2006
DOI: 10.2174/092986606775974474
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Fate of Influenza A Virus Proteins

Abstract: In this review we summarize the current state, history, future, mutation tendency and species susceptibility of influenza A virus proteins based on our probabilistic analyses on amino acid pairs, and compare the current state of influenza A virus proteins with that of proteins which we have studied in the past.

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Cited by 29 publications
(41 citation statements)
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“…Among our three random approaches (for review, see [5,6,7,8]), the simplest one is the amino-acid pair predictability, by which we view if the combination of two adjacent amino acids can be explained by the permutation. For a whole protein, we can determine the percentage of how many amino-acid pairs can be predicted according to the permutation.…”
Section: Converting Pb2 Proteins Into Scalar Datamentioning
confidence: 99%
See 1 more Smart Citation
“…Among our three random approaches (for review, see [5,6,7,8]), the simplest one is the amino-acid pair predictability, by which we view if the combination of two adjacent amino acids can be explained by the permutation. For a whole protein, we can determine the percentage of how many amino-acid pairs can be predicted according to the permutation.…”
Section: Converting Pb2 Proteins Into Scalar Datamentioning
confidence: 99%
“…Since 1999, our group has developed three approaches to convert either a single amino acid or a protein into a scalar datum based on random principle (for review, see [5,6,7,8]). Using our approaches, we can effectively represent a protein family over time, which provides the basis for conducting the study on analyzing the trends in global warming and evolution of proteins of interest.…”
Section: Introductionmentioning
confidence: 99%
“…Since 1999, our group has developed three approaches to change a 20-letter symbolized protein into a scalar datum based on the random mechanism [2][3][4][5] , not only because pure chance is now considered to lie at the very heart of nature [6] , but also more importantly the random approach is frequently used when we have no detailed knowledge on a process, in our case, we have no detailed knowledge on all the mutation causes. On the other hand, the data changed by random approach reflects only a single aspect of a protein, as height and weight reflect different aspects of life.…”
Section: Introductionmentioning
confidence: 99%
“…In this way, we can present each hemagglutinin with an unambiguous value seeing that we can view each hemagglutinin as a sample from its evolution and a sample from the evolution of influenza A virus. Also, both amino-acid pair predictability and amino-acid distribution rank are very sensitive to mutations in hemagglutinins [3,8,12] , in particular, our first approach reveals the mutation in individual amino-acid pair and the second one indicates the sensitive position. We can therefore compare different hemagglutinins with respect to species, subtypes, etc.…”
Section: Resultsmentioning
confidence: 96%
“…117 Avian 141 1966-2003 Human 7 1998-1999 Swine 23 1998-2003 H10 Avian 3 1949 Minks 3 1984 H11 Avian 3 1956 H12 Avian 2 1976 H13 Avian 8 1977-1984 Whale 3 1984 H14 Avian 3 1982 H15 Avian 2 1979, 1983 H16 Avian 3 1999 Unidentified Avian 5 1963-2000 Equine 2 1971, 1976 Human 14 1994-1998 Swine 5 [1986][1987][1988][1989][1990][1991][1992][1993][1994][1995][1996][1997][1998] Computational mutation calculation: The rationale and detailed description of our approaches have been published in our previous publications (for details, see review articles [3,7,8] ) and we describe our approaches with the example of the hemagglutinin of 1918 "Spanish" influenza A virus (accession number AF117241), which is the earliest complete sequence documented in the data bank [9,10] .…”
Section: Am J Infectious Dis 1 (2): 116-123 2005mentioning
confidence: 99%