Results 311 to 320 of about 558,186 (382)
Determination and significance of nitrate reductase in marine fungi. Proc. 4th Europ. Marine Microbiol. Symp. 1990 [PDF]
Molitoris, Hans-Peter, Rau, R.
core
Identification of transcription factors of nitrate reductase gene promoters and NRE2 cis-element through yeast one-hybrid screening in Nicotiana tabacum. [PDF]
Yang H, Zhou Y, Zhang Y, Wang J, Shi H.
europepmc +1 more source
Activity of Spore-Specific Respiratory Nitrate Reductase 1 of Streptomyces coelicolor A3(2) Requires a Functional Cytochrome bcc-aa3 Oxidase Supercomplex. [PDF]
Falke D+5 more
europepmc +1 more source
Diatom triacylglycerol metabolism: from carbon fixation to lipid droplet degradation
ABSTRACT Diatoms are a prominent microalgae family that has attracted interest for its production of molecules of biotechnological interest. Their fatty acid profile is rich in health‐beneficial omega‐3 eicosapentaenoic acid (EPA). Furthermore, under nutrient‐deprived conditions, many diatom species, notably Phaeodactylum tricornutum, Thalassiosira ...
Victor Murison+3 more
wiley +1 more source
GLS1‐mediated glutaminolysis supports GSH synthesis in cancer cells. GLS1 KO increases ROS, downregulates GPX4, and upregulates GPX1, making cells more sensitive to ferroptosis. Combining GLS1 or GPX1 inhibitors with a GPX4 inhibitor synergistically suppresses cancer growth.
Changsen Bai+13 more
wiley +1 more source
Development of selective growth media for denitrifying bacteria using an evolutionary algorithm: a strategy outline [PDF]
Boon, Nico+5 more
core
The radical SAM enzyme NirJ is responsible for the removal of two propionate side chains from its substrate didecarboxy‐siroheme during heme d1 biosynthesis. The cleavage products of the NirJ reaction were not known so far. In this study, it is shown that acrylate is formed as the reaction byproduct and that the resulting tetrapyrrole product carries ...
Heike Meyer+5 more
wiley +1 more source
The authors identify PbfF (previously annotated as a NAD‐dependent dehydrogenase) as a hitherto unknown enzyme in phosphonate catabolism. Guided by genome context analysis, they show that PbfF is actually a racemase, serving to degrade the natural compound (S)‐2‐amino‐1‐hydroxyethylphosphonate (S‐HAEP).
Francesca Ruffolo+8 more
wiley +1 more source