |
P2860 | cites work | The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA | Q24300447 |
The Protein Data Bank | Q24515306 | ||
Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing | Q24537302 | ||
ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding | Q24646651 | ||
PHENIX: a comprehensive Python-based system for macromolecular structure solution | Q24654617 | ||
Multifunctional DDX3: dual roles in various cancer development and its related signaling pathways | Q26749143 | ||
DDX3, a potential target for cancer treatment | Q26779054 | ||
DEAD-box helicases as integrators of RNA, nucleotide and protein binding | Q26999638 | ||
Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain | Q27644316 | ||
Crystal structure of conserved domains 1 and 2 of the human DEAD-box helicase DDX3X in complex with the mononucleotide AMP | Q27646741 | ||
The DEXD/H-box RNA Helicase DDX19 Is Regulated by an -Helical Switch | Q27653950 | ||
Structure of the Yeast DEAD Box Protein Mss116p Reveals Two Wedges that Crimp RNA | Q27657414 | ||
A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export | Q27667333 | ||
Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p | Q27671834 | ||
HKL-3000: the integration of data reduction and structure solution--from diffraction images to an initial model in minutes | Q27860502 | ||
Coot: model-building tools for molecular graphics | Q27860505 | ||
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Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function | Q28289911 | ||
Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa | Q29616424 | ||
New developments in the ATSAS program package for small-angle scattering data analysis | Q29616858 | ||
X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution | Q29619405 | ||
CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates | Q29642130 | ||
Cancer-associated mutants of RNA helicase DDX3X are defective in RNA-stimulated ATP hydrolysis | Q35470624 | ||
Autoinhibitory Interdomain Interactions and Subfamily-specific Extensions Redefine the Catalytic Core of the Human DEAD-box Protein DDX3. | Q36518348 | ||
DEAD-box proteins can completely separate an RNA duplex using a single ATP. | Q37068571 | ||
From unwinding to clamping - the DEAD box RNA helicase family | Q37903659 | ||
ATP utilization and RNA conformational rearrangement by DEAD-box proteins | Q37992169 | ||
Super-resolution in solution X-ray scattering and its applications to structural systems biology. | Q38089813 | ||
Looking back on the birth of DEAD-box RNA helicases | Q38094554 | ||
The Ded1/DDX3 subfamily of DEAD-box RNA helicases | Q38231370 | ||
RNA helicase DDX3: at the crossroad of viral replication and antiviral immunity. | Q38547052 | ||
The Functional Cycle of Rnt1p: Five Consecutive Steps of Double-Stranded RNA Processing by a Eukaryotic RNase III. | Q39006841 | ||
Division of Labor in an Oligomer of the DEAD-Box RNA Helicase Ded1p | Q40694722 | ||
A double-edged function of DDX3, as an oncogene or tumor suppressor, in cancer progression (Review). | Q47554495 | ||
Biochemical Differences and Similarities between the DEAD-Box Helicase Orthologs DDX3X and Ded1p | Q47610758 | ||
Duplex unwinding with DEAD-box proteins. | Q54687163 | ||
Automated matching of high- and low-resolution structural models | Q56444545 | ||
PRIMUS: a Windows PC-based system for small-angle scattering data analysis | Q57091059 | ||
The helicase Ded1p controls use of near-cognate translation initiation codons in 5' UTRs | Q57753804 | ||
Chemical genetic inhibition of DEAD-box proteins using covalent complementarity | Q58794848 | ||
P433 | issue | 1 | |
P304 | page(s) | 3085 | |
P577 | publication date | 2019-07-12 | |
P1433 | published in | Nature Communications | Q573880 |
P1476 | title | The mechanism of RNA duplex recognition and unwinding by DEAD-box helicase DDX3X | |
P478 | volume | 10 |
Q97885936 | A de novo DDX3X Variant Is Associated With Syndromic Intellectual Disability: Case Report and Literature Review |
Q92445481 | DDX3X Multifunctionally Modulates Tumor Progression and Serves as a Prognostic Indicator to Predict Cancer Outcomes |
Q89896482 | DEAD-box RNA Helicase DDX3: Functional Properties and Development of DDX3 Inhibitors as Antiviral and Anticancer Drugs |
Q92636216 | RK-33 Is a Broad-Spectrum Antiviral Agent That Targets DEAD-Box RNA Helicase DDX3X |
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