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Free Radical Biology and Medicine, ISSN 0891-5849, 03/2015, Volume 80, pp. 171 - 182
This review examines oxidative protein folding within the mammalian endoplasmic reticulum (ER) from an enzymological perspective. In protein disulfide... 
Peroxiredoxin | Protein disulfide isomerase | Quiescin sulfhydryl oxidase | Oxidative protein folding | Disulfide exchange | Ratiometric mass spectrometry | Redox potential | Endoplasmic reticulum | Ero1 | Glutathione | ERO1 FAMILY | THIOREDOXIN-LIKE DOMAINS | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | BOND FORMATION | STATE | GLUTATHIONE DISULFIDE | ISOMERASE | ENDOCRINOLOGY & METABOLISM | QUIESCIN-SULFHYDRYL OXIDASE | GENERATING DISULFIDES | Disulfides - metabolism | Glutathione - metabolism | Protein Disulfide-Isomerases - metabolism | Humans | Trypanosoma brucei brucei - cytology | Endoplasmic Reticulum - metabolism | Glutathione Disulfide - metabolism | Trypanosoma brucei brucei - enzymology | Endoplasmic Reticulum - ultrastructure | Endoplasmic Reticulum - chemistry | Sulfhydryl Compounds - metabolism | Protozoan Proteins - metabolism | Oxidoreductases Acting on Sulfur Group Donors - chemistry | Disulfides - chemistry | Protozoan Proteins - chemistry | Sulfhydryl Compounds - chemistry | Eukaryotic Cells - enzymology | Oxidoreductases Acting on Sulfur Group Donors - metabolism | Oxidation-Reduction | Models, Molecular | Protein Folding | Animals | Protein Disulfide-Isomerases - chemistry | Eukaryotic Cells - cytology | Glutathione - chemistry | Glutathione Disulfide - chemistry | Kinetics | Oxidases | Proteins | Thiols | Protein folding | Analysis | Isomerization | Hydrogen peroxide | Protein Disulfide Isomerase | Ratiometric Mass Spectrometry | Oxidative Protein Folding | Endoplasmic Reticulum | Redox Potential
Journal Article
PLoS ONE, ISSN 1932-6203, 03/2017, Volume 12, Issue 3, p. e0174753
Protein disulfide isomerases are overwhelmingly multi-modular redox catalysts able to perform the formation, reduction or isomerisation of disulfide bonds. We... 
OXIDATION-REDUCTION PROPERTIES | SULFUR CLUSTER BINDING | ACTIVE-SITE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | BOND FORMATION | ENDOPLASMIC-RETICULUM | THIOREDOXIN REDUCTASE | QUIESCIN-SULFHYDRYL OXIDASE | SEED-STORAGE PROTEINS | Thioredoxin-Disulfide Reductase - genetics | Malate Dehydrogenase (NADP+) - genetics | Protein Disulfide-Isomerases - metabolism | Humans | Peroxiredoxins - metabolism | Oxidoreductases - chemistry | Malate Dehydrogenase (NADP+) - metabolism | Protein Isoforms - metabolism | Thioredoxin-Disulfide Reductase - metabolism | Protein Isoforms - chemistry | Sulfides - metabolism | Catalysis | Dithionitrobenzoic Acid - metabolism | Malate Dehydrogenase (NADP+) - chemistry | Thioredoxin-Disulfide Reductase - chemistry | Amino Acid Sequence | Mutagenesis, Site-Directed | Oxidoreductases - metabolism | Oxidoreductases - genetics | Iron - metabolism | Sequence Homology, Amino Acid | Insulin - metabolism | Protein Disulfide-Isomerases - genetics | Protein Disulfide-Isomerases - chemistry | Hydrogen-Ion Concentration | Protein Isoforms - genetics | Research | Thioredoxin | Recombinant proteins | Health aspects | NADP (Coenzyme) | Protein disulfide isomerases | Ribonuclease A | Catalysts | Amino acids | pH effects | Proteins | Chemical reduction | E coli | Protein folding | Chemical bonds | Physiology | Oxidation | NADP | Redox properties | Enzymes | Disulfide bonds | Malate dehydrogenase | Insulin | Substrates | Chromatography | Mutagenesis | Malate | Isoforms | Endoplasmic reticulum | Reductase | Life Sciences
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2009, Volume 106, Issue 22, pp. 9109 - 9114
Tight control of cellular redox homeostasis is essential for protection against oxidative damage and for maintenance of normal metabolism as well as redox... 
Gametophytes | Oxidative stress | Leaves | Enzymes | Phenotypes | Pollen | Oxidation | Plants | Thioredoxin | Cytosol | Redox imaging | Redox-sensitive GFP | Thioredoxin reductase | Redox homeostasis | redox-sensitive GFP | REDOX STATE | MECHANISM | MULTIDISCIPLINARY SCIENCES | MITOCHONDRIA | POLLEN | redox homeostasis | GLUTAREDOXIN | IDENTIFICATION | thioredoxin reductase | REACTIVE OXYGEN | THALIANA | BIOSYNTHESIS | PLANTS | redox imaging | Arabidopsis Proteins - genetics | Arabidopsis - enzymology | Thioredoxin-Disulfide Reductase - genetics | Glutathione Reductase - metabolism | Cell Cycle Proteins - metabolism | Glutathione Disulfide - metabolism | Gene Knockout Techniques | Glutathione Reductase - genetics | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Thioredoxin-Disulfide Reductase - metabolism | Fertility | Pollen - genetics | Cell Cycle Proteins - genetics | Cytosol - metabolism | Pollen - enzymology | Thioredoxins - metabolism | NADP - metabolism | Physiological aspects | Properties | Arabidopsis | NADP (Coenzyme) | Populations and Evolution | Genomics | Biodiversity | Cellular Biology | Life Sciences | Arabidopsis Proteins | Computer Science | Genetics | Biomolecules | NADP | Vegetal Biology | Thioredoxin-Disulfide Reductase | Bioinformatics | Plants genetics | Quantitative Methods | Biochemistry, Molecular Biology | Glutathione Reductase | Systematics, Phylogenetics and taxonomy | Plant breeding | Thioredoxins | Molecular Networks | Molecular biology | Cell Cycle Proteins | Glutathione Disulfide | Biological Sciences
Journal Article
Journal Article
ACS Nano, ISSN 1936-0851, 11/2014, Volume 8, Issue 11, pp. 11522 - 11528
The transfer of synthesized 2D MoS2 films is important for fundamental and applied research. However, it is problematic to translate the well-established... 
Molybdenum disulfide | Large scale | Tungsten disulfide | Surface energy | 2D materials
Journal Article