cystine has been researched along with heme in 9 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 4 (44.44) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (22.22) | 29.6817 |
| 2010's | 3 (33.33) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Dowell, VR; Killgore, GE; Starr, SE | 1 |
| Bel, FR; Goodman, YE; Jackson, FL; Whitehouse, RL; Wong, PC | 1 |
| Mansouri, A | 1 |
| Kimura, H; Murata, H; Uematsu, H | 1 |
| Ferguson, SJ; Tomlinson, EJ | 1 |
| Adlercreutz, P; Grey, CE; Hedström, M | 1 |
| He, C; Knipp, M; Taing, JJ | 1 |
| Kukino, K; Nose, A; Sawai, H; Shiro, Y; Tsujino, H; Uno, T; Yamashita, T | 1 |
| Daldal, F; Hwang, J; Khalfaoui-Hassani, B; Khatchikian, CE; Sanders, C; Selamoglu, N; Steimle, S; Verissimo, AF | 1 |
9 other study(ies) available for cystine and heme
| Article | Year |
|---|---|
Comparison of Schaedler agar and trypticase soy-yeast extract agar for the cultivation of anaerobic bacteria.
Topics: Agar; Anaerobiosis; Animals; Bacteriological Techniques; Bacteroides; Blood; Clostridium; Culture Media; Cystine; Fusobacterium; Glucose; Glycine max; Heme; Hydrogen-Ion Concentration; Peptones; Rabbits; Saccharomyces; Species Specificity; Tromethamine; Vitamin K; Yeasts | 1971 |
Taxonomic status of facultative and strictly anaerobic "corroding bacilli" that have been classified as Bacteroides corrodens.
Topics: Anaerobiosis; Bacteroides; Carboxy-Lyases; Caseins; Catalase; Cell Movement; Cystine; Cytosine Nucleotides; Fermentation; Gelatin; Guanine Nucleotides; Heme; Humans; Hydrolysis; Indoles; Lysine; Microscopy, Electron; Nitrates; Oxidation-Reduction; Oxidoreductases; Peptide Hydrolases; Urease | 1971 |
The influence of beta-93 sulfhydryl groups, organic phosphate and heme concentration on methemoglobin reduction.
Topics: Cystine; Cytochrome-B(5) Reductase; Heme; Hemoglobin A; Humans; Iodoacetamide; Iodoacetates; Kinetics; Methemoglobin; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Phytic Acid; Protein Conformation; Sulfhydryl Compounds | 1981 |
Increase in the susceptibility of hemoglobin to trypsin on treatment with glutathione or cysteine.
Topics: Binding Sites; Cysteine; Cystine; Globins; Glutathione; Heme; Hemoglobin A; Humans; Kinetics; Oxidation-Reduction; Protein Binding; Protein Conformation; Trypsin | 1980 |
Conversion of a c type cytochrome to a b type that spontaneously forms in vitro from apo protein and heme: implications for c type cytochrome biogenesis and folding.
Topics: Alanine; Amino Acid Substitution; Apoproteins; Cystine; Cytochrome b Group; Cytochrome c Group; Escherichia coli; Genetic Variation; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Denaturation; Protein Folding; Recombinant Proteins; Thermodynamics | 2000 |
A mass spectrometric investigation of native and oxidatively inactivated chloroperoxidase.
Topics: Chloride Peroxidase; Cysteine; Cystine; Enzymes, Immobilized; Heme; Hydrogen Peroxide; Indoles; Mass Spectrometry; Oxidants; Spectrometry, Mass, Electrospray Ionization; Stereoisomerism | 2007 |
Reduction of the lipocalin type heme containing protein nitrophorin -- sensitivity of the fold-stabilizing cysteine disulfides toward routine heme-iron reduction.
Topics: Cystine; Dithionite; Glutathione Disulfide; Heme; Hemeproteins; Insect Proteins; Iron; Lipocalins; Molecular Weight; Oxidation-Reduction; Protein Stability; Reducing Agents; Salivary Proteins and Peptides; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thiosulfates; Titrimetry | 2011 |
Disulfide bonds regulate binding of exogenous ligand to human cytoglobin.
Topics: Amino Acid Substitution; Carbon Monoxide; Cystine; Cytoglobin; Globins; Heme; Humans; Kinetics; Ligands; Mutagenesis, Site-Directed; Oxidation-Reduction; Potassium Cyanide; Protein Binding; Protein Multimerization; Spectrum Analysis, Raman | 2014 |
The thioreduction component CcmG confers efficiency and the heme ligation component CcmH ensures stereo-specificity during cytochrome
Topics: Amino Acid Substitution; Apoenzymes; Bacterial Outer Membrane Proteins; Bacterial Proteins; Binding Sites; Cysteine; Cystine; Cytochromes c; Heme; Models, Biological; Mutation; Oxidation-Reduction; Peptide Fragments; Protein Disulfide Reductase (Glutathione); Protein Interaction Domains and Motifs; Protein Multimerization; Recombinant Fusion Proteins; Recombinant Proteins; Rhodobacter capsulatus; Stereoisomerism | 2017 |