Results 31 to 40 of about 764,898 (194)
Methionine sulfoxide reductase A is a stereospecific methionine oxidase
, 2011 Methionine sulfoxide reductase A (MsrA) catalyzes the reduction of methionine sulfoxide to methionine and is specific for the S epimer of methionine sulfoxide. The enzyme participates in defense against oxidative stresses by reducing methionine sulfoxide
Zheng You +3 more
core +1 more source
Quantitative Analysis of in Vivo Methionine Oxidation of the Human Proteome
, 2019 The oxidation of methionine is an important post-translational modification of proteins with numerous roles in physiology and pathology. However, the quantitative analysis of methionine oxidation on a proteome-wide scale has been hampered by technical ...
Kevin A. Welle (4858720) +3 more
core +2 more sources
Tumour‐proximal deep serum proteomics identifies biomarkers associated with ovarian cancer
Molecular Oncology, EarlyView.New biomarkers are needed for early ovarian cancer detection. Ovarian (tumour‐proximal) and peripheral vein serum from healthy women and patients with benign or malignant tumours underwent nanoparticle‐enriched deep proteomics. Ovarian serum yielded more protein identifications and revealed tumour‐reflective signatures.
Darren Lau +9 more
wiley +1 more source
Characterization of methionine oxidation and methionine sulfoxide reduction using methionine-rich cysteine-free proteins [PDF]
BMC Biochemistry, 2012 Abstract Background Methionine (Met) residues in proteins can be readily oxidized by reactive oxygen species to Met sulfoxide (MetO). MetO is a promising physiological marker of oxidative stress and its inefficient repair by MetO reductases (Msrs) has been linked to neurodegeneration and aging. Conventional methods of
Liang, Xinwen +5 more
openaire +4 more sources
FEBS Open Bio, EarlyView.NMR metabolomics revealed concentration‐dependent metabolic perturbations in HepG2 cells exposed to H2O2. Rifampicin pretreatment enhanced metabolic competence, attenuated toxin‐induced alterations and produced metabolite profiles more consistent with human liver physiology, supporting the use of CYP450‐induced HepG2 models for improved in vitro ...
Maren Jinks +4 more
wiley +1 more source
The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity
FEBS Open Bio, EarlyView.Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav +4 more
wiley +1 more source
Recent insights into the molecular mechanism of ubiquinol oxidation by cytochrome bc1
FEBS Open Bio, EarlyView.The review reflects on the mechanism of the catalytic reaction in cytochrome bc1: the electron bifurcation that involves the separation of two electrons derived from the quinol oxidation to opposite sides of the enzyme across the membrane. This review summarizes the long‐standing effort to understand the mechanism of quinol oxidation catalyzed by ...
Anna Wójcik‐Augustyn +2 more
wiley +1 more source
Characterization of the key membrane protein cytochrome Cyc2 from Ghiorsea bivora
FEBS Open Bio, EarlyView.This study reports the first detailed biochemical analysis of Cyc2TAG1_1, a cytochrome protein involved in microbial iron oxidation. We produced and purified this enzyme in E. coli, then measured its iron‐oxidizing efficiency, and characterized its electrical and structural properties.
Josiane Azizi +6 more
wiley +1 more source
Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems [PDF]
Proceedings of the National Academy of Sciences, 1997 Aging and some pathological conditions are associated with the accumulation of altered (inactive or less active) forms of enzymes. It was suggested that these age-related alterations reflect spontaneous changes in protein conformation and/or posttranslational modifications (e.g., oxidation). Because changes in protein conformations
C C, Chao, Y S, Ma, E R, Stadtman
openaire +2 more sources
Conformational Switching of Proteins on Material Surfaces Enabled by Peptide‐Oriented Adsorption
Advanced Functional Materials, EarlyView.Responsive biointerfaces could be achieved using conformationally responsive proteins; however, their interconversion can be lost upon surface adsorption. Herein, we demonstrate that the incorporation a Au binding peptide into calmodulin allows for binding control on Au wherein the protein retains conformational switching. This capability was confirmed
Sakthirupini Ramamurthy +7 more
wiley +1 more source