{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nA review of the provided abstracts reveals that none address the function of SNORD33. In fact, rather than discussing this small nucleolar RNA—typically known for guiding 2′-O-methylation of ribosomal RNA—the studies focus on proteins and mechanisms related to endoplasmic reticulum (ER) quality control. For example, one report examines a 15‐kDa selenoprotein (Sep15) and its critical, cysteine‐rich domain–mediated interaction with UDP‐glucose:glycoprotein glucosyltransferase (GT), which is instrumental in ER protein processing and quality control."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOther abstracts detail the essential role of UGGT1 in monitoring glycoprotein folding within the ER, including its involvement in monoglucosylating misfolded proteins to facilitate chaperone binding, a process that contributes to cellular proteostasis and can influence disease outcomes such as viral replication."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Additional studies extend these findings by implicating UGGT1 in enhancing viral replication in the context of enterovirus A71 infection, in mediating hormonal effects on protein quality control, and even in modulating the trafficking of proinsulin thereby affecting insulin secretion."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "4", "end_ref": "7"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional work in the collection examines unrelated pathways—including the protection of the cerebellum from bilirubin toxicity mediated by Abcb1—but again, none of these investigations mention or shed light on a role for SNORD33."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " Thus, while the abstracts offer significant insights into the mechanisms governing glycoprotein processing and ER homeostasis via specialized protein factors, they provide no evidence or discussion regarding SNORD33’s function.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Vyacheslav M Labunskyy, Andrew D Ferguson, Dmitri E Fomenko, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.200912105"}], "href": "https://doi.org/10.1083/jcb.200912105"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20498017"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20498017"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Peng-Nien Huang, Jia-Rong Jheng, Jamie J Arnold, et al. "}, {"type": "b", "children": [{"type": "t", "text": "UGGT1 enhances enterovirus 71 pathogenicity by promoting viral RNA synthesis and viral replication."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Pathog (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.ppat.1006375"}], "href": "https://doi.org/10.1371/journal.ppat.1006375"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28545059"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28545059"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "María B Prados, Julio J Caramelo, Silvia E Miranda "}, {"type": "b", "children": [{"type": "t", "text": "Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: glycoprotein glucosyltransferase (UGGT)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbamcr.2013.09.022"}], "href": "https://doi.org/10.1016/j.bbamcr.2013.09.022"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24140206"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24140206"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Jaeyong Cho, Masaki Hiramoto, Yuka Masaike, et al. "}, {"type": "b", "children": [{"type": "t", "text": "UGGT1 retains proinsulin in the endoplasmic reticulum in an arginine dependent manner."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2020.04.158"}], "href": "https://doi.org/10.1016/j.bbrc.2020.04.158"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32423812"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32423812"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Jaeyong Cho, Yoji Tsugawa, Takeshi Imai "}, {"type": "b", "children": [{"type": "t", "text": "R1526 residue in arginine/proinsulin binding domain of UGGT1 is involved in proinsulin binding."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2022.05.060"}], "href": "https://doi.org/10.1016/j.bbrc.2022.05.060"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35613513"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35613513"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Luka Bockor, Giulia Bortolussi, Simone Vodret, et al. 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