X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
dithionitrobenzoic acid - pharmacology (838) 838
animals (782) 782
kinetics (656) 656
biochemistry & molecular biology (473) 473
binding sites (277) 277
humans (262) 262
dithionitrobenzoic acid (260) 260
rats (237) 237
oxidation-reduction (210) 210
dithionitrobenzoic acid - metabolism (196) 196
protein binding (185) 185
protein conformation (181) 181
hydrogen-ion concentration (167) 167
ethylmaleimide - pharmacology (157) 157
sulfhydryl compounds - metabolism (155) 155
sulfhydryl reagents - pharmacology (155) 155
amino acid sequence (146) 146
dithiothreitol - pharmacology (146) 146
rabbits (141) 141
male (137) 137
molecular weight (131) 131
cysteine (128) 128
cattle (122) 122
molecular sequence data (120) 120
dithionitrobenzoic acid - chemistry (118) 118
biophysics (112) 112
in vitro techniques (101) 101
escherichia coli - enzymology (94) 94
cysteine - metabolism (92) 92
macromolecular substances (91) 91
sulfhydryl compounds - analysis (88) 88
female (86) 86
index medicus (86) 86
structure-activity relationship (83) 83
electrophoresis, polyacrylamide gel (79) 79
liver - enzymology (78) 78
proteins (74) 74
cysteine - chemistry (73) 73
substrate specificity (73) 73
spectrometry, fluorescence (71) 71
mutagenesis, site-directed (70) 70
purification (70) 70
escherichia-coli (69) 69
nitrobenzoates - pharmacology (69) 69
recombinant proteins - metabolism (69) 69
catalysis (67) 67
disulfides - metabolism (67) 67
mice (67) 67
time factors (66) 66
circular dichroism (65) 65
amino acids - analysis (63) 63
research (62) 62
enzymes (61) 61
research article (58) 58
sulfhydryl compounds (58) 58
escherichia coli - genetics (57) 57
calcium - metabolism (56) 56
glutathione - metabolism (56) 56
muscles - enzymology (56) 56
enzyme activation (55) 55
models, molecular (55) 55
disulfides (54) 54
analysis (52) 52
swine (52) 52
thiols (52) 52
spectrophotometry (50) 50
enzyme inhibitors - pharmacology (49) 49
chloromercuribenzoates - pharmacology (48) 48
chromatography, high pressure liquid (48) 48
myosins - metabolism (48) 48
base sequence (47) 47
dose-response relationship, drug (47) 47
glutathione (47) 47
protein (47) 47
temperature (47) 47
binding (46) 46
oxidative stress (46) 46
protein denaturation (46) 46
recombinant proteins - chemistry (46) 46
spectrophotometry, ultraviolet (46) 46
chemistry (45) 45
neurosciences (45) 45
expression (43) 43
k cq biochemistry & molecular biology (43) 43
cell biology (41) 41
chemical phenomena (41) 41
enzyme activation - drug effects (41) 41
magnesium - pharmacology (41) 41
iodoacetamide - pharmacology (40) 40
adenosine triphosphate - metabolism (39) 39
adenosine triphosphatases - metabolism (38) 38
ligands (38) 38
sulfhydryl compounds - chemistry (38) 38
thioredoxin-disulfide reductase - metabolism (38) 38
chickens (37) 37
rats, inbred strains (37) 37
chromatography, gel (36) 36
cysteine - genetics (36) 36
mechanism (36) 36
thioredoxin (36) 36
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (1373) 1373
Russian (23) 23
French (2) 2
German (2) 2
Chinese (1) 1
Japanese (1) 1
Serbian (1) 1
Spanish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Free Radical Biology and Medicine, ISSN 0891-5849, 2011, Volume 50, Issue 6, pp. 689 - 699
Journal Article
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 05/2012, Volume 521, Issue 1-2, pp. 102 - 110
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
Free Radical Biology and Medicine, ISSN 0891-5849, 08/2016, Volume 97, pp. 1 - 13
Low molecular mass thiols and antioxidant enzymes have essential functions to detoxify reactive oxygen and nitrogen species maintaining cellular redox balance.... 
Peroxiredoxin | Redox metabolism | Thioredoxin reductase | Leptospira | DTNB 5,5′-dithiobis(2-nitrobenzoic acid) | L-TrxR low molecular mass thioredoxin reductase | CDNB 1-chloro-2,4-dinitrobenzene | MBQ 2-methyl-benzoquinone | t-BuOOH tert-butyl hydroperoxide | GSSG glutathione disulfide | Trx thioredoxin | DTT dithiothreitol | H-TrxR high molecular mass thioredoxin reductase | Abbreviations AhpC bacterial 2-Cys peroxiredoxin | bis-γ-GC bis-γ-glutamylcysteine | TrxR thioredoxin reductase | SYSTEM | METHYLENE-BLUE | OXIDATIVE STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENTAMOEBA-HISTOLYTICA | IN-VITRO SUSCEPTIBILITIES | INTRACELLULAR REDOX | TREPONEMA-PALLIDUM | METABOLISM | GLUTATHIONE | ENDOCRINOLOGY & METABOLISM | PARASITE PLASMODIUM-FALCIPARUM | Recombinant Proteins - metabolism | Reactive Oxygen Species - metabolism | Oxidation-Reduction | Thioredoxin-Disulfide Reductase - genetics | Reactive Nitrogen Species - metabolism | Antioxidants - metabolism | Humans | Peroxiredoxins - metabolism | Oxidative Stress - genetics | Leptospira interrogans - pathogenicity | Glutathione Disulfide - metabolism | Recombinant Proteins - genetics | Leptospirosis - metabolism | Thioredoxins - genetics | Thioredoxin-Disulfide Reductase - metabolism | Escherichia coli - genetics | Leptospira interrogans - metabolism | Sulfhydryl Compounds - chemistry | Thioredoxins - metabolism | Kinetics | Leptospirosis - microbiology | Thioredoxins - chemistry | Dithionitrobenzoic Acid - metabolism | Thioredoxin-Disulfide Reductase - chemistry | Antioxidants | Enzymes | Cysteine | Thiols | Analysis | Escherichia coli | Thioredoxin | Cystine | Physiological aspects
Journal Article
Journal Article
Methods in molecular biology (Clifton, N.J.), ISSN 1064-3745, 2010, Volume 648, pp. 269 - 277
Glutathione (GSH) is the most abundant antioxidant in aerobic cells, present in micromolar (microM)-concentrations in bodily fluids and in millimolar (mM)... 
GSSG | Glutathione disulfide | Redox potential | GSH/GSSG ratio | GSH | Glutathione | Animals | Metabolic Networks and Pathways | Oxidation-Reduction | Glutathione - metabolism | Biological Assay - methods | Glutathione Disulfide - metabolism | Dithionitrobenzoic Acid - metabolism | Glutathione - blood
Journal Article
Neurotoxicity Research, ISSN 1029-8428, 05/2018, Volume 33, Issue 4, pp. 749 - 758
Journal Article
Journal Article
Journal Article
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 10/2018, Volume 656, pp. 38 - 45
Thioredoxin glutathione reductase (TGRsec) is a multi-domain flavoprotein that plays a principal role in redox homeostasis maintenance. We have previously... 
Stability | Thioredoxin glutathione reductase | Glutathione reductase | Liver fluke | Parasite | FAD | Fluorescence | Activity | Thioredoxin reductase | TRICLABENDAZOLE RESISTANCE | PROTEIN DENATURATION | SCHISTOSOMA-MANSONI | BIOCHEMISTRY & MOLECULAR BIOLOGY | GUANIDINE-HYDROCHLORIDE | BOLIVIAN ALTIPLANO | CHEMICAL DENATURATION | BIOPHYSICS | PLASMODIUM-FALCIPARUM | HUMAN FASCIOLIASIS | UREA | Flavin-Adenine Dinucleotide - chemistry | Protein Unfolding - drug effects | Protein Conformation - drug effects | Helminth Proteins - chemistry | Multienzyme Complexes - metabolism | Tryptophan - chemistry | Fasciola - enzymology | Urea - chemistry | Flavin-Adenine Dinucleotide - metabolism | Thioredoxins - genetics | Glutaredoxins - chemistry | Glutaredoxins - genetics | Protein Domains | NADH, NADPH Oxidoreductases - chemistry | Thioredoxins - metabolism | Catalysis | NADP - metabolism | Protein Stability | Thioredoxins - chemistry | NADH, NADPH Oxidoreductases - metabolism | Dithionitrobenzoic Acid - metabolism | Helminth Proteins - metabolism | Glutaredoxins - isolation & purification | Glutaredoxins - metabolism | NADH, NADPH Oxidoreductases - genetics | Helminth Proteins - isolation & purification | Helminth Proteins - genetics | Multienzyme Complexes - genetics | NADH, NADPH Oxidoreductases - isolation & purification | Thioredoxins - isolation & purification | Multienzyme Complexes - chemistry | Animals | Protein Binding | Mutation | Multienzyme Complexes - isolation & purification | Thioredoxin | Liver
Journal Article
Journal Article
Experimental Parasitology, ISSN 0014-4894, 06/2017, Volume 177, pp. 82 - 92
We report, herein, the purification to homogeneity and the biochemical and kinetic characterization of HcTrxR3, a new isoform of thioredoxin reductase (TrxR)... 
Glutathione system | Helminthes | Haemonchosis | Thioredoxin system |