ArticleMolecular and cellular biology2002
Mammalian selenoprotein in which selenocysteine (Sec) incorporation is supported by a new form of Sec insertion sequence element.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 157 citations in OpenAlex.
- Assessment of the Selenoprotein M (SELM) over-expression on human hepatocellular carcinoma tissues by immunohistochemistry.European journal of histochemistry : EJH · 2014Trial
- Selenoproteins: Minute yet vital players governing cellular fate.Genes & diseases · 2026Review
- Selenoprotein M Inhibits the Replication of Influenza A Virus by Regulating Reactive Oxygen Species Levels.Life (Basel, Switzerland) · 2025Article
- Regulatory Role and Cytoprotective Effects of Exogenous Recombinant SELENOM under Ischemia-like Conditions and Glutamate Excitotoxicity in Cortical Cells In Vitro.Biomedicines · 2024Article
- "Alphabet" Selenoproteins: Their Characteristics and Physiological Roles.International journal of molecular sciences · 2023Review
- Deciphering the Role of Selenoprotein M.Antioxidants (Basel, Switzerland) · 2023Review
- Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon.Science (New York, N.Y.) · 2022Article
- Article
- One-Pot Chemical Protein Synthesis Utilizing Fmoc-Masked Selenazolidine to Address the Redox Functionality of Human Selenoprotein F.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- MicroSalmon: A Comprehensive, Searchable Resource of Predicted MicroRNA Targets and 3'UTR Cis-Regulatory Elements in the Full-Length Sequenced Atlantic Salmon Transcriptome.Non-coding RNA · 2021Article
- Chemical Synthesis of the Sec-To-Cys Homologue of Human Selenoprotein F and Elucidation of Its Disulfide-pairing Mode.Frontiers in chemistry · 2021Article
- Macrophage Selenoproteins Restrict Intracellular Replication ofFrontiers in immunology · 2021Article
- Selenium and selenoproteins in prostanoid metabolism and immunity.Critical reviews in biochemistry and molecular biology · 2019Review
- Protein Partners of Selenoprotein SELM and the Role of Selenium Compounds in Regulation of Its Expression in Human Cancer Cells.Doklady. Biochemistry and biophysics · 2019Article
- Elemental Metabolomics and Pregnancy Outcomes.Nutrients · 2019Review
- Lifestyle modifications: coordinating the tRNA epitranscriptome with codon bias to adapt translation during stress responses.Genome biology · 2018Article
- Selenoproteins in colon cancer.Free radical biology & medicine · 2018Review
- Endoplasmic reticulum-resident selenoproteins as regulators of calcium signaling and homeostasis.Cell calcium · 2018Review
- Correlations of SELENOF and SELENOP genotypes with serum selenium levels and prostate cancer.The Prostate · 2018Article
- Selenocysteine-Mediated Expressed Protein Ligation of SELENOM.Methods in molecular biology (Clifton, N.J.) · 2018Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Selenocysteine (Sec), the 21st amino acid in protein, is encoded by UGA. The Sec insertion sequence (SECIS) element, which is the stem-loop structure present in 3' untranslated regions (UTRs) of eukaryotic selenoprotein-encoding genes, is essential for recognition of UGA as a codon for Sec rather than as a stop signal. We now report the identification of a new eukaryotic selenoprotein, designated selenoprotein M (SelM). The 3-kb human SelM-encoding gene has five exons and is located on chromosome 22 but has not been correctly identified by either Celera or the public Human Genome Project. We characterized human and mouse SelM cDNA sequences and expressed the selenoprotein in various mammalian cell lines. The 3" UTR of the human, mouse, and rat SelM-encoding genes lacks a canonical SECIS element. Instead, Sec is incorporated in response to a conserved mRNA structure, in which cytidines are present in place of the adenosines previously considered invariant. Substitution of adenosines for cytidines did not alter Sec incorporation; however, other mutant structures did not support selenoprotein synthesis, demonstrating that this new form of SECIS element is functional. SelM is expressed in a variety of tissues, with increased levels in the brain. It is localized to the perinuclear structures, and its N-terminal signal peptide is necessary for protein translocation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.