Recombinant Human Probable ATP-dependent RNA helicase DDX41 (DDX41)

1. Results show that the DDX41 DEAD domain recognizes both double-stranded DNA (dsDNA) and cyclic dinucleotides (CDN) at the same binding site. A structural comparison between the open and closed forms of the DDX41 DEAD domain revealed the structural rearrangement in the N-terminal region, which drastically changes the conformation of the ATP-binding site. PMID:27721487
2. analysis suggests that rather than establishing a causal Mendelian link between DDX41 germline LOF variants and MDS/AML it is appropriate to consider these as genetic risk factors PMID:27133828
3. Two novel germline DDX41 mutations in a family with inherited myelodysplasia/acute myeloid leukemia. PMID:26944477
4. Structural and functional analyses of human DDX41 DEAD domain. PMID:27928732
5. DDX41 mutations lead to development of high-risk myelodysplastic syndrome.(review) PMID:28547672
6. An increasing number of both inherited and acquired mutations in DDX41 gene are identified from myelodysplastic syndrome and/or acute myeloid leukemia (MDS/AML) patients. PMID:27502187
7. data demonstrate that DDX41 suppresses p21 translation without disturbing the function of p53 to directly induce p21 mRNA expression, this process indirectly requires p53, perhaps in the form of another p53 target gene or as a still undefined posttranscriptional function of p53. PMID:28348086
8. This study uncovered a pathogenic role of p.R525H DDX41 in the slow growth rate of tumor cells. Age-dependent epigenetic alterations or other somatic changes might collaborate with the mutation to cause AML. PMID:27174803
9. This study expands both the mutation and phenotypic spectra observed in families with germ line DDX41 mutations. PMID:26712909
10. corresponding deletions on 5q35.3 present in 6% of cases led to haploinsufficient DDX41 expression. DDX41 lesions caused altered pre-mRNA splicing and RNA processing PMID:25920683
11. results suggest a mechanism whereby c-di-GMP and c-di-AMP are detected by DDX41, which forms a complex with STING to signal to TBK1-IRF3 and activate the interferon response PMID:23142775
12. DDX41 is an additional DNA sensor that depends on STING to sense pathogenic DNA. PMID:21892174
13. The N-terminal domain of Abs interacts with the phox homology (PX) domain of SNX2 suggesting that PX domains may also participate in protein-protein interaction. PMID:15690390

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HGNC: 18674

UNIGENE: Hs.484288

KEGG: hsa:51428

STRING: 9606.ENSP00000422753

OMIM: 608170