Results 81 to 90 of about 19,795 (176)
Measurement of thioredoxin and thioredoxin reductase
, 2001 The thioredoxin system is ubiquitous, providing reducing equivalents to essential biosynthetic enzymes like ribonucleotide reductase. It is essential for cellular redox regulation, control of oxidative stress, and protection against oxidative damage ...
Holmgren, A,, Arnér, ES
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LUCID: An Integrative Approach for Target Discovery and dsRNA Design in Plant Fungal Pathogens
Plant Biotechnology Journal, Volume 24, Issue 6, Page 3597-3615, June 2026.LUCID: A computational pipeline for RNAi‐based biofungicide design. ABSTRACT Phytopathogenic fungi pose an escalating threat to global food security and ecosystem stability, as resistance and environmental concerns diminish the effectiveness of conventional fungicides.
Lucía Jiménez‐Castro +4 more
wiley +1 more source
Mycothiol disulfide reductase as a drug target
, 2010 Includes abstract. Includes bibliographical references (leaves 154-171)
Mavumengwana, Vuyo Bhongolethu
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Structure-functional Characterization of Mammalian Redox Proteins: Methionine sulfoxide reductase B1 (MsrB1), Glutaredoxin domain (Grx) of TGR, and Thioredoxin (Trx) [PDF]
, 2013 This thesis was written at the Department of Biotechnology of Norwegian University of Science and Technology (NTNU) and made as a completion of the three-year PhD program.
Dobrovolska, Olena
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, 2022 Lymphoma refers to a group of cancers that arise from lymphocytes and is the most common form of hematological malignancy in adults. While the recent availability of specific chemotherapy regimes has resulted in good patient outcomes for some lymphoma ...
Wang, Sicong +2 more
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, 2010 The enzymatic activity of thioredoxin reductase enzymes is endowed by at least two redox centers: a flavin and a dithiol/disulfide CXXC motif. The interaction between thioredoxin reductase and thioredoxin is generally species-specific, but the molecular ...
Netto, Luis E. S. +6 more
core +2 more sources
Crystal structure of the Plasmodium falciparum thioredoxin reductase-thioredoxin complex
, 2013 Over the last decades, malaria parasites have been rapidly developing resistance against antimalarial drugs, which underlines the need for novel drug targets.
Jortzik, E. +6 more
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Frontiers in Bioengineering and Biotechnology, 2019 Peptides and proteins containing disulfide bonds can be produced in Escherichia coli by targeting the oxidizing periplasm, co-expressing isomerases or chaperons, refolding from inclusion bodies, or by using redox-engineered E. coli strains.
Mathias Joachim +7 more
doaj +1 more source
Endoplasmic reticulum H₂O₂ : Ero1-driven generation and GPx-mediated detoxification [PDF]
, 2014 Endoplasmic reticulum (ER) oxidoreductin 1 alpha (Ero1alpha) is an ER-resident oxidase, which utilizes molecular oxygen (O2) as terminal electron acceptor to produce disulfide bonds and hydrogen peroxide (H2O2).
Ramming, Thomas
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PLoS Genetics, 2017 The thioredoxin and glutaredoxin pathways are responsible of recycling several enzymes which undergo intramolecular disulfide bond formation as part of their catalytic cycles such as the peroxide scavengers peroxiredoxins or the enzyme ribonucleotide ...
Susanna Boronat +6 more
doaj +1 more source