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148 Newest Publications of Portland Press

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Processing of Protein ADP-ribosylation by Nudix Hydrolases

19-Mar-2015 | Palazzo L; Thomas B; Jemth A; Colby T; Leidecker O; Feijs K; Zaja R; Loseva O; Puigvert J; Matic I; Helleday T; Ahel I, Biochemical Journal, 2015

ADP-ribosylation is a post-translational modification of proteins found in organisms from all kingdoms of life which regulates many important biological functions including DNA repair, chromatin structure, unfolded protein response, and apoptosis. Several cellular enzymes, such as macrodomain ...

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Ubiquitin C-terminal hydrolases cleave isopeptide- and peptide-linked ubiquitin from structured proteins but do not edit ubiquitin homopolymers

15-Mar-2015 | Bett JS; Ritorto MS; Ewan R; Jaffray EG; Virdee S; Chin JW; Knebel A; Kurz T; Trost M; Tatham MH; Hay RT, Biochemical Journal, 2015

Modification of proteins with ubiquitin (Ub) occurs through a variety of topologically distinct Ub linkages, including Ube2W-mediated monoubiquitylation of N-terminal alpha amines to generate peptide-linked linear mono-Ub fusions. Protein ubiquitylation can be reversed by the action of ...

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The purification and characterization of ATP synthase complexes from the mitochondria of four fungal species

11-Mar-2015 | Liu S; Charlesworth T; Bason J; Montgomery M; Harbour M; Fearnley I; Walker J, Biochemical Journal, 2015

The ATP synthases have been isolated by affinity chromatography from the mitochondria of the fungal species, Yarrowia histolytica, Pichia pastoris, Pichia angusta and Saccharomyces cerevisae. The subunit compositions of the purified enzyme complexes depended upon the detergent used to solubilise ...

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Solution Structure of the Reduced Form of Human Peroxiredoxin-6 Elucidated Using Zero-Length Chemical Cross-linking And Homology Modeling

06-Mar-2015 | Rivera-Santiago R; Harper S; Zhou S; Sriswasdi S; Feinstein S; Fisher A; Speicher D, Biochemical Journal, 2015

Peroxiredoxin-6 (PRDX6) is an unusual member of the peroxiredoxin family of antioxidant enzymes that has only one evolutionarily conserved cysteine. It reduces oxidized lipids and ROS by oxidation of the active site cysteine (Cys-47) to a sulfenic acid, but the mechanism for conversion back to a ...

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Electron transfer by human wild-type and A287P mutant P450 oxidoreductase assessed by transient kinetics: Functional Basis of P450 Oxidoreductase Deficiency

02-Mar-2015 | Jin Y; Chen M; Penning T; Miller W, Biochemical Journal, 2015

Cytochrome P450 oxidoreductase (POR) is a 2-flavin protein that transfers electrons from NADPH via its FAD and FMN moieties to all microsomal cytochrome P450 enzymes, including steroidogenic and drug-metabolizing P450s. Defects in the POR gene can cause POR deficiency (PORD), manifested ...

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Assembly and structure of Lys33-linked polyubiquitin reveals distinct conformations

27-Feb-2015 | Kristariyanto Y; Choi S; Abdul Rehman S; Ritorto M; Campbell D; Morrice N; Toth R; Kulathu Y, Biochemical Journal, 2015

Ubiquitylation regulates a multitude of biological processes and this versatility stems from the ability of ubiquitin to form topologically different polymers of eight different linkage types. While some linkages have been studied in detail, other linkage types including Lys33-linked ...

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Defining the Cytosolic Pathway of Glutathione Degradation in {Less than}i{Greater than}Arabidopsis thaliana{Less than}/i{Greater than}: Role of the ChaC/GCG Family of {gamma}-glutamyl cyclotransferases as Glutathione Degrading Enzymes and AtLAP1 as the Cys-Gly Peptidase

26-Feb-2015 | Kumar S; Kaur A; Chattopadhyay B; Bachhawat A, Biochemical Journal, 2015

Glutathione homeostasis is critical to plant life and its adaptation to stress. The γ-glutamyl cycle of glutathione biosynthesis and degradation plays a pre-eminent role in glutathione homeostasis. The genes encoding two enzymatic steps of glutathione degradation, the γ-glutamyl cyclotransferase ...

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Yeast Hmt1 catalyzes asymmetric dimethylation of histone H3 arginine 2 {Less than}i{Greater than}in vitro{Less than}/i{Greater than}

26-Feb-2015 | Li H; Gong T; Zhou Z; Liu Y; Cao X; He Y; Chen C; Zhou J, Biochemical Journal, 2015

Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate protein arginine residues. PRMTs’ substrates include histones and a variety of non-histone proteins. Previous studies have shown that yeast Hmt1 is a type I PRMT, and methylates histone H4 arginine 3 and ...

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Ubiquitin-C-terminal hydrolases cleave isopeptide and peptide-linked ubiquitin from structured proteins but do not edit ubiquitin homopolymers

09-Dec-2014 | Bett J; Ritorto M; Ewan R; Jaffray E; Virdee S; Chin J; Knebel A; Kurz T; Trost M; Tatham M; Hay R, Biochemical Journal, 2014

Modification of proteins with ubiquitin (Ub) occurs through a variety of topologically distinct Ub linkages, including Ube2W-mediated monoubiquitylation of N-terminal alpha amines to generate peptide-linked linear mono-Ub fusions. Protein ubiquitylation can be reversed by the action of ...

more

Kinetic Characterization of a Cocaine Hydrolase Engineered from Mouse Butyrylcholinesterase

08-Dec-2014 | Chen X; Huang X; Geng L; Xue L; Hou S; Zheng X; Brimijoin S; Zheng F; Zhan C, Biochemical Journal, 2014

Mouse butyrylcholinesterase (mBChE) and an mBChE-based cocaine hydrolase (mCocH, i.e. the A199S/S227A/S287G/A328W/Y332G mutant) have been characterized for their catalytic activities against cocaine, i.e. naturally occurring (-)-cocaine, in comparison with the corresponding human BChE (hBChE) and ...

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