Compounds > 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid
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4,4'-diisothiocyanostilbene-2,2'-disulfonic acid and peroxynitric acid

4,4'-diisothiocyanostilbene-2,2'-disulfonic acid has been researched along with peroxynitric acid in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (75.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bartosz, G; Soszyński, M1
Denicola, A; Radi, R; Souza, JM1
Beckman, JS; Macfadyen, AJ; Reiter, C; Zhuang, Y1
Di Stasi, MA; Mallozzi, C; Minetti, M1

Other Studies

4 other study(ies) available for 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid and peroxynitric acid

ArticleYear
Penetration of erythrocyte membrane by peroxynitrite: participation of the anion exchange protein.
    Biochemistry and molecular biology international, 1997, Volume: 43, Issue:2

    Topics: 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Adult; Anion Exchange Protein 1, Erythrocyte; Anions; Biological Transport; Erythrocyte Membrane; Hemoglobins; Humans; Hydrogen-Ion Concentration; Nitrates; Oxidation-Reduction

1997
Diffusion of peroxynitrite across erythrocyte membranes.
    Proceedings of the National Academy of Sciences of the United States of America, 1998, Mar-31, Volume: 95, Issue:7

    Topics: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Biological Transport; Erythrocyte Membrane; Humans; Hydrogen-Ion Concentration; Nitrates; Oxidants; Oxidation-Reduction

1998
A novel superoxide dismutase-based trap for peroxynitrite used to detect entry of peroxynitrite into erythrocyte ghosts.
    Chemical research in toxicology, 1999, Volume: 12, Issue:3

    Topics: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Animals; Blotting, Western; Cattle; Erythrocyte Membrane; Humans; In Vitro Techniques; Isothiocyanates; Kinetics; Membrane Proteins; Mutation; Nitrates; Oxidants; Superoxide Dismutase; Thiocyanates

1999
Peroxynitrite-dependent activation of src tyrosine kinases lyn and hck in erythrocytes is under mechanistically different pathways of redox control.
    Free radical biology & medicine, 2001, May-15, Volume: 30, Issue:10

    Topics: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Alkylation; Cysteine; Diffusion; Dithiothreitol; Enzyme Activation; Erythrocytes; Ethylmaleimide; Glucose; Humans; Hydrogen Peroxide; Immunochemistry; Nitrates; Oxidation-Reduction; Protein Tyrosine Phosphatases; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-hck; Sequence Homology; Signal Transduction; Sodium Bicarbonate; src-Family Kinases; Substrate Specificity

2001