Ask about this productRelated genes to: UXS1 Blocking Peptide
- Gene:
- UXS1 NIH gene
- Name:
- UDP-glucuronate decarboxylase 1
- Previous symbol:
- -
- Synonyms:
- FLJ23591, UGD, SDR6E1
- Chromosome:
- 2q12.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-05-01
- Date modifiied:
- 2015-08-26
Related products to: UXS1 Blocking Peptide
Related articles to: UXS1 Blocking Peptide
- DNA methylation is implicated in type 2 diabetes (T2D); however, its role in prediabetes remains poorly understood. - Source: PubMed
Publication date: 2026/04/03
Mencucci María VictoriaLacunza EzequielAbba Martín CarlosAhrtz LucíaDumrauf BárbaraVillagarcía Hernán GonzaloCastro María CeciliaRomán Carolina LisiFlores Luis EmilioFrancini FlavioMaiztegui Bárbara - Identifying novel molecular drivers is crucial to improving therapeutic strategies for hepatocellular carcinoma (HCC). This study aimed to investigate the clinical significance and biological function of UDP-glucuronate decarboxylase 1 (UXS1) in HCC. - Source: PubMed
Publication date: 2026/03/17
Lv JunHan KangGan Fu-YuanLi Ming-HaoYin Qing-Jun - White adipose tissue (WAT) is a key endocrine organ regulating lipid and glucose homeostasis. Early metabolic disturbances may disrupt its endocrine function through epigenetic mechanisms; however, how DNA methylation contributes to prediabetes and its reversal remains largely unexplored. - Source: PubMed
Publication date: 2026/02/24
Dumrauf BárbaraMencucci María VictoriaLacunza EzequielAbba Martín CarlosFlores Luis EmilioMaiztegui BárbaraGagliardino Juan JoséFrancini FlavioLisi Román Carolina - Glycosaminoglycan assembly on proteoglycans involves a common tetrasaccharide linker that starts with xylose attached to a serine on the protein. Defective linker biosynthesis caused by a missense mutation of human UDP-xylose synthase (hUXS1) is associated with connective tissue disorders characterized by skeletal abnormality and short stature. The Ile181Asn variant of hUXS1 was reported as inactive in releasing UDP-xylose from UDP-glucuronic acid. Here, we show that Ile181Asn-hUXS1 exhibited catalytic properties similar to the wild-type enzyme but featured a significant decrease in stability, expressed in melting temperature lowered from 48.2 °C to 35.2 °C. At 37 °C, Ile181Asn-hUXS1 was ~10-fold less stable and more prone to precipitation than wild-type hUXS1. The loss of function in Ile181Asn-hUXS1 is thus explained by instability, consistent with molecular dynamics simulations predicting structural destabilization. Impact statement The Ile181Asn variant of human UDP-xylose synthase (hUXS1), associated with a short-stature genetic syndrome, has previously been reported as inactive. We show here with experiments and molecular simulations that hUXS1 malfunction arises from structural instability rather than from a catalytic defect. - Source: PubMed
Publication date: 2026/01/13
Li TuoSánchez-Murcia Pedro ANidetzky Bernd - Loss-of-function mutations in KEAP1 are found in more than 20% of non-small cell lung cancers. These mutations stabilize the transcription factor NRF2 to induce a battery of antioxidative and cytoprotective genes. Although NRF2 accumulation promotes cancer cell fitness, it also creates several targetable vulnerabilities. In this issue of Cancer Research, Gebru and colleagues reveal the dependency of KEAP1-mutant non-small cell lung cancers on UDP-xylose synthase 1 (UXS1). The authors found that NRF2-driven expression of UDP-glucose 6-dehydrogenase leads to the accumulation of UDP-glucuronic acid. Consequently, loss of UXS1-mediated UDP-glucuronic acid decarboxylation causes sequestration of UDP, depletion of pyrimidine pools, and replication stress, thereby inducing apoptosis and senescence. Importantly, these effects are selective to KEAP1-mutant tumors, with KEAP1 wild-type cells and normal tissue unaffected by UXS1 loss. DNA damage induction with cell-cycle kinase inhibitors synergized with UXS1 loss to promote the death of KEAP1-mutant cells. These findings suggest that UXS1 loss is synthetic lethal with NRF2 activation and may be a promising target for therapy. See related article by Gebru et al., p. 4806. - Source: PubMed
Yasseen Basma ADeNicola Gina M