The oxidative environment and protein damage.

By M. Davies. Biochimica et Biophysica Acta, 2005

1,364 citations recorded by the source corpus.

Subfields: Inorganic Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c4a5dc9a20a99725b6c2b0979099726b0d19d31d

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Inorganic Chemistry

1. Barry Halliwell
2. Wangang Zhang
3. A. Ali
4. D. Ahn
5. Shan Xiao
6. A. Elozeiri
7. M. Davies

In Molecular Biology

1. M. Davies
2. Barry Halliwell
3. Wangang Zhang
4. D. Ahn
5. Shan Xiao
6. A. Ali
7. A. Elozeiri
8. I. Dalle-Donne

Citations in the corpus

• Effects of Ionizing Radiation on Biological Molecules—Mechanisms of Damage and Emerging Methods of Detection (2014, background): “OH, generated via IR and other processes, initiates cleavage of the protein backbone and reacts with each of the twenty standard amino acids and selenocysteine, with associated rate constants for all such reactions in the 10(7)–10(10) M - 1 s - 1 range (pH 7), reaching diffusion-limited rates for cy”
• Protein Oxidation: Basic Principles and Implications for Meat Quality (2013, background): “…in the presence of a sensitizer), chemical reagents (metal ions such as Fe2+ and Cu+, HONOO, ozone, N2O2, deoxyosones, ketoamines, H2O2, HOCl, and HOBr), environmental pollutants, drug and their metabolites, xenobiotics, and even cigarette smoke (Shacter, 2000; Davies, 2005; Tetik et al., 2007).”
• Biomarkers of oxidative damage in human disease. (2006, background): “5); by the formation of Michael adducts between Lys, His, and Cys residues and , -unsaturated aldehydes, forming ALEs; and by glycation/glycoxidation of Lys amino groups, forming advanced glycation end products (4, 11, 28, 29, 33, 142).”
• Antioxidant Activity of Proteins and Peptides (2008, background): “…of individual amino acid residues within proteins, with particular emphasis given to those residues containing sulfur or aromatic R-groups (Davies, 2005; Hernandez-Ledesma et al., 2005; Levine and Stadtman, 2001; Stadtman and Levine, 2001; Stadtman and Levine, 2003; Stadtman et al., 2003).”
• Oxidative stress and neurodegeneration: where are we now? (2006, background): “However, singlet O2 can form during lipid peroxidation and contribute to damage because of its ability to readily oxidize lipids, proteins and DNA (Girotti and Kriska 2004; Davies 2005).”
• Oxidative stress in neurodegenerative diseases (2012, background): “ROS mediated oxidation of protein side-chains and resulted in the introduction of hydroxyl groups or in the generation of protein based carbonyls [42] .”
• Metabolic Processes During Seed Germination (2017, background): “Oxidation of protein by ROS result in alteration of protein functions due to enzymatic and binding properties modifications [105].”
• Α-synuclein misfolding and Parkinson's disease. (2012, background): “Oxidized methionines often disrupt protein structure, since methionine sulfoxide is significantly more polar and rigid than methionine [145].”
• Protein oxidation and peroxidation (2016, methodology): “2, 1047–1052 CrossRef 89 Davies, M.J. and Gilbert, B.C. (1991) Free radical reactions. Fragmentation and rearrangements in aqueous solution. Adv. Detailed Reaction Mechanisms. 1, 35–81 90 Alfassi, Z. (1997) In Peroxyl Radicals, John Wiley and Sons, Chichester 91 Nauser, T., Casi, G., Koppenol, W.H. ”
• Effects of Dielectric Barrier Discharge (DBD) Cold Plasma Treatment on Physicochemical and Functional Properties of Peanut Protein (2018, background): “Aromatic and sulfur-containing amino acid side chains are known to be particularly susceptible to oxidation, given the extreme sensitivity of cysteine residues (Cataldo 2003; Davies 2005; Segat et al. 2014).”