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Sugiyama, K., Obayashi, E., Kawaguchi, A., Suzuki, Y., Tame, J.R.H., Nagata, K. and Park, S.-Y. (2009) Structural insight into the essential PB1-PB2 subunit contact of the Influenza virus RNA polymerase. EMBO Journal, 28, 1803-1811. doi:10.1038/emboj.2009.138

has been cited by the following article:

• TITLE: The nature of proteins in influenza

  AUTHORS: K. Akila, P. Balamurugan, E. Rajasekaran

  KEYWORDS: Carbon Distribution; Influenza Virus; H1N1; Carbon Study; Protein Analysis; Swine Flu; Proteomics; Transcriptomics

  JOURNAL NAME: Health, Vol.4 No.10A, November 1, 2012

  ABSTRACT: Mutation can alter the structure of viral proteins to form different structure. Carbon distribution is responsible for these changes in structure. The carbon distribution in proteins of human Influenza A virus is analyzed here. Results reveal that the carbon contents are high in surface proteins, optimum in polymerase proteins and less in nuclear proteins. Polymerase proteins have better carbon distribution pattern than the other proteins. Thymine distribution in different frames of mRNAs are checked as it has link with carbon distribution pattern in the corresponding proteins. Results show that frame 4 is violating from thymine distribution. This is responsible for production of protein with different carbon distribution. Unusual thymine distribution in frame 3 are observed. The thymine distributions are different in viral mRNA compared to normal one. Minimizing the excess thymine in H1N1 mRNAs might improve the protein performance. Mutational study based on carbon distribution should be better exploited for further improving the protein stability, activity and ultimately for gene therapy.