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- W4234897643 abstract "Lung cancer results when normal check and balance system of cell division is disrupted and ultimately the cells divide and proliferate in an uncontrollable manner forming a mass of cells in our body, known as tumor. Frequent mutations in Protein Kinase Domain alter the process of phosphorylation which results in abnormality in regulations of cell apoptosis and differentiation. Tyrosine Protein kinases and Serine/Threonine Protein Kinases are the two broad classes of protein kinases in accordance to their substrate specificity. The study of Tyrosine protein kinase and serine Kinase coding regions have the importance of sequence and structure determinants of cancer-causing mutations from mutation-dependent activation process. In the present study, we analyzed huge amounts of data extracted from various biological databases and NCBI. Out of the 534 proteins that may play a role in lung cancer, 71 proteins were selected that are likely to be actively involved in lung cancer. These proteins were evaluated by employing Multiple Sequence Alignment and a Phylogenetic tree was constructed using Neighbor-Joining Algorithm. From the constructed phylogenetic tree, protein kinase domain and motif study was performed. The results of this study revealed that the presence of Protein Kinase Domain and Tyrosine or Serine/Threonine Kinase signatures in some of the proteins are mutated, which play a dominant role in the pathogenesis of Lung Cancer and these may be addressed with the help of inhibitors to develop an efficient anticancer drugs. Furthermore, the present study contributes to the possibility that genetic components are more important in Lung Cancer as compared to environmental and smoking(carcinogens) factors." @default.
- W4234897643 created "2022-05-12" @default.
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- W4234897643 date "2014-06-17" @default.
- W4234897643 modified "2023-10-14" @default.
- W4234897643 title "Analysis of Protein Kinase Domain and Tyrosine Kinase or Serine/Threonine Kinase signatures Involved In Lung Cancer" @default.
- W4234897643 doi "https://doi.org/10.7287/peerj.preprints.414" @default.
- W4234897643 hasPublicationYear "2014" @default.
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