Compounds > bathocuproine disulfonate
Page last updated: 2024-09-05

bathocuproine disulfonate and acetylcysteine

bathocuproine disulfonate has been researched along with acetylcysteine in 3 studies

Compound Research Comparison

Studies
(bathocuproine disulfonate)		Trials
(bathocuproine disulfonate)		Recent Studies (post-2010)
(bathocuproine disulfonate)		Studies
(acetylcysteine)		Trials
(acetylcysteine)		Recent Studies (post-2010) (acetylcysteine)
10302514,5801,0465,960

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (33.33)18.2507
2000's2 (66.67)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Hainaut, P; Richard, MJ; Verhaegh, GW1
Hayakawa, T; Iseki, A; Kambe, F; Okumura, K; Seo, H1
Andersson, A; Hultberg, B; Isaksson, A1

Other Studies

3 other study(ies) available for bathocuproine disulfonate and acetylcysteine

ArticleYear
Regulation of p53 by metal ions and by antioxidants: dithiocarbamate down-regulates p53 DNA-binding activity by increasing the intracellular level of copper.
    Molecular and cellular biology, 1997, Volume: 17, Issue:10

    Topics: Acetylcysteine; Antioxidants; Ataxia Telangiectasia Mutated Proteins; Cell Cycle; Cell Cycle Proteins; Cell Line; Chelating Agents; Copper; Cyclin-Dependent Kinase Inhibitor p21; Cyclins; DNA; DNA Damage; DNA-Binding Proteins; Humans; Hydrogen Peroxide; Intercalating Agents; Ion Transport; Lipid Peroxidation; Oxidation-Reduction; Oxidative Stress; Phenanthrolines; Protein Binding; Protein Conformation; Protein Serine-Threonine Kinases; Proteins; Pyrrolidines; Thiocarbamates; Tumor Cells, Cultured; Tumor Suppressor Protein p53; Tumor Suppressor Proteins

1997
Regulation of thyroid follicular cell function by intracellular redox-active copper.
    Endocrinology, 2000, Volume: 141, Issue:12

    Topics: Acetylcysteine; Animals; Antioxidants; Cell Division; Cell Line; Chelating Agents; Copper; DNA; DNA-Binding Proteins; Gene Expression; Hydrogen Peroxide; Iodide Peroxidase; Nuclear Proteins; Oxidation-Reduction; Paired Box Transcription Factors; PAX8 Transcription Factor; Phenanthrolines; Pyrrolidines; Rats; RNA, Messenger; Thiocarbamates; Thyroglobulin; Thyroid Gland; Thyroid Nuclear Factor 1; Trans-Activators; Transcription Factors; Tumor Suppressor Protein p53

2000
Thiol redox status influences extracellular concentration of homocysteine in HeLa cell cultures.
    Clinical chemistry and laboratory medicine, 2000, Volume: 38, Issue:12

    Topics: Acetylcysteine; Copper; Dithiothreitol; Dose-Response Relationship, Drug; HeLa Cells; Homocysteine; Humans; Indicators and Reagents; Ions; Oxidation-Reduction; Oxygen; Phenanthrolines; Sulfhydryl Compounds

2000