Selenoproteins

"Selenoproteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

Selenoproteins are proteins that specifically incorporate SELENOCYSTEINE into their amino acid chain. Most selenoproteins are enzymes with the selenocysteine residues being responsible for their catalytic functions.

Descriptor ID	D051140
MeSH Number(s)	D12.776.864
Concept/Terms	Selenoproteins Selenoproteins Selenoprotein Selenoprotein P1 Selenoprotein P1

Below are MeSH descriptors whose meaning is more general than "Selenoproteins".

Chemicals and Drugs [D]
Amino Acids, Peptides, and Proteins [D12]
Proteins [D12.776]
Selenoproteins [D12.776.864]

Below are MeSH descriptors whose meaning is related to "Selenoproteins".

Below are MeSH descriptors whose meaning is more specific than "Selenoproteins".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Selenoproteins" by people in this website by year, and whether "Selenoproteins" was a major or minor topic of these publications.

Bar chart showing 87 publications over 28 distinct years, with a maximum of 7 publications in 2021

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1996	0	1	1
1997	0	1	1
1999	0	1	1
2000	0	4	4
2001	0	3	3
2002	0	3	3
2003	0	2	2
2005	4	0	4
2006	3	1	4
2007	4	2	6
2008	3	0	3
2009	3	0	3
2010	1	0	1
2011	3	1	4
2012	1	2	3
2013	3	0	3
2014	6	0	6
2015	2	1	3
2016	3	0	3
2017	3	0	3
2018	3	1	4
2019	2	0	2
2020	2	0	2
2021	5	2	7
2022	0	6	6
2023	0	1	1
2024	2	0	2
2025	1	1	2

Below are the most recent publications written about "Selenoproteins" by people in Profiles.

Shimada BK, Ogawa-Wong AN, Soares AG, Hallam KA, Santiago PJD, Saelua K, Nakahara-Akita KK, Torres DJ, Brockman JD, Kurokawa S, Ewell KL, Bellinger MT, Toh P, Lagatta Pamplona Remedios G, Alfulaij N, Swanson SM, Seyedali A, Zavacki AM, Berry MJ, Seale LA. Global loss of selenocysteine lyase in mice drives lipid accumulation in brown adipocytes. Am J Physiol Endocrinol Metab. 2026 02 01; 330(2):E000.

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Shimada BK, Watanabe M, Apo Takayama NK, Soares AG, Hallam KA, Rivers OS, Ewell K, Santiago PJD, Swanson SM, Toh P, Alfulaij N, Berry MJ, Seale LA. Cardiac redox imbalance upon disruption of selenocysteine decomposition in mice. Am J Physiol Heart Circ Physiol. 2025 Dec 01; 329(6):H1480-H1496.

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Ma C, Wurlitzer K, Nunes LGA, Hoffmann PR, Pitts MW. Iron and selenium: At the crossroads of development and death in oligodendrocytes. Arch Biochem Biophys. 2025 Sep; 771:110509.

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Nunes LGA, Ma C, Pitts MW, Hoffmann PR. Insights from selenoprotein I mouse models for understanding biological roles of this enzyme. Arch Biochem Biophys. 2025 Jun; 768:110394.

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Ma C, Hoffmann FW, Shay AE, Koo I, Green KA, Green WR, Hoffmann PR. Upregulated selenoprotein I during lipopolysaccharide-induced B cell activation promotes lipidomic changes and is required for effective differentiation into IgM-secreting plasma B cells. J Leukoc Biol. 2024 06 28; 116(1):6-17.

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Nunes LGA, Ma C, Hoffmann FW, Shay AE, Pitts MW, Hoffmann PR. Selenoprotein I is indispensable for ether lipid homeostasis and proper myelination. J Biol Chem. 2024 05; 300(5):107259.

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Diamond AM, Hoffmann PR. Advances in the biology of selenium and selenoproteins. Arch Biochem Biophys. 2023 02; 735:109514.

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Toh P, Nicholson JL, Vetter AM, Berry MJ, Torres DJ. Selenium in Bodily Homeostasis: Hypothalamus, Hormones, and Highways of Communication. Int J Mol Sci. 2022 Dec 06; 23(23).

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Shimada BK, Swanson S, Toh P, Seale LA. Metabolism of Selenium, Selenocysteine, and Selenoproteins in Ferroptosis in Solid Tumor Cancers. Biomolecules. 2022 10 28; 12(11).

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Shimada BK, Watanabe LM, Swanson S, Toh P, Seale LA. Selenium and selenoproteins in thermogenic adipocytes. Arch Biochem Biophys. 2022 11 30; 731:109445.

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