Primary and secondary oxidative stress in Bacillus [PDF]
, 2011 Coping with oxidative stress originating from oxidizing compounds or reactive oxygen species (ROS), associated with the exposure to agents that cause environmental stresses, is one of the prerequisites for an aerobic lifestyle of Bacillus spp. such as B.
Abee, T., Mols, J.M.
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ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor [PDF]
, 2013 ERdj5 is a member of the protein disulfide isomerase family of proteins localized to the endoplasmic reticulum (ER) of mammalian cells. To date, only a limited number of substrates for ERdj5 are known.
Braakman, Ineke +4 more
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Solution Structures of \u3cem\u3eMycobacterium tuberculosis\u3c/em\u3e Thioredoxin C and Models of Intact Thioredoxin System Suggest New Approaches to Inhibitor and Drug Design [PDF]
, 2013 Here, we report the NMR solution structures of Mycobacterium tuberculosis (M. tuberculosis) thioredoxin C in both oxidized and reduced states, with discussion of structural changes that occur in going between redox states.
Cai, Sheng +3 more
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Peroxidasin enables melanoma immune escape by inhibiting natural killer cell cytotoxicity
Molecular Oncology, EarlyView.Peroxidasin (PXDN) is secreted by melanoma cells and binds the NK cell receptor NKG2D, thereby suppressing NK cell activation and cytotoxicity. PXDN depletion restores NKG2D signaling and enables effective NK cell–mediated melanoma killing. These findings identify PXDN as a previously unrecognized immune evasion factor and a potential target to improve
Hsu‐Min Sung +17 more
wiley +1 more source
Structure of Hordeum vulgare NADPH-dependent thioredoxin reductase 2. Unwinding the reaction mechanism [PDF]
, 2009 Thioredoxins (Trxs) are protein disulfide reductases that regulate the intracellular redox environment and are important for seed germination in plants.
Finnie, Christine +4 more
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Advanced Science, EarlyView.Understanding protein sequence–function relationships remains challenging due to poorly defined motifs and limited residue‐level annotations. An annotation‐agnostic framework is introduced that segments protein sequences into “protein words” using attention patterns from protein language models.
Hedi Chen +9 more
wiley +1 more source
キイロショウジョウバエ由来のチオレドキシン還元酵素のC未端テトラペプチド配列は、ヒト肺由来のチオレドキシン還元酵素では酸化還元活性を示さない [PDF]
, 2007 The isozymes of mammalian thioredoxin reductase (TrxR) contain the penultimate selenocysteineresidue (SeCys) in the redox-active C-terminal tetrapeptide, -Gly-Cys-SeCys-Gly (end). Amutant form of the mammalian enzyme TrxR-X498C in which SeCys is replaced
Inagaki, Kenji +3 more
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Electron Transfer Pathways and Dynamics of Chloroplast NADPH-dependent Thioredoxin Reductase C (NTRC) [PDF]
, 2012 NADPH-dependent thioredoxin reductases (NTRs) contain a flavin cofactor and a disulfide as redox-active groups. The catalytic mechanism of standard NTR involves a large conformational change between two configurations.
Bernal Bayard, Pilar +3 more
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Role of selenium in the pathophysiology of cardiorenal anaemia syndrome
ESC Heart Failure, Volume 12, Issue 2, Page 770-780, April 2025.Abstract Chronic kidney disease (CKD) and cardiovascular disease (CVD) have multiple bidirectional mechanisms, and anaemia is one of the critical factors that are associated with the progression of the two disorders [referred to as cardiorenal anaemia syndrome (CRAS)].
Shigeyuki Arai +2 more
wiley +1 more source
Improving Digestibility of Soy Flour by Reducing Disulfide Bonds with Thioredoxin [PDF]
, 2008 The Kunitz trypsin inhibitor (KTI) and the Bowman−Birk inhibitor (BBI) of trypsin and chymotrypsin contain disulfide bonds. Glycinin, the major storage protein in soybeans also contains disulfide bonds.
Faris, Richard +3 more
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