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Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, ISSN 1474-905X, 01/2012, Volume 11, Issue 1, pp. 38 - 53
Photo-induced damage to proteins occurs via multiple pathways. Direct damage induced by UVB (λ 280-320 nm) and UVA radiation (λ 320-400 nm) is limited to a... 
Proteins - chemistry | Disease | Oxidation-Reduction | Humans | Photochemistry
Journal Article
Photochemical and Photobiological Sciences, ISSN 1474-905X, 01/2012, Volume 11, Issue 1, pp. 38 - 53
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 07/2016, Volume 138, Issue 27, pp. 8476 - 8488
Enzymes in the sulfur network generate the signaling molecule, hydrogen sulfide (H2S), from the amino acids cysteine and homocysteine. Since it is toxic at... 
CYTOCHROME-C-OXIDASE | ATOMS LI | PROTEIN | ELECTRON-PARAMAGNETIC-RESONANCE | RAY-ABSORPTION-SPECTROSCOPY | CYSTATHIONINE BETA-SYNTHASE | ETHYLMALONIC ENCEPHALOPATHY | CHEMISTRY, MULTIDISCIPLINARY | GAUSSIAN-BASIS SETS | CYSTEINE PERSULFIDES | POLYSULFIDES | Index Medicus
Journal Article
Journal Article
Biochimica et Biophysica Acta - Proteins and Proteomics, ISSN 1570-9639, 01/2005, Volume 1703, Issue 2, pp. 135 - 140
Journal Article
Journal of Neuroscience, ISSN 0270-6474, 03/2012, Volume 32, Issue 12, pp. 4133 - 4144
Potassium (K+) channels are essential to neuronal signaling and survival. Here we show that these proteins are targets of reactive oxygen species in mammalian... 
ALZHEIMERS-DISEASE BRAIN | CAENORHABDITIS-ELEGANS | LIPID-PEROXIDATION | PROTEIN OXIDATION | AMYLOID-BETA-PEPTIDE | A-BETA | MITOCHONDRIAL DYSFUNCTION | FREE-RADICAL GENERATION | TRANSGENIC MOUSE MODEL | NEUROSCIENCES | POTASSIUM CHANNEL | Fluoresceins - pharmacology | Membrane Potentials - genetics | Electric Stimulation | Age Factors | Cricetulus | Apoptosis - drug effects | Disulfides - toxicity | Embryo, Mammalian | Peptide Fragments - toxicity | 2,2'-Dipyridyl - analogs & derivatives | Humans | Oxidative Stress - physiology | Apoptosis - genetics | Male | 2,2'-Dipyridyl - toxicity | Propanols - pharmacology | Shab Potassium Channels - physiology | Alzheimer Disease - pathology | Cysteine - genetics | Transfection | Alanine - genetics | Neurons - physiology | Oxidation-Reduction - drug effects | Female | Neurons - drug effects | Disease Models, Animal | Shab Potassium Channels - genetics | Alzheimer Disease - physiopathology | Brain - cytology | Cricetinae | Amyloid beta-Peptides - toxicity | Animals, Genetically Modified | Cells, Cultured | Hydrogen Peroxide - pharmacology | Oxidants - toxicity | Oxidative Stress - genetics | Presenilin-1 - genetics | Membrane Potentials - physiology | Caenorhabditis elegans | Patch-Clamp Techniques | Amyloid beta-Protein Precursor - genetics | Animals | Analysis of Variance | Mice | Apoptosis - physiology | Oxidative Stress - drug effects | Alzheimer Disease - genetics | Mass Spectrometry - methods
Journal Article
Free Radical Biology and Medicine, ISSN 0891-5849, 08/2017, Volume 109, pp. 141 - 155
Protein function can be regulated post-translational modifications by numerous enzymatic and non-enzymatic mechanisms, including oxidation of cysteine and... 
Scaffolding proteins | DUF3585 | Methionine sulfoxide | Actin | Methionine | Methionine sulfoxide reductase | MICAL | Monooxygenase | Redox signaling | Methionine oxidation | Multidomain proteins | BIOCHEMISTRY & MOLECULAR BIOLOGY | MEDIATED OXIDATION | ACTIN CYTOSKELETAL ORGANIZATION | EPITHELIAL-MESENCHYMAL TRANSITION | LONGEVITY-ASSOCIATED GENES | CALORIC RESTRICTION | ENDOCRINOLOGY & METABOLISM | SERUM RESPONSE FACTOR | CALPONIN HOMOLOGY DOMAIN | HYDROGEN-PEROXIDE | FLAVIN-CONTAINING MONOOXYGENASE | SULFOXIDE REDUCTASES | Adaptor Proteins, Signal Transducing - chemistry | Reactive Oxygen Species - metabolism | Cytoskeletal Proteins - genetics | Humans | Isoenzymes - chemistry | Methionine Sulfoxide Reductases - genetics | LIM Domain Proteins - metabolism | Isoenzymes - metabolism | Protein Domains | Cytoskeletal Proteins - metabolism | Cysteine - metabolism | NADP - metabolism | LIM Domain Proteins - chemistry | Oxidation-Reduction | Protein Structure, Secondary | Isoenzymes - genetics | Methionine - metabolism | Models, Molecular | Cytoskeletal Proteins - chemistry | Methionine Sulfoxide Reductases - metabolism | Animals | Methionine - chemistry | Adaptor Proteins, Signal Transducing - genetics | LIM Domain Proteins - genetics | Protein Processing, Post-Translational | Kinetics | Adaptor Proteins, Signal Transducing - metabolism | Enzymes | Oxidation-reduction reaction | Cysteine | Proteins | Stem cells | Cystine | Protein binding | methionine oxidation | actin | redox signaling | methionine sulfoxide reductase | methionine | multidomain proteins | scaffolding proteins | methionine sulfoxide | monooxygenase
Journal Article
Current Opinion in Chemical Biology, ISSN 1367-5931, 2008, Volume 12, Issue 1, pp. 18 - 24
Journal Article