Редактирование: DHX9 (раздел)

==Publications==

{{medline-entry
|title=The biology of [[DHX9]] and its potential as a therapeutic target.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/27034008
|abstract=[[DHX9]] is member of the DExD/H-box family of helicases with a "DEIH" sequence at its eponymous DExH-box motif. Initially purified from human and bovine cells and identified as a homologue of the Drosophila Maleless (MLE) protein, it is an NTP-dependent helicase consisting of a conserved helicase core domain, two double-stranded RNA-binding domains at the N-terminus, and a nuclear transport domain and a single-stranded DNA-binding RGG-box at the C-terminus. With an ability to unwind DNA and RNA duplexes, as well as more complex nucleic acid structures, [[DHX9]] appears to play a central role in many cellular processes. Its functions include regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. Because of its central role in gene regulation and RNA metabolism, there are growing implications for [[DHX9]] in human diseases and their treatment. This review will provide an overview of the structure, biochemistry, and biology of [[DHX9]], its role in cancer and other human diseases, and the possibility of targeting [[DHX9]] in chemotherapy.
|mesh-terms=* Aging
* Animals
* Autoimmune Diseases
* Cattle
* Crystallography, X-Ray
* DEAD-box RNA Helicases
* DNA
* DNA Replication
* Drosophila
* Gene Expression Regulation, Neoplastic
* Humans
* MicroRNAs
* Neoplasm Proteins
* Protein Domains
* RNA
* RNA Helicases
|keywords=* DExD/H-box
* DHX9
* Maleless
* RNA helicase A
* helicase
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5173168
}}
{{medline-entry
|title=Suppression of the [[DHX9]] helicase induces premature senescence in human diploid fibroblasts in a p53-dependent manner.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/24990949
|abstract=[[DHX9]] is an ATP-dependent DEXH box helicase with a multitude of cellular functions. Its ability to unwind both DNA and RNA, as well as aberrant, noncanonical polynucleotide structures, has implicated it in transcriptional and translational regulation, DNA replication and repair, and maintenance of genome stability. We report that loss of [[DHX9]] in primary human fibroblasts results in premature senescence, a state of irreversible growth arrest. This is accompanied by morphological defects, elevation of senescence-associated β-galactosidase levels, and changes in gene expression closely resembling those encountered during replicative (telomere-dependent) senescence. Activation of the p53 signaling pathway was found to be essential to this process. ChIP analysis and investigation of nascent DNA levels revealed that [[DHX9]] is associated with origins of replication and that its suppression leads to a reduction of DNA replication. Our results demonstrate an essential role of [[DHX9]] in DNA replication and normal cell cycle progression. 
|mesh-terms=* Cell Cycle Checkpoints
* Cellular Senescence
* DEAD-box RNA Helicases
* DNA Replication
* Diploidy
* Fibroblasts
* HEK293 Cells
* Humans
* Neoplasm Proteins
* Signal Transduction
* Tumor Suppressor Protein p53
* beta-Galactosidase
|keywords=* Cell Cycle
* Cell Growth
* DNA Replication
* Helicase
* Senescence
* p53
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4132785
}}