Results 41 to 50 of about 91,003 (373)

Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases [PDF]

open access: yes, 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

Synthèse bibliographique: la divinyl éther synthase de plantes [PDF]

open access: yesBiotechnologie, Agronomie, Société et Environnement, 2001
Divinyl ether synthase in plants: a review. Divinyl ether synthase, an enzyme of the lipoxygenase pathway transforms, in potato tubers, 9-hydroperoxides of fatty acids into colneleic and colnelenic acid, two divinyl ethers of fatty acids.
Fauconnier M.L.   +4 more
doaj  

FAD/NADH Dependent Oxidoreductases: From Different Amino Acid Sequences to Similar Protein Shapes for Playing an Ancient Function

open access: yesJournal 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

How are proteins reduced in the endoplasmic reticulum? [PDF]

open access: yes, 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]

open access: yesPLoS 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

Electrodes modified with lipid membranes to study quinone oxidoreductases

open access: yes, 2009
Quinone oxidoreductases are a class of membrane enzymes that catalyse the oxidation or reduction of membrane-bound quinols/quinones. The conversion of quinone/quinol by these enzymes is difficult to study because of the hydrophobic nature of the enzymes ...
Jeuken, LJC, Weiss, SA
core   +1 more source

Structures and proton-pumping strategies of mitochondrial respiratory enzymes [PDF]

open access: yes, 2001
Enzymes of the mitochondrial respiratory chain serve as proton pumps, using the energy made available from electron transfer reactions to transport protons across the inner mitochondrial membrane and create an electrochemical gradient used for the ...
Chan, Sunney I., Schultz, Brian E.
core   +1 more source

Ancestral Absence of Electron Transport Chains in Patescibacteria and DPANN

open access: yesFrontiers in Microbiology, 2020
Recent discoveries suggest that the candidate superphyla Patescibacteria and DPANN constitute a large fraction of the phylogenetic diversity of Bacteria and Archaea.
Jacob P. Beam   +21 more
doaj   +1 more source

Relating the metatranscriptome and metagenome of the human gut [PDF]

open access: yes, 2014
Although the composition of the human microbiome is now wellstudied, the microbiota’s \u3e8 million genes and their regulation remain largely uncharacterized.
Boylan, Matthew R.   +13 more
core   +2 more sources

Role of glutathionylation in infection and inflammation [PDF]

open access: yes, 2019
Glutathionylation, that is, the formation of mixed disulfides between protein cysteines and glutathione (GSH) cysteines, is a reversible post-translational modification catalyzed by dierent cellular oxidoreductases, by which the redox state of the cell
Baldelli, S.   +5 more
core   +1 more source

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