| Name | microRNA 5588 |
| Description | microRNAs (miRNAs) are short (20-24 nt) non-coding RNAs that are involved in post-transcriptional regulation of gene expression in multicellular organisms by affecting both the stability and translation of mRNAs. miRNAs are transcribed by RNA polymerase II as part of capped and polyadenylated primary transcripts (pri-miRNAs) that can be either protein-coding or non-coding. The primary transcript is cleaved by the Drosha ribonuclease III enzyme to produce an approximately 70-nt stem-loop precursor miRNA (pre-miRNA), which is further cleaved by the cytoplasmic Dicer ribonuclease to generate the mature miRNA and antisense miRNA star (miRNA*) products. The mature miRNA is incorporated into a RNA-induced silencing complex (RISC), which recognizes target mRNAs through imperfect base pairing with the miRNA and most commonly results in translational inhibition or destabilization of the target mRNA. The RefSeq represents the predicted microRNA stem-loop. [provided by RefSeq, Sep 2009] |
| Summary |
{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe collection of studies provided builds a comprehensive picture of the critical roles played by the HNK-1 carbohydrate epitope and its associated biosynthetic enzymes—such as GlcAT‐P, GlcAT‐S, and other glycosyltransferases—in processes ranging from synaptic plasticity and neural receptor stability to nerve regeneration and central nervous system development."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": " In these studies, genetic deletion or altered expression of key enzymes resulted in marked effects on long-term potentiation, spatial memory, and proper receptor trafficking, underscoring the importance of glycan modifications for proper neural function."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional research among neural stem cells, extracellular matrix constituents, and even in in vivo models of nerve injury highlighted a diverse set of roles, including the maintenance of stemness during development, modulation of neural cell adhesion, and promising avenues for therapeutic intervention in nerve repair."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "9"}]}, {"type": "t", "text": " Moreover, studies investigating the biochemical pathways in aggrecan and glycosaminoglycan linkage have expanded the scope of HNK-1 biosynthesis and its influence on neural plasticity and protection during demyelinating conditions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, a host-directed antiviral approach identified through a CRISPR activation screen further emphasizes the potential broader implications of glycosylation pathways in cellular functions, although in that context the enzyme B3GAT1 was implicated in modulating cell surface sialic acid expression rather than HNK-1 per se."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nNotably, despite the query’s focus, none of the above abstracts mention or provide evidence regarding the microRNA MIR5588. Consequently, from these studies no functional insights or roles for MIR5588 can be derived. Further investigation or clarification would be needed to understand if and how MIR5588 might interact with or regulate the glycosylation pathways or neural functions described in these works.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Shoji Yamamoto, Shogo Oka, Fumiko Saito-Ohara, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Molecular cloning and genomic analysis of mouse glucuronyltransferase involved in biosynthesis of the HNK-1 epitope."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biochem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/oxfordjournals.jbchem.a003108"}], "href": "https://doi.org/10.1093/oxfordjournals.jbchem.a003108"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11872162"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11872162"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Shoji Yamamoto, Shogo Oka, Mitsuhiro Inoue, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mice deficient in nervous system-specific carbohydrate epitope HNK-1 exhibit impaired synaptic plasticity and spatial learning."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.C200296200"}], "href": "https://doi.org/10.1074/jbc.C200296200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12032138"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12032138"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Harukazu Saito, Yasushi Nakao, Shinichiro Takayama, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Specific expression of an HNK-1 carbohydrate epitope and NCAM on femoral nerve Schwann cells in mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neurosci Res (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.neures.2005.08.006"}], "href": "https://doi.org/10.1016/j.neures.2005.08.006"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16171882"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16171882"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Mitsuhiro Inoue, Keiko Kato, Hitomi Matsuhashi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Distributions of glucuronyltransferases, GlcAT-P and GlcAT-S, and their target substrate, the HNK-1 carbohydrate epitope in the adult mouse brain with or without a targeted deletion of the GlcAT-P gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Brain Res (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.brainres.2007.05.012"}], "href": "https://doi.org/10.1016/j.brainres.2007.05.012"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17935701"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17935701"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Akihiko Hiyama, Sachin Gajghate, Daisuke Sakai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Activation of TonEBP by calcium controls {beta}1,3-glucuronosyltransferase-I expression, a key regulator of glycosaminoglycan synthesis in cells of the intervertebral disc."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M807081200"}], "href": "https://doi.org/10.1074/jbc.M807081200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19147493"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19147493"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Ippei Morita, Shinako Kakuda, Yusuke Takeuchi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "HNK-1 glyco-epitope regulates the stability of the glutamate receptor subunit GluR2 on the neuronal cell surface."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109.024208"}], "href": "https://doi.org/10.1074/jbc.M109.024208"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19729452"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19729452"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Hirokazu Yagi, Makoto Yanagisawa, Yusuke Suzuki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "HNK-1 epitope-carrying tenascin-C spliced variant regulates the proliferation of mouse embryonic neural stem cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M110.157081"}], "href": "https://doi.org/10.1074/jbc.M110.157081"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20855890"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20855890"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Andrey Irintchev, Ming-Mei Wu, Hyun Joon Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Glycomimetic improves recovery after femoral injury in a non-human primate."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurotrauma (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1089/neu.2011.1775"}], "href": "https://doi.org/10.1089/neu.2011.1775"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21463132"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21463132"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Tetsuya Kouno, Yasuhiko Kizuka, Naoki Nakagawa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Specific enzyme complex of beta-1,4-galactosyltransferase-II and glucuronyltransferase-P facilitates biosynthesis of N-linked human natural killer-1 (HNK-1) carbohydrate."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111.233353"}], "href": "https://doi.org/10.1074/jbc.M111.233353"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21771787"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21771787"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Keiko Akasaka-Manya, Hiroshi Manya, Yasuhiko Kizuka, et al. "}, {"type": "b", "children": [{"type": "t", "text": "α-Klotho mice demonstrate increased expression of the non-sulfated N-glycan form of the HNK-1 glyco-epitope in kidney tissue."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biochem (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/jb/mvu024"}], "href": "https://doi.org/10.1093/jb/mvu024"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24723043"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24723043"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Keiko Yabuno, Jyoji Morise, Yasuhiko Kizuka, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A Sulfated Glycosaminoglycan Linkage Region is a Novel Type of Human Natural Killer-1 (HNK-1) Epitope Expressed on Aggrecan in Perineuronal Nets."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0144560"}], "href": "https://doi.org/10.1371/journal.pone.0144560"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26659409"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26659409"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Kanoko Sakuda, Yasuhiko Kizuka, Yoshiki Yamaguchi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Reactivity of anti-HNK-1 antibodies to branched O-mannose glycans associated with demyelination."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2017.04.085"}], "href": "https://doi.org/10.1016/j.bbrc.2017.04.085"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28427937"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28427937"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Joseph D Trimarco, Sarah L Nelson, Ryan R Chaparian, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cellular glycan modification by B3GAT1 broadly restricts influenza virus infection."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-022-34111-0"}], "href": "https://doi.org/10.1038/s41467-022-34111-0"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36309510"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36309510"}]}]}]}
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| NCBI Gene ID | 100847054 |
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| Expression in Tissues and Cell Lines |
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MIR5588 has 0 functional associations with biological entities spanning 0 categories () extracted from 0 datasets.
Click the + buttons to view associations for MIR5588 from the datasets below.
If available, associations are ranked by standardized value
| Dataset | Summary |
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