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for: penultimate selenocysteine residue replaced by cysteine in thioredoxin
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Penultimate selenocysteine residue replaced by cysteine in thioredoxin reductase from selenium-deficient rat liver
Lu, Jun; Zhong, Liangwei; Lönn, Maria Elisabet; Burk, Raymond F.; Hill, Kristina E.; Holmgren, Arne
Follow The FASEB Journal , Volume 23 (8): 2394
Fed of American Socs for Experimental Biology – Aug 1, 2009., Holmgren, A. Penultimate selenocysteine residue replaced by cysteine in thioredoxin reductase from selenium-deficient rat liver. Abstract Selenium is an essential micronutrient for humans ...
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Selenocysteine in proteins—properties and biotechnological use
Johansson, Linda; Gafvelin, Guro; Arnér, Elias S.J.
Follow Biochimica et Biophysica Acta (BBA) - General Subjects , Volume 1726 (1)
Elsevier – Oct 30, 2005Selenocysteine (Sec), the 21st amino acid, exists naturally in all kingdoms of life as the defining entity of selenoproteins. Sec is a cysteine (Cys) residue analogue with a selenium-containing ...
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Thioredoxin glutathione reductase: Its role in redox biology and potential as a target for drugs against neglected diseases
Prast-Nielsen, Stefanie; Huang, Hsin-Hung; Williams, David L.
Follow Biochimica et Biophysica Acta (BBA) - General Subjects , Volume 1810 (12)
Elsevier – Dec 1, 2011Background There are two, largely autonomous antioxidant pathways in many organisms, one based on thioredoxin and one based on glutathione, with each pathway having a unique flavoprotein ...
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Cysteine mutant of mammalian GPx4 rescues cell death induced by disruption of the wild-type selenoenzyme
Mannes, Alexander M.; Seiler, Alexander; Bosello, Valentina; Maiorino, Matilde; Conrad, Marcus
Follow The FASEB Journal , Volume 25 (7): 2135
Fed of American Socs for Experimental Biology – Jul 1, 2011in all domains of life. However, in homologous enzymes within the same or other proteomes, Sec is frequently replaced by the most common functional analog, cysteine (Cys), which differs only in a single ...
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The thioredoxin system—From science to clinic
Gromer, Stephan; Urig, Sabine; Becker, Katja
Follow Medicinal Research Reviews , Volume 24 (1)
Wiley – Oct 28, 2003subtrate, Hg2 þ -ions, inactivateTrxRs. Inversely, thioredoxin is not reduced by HgR. of the two catalytically redox active cysteine residues (Cys32 and Cys35 in human Trx-1) is burried (Cys35), whereas ...
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Investigation of a potential mechanism for the inhibition of Sm TGR by Auranofin and its implications for Plasmodium falciparum inhibition
Caroli, Antonia; Simeoni, Silvia; Lepore, Rosalba; Tramontano, Anna; Via, Allegra
Follow Biochemical and Biophysical Research Communications , Volume 417 (1)
Elsevier – Jan 6, 2012) domain (residues 1–106) and a Thioredoxin Reductase (TR) domain (residues 107–598) [4] , which contains a selenocysteine (Sec597) as the penultimate C-terminal amino acid [5] . Each monomer has a large ...
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The Structure of Human Thioredoxin Reductase 1 Provides Insights into C-terminal Rearrangements During Catalysis
Fritz-Wolf, Karin; Urig, Sabine; Becker, Katja
Follow Journal of Molecular Biology , Volume 370 (1)
Elsevier – Jun 29, 2007Human thioredoxin reductase (hTrxR) is a homodimeric flavoprotein crucially involved in the regulation of cellular redox reactions, growth and differentiation. The enzyme contains a selenocysteine ...
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