Ask about this productRelated genes to: B3GALT6 antibody
- Gene:
- B3GALT6 NIH gene
- Name:
- beta-1,3-galactosyltransferase 6
- Previous symbol:
- -
- Synonyms:
- beta3GalT6
- Chromosome:
- 1p36.33
- Locus Type:
- gene with protein product
- Date approved:
- 2002-01-09
- Date modifiied:
- 2019-04-23
Related products to: B3GALT6 antibody
Related articles to: B3GALT6 antibody
- This study aims to reveal drug targets for sepsis: an association study integrating Mendelian randomization (MR), expression quantitative trait loci, protein quantitative trait loci, and protein-protein interaction networks. We identified 43 druggable proteins associated with sepsis, with B3GALT6 emerging as a key player (P = 5.24E-06). Sensitivity analyses indicated no significant heterogeneity among the proteins tested, reinforcing the robustness of our findings. Bioinformatics analyses demonstrated that B3GALT6 expression was significantly lower in sepsis patients compared to healthy controls across multiple datasets (P < .001), suggesting its potential utility as a diagnostic biomarker. Additionally, Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses revealed critical pathways altered in sepsis, including multivesicular body assembly and ubiquitin-dependent protein catabolic processes. Our results highlight B3GALT6 as a promising therapeutic target and prognostic marker for sepsis, with implications for future research aimed at developing innovative treatment strategies. Overall, this study provides a foundation for further exploration of druggable proteins in sepsis, emphasizing the need for additional investigations to validate these findings in clinical settings and facilitate the translation of these insights into effective therapeutic interventions. - Source: PubMed
Lu EnkuiZhang YananShao XueboChen JunnanJiang MengpingTang Weidong - Proteoglycans are a major component of the connective tissue matrix, which consists of a core protein and covalently attached glycosaminoglycan (GAG) chains, which are highly sulfated polysaccharides with a tetrasaccharide linker for the core protein attachment. Impaired synthesis or degradation of GAG causes genetic disorders. In the 1950s, deficient lysosomal GAG degradation was discovered in mucopolysaccharidoses. In the 1990s, a defective enzyme for GAG synthesis was implicated in a variant of Ehlers-Danlos syndrome and an impaired GAG sulfation in diastrophic dysplasia. Newer studies have uncovered that abnormal GAG synthesis causes a large group of genetic skeletal disorders with joint and skin abnormalities. - Source: PubMed
Publication date: 2026/02/26
Tsujioka YukoSimsek Kiper Pelin OzlemUnger SheilaHanda AtsuhikoKono TatsuoJinzaki MasahiroRossi AntonioSuperti-Furga AndreaNishimura Gen - To explore the clinical phenotype and genetic etiology of a child with Ehlers-Danlos syndrome, spondylodysplastic type 2 (EDSSPD2). - Source: PubMed
Lan ShaocongLi ChengyanHuang BinglongChen YinhuiXie ZaoyeDeng WenhaoAo Dang - Prostate cancer (PCa) is characterized not merely as a malignant tumor, but also as a metabolic disorder encompassing dysregulation of glycolysis. This study was purposed to develop a new effective prognostic model correlated with glycolysis-related genes (GRGs) and investigate its potential mechanisms in PCa. - Source: PubMed
Publication date: 2026/02/23
Wang JinhuaChen XiongYang GuoWang Xiaorong - We selected the N,O-glycosylated proteoglycan bikunin as a model to establish a chemoenzymatic approach to defined proteoglycans using native chemical ligation. Overexpression of the human linkage region glycosyltransferases B4GalT7, B3GalT6 and B3GlcAT-1 as N-terminal SUMO-fusions gave high yields of soluble and active enzymes in E. coli. When starting with xylosylated bikunin peptides the transferases performed well in enzymatic cascade reactions and provided the desired linkage region tetrasaccharide glycopeptides. B3GalT6 and B3GlcAT-1 led to side products with N,O-glycosylated bikunin peptides revealing unexpected promiscuity of both enzymes towards complex type N-glycans. Additionally, B3GalT6 was found to synthesize short poly-β3 Gal structures. B3GlcAT-1 can slowly convert the biosynthetic intermediate Gal-Xyl to the non-canonical trisaccharide GlcA-Gal-Xyl. This reaction independently confirmed the recently detected biosynthetic bypass to GAGs in the case of dysfunctional B3GalT6 (spondylodysplastic Ehlers-Danlos-syndrome). The three linkage region glycosyltransferases B4GalT7, B3GalT6 and B3GlcAT-1 were dimeric in solution and the crystal structure of B3GalT6 was solved showing a covalent dimer linked by a disulfide in the center of the large dimerization domain. This motif appears to be conserved in higher organisms and reinforces the concept of dimeric glycosyltransferases lining the Golgi. - Source: PubMed
Publication date: 2025/11/29
Weidler SaschaBundgaard OleHessefort MarkusRädisch MarisaGraf Christopher Günther FranzLam KevinNeubauer Vanessa JEisenreich JohannaKöhler LeonhardMoremen Kelley WSteentoft CatharinaClausen HenrikHuang Teng-YiHung Shang-ChengSteegborn ClemensWeyand MichaelUnverzagt Carlo