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February 2020
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Cover Image
Structural analysis of tyrosine residues in human MnSOD (PDB ID: 2ADP) support the metal-catalyzed and site-specific formation of nitro-Tyr34. This oxidative posttranslational modification in the active site leads to enzyme inactivation. For more information see the review by Campolo and colleagues (pp. 111–133). Image courtesy of Rafael Radi.
ISSN 0071-1365
EISSN 1744-1358
In this Issue
Protein Oxidation
Review Articles
Introduction to approaches and tools for the evaluation of protein cysteine oxidation
Essays Biochem (2020) 64 (1): 1–17.
Modification of proteins by reactive lipid oxidation products and biochemical effects of lipoxidation
Essays Biochem (2020) 64 (1): 19–31.
Photo-induced protein oxidation: mechanisms, consequences and medical applications
Essays Biochem (2020) 64 (1): 33–44.
Mechanisms and consequences of protein cysteine oxidation: the role of the initial short-lived intermediates
Essays Biochem (2020) 64 (1): 55–66.
Antioxidants and radical damage in a hydrophilic environment: chemical reactions and concepts
Essays Biochem (2020) 64 (1): 67–74.
Dicarbonyl derived post-translational modifications: chemistry bridging biology and aging-related disease
Essays Biochem (2020) 64 (1): 97–110.
3-Nitrotyrosine and related derivatives in proteins: precursors, radical intermediates and impact in function
Essays Biochem (2020) 64 (1): 111–133.
Persulfides, at the crossroads between hydrogen sulfide and thiols
Essays Biochem (2020) 64 (1): 155–168.
Reading patterns of proteome damage by glycation, oxidation and nitration: quantitation by stable isotopic dilution analysis LC-MS/MS
Essays Biochem (2020) 64 (1): 169–183.
