DHX35 antibody - N-terminal region (ARP36485_P050)
- Known as:
- DHX35 (anti-) - N-terminal region (ARP36485_P050)
- Catalog number:
- arp36485_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- DHX35 antibody - N-terminal region (ARP36485_P050)
Related genes to: DHX35 antibody - N-terminal region (ARP36485_P050)
- Gene:
- DHX35 NIH gene
- Name:
- DEAH-box helicase 35
- Previous symbol:
- C20orf15, DDX35
- Synonyms:
- FLJ22759, KAIA0875
- Chromosome:
- 20q11.23-q12
- Locus Type:
- gene with protein product
- Date approved:
- 2001-11-27
- Date modifiied:
- 2018-02-13
Related products to: DHX35 antibody - N-terminal region (ARP36485_P050)
Related articles to: DHX35 antibody - N-terminal region (ARP36485_P050)
- Keratoconus (KC) is a progressive corneal ectatic disorder with genetic heterogeneity, yet the genetic variants underlying familial cases remain poorly characterized. We performed Trio-based whole-exome sequencing (Trio-WES) on 243 individuals from 81 KC families in Northwestern China and analyzed rare deleterious variants under three inheritance models. Following stringent quality control and filtering, we identified 706 rare deleterious candidate variants (576 compound heterozygous, 43 homozygous, and 87 de novo). The affected genes (n = 469) were enriched in pathways related to extracellular matrix (ECM) organization, cytoskeletal remodeling, cell adhesion, and PI3K-Akt signaling. Further assessment integrating family co-segregation, in silico prediction, American College of Medical Genetics and Genomics (ACMG) classification, cornea-related biological relevance, and database evidence identified 14 variants in 8 candidate genes (ATAD3A, COL6A3, FBXW9, VPS11, SELENBP1, DHX35, CDH23, and TTN) across 9 families. All variants were confirmed by Sanger sequencing and segregation analysis, and were additionally supported by cross-species conservation, protein structural localization, and validation in independent transcriptome datasets. These results expand the genetic landscape of familial KC in Northwestern China and provide a set of candidate genes for downstream functional studies and future clinical translation. - Source: PubMed
Publication date: 2026/05/19
Lin ZichunZhang JinjinCai BoLi RuiLi WenjingLi BingtaoWang ZhenglaiLiu KeyanZhuang Wenjuan - Transcriptomic analysis of bronchial brushes reveals asthma-associated gene signatures but is limited by the invasiveness of bronchoscopy. Based on the "united airways" hypothesis, we evaluated whether and to what extent nasal brushes reflect asthma-associated transcriptomic changes in the lower airways. - Source: PubMed
Publication date: 2026/03/10
Wen HuiKole TessaCarpaij Orestes AKarp TatianaGuryev VictorFaiz AlenChung Kian FanBhavsar PankajAdcock Ian MSiddiqui SalmanLan AndyRaby Katie LZounemat-Kermani NazaninBrightling ChrisSingh DaveKocks JanwillemKraft MonicaBeghé BiancaRabe Klaus FPapi AlbertoHylkema Machteld NNawijn Martijn Cvan den Berge Maarten - Pre-mRNA splicing is orchestrated by the spliceosome through coordinated RNA and protein rearrangements driven by ATP-dependent RNA helicases. DEAH-box helicases serve as principal motors, controlling catalytic activation, exon ligation, and complex disassembly. Early mechanistic understanding was limited by low-resolution cryo-electron microscopy (cryo-EM) structures, leaving RNA substrate interactions largely inferred from biochemical and genetic studies. Recent high-resolution cryo-EM structures (2021-present) have captured all five spliceosomal DEAH-box helicases-DHX16/Prp2, DHX38/Prp16, DHX8/Prp22, DHX15/Prp43, and DHX35-bound to their RNA targets within distinct spliceosomal states. These structures reveal precise recruitment, substrate recognition, and stage-specific actions. In this review, I integrate these insights into a unified framework, highlighting structural, biochemical, and evolutionary perspectives to guide future investigations of helicase regulation and their role in maintaining the fidelity of eukaryotic RNA splicing. - Source: PubMed
Chen Zhe - The spliceosome, a highly dynamic macromolecular assembly, catalyzes the precise removal of introns from pre-mRNAs. Recent studies have provided comprehensive structural insights into the step-wise assembly, catalytic splicing and final disassembly of the spliceosome. However, the molecular details of how the spliceosome recognizes and rejects suboptimal splicing substrates remained unclear. Here, we show cryo-electron microscopy structures of spliceosomal quality control complexes from a thermophilic eukaryote, Chaetomium thermophilum. The spliceosomes, henceforth termed B*, are stalled at a catalytically activated state but prior to the first splicing reaction due to an aberrant 5' splice site conformation. This state is recognized by G-patch protein GPATCH1, which is docked onto PRP8-EN and -RH domains and has recruited the cognate DHX35 helicase to its U2 snRNA substrate. In B*, DHX35 has dissociated the U2/branch site helix, while the disassembly helicase DHX15 is docked close to its U6 RNA 3'-end substrate. Our work thus provides mechanistic insights into the concerted action of two spliceosomal helicases in maintaining splicing fidelity by priming spliceosomes that are bound to aberrant splice substrates for disassembly. - Source: PubMed
Publication date: 2025/02/28
Li YiFischer PaulinaWang MengjiaoZhou QianxingSong AixiaYuan RuiMeng WanyuChen Fei XavierLührmann ReinhardLau BenjaminHurt EdCheng Jingdong - Intron removal during pre-mRNA splicing is of extraordinary complexity and its disruption causes a vast number of genetic diseases in humans. While key steps of the canonical spliceosome cycle have been revealed by combined structure-function analyses, structural information on an aberrant spliceosome committed to premature disassembly is not available. Here, we report two cryo-electron microscopy structures of post-B spliceosome intermediates from Schizosaccharomyces pombe primed for disassembly. We identify the DEAH-box helicase-G-patch protein pair (Gih35-Gpl1, homologous to human DHX35-GPATCH1) and show how it maintains catalytic dormancy. In both structures, Gpl1 recognizes a remodeled active site introduced by an overstabilization of the U5 loop I interaction with the 5' exon leading to a single-nucleotide insertion at the 5' splice site. Remodeling is communicated to the spliceosome surface and the Ntr1 complex that mediates disassembly is recruited. Our data pave the way for a targeted analysis of splicing quality control. - Source: PubMed
Publication date: 2025/01/20
Soni KomalHorvath AttilaDybkov OlexandrSchwan MerlinTrakansuebkul SasananFlemming DirkWild KlemensUrlaub HenningFischer TamásSinning Irmgard