Quantitative analysis of in vivo methionine oxidation of the human proteome.
Sign Up to like & getrecommendations! Published in 2019 at "Journal of proteome research"
DOI: 10.1021/acs.jproteome.9b00505
Abstract: The oxidation of methionine is an important posttranslational 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 limitations.… read more here.
Keywords: methodology; oxidation; analysis; methionine oxidation ... See more keywords
Detecting Differences in Prion Protein Conformation by Quantifying Methionine Oxidation
Sign Up to like & getrecommendations! Published in 2022 at "ACS Omega"
DOI: 10.1021/acsomega.1c04989
Abstract: A prion’s pathogenic character is enciphered in its conformation, which also defines the chemical environments of its amino acids. Differences in chemical environments influence the reactivity of amino acid side chains, in a conformation-dependent manner.… read more here.
Keywords: methionine oxidation; prion; conformation; prion protein ... See more keywords
Identification of methionine oxidation in human recombinant erythropoietin by mass spectrometry: Comparative isoform distribution and biological activity analysis
Sign Up to like & getrecommendations! Published in 2017 at "Preparative Biochemistry and Biotechnology"
DOI: 10.1080/10826068.2017.1365243
Abstract: ABSTRACT Background: Oxidative degradation of human recombinant erythropoietin (hrEPO) may occur in manufacturing process or therapeutic applications. This unfavorable alteration may render EPO inefficient or inactive. We investigated the effect of methionine/54 oxidative changes on… read more here.
Keywords: biological activity; methionine oxidation; activity; distribution ... See more keywords
Methionine oxidation under anaerobic conditions in Escherichia coli
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DOI: 10.1111/mmi.14971
Abstract: Repairing oxidative‐targeted macromolecules is a central mechanism necessary for living organisms to adapt to oxidative stress. Reactive oxygen and chlorine species preferentially oxidize sulfur‐containing amino acids in proteins. Among these amino acids, methionine can be… read more here.
Keywords: oxidation; escherichia coli; oxidation anaerobic; methionine oxidation ... See more keywords
Methionine oxidation in bacteria: A reversible post‐translational modification
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DOI: 10.1111/mmi.15000
Abstract: Methionine is a sulfur‐containing residue found in most proteins which are particularly susceptible to oxidation. Although methionine oxidation causes protein damage, it can in some cases activate protein function. Enzymatic systems reducing oxidized methionine have… read more here.
Keywords: reversible post; oxidation; post translational; methionine oxidation ... See more keywords
Viperin catalyzes methionine oxidation to promote protein expression and function of helicases
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DOI: 10.1126/sciadv.aax1031
Abstract: Methionine oxidation by viperin is critical for the expression and function of helicases. Helicases play pivotal roles in fundamental biological processes, and posttranslational modifications regulate the localization, function, and stability of helicases. Here, we report… read more here.
Keywords: oxidation; methionine oxidation; catalyzes methionine; function helicases ... See more keywords
A novel method for in silico assessment of Methionine oxidation risk in monoclonal antibodies: Improvement over the 2-shell model
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DOI: 10.1371/journal.pone.0279689
Abstract: Over the past decade, therapeutic monoclonal antibodies (mAbs) have established their role as valuable agents in the treatment of various diseases ranging from cancers to infectious, cardiovascular and autoimmune diseases. Reactive groups of the amino… read more here.
Keywords: oxidation; silico; methionine; methionine oxidation ... See more keywords