 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.
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
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| MeSH Number(s) |
D12.776.864
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Selenoproteins".
Below are MeSH descriptors whose meaning is more specific than "Selenoproteins".
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.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2001 | 0 | 2 | 2 | | 2002 | 0 | 1 | 1 | | 2005 | 1 | 0 | 1 | | 2007 | 0 | 1 | 1 | | 2009 | 1 | 0 | 1 | | 2011 | 1 | 0 | 1 | | 2013 | 0 | 1 | 1 | | 2016 | 1 | 0 | 1 | | 2017 | 0 | 1 | 1 |
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Below are the most recent publications written about "Selenoproteins" by people in Profiles.
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Fu J, Fujisawa H, Follman B, Liao XH, Dumitrescu AM. Thyroid Hormone Metabolism Defects in a Mouse Model of SBP2 Deficiency. Endocrinology. 2017 12 01; 158(12):4317-4330.
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Cox AG, Tsomides A, Kim AJ, Saunders D, Hwang KL, Evason KJ, Heidel J, Brown KK, Yuan M, Lien EC, Lee BC, Nissim S, Dickinson B, Chhangawala S, Chang CJ, Asara JM, Houvras Y, Gladyshev VN, Goessling W. Selenoprotein H is an essential regulator of redox homeostasis that cooperates with p53 in development and tumorigenesis. Proc Natl Acad Sci U S A. 2016 09 20; 113(38):E5562-71.
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Fu J, Dumitrescu AM. Inherited defects in thyroid hormone cell-membrane transport and metabolism. Best Pract Res Clin Endocrinol Metab. 2014 Mar; 28(2):189-201.
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Dumitrescu AM, Refetoff S. Inherited defects of thyroid hormone metabolism. Ann Endocrinol (Paris). 2011 Apr; 72(2):95-8.
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Schomburg L, Dumitrescu AM, Liao XH, Bin-Abbas B, Hoeflich J, Köhrle J, Refetoff S. Selenium supplementation fails to correct the selenoprotein synthesis defect in subjects with SBP2 gene mutations. Thyroid. 2009 Mar; 19(3):277-81.
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Dumitrescu AM, Refetoff S. Novel biological and clinical aspects of thyroid hormone metabolism. Endocr Dev. 2007; 10:127-139.
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Ferguson AD, Labunskyy VM, Fomenko DE, Araç D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J. NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. J Biol Chem. 2006 Feb 10; 281(6):3536-43.
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Bianco AC, Salvatore D, Gereben B, Berry MJ, Larsen PR. Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases. Endocr Rev. 2002 Feb; 23(1):38-89.
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Curcio C, Baqui MM, Salvatore D, Rihn BH, Mohr S, Harney JW, Larsen PR, Bianco AC. The human type 2 iodothyronine deiodinase is a selenoprotein highly expressed in a mesothelioma cell line. J Biol Chem. 2001 Aug 10; 276(32):30183-7.
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Hu YJ, Korotkov KV, Mehta R, Hatfield DL, Rotimi CN, Luke A, Prewitt TE, Cooper RS, Stock W, Vokes EE, Dolan ME, Gladyshev VN, Diamond AM. Distribution and functional consequences of nucleotide polymorphisms in the 3'-untranslated region of the human Sep15 gene. Cancer Res. 2001 Mar 01; 61(5):2307-10.
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