MGC42174 Blocking Peptide
- Known as:
- MGC42174 Blocking Peptide
- Catalog number:
- 33r-9966
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- MGC42174 Blocking Peptide
Related genes to: MGC42174 Blocking Peptide
- Gene:
- DIS3L2 NIH gene
- Name:
- DIS3 like 3'-5' exoribonuclease 2
- Previous symbol:
- FAM6A
- Synonyms:
- FLJ36974, MGC42174
- Chromosome:
- 2q37.1
- Locus Type:
- gene with protein product
- Date approved:
- 2007-01-17
- Date modifiied:
- 2019-04-23
Related products to: MGC42174 Blocking Peptide
Related articles to: MGC42174 Blocking Peptide
- Nonsense-mediated decay (NMD) is a vital RNA surveillance mechanism in eukaryotic cells that ensures mRNA quality and regulates gene expression. NMD targets mRNAs with premature translation-termination codons to prevent the production of potentially harmful truncated proteins. But NMD is also involved in modulating the expression of physiological mRNAs to maintain cellular homeostasis. This NMD function is particularly relevant to calibrate the cellular transcriptome in response to environmental signals and stress. Its conservation across eukaryotes highlights its essential role. When active, NMD promotes mRNA degradation involving exoribonucleases such as XRN1 (5'-3') and the exosome (3'-5'). DIS3L2, an exosome-independent exonuclease that primarily targets substrates marked by the non-templated addition of uridine residues to the 3' end of RNA molecules by terminal uridylyl transferases, can also degrade some NMD substrates, especially those that underwent 3' end uridylation. This review explores DIS3L2's interaction with the NMD pathway (DIS3L2/NMD pathway) and the human disorders associated with a dysfunctional DIS3L2/NMD pathway. A better understanding of the interplay between NMD and DIS3L2 will certainly allow the development of novel treatments for disorders associated with an affected DIS3L2/NMD pathway. - Source: PubMed
Publication date: 2026/07/13
Lacerda RafaelaCarvalho MiguelRomão Luísa - The growing demand for animal products, combined with declining livestock production due to urbanization and climate change, underscores the need for sustainable breeding strategies. In sheep production, liveweight and weight gain until weaning are key economic traits. Selection signature analyses have previously identified the DIS3L2 gene, located on OAR2 (~233 Mbp), as a candidate under positive selection for body weight and morphology in sheep. However, its direct association with growth traits remained uninvestigated. This study explored the association between a splice region variant in the DIS3L2 gene (rs421664828) and pre-weaning growth traits in four indigenous sheep breeds in Türkiye: Central Anatolian Merino, Karayaka, Akkaraman, and Morkaraman. A total of 1862 lambs from 10 herds were genotyped using a custom TaqMan Genotyping assay. Body weights were recorded at birth and on Days 30, 60, and 90, with average daily gain (ADG) calculated until weaning. The AG genotype was the most prevalent (92.1%), and all breeds deviated from Hardy-Weinberg equilibrium. Association analysis revealed significant effects of rs421664828 on weight at Days 60 and 90 and on ADG-90. The AG genotype was consistently associated with higher growth performance. These findings support the use of DIS3L2-rs421664828 in marker-assisted selection to enhance growth traits in sheep. - Source: PubMed
Akyüz BilalDaldaban FadimeBayram DavutKarakuş FerdaÖzdemir MustafaŞirin EmreArslan KorhanCinar Mehmet Ulas - Molecular biomarkers are increasingly used for risk stratification, particularly in up-front surgery settings (Children's Oncology Group trials), whereas in preoperative chemotherapy setting, the ongoing International Society of Pediatric Oncology (SIOP)-Renal Tumor Study Group-2016 UMBRELLA study aims to validate selected biomarkers for future risk-adapted treatment strategies. This systematic review summarizes all literature on the prognostic value of these biomarkers. - Source: PubMed
Publication date: 2026/05/18
Oller AgustinaKemmeren PatrickPerotti Danielavan Tinteren HarmVerschuur ArnauldSpreafico FilippoBrok JesperFurtwängler Rhoikos C JChowdhury TanzinaAl-Saadi ReemVujanic Gordan MTreece Amy LDrost Jarnovan Grotel MartineMullen Elizabeth AEvageliou Nicholas FGraf NorbertHong Andrew LGessler ManfredGeller James Ivan den Heuvel-Eibrink Marry M - Stresses like starvation trigger degradation of mature 40S ribosomes, requiring the coordinated breakdown of large and stable RNA-protein complexes. The atypical kinase RIOK3 orchestrates degradation by binding ubiquitylated 40S ribosomes and promoting rRNA decay. However, the mechanisms and factors that mediate rRNA decay remain unknown. Here we find that in response to starvation, RIOK3 recruits the terminal uridylyl-transferase TUT7 and the exonuclease DIS3L2 to 40S ribosomes. Sequencing analyses show that TUT7 adds oligo(uridine) tails to the 3' end of the 18S rRNA in these ribosomes. DIS3L2 subsequently recognizes uridylated 18S rRNA and carries out 3'-5' decay. We identify major decay intermediates that undergo further uridylation in a process of iterative uridylation and decay. Loss of DIS3L2 impairs 18S rRNA decay during starvation and leads to accumulation of uridylated 18S rRNA. Together these findings define a mechanism for ribosome degradation in which 3' oligo(uridine) tailing drives decay of rRNA from ribosomes. - Source: PubMed
Publication date: 2026/04/27
Diehl Frances FBuskirk Allen RGreen Rachel - Zinc-finger antiviral protein (ZAP)-mediated RNA decay (ZMD) restricts the replication of viruses containing CpG dinucleotide clusters. However, why ZAP isoforms differ in antiviral activity and how they recruit cofactors to mediate RNA decay is unclear. Therefore, we determined the ordered events of the ZMD pathway. The long ZAP isoform preferentially binds viral RNA and has distinct binding motifs compared to the short isoform. The endoribonuclease KHNYN then cleaves viral RNA at positions of ZAP binding. The 5' cleavage fragment undergoes TUT4/TUT7-mediated 3' uridylation and degradation by DIS3L2. The 3' cleavage fragment is degraded by XRN1. ZAP and TRIM25 interact with KHNYN, TUT7, DIS3L2, and XRN1 in an RNase-resistant manner. Viral infection promotes the interaction between TRIM25 with these enzymes, leading to viral RNA decay while also decreasing the abundance of cellular transcripts. Overall, the long isoform of ZAP recruits key enzymes to assemble an RNA decay complex on viral RNA. - Source: PubMed
Publication date: 2026/04/28
Bouton Clément RGimpelj Domjanič GregaLista María JoséGalão Rui PedroCourty ThomasKwiatkowski PiotrWilson Harry DHill Peter W SMischo Hannah EChakrabarti Anob MPoljak MarioUle JernejNeil Stuart J DSwanson Chad M