Results 31 to 40 of about 206,003 (304)

‐dependent thioredoxin reductases [PDF]

open access: yes, 2023
The thioredoxin pathway is an antioxidant system present in most organisms. Electrons flow from a thioredoxin reductase to thioredoxin at the expense of a specific electron donor. Most known thioredoxin reductases rely on NADPH as reducing cofactor. Yet,
Guang Yang   +14 more
core   +1 more source

The Barley Grain Thioredoxin System – an Update

open access: yesFrontiers in Plant Science, 2013
Thioredoxin reduces disulfide bonds and play numerous important functions in plants. In cereal seeds, cytosolic h-type thioredoxin facilitates the release of energy reserves during the germination process and is recycled by NADPH-dependent thioredoxin ...
Per eHägglund   +13 more
doaj   +1 more source

A Crystalline and Thermally Stable Selenocysteine Selenenic Acid

open access: yesAngewandte Chemie, EarlyView.
The long‐sought catalytic intermediate of selenoproteins, selenocysteine selenenic acid (Sec–SeOH), is isolated for the first time at ambient temperature. A bioinspired selenopeptide sequence encapsulated within a protective molecular cradle and an oxidant‐free route from selenenyl iodide (Sec–SeI) enable the isolation of Sec–SeOH. Contrary to the long‐
Ryosuke Masuda, Satoru Kuwano, Kei Goto
wiley   +2 more sources

Antioxidant Defense by Thioredoxin Can Occur Independently of Canonical Thiol-Disulfide Oxidoreductase Enzymatic Activity

open access: yesCell Reports, 2016
The thiol-disulfide oxidoreductase CXXC catalytic domain of thioredoxin contributes to antioxidant defense in phylogenetically diverse organisms. We find that although the oxidoreductase activity of thioredoxin-1 protects Salmonella enterica serovar ...
Miryoung Song   +4 more
doaj   +1 more source

Data on using single- and mixed-mode resins for capture chromatography of recombinant human thioredoxin from Escherichia coli

open access: yesData in Brief, 2020
This paper provides the data collected from screening chromatographic resins for their ability to bind and purify recombinant human thioredoxin from Escherichia coli lysate.
Ayswarya Ravi   +2 more
doaj   +1 more source

Thioredoxin Reductase Inhibitors as Potential Antitumors: Mercury Compounds Efficacy in Glioma Cells

open access: yesFrontiers in Molecular Biosciences, 2022
Glioblastoma multiforme (GBM) is the most aggressive and common form of glioma. GBM, like many other tumors, expresses high levels of redox proteins, such as thioredoxin (Trx) and thioredoxin reductase (TrxR), allowing tumor cells to cope with high ...
Vanessa Pires   +5 more
doaj   +1 more source

Thioredoxin system protein expression is associated with poor clinical outcome in adult and paediatric gliomas and medulloblastomas

open access: yes, 2020
The thioredoxin (Trx) system is an important enzyme family that regulates cellular redox homeostasis. Protein expression of Trx system family members has been assessed in various cancers and linked to various clinicopathological variables, disease ...
Smith, Stuart   +7 more
core   +1 more source

Thioredoxin VdTrx1, an unconventional secreted protein, is a virulence factor in Verticillium dahliae

open access: yesFrontiers in Microbiology, 2023
Understanding how plant pathogenic fungi adapt to their hosts is of critical importance to securing optimal crop productivity. In response to pathogenic attack, plants produce reactive oxygen species (ROS) as part of a multipronged defense response ...
Li Tian   +12 more
doaj   +1 more source

The roles of thioredoxin and thioredoxin-binding protein-2 in endometriosis [PDF]

open access: yesHuman Reproduction, 2010
Oxidative stress is considered to be involved in the establishment and development of endometriosis. Thioredoxin (TRX) is an endogenous redox regulator that protects cells against oxidative stress, and TRX-binding protein-2 (TBP-2) is a negative regulator of TRX in the biological function and expression.
Seok Kyo, Seo   +6 more
openaire   +3 more sources

Tuning of thioredoxin redox properties by intramolecular hydrogen bonds.

open access: yesPLoS ONE, 2013
Thioredoxin-like proteins contain a characteristic C-x-x-C active site motif and are involved in a large number of biological processes ranging from electron transfer, cellular redox level maintenance, and regulation of cellular processes.
Åsmund Kjendseth Røhr   +2 more
doaj   +1 more source

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