Results 101 to 110 of about 19,795 (176)

Poster Sessions

open access: yes
HemaSphere, Volume 10, Issue S1, June 2026.
wiley   +1 more source

Mammalian Selenoprotein Thioredoxin-glutathione Reductase

open access: yes, 2005
Thioredoxin reductases (TRs) are important redox regulatory enzymes, which control the redox state of thioredoxins. Mammals have cytosolic and mitochondrial TRs, which contain an essential selenocysteine residue and reduce cytosolic and mitochondrial ...
Novoselov, Sergey V.   +7 more
core  

Guiding bar motif of thioredoxin reductase 1 modulates enzymatic activity and inhibitor binding by communicating with the co-factor FAD and regulating the flexible C-terminal redox motif

open access: yesRedox Biology
Thioredoxin reductase (TXNRD) is a selenoprotein that plays a crucial role in cellular antioxidant defense. Previously, a distinctive guiding bar motif was identified in TXNRD1, which influences the transfer of electrons.
Wuyang Shi   +14 more
doaj   +1 more source

Functional diversity of YbbN/CnoX proteins: Insights from a comparative analysis of three thioredoxin-like oxidoreductases from Pseudomonas aeruginosa, Xylella fastidiosa and Escherichia coli

open access: yesRedox Biology
YbbN/CnoX are proteins that display a Thioredoxin (Trx) domain linked to a tetratricopeptide domain. YbbN from Escherichia coli (EcYbbN) displays a co-chaperone (holdase) activity that is induced by HOCl.
Diogo de Abreu Meireles   +6 more
doaj   +1 more source

Western blots of cytosolic Thioredoxin and Thioredoxin reductase.

open access: yes, 2016
Representative western blots used for the protein estimations of cytosolic thioredoxin (A) and cytosolic thioredoxin reductase (B).
Galina Zeltcer (2890028)   +4 more
core   +1 more source

FLUORESCENT ASSAY TO TEST PROTEIN DISULFIDE ISOMERASE ACTIVITY INDUCED BY THIOREDOXIN REDUCTASE.

open access: yes, 2004
In eukaryotic cells the ubiquitous thioredoxin reductase-thioredoxin system (TrxR-Trx) catalyses substrate disulfide reduction using NADPH as a source of reducing equivalents.
G. Guella   +4 more
core  

Study of the reductive and oxidative half reactions of Escherichia coli thioredoxin reductase: Implications for catalysis.

open access: yes, 1995
Thioredoxin reductase from E. coli is a dimeric flavoenzyme containing an FAD and a redox active disulfide in each subunit. Recent structural work indicates that thioredoxin reductase exists in two conformations, both of which are necessary for catalysis.
Lennon, Brett William
core  

Crosstalk of thioredoxin system and programmed cell death: from pathophysiology to novel therapy. [PDF]

open access: yesRedox Biol
Wu Y   +11 more
europepmc   +1 more source

1,2,3-Benzoxathiazine-2,2-Dioxides as Inhibitors of Thioredoxin Reductase. [PDF]

open access: yesChemMedChem
Ivanova J   +4 more
europepmc   +1 more source

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