Inhibition by two lavendustins of the tyrosine kinase activity of pp60F527 in vitro and in intact cells.

doi:10.1016/0922-4106(94)90019-1

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Article

Inhibition by two lavendustins of the tyrosine kinase activity of pp60F527 in vitro and in intact cells.

European journal of pharmacology - 15 Sept 1994

Agbotounou W K, Umezawa K, Jacquemin-Sablon A, Pierre J

Abstract excerpt

The mutant pp60F527 protein possesses an activated protein-tyrosine kinase (PTK) activity correlated with a transforming activity. We have studied the inhibition of the pp60F527 PTK activity by two EGF-R tyrosine kinase inhibitors, lavendustin A and one of its derivatives, lavendustin C6. In vitr...

Topics

3T3 Cells
Adenosine Triphosphate
Animals
Binding, Competitive
Blotting, Western
Cell Division
Electrophoresis, Polyacrylamide Gel
Enzyme Activation
ErbB Receptors
Gene Expression Regulation, Viral
Mice
Mice, Inbred BALB C

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phenols

Phosphopyruvate Hydratase

Phosphorylation

Protein-Tyrosine Kinases

Retroviridae Proteins, Oncogenic

Source

Open in PubMed

Identifiers

PMID: 7828651
DOI: 10.1016/0922-4106(94)90019-1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7828651-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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