Výsledky vyhledávání - "Tyrphostin AG 879"

A cell-based high-throughput screen identifies tyrphostin AG 879 as an inhibitor of animal cell phospholipid and fatty acid biosynthesis

Autor: Raphael A. Zoeller, Kathleen Geoghegan-Barek

Publikováno v: Biochemistry and Biophysics Reports
Biochemistry and Biophysics Reports, Vol 18, Iss, Pp-(2019)

Inhibition of animal cell phospholipid biosynthesis has been proposed for anticancer and antiviral therapies. Using CHOK1 derived cell lines, we have developed and used a cell-based high-throughput procedure to screen a 1280 compound, small molecu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a21e496c3576d35e981d6716212c5769
http://europepmc.org/articles/PMC6406593

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Novel actions of tyrphostin AG 879: inhibition of RAF-1 and HER-2 expression combined with strong antitumoral effects on breast cancer cells

Autor: Larsson Li

Publikováno v: Cellular and Molecular Life Sciences. 61:2624-2631

Binding of growth factors to cell surface receptors activates protein tyrosine kinases (PTKs) that initiate cascades of downstream signaling events including the mitogen-activated protein (MAP) kinase cascade. This study reports that the PTK inhibito

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5657493ebfe5a08acd71612c7686f0f
https://doi.org/10.1007/s00018-004-4279-5

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Epidermal growth factor stimulates 3-hydroxy-3-methylglutaryl-coenzyme A reductase expression via the ErbB-2 pathway in human breast adenocarcinoma cells

Autor: Corélia Pratx, Francis Le Gaillard, Anne Pradines, Gilles Favre, Raghda Asslan, Cuider Allal

Publikováno v: Biochemical and biophysical research communications. 260(3)

HMG-CoA reductase is the key enzyme for the biosynthesis of isoprenoid compounds essential for cell growth and differentiation. Its tyrosine kinase-dependent modulation has recently been suggested and described in the ErbB-2 overexpressing cell line

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::007457341090e9fb87329099c0e408f2
https://pubmed.ncbi.nlm.nih.gov/10403829

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