Results 51 to 60 of about 90,159 (370)
Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass
Microbiology and Molecular Biology Reviews, 2018 Biomass constitutes an appealing alternative to fossil resources for the production of materials and energy. The abundance and attractiveness of vegetal biomass come along with challenges pertaining to the intricacy of its structure, evolved during ...
Bastien Bissaro +3 more
semanticscholar +1 more source
Functional design of bacterial superoxide:quinone oxidoreductase [PDF]
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2021 AbstractThe superoxide anion - molecular oxygen reduced by a single electron - is produced in large amounts by enzymatic and adventitious reactions and can perform a range of cellular functions, including bacterial warfare and iron uptake, signalling and host immune response in eukaryotes.
Abbas Abou-Hamdan +7 more
openaire +4 more sources
Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space [PDF]
, 2017 Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways.
Cardenas-Rodriguez, Mauricio +1 more
core +1 more source
ER-Mitochondria contact sites : a new regulator of cellular calcium flux comes into play [PDF]
, 2016 Endoplasmic reticulum (ER)-mitochondria membrane contacts are hotspots for calcium signaling. In this issue, Raturi et al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201512077) show that the thioredoxin TMX1 inhibits the calcium pump SERCA2b at ...
Anelli +22 more
core +2 more sources
, 2020 The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium ...
Moroder, L., Musiol, H.
core +1 more source
Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases [PDF]
, 2014 Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as protein disulfide isomerase and a mechanism to form disulfides de novo.
Appenzeller-Herzog +22 more
core +1 more source
Journal of Clinical Medicine, 2019 Flavoprotein oxidoreductases are members of a large protein family of specialized dehydrogenases, which include type II NADH dehydrogenase, pyridine nucleotide-disulphide oxidoreductases, ferredoxin-NAD+ reductases, NADH oxidases, and NADH peroxidases ...
Lucia Trisolini +8 more
semanticscholar +1 more source
Applications of Oxidoreductases
, 2021 Oxidoreductases comprise of a large group of enzymes catalyzing the transfer of electrons from an electron donor to an electron acceptor molecule, commonly taking nicotinamide adenine dinucleotide phosphate (NADP) or nicotinamide adenine dinucleotide (NAD) as cofactors.
openaire +3 more sources
How are proteins reduced in the endoplasmic reticulum? [PDF]
, 2018 The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for protein folding, degradation, chaperone function, and the ER stress response. Our understanding of this process is generally poor but progress has been made.
Bulleid, Neil +2 more
core +2 more sources
A structure-based approach for detection of thiol oxidoreductases and their catalytic redox-active cysteine residues. [PDF]
PLoS Computational Biology, 2009 Cysteine (Cys) residues often play critical roles in proteins, for example, in the formation of structural disulfide bonds, metal binding, targeting proteins to the membranes, and various catalytic functions.
Stefano M Marino, Vadim N Gladyshev
doaj +1 more source