Selenium in thioredoxin reductase: a mechanistic perspective. - Wikidata - wikimedia - TriplyDB

Selenium in thioredoxin reductase: a mechanistic perspective.

Selenium in thioredoxin reductase: a mechanistic perspective.

http://www.wikidata.org/entity/Q36927962

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The human selenoproteome: recent insights into functions and regulation Differing views of the role of selenium in thioredoxin reductase Direct synthesis of sensitive selenocysteine peptides by the Ugi reaction.Using chemical approaches to study selenoproteins-focus on thioredoxin reductases Selenoproteins: molecular pathways and physiological roles.Methaneseleninic acid is a substrate for truncated mammalian thioredoxin reductase: implications for the catalytic mechanism and redox signaling Selenocysteine in thiol/disulfide-like exchange reactions.No selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue.Why is mammalian thioredoxin reductase 1 so dependent upon the use of selenium?Selenium as an electron acceptor during the catalytic mechanism of thioredoxin reductase Brevetoxin-2, is a unique inhibitor of the C-terminal redox center of mammalian thioredoxin reductase-1.The Architecture of Thiol Antioxidant Systems among Invertebrate Parasites.Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis.A "Seleno Effect" Differentiates the Roles of Redox Active Cysteine Residues in Plasmodium falciparum Thioredoxin Reductase.

P2860

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P2860

Selenium in thioredoxin reductase: a mechanistic perspective.

http://www.wikidata.org/entity/Q36927962

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

@zh-tw

2008年论文

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2008年论文

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2008年论文

@zh-cn

name

Selenium in thioredoxin reductase: a mechanistic perspective.

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type

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Selenium in thioredoxin reductase: a mechanistic perspective.

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Selenium in thioredoxin reductase: a mechanistic perspective.

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Selenium in thioredoxin reductase: a mechanistic perspective.

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P2093

Brian E Eckenroth

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Brian M Lacey

http://www.w3.org/2001/XMLSchema#string

Robert J Hondal

http://www.w3.org/2001/XMLSchema#string

Stevenson Flemer

http://www.w3.org/2001/XMLSchema#string

P2860

The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli

Structural and Biochemical Studies Reveal Differences in the Catalytic Mechanisms of Mammalian and Drosophila melanogaster Thioredoxin Reductases †

Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster

Thioredoxin and glutaredoxin systems

Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations

Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene

Physiological functions of thioredoxin and thioredoxin reductase

Selenium in chemistry and biochemistry in comparison to sulfur.

Conformational analysis of the eight-membered ring of the oxidized cysteinyl-cysteine unit implicated in nicotinic acetylcholine receptor ligand recognition.

Crystal structures of oxidized and reduced mitochondrial thioredoxin reductase provide molecular details of the reaction mechanism.

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12810-12821

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10.1021/BI800951F

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48

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47

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18986163

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