ArticleBritish journal of cancer1996
Tyrosine phosphorylation of 100-130 kDa proteins in lung cancer correlates with poor prognosis.
Article in British journal of cancer, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 29 citations in OpenAlex.
- Functional and clinical characteristics of focal adhesion kinases in cancer progression.Frontiers in cell and developmental biology · 2022Review
- Development of a High-Throughput Fluorescence Polarization Assay to Detect Inhibitors of the FAK-Paxillin Interaction.SLAS discovery : advancing life sciences R & D · 2020Article
- Increased Expression and Activation of FAK in Small-Cell Lung Cancer Compared to Non-Small-Cell Lung Cancer.Cancers · 2019Article
- The prognostic significance of focal adhesion kinase expression in stage I non-small-cell lung cancer.Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer · 2014Article
- Focal adhesion kinase as a cancer therapy target.Anti-cancer agents in medicinal chemistry · 2010Review
- Phosphorylated tyrosine-containing proteins in primary lung cancer correlates with proliferation and prognosis.British journal of cancer · 2002Article
- Tumor-specific activation of mitogen-activated protein kinase in human colorectal and gastric carcinoma tissues.Japanese journal of cancer research : Gann · 1998Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To search for the signalling pathways in lung cancer relevant to its aggressive behaviour, we studied tyrosine phosphorylated proteins in lung cancer cell lines and surgical specimens. We found that the profiles of protein phosphorylation were closely matched among these cell lines and cancer tissues of different histological origins, and 100-130 kDa proteins were the major components of phosphorylated proteins. In surgical specimens, approximately half of the cases showed tyrosine phosphorylation of these proteins in a tumour-specific manner, and phosphorylation of these proteins showed good correlation with the survival length of patients after operation. By immunoprecipitation with specific antibodies, we found that p125FAK, p120 and beta-catenin were the major components of tyrosine-phosphorylated proteins in the surgical specimens. These results suggest that tyrosine phosphorylation of these proteins may play a role in tumour relapse and is available as a clinical marker.
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