Results 11 to 20 of about 670,508 (357)
Quinone Reductase 2 Is a Catechol Quinone Reductase [PDF]
Journal of Biological Chemistry, 2008 The functions of quinone reductase 2 have eluded researchers for decades even though a genetic polymorphism is associated with various neurological disorders. Employing enzymatic studies using adrenochrome as a substrate, we show that quinone reductase 2 is specific for the reduction of adrenochrome, whereas quinone reductase 1 shows no activity.
Leonid Buryanovskyy +2 more
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RIBONUCLEOTIDE REDUCTASES [PDF]
Annual Review of Biochemistry, 1998 Ribonucleotide reductases provide the building blocks for DNA replication in all living cells. Three different classes of enzymes use protein free radicals to activate the substrate. Aerobic class I enzymes generate a tyrosyl radical with an iron-oxygen center and dioxygen, class II enzymes employ adenosylcobalamin, and the anaerobic class III enzymes
A, Jordan, P, Reichard
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Production of Long Chain Fatty Alcohols Found in Bumblebee Pheromones by Yarrowia lipolytica
Frontiers in Bioengineering and Biotechnology, 2021 Fatty alcohols (FA-OH) are aliphatic unbranched primary alcohols with a chain of four or more carbon atoms. Besides potential industrial applications, fatty alcohols have important biological functions as well. In nature, fatty alcohols are produced as a
Jaroslav Hambalko +6 more
doaj +1 more source
Advanced NanoBiomed Research, 2021 The development of dark pro‐aggregation‐induced‐emission luminogens (pro‐AIEgens) based on the solid‐state intramolecular motion–caused quenching effect has been rarely reported in biochemical analysis.
Changhuo Xu +10 more
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Metagenomic Evidence for a Methylocystis Species Capable of Bioremediation of Diverse Heavy Metals
Frontiers in Microbiology, 2019 Heavy metal pollution has become an increasingly serious problem worldwide. Co-contamination with toxic mercury (Hg) and arsenic (As) presents a particularly difficult bioremediation trouble.
Ling-Dong Shi +9 more
doaj +1 more source
Frontiers in Molecular Biosciences, 2023 Thioredoxin/glutathione reductase (TGR) from the platyhelminthic parasitic worms has recently been identified as a drug target for the treatment of schistosomiasis.
Madison M. Smith, Graham R. Moran
doaj +1 more source
Fragment-based discovery of a regulatory site in thioredoxin glutathione reductase acting as "doorstop" for NADPH entry [PDF]
, 2018 Members of the FAD/NAD-linked reductase family are recognized as crucial targets in drug development for cancers, inflammatory disorders, and infectious diseases.
Angelucci, Francesco +16 more
core +3 more sources
Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State [PDF]
, 2016 The mitochondrial thioredoxin system (NADPH, thioredoxin reductase, thioredoxin) is a major redox regulator. Here we have investigated the redox correlation between this system and the mitochondrial enzyme cyclophilin D.
Bindoli, Alberto +7 more
core +1 more source
A hidden cause of infertility in hypothyroid patients [PDF]
, 2020 Methylene tetrahydrofolate reductase (MTHFR) gene mutations could be the cause of infertility in hypothyroid patients. Hence, it is worthy to screen for MTHFR gene mutations in infertile hypothyroid females and their partners if infertility persists ...
Ahmed, Soha Magdy +4 more
core +1 more source
Biochemical Journal, 2000 The mammalian thioredoxin reductases (TrxRs) are a family of selenium-containing pyridine nucleotide-disulphide oxidoreductases with mechanistic and sequence identity, including a conserved -Cys-Val-Asn-Val-Gly-Cys- redox catalytic site, to glutathione reductases.
D, Mustacich, G, Powis
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