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
Systems-Based Design of Bi-Ligand Inhibitors of Oxidoreductases: Filling the Chemical Proteomic Toolbox [PDF]
, 2004 Genomics-driven growth in the number of enzymes of unknown function has created a need for better strategies to characterize them. Since enzyme inhibitors have traditionally served this purpose, we present here an efficient systems-based inhibitor design
Baker, Brian +18 more
core +2 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
The evolution of enzyme function in the isomerases. [PDF]
, 2014 The advent of computational approaches to measure functional similarity between enzymes adds a new dimension to existing evolutionary studies based on sequence and structure.
Furnham, Nicholas +4 more
core +1 more source
, 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
Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated [PDF]
, 2010 The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells are incompletely understood. Here, we show that after reductive challenge the ER steady-state disulphide content is restored on a time scale of seconds ...
Appenzeller-Herzog, Christian +6 more
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The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotides [PDF]
The journal of biological chemistry, American Society for
Biochemistry and Molecular Biology, 1999, 274, pp.18252-60, 2015 The NAD(P)H:flavin oxidoreductase from Escherichia coli, named Fre, is a monomer of 26.2 kDa that catalyzes the reduction of free flavins using NADPH or NADH as electron donor. The enzyme does not contain any prosthetic group but accommodates both the reduced pyridine nucleotide and the flavin in a ternary complex prior to oxidoreduction.
arxiv +1 more source
Scaling perspective on Intramolecular vibrational energy flow: analogies, insights, and challenges [PDF]
Advances in Chemical Physics, Eds. S. A. Rice and A. R. Dinner,
vol. 153, 43-110 (2013), 2013 Review of the scaling approach to intramolecular vibrational energy flow emphasizing the classical-quantum correspondence perspective.
arxiv +1 more source
Understanding the role of intramolecular ion-pair interactions in conformational stability using an ab initio thermodynamic cycle [PDF]
, 2022 Intramolecular ion-pair interactions yield shape and functionality to many molecules. With proper orientation, these interactions overcome steric factors and are responsible for the compact structures of several peptides. In this study, we present a thermodynamic cycle based on isoelectronic and alchemical mutation to estimate intramolecular ion-pair ...
arxiv +1 more source
Dramatic down-regulation of oxidoreductases in human hepatocellular carcinoma hepG2 cells: proteomics and gene ontology unveiling new frontiers in cancer enzymology [PDF]
, 2008 Background Oxidoreductases are enzymes that catalyze many redox reactions in normal and neoplastic cells. Their actions include catalysis of the transformation of free, neutral oxygen gas into oxygen free radicals, superoxide, hydroperoxide, singlet ...
Ngoka, Lambert CM
core +4 more sources