ReviewActa pharmacologica Sinica2006
Mutation trend of hemagglutinin of influenza A virus: a review from a computational mutation viewpoint.
Review in Acta pharmacologica Sinica, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Forecasting influenza hemagglutinin mutations through the lens of anomaly detection.Scientific reports · 2023Article
- Possibility of cross-species/subtype reassortments in influenza A viruses: an analysis of nonstructural protein variations.Virulence · 2013Article
- Mutation patterns in human alpha-galactosidase A.Molecular diversity · 2010Article
- Trends in global warming and evolution of matrix protein 2 family from influenza A virus.Interdisciplinary sciences, computational life sciences · 2009Article
- Connecting mutant phenylalanine hydroxylase with phenylketonuria.Journal of clinical monitoring and computing · 2008Article
- Prediction of mutations engineered by randomness in H5N1 hemagglutinins of influenza A virus.Amino acids · 2008Article
- Quantitative relationship between mutated amino-acid sequence of human copper-transporting ATPases and their related diseases.Molecular diversity · 2008Article
- The Influenza Primer Design Resource: a new tool for translating influenza sequence data into effective diagnostics.Influenza and other respiratory viruses · 2008Article
- Prediction of mutations engineered by randomness in H5N1 neuraminidases from influenza A virus.Amino acids · 2008Article
- Prediction of mutations in H1 neuraminidases from North America influenza A virus engineered by internal randomness.Molecular diversityArticle
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Since 1999 we have developed two computational mutation approaches to analyze the protein primary structure whose methodology and implications were reviewed in 2002. Our first approach is the calculation of predictable and unpredictable portions of amino-acid pairs in a protein, and the second is the calculation of amino-acid distribution rank in a protein. Both approaches provide quantitative measures to present a protein, which we have used to study a number of proteins with numerous mutations such as p53 proteins. More recently, we focussed our efforts on analyzing the proteins mutating frequently over time such as hemagglutinins of influenza A viruses. In this review we summarise our findings and their implications for hemagglutinin mutations in combination with some newly available data. Our approaches throw light on the true nature of genetic heterogeneity of influenza virus hemagglutinins; that is, the protein variability is highly relevant to its amino-acid construction. Using these approaches, we can monitor new mutations from influenza virus hemagglutinins and may predict their mutations in the future.
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