Page last updated: 2024-08-22

dithiothreitol and herbimycin

dithiothreitol has been researched along with herbimycin in 3 studies

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
Mahon, TM; O'Neill, LA1
Ardati, A; Clark, K; Hamel, L; Jayyosi, Z; Kaplow, J; Kenney, M; Merkel, L; Perrone, M; Rojas, C; Spada, A; Zilberstein, A1
Nomura, Y; Ogino, S; Tsuruma, K; Uehara, T1

Other Studies

3 other study(ies) available for dithiothreitol and herbimycin

ArticleYear
Evidence for direct modification of NF kappa B by the tyrosine kinase inhibitor, herbimycin A.
    Biochemical Society transactions, 1995, Volume: 23, Issue:1

    Topics: Animals; Benzoquinones; Cell Line; Dithiothreitol; Interleukin-1; Lactams, Macrocyclic; Mercaptoethanol; Mice; NF-kappa B; Phosphotyrosine; Protein-Tyrosine Kinases; Quinones; Rifabutin; Tetradecanoylphorbol Acetate; Tumor Cells, Cultured; Tyrosine

1995
Induction of heat shock protein 70 by herbimycin A and cyclopentenone prostaglandins in smooth muscle cells.
    Cell stress & chaperones, 2000, Volume: 5, Issue:2

    Topics: Anti-Bacterial Agents; Antiviral Agents; Benzoquinones; Blotting, Western; Cells, Cultured; Dithiothreitol; DNA-Binding Proteins; Enzyme-Linked Immunosorbent Assay; Heat Shock Transcription Factors; HSP70 Heat-Shock Proteins; Humans; Lactams, Macrocyclic; Muscle, Smooth; Prostaglandin D2; Protein Binding; Quinones; Rifabutin; Transcription Factors

2000
Herbimycin A abrogates nuclear factor-kappaB activation by interacting preferentially with the IkappaB kinase beta subunit.
    Molecular pharmacology, 2004, Volume: 65, Issue:6

    Topics: Benzoquinones; Catalytic Domain; Cell Line; Cells, Cultured; Cysteine; Dithiothreitol; Enzyme Inhibitors; Humans; I-kappa B Kinase; I-kappa B Proteins; Immunohistochemistry; Lactams, Macrocyclic; Mutagenesis, Site-Directed; NF-kappa B; NF-KappaB Inhibitor alpha; Phosphorylation; Protein Serine-Threonine Kinases; Quinones; Rifabutin; Signal Transduction; Transfection

2004
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