Phylogenetic analyses of amino acid variation in the serpin proteins

Atchley WR, Lokot T, Wollenberg K, Dress A, Ragg H (2001)
MOLECULAR BIOLOGY AND EVOLUTION 18(8): 1502-1511.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Atchley, William R.; Lokot, Tatjana; Wollenberg, Kurt; Dress, AndreasUniBi; Ragg, HermannUniBi
Abstract / Bemerkung
Phylogenetic analyses of 110 serpin protein sequences revealed clades consistent with independent phylogenetic analyses based on exon-intron structure and diagnostic amino acid sites. Trees were estimated by maximum likelihood, neighbor joining and partial split decomposition using both the BLOSUM 62 and Jones-Taylor-Thornton substitution matrices. Neighbor-joining trees gave results closest to those based on independent analyses using genomic and chromosomal data. The maximum-likelihood trees derived using the quartet puzzling algorithm were very conservative, producing many small clades that separated groups of proteins that other results suggest were related. Independent analyses based on exon-intron structure suggested that a neighbor-joining tree was more accurate than maximum-likelihood trees obtained using the quartet puzzling algorithm.
Stichworte
likelihood; maximum; molecular evolution; neighbor joining; serpins; protein evolution; phylogeny
Erscheinungsjahr
2001
Zeitschriftentitel
MOLECULAR BIOLOGY AND EVOLUTION
Band
18
Ausgabe
8
Seite(n)
1502-1511
ISSN
0737-4038
Page URI
https://pub.uni-bielefeld.de/record/1616585

Zitieren

Atchley WR, Lokot T, Wollenberg K, Dress A, Ragg H. Phylogenetic analyses of amino acid variation in the serpin proteins. MOLECULAR BIOLOGY AND EVOLUTION. 2001;18(8):1502-1511.
Atchley, W. R., Lokot, T., Wollenberg, K., Dress, A., & Ragg, H. (2001). Phylogenetic analyses of amino acid variation in the serpin proteins. MOLECULAR BIOLOGY AND EVOLUTION, 18(8), 1502-1511. https://doi.org/10.1093/oxfordjournals.molbev.a003936
Atchley, William R., Lokot, Tatjana, Wollenberg, Kurt, Dress, Andreas, and Ragg, Hermann. 2001. “Phylogenetic analyses of amino acid variation in the serpin proteins”. MOLECULAR BIOLOGY AND EVOLUTION 18 (8): 1502-1511.
Atchley, W. R., Lokot, T., Wollenberg, K., Dress, A., and Ragg, H. (2001). Phylogenetic analyses of amino acid variation in the serpin proteins. MOLECULAR BIOLOGY AND EVOLUTION 18, 1502-1511.
Atchley, W.R., et al., 2001. Phylogenetic analyses of amino acid variation in the serpin proteins. MOLECULAR BIOLOGY AND EVOLUTION, 18(8), p 1502-1511.
W.R. Atchley, et al., “Phylogenetic analyses of amino acid variation in the serpin proteins”, MOLECULAR BIOLOGY AND EVOLUTION, vol. 18, 2001, pp. 1502-1511.
Atchley, W.R., Lokot, T., Wollenberg, K., Dress, A., Ragg, H.: Phylogenetic analyses of amino acid variation in the serpin proteins. MOLECULAR BIOLOGY AND EVOLUTION. 18, 1502-1511 (2001).
Atchley, William R., Lokot, Tatjana, Wollenberg, Kurt, Dress, Andreas, and Ragg, Hermann. “Phylogenetic analyses of amino acid variation in the serpin proteins”. MOLECULAR BIOLOGY AND EVOLUTION 18.8 (2001): 1502-1511.

26 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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SERPINA2 is a novel gene with a divergent function from SERPINA1.
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Roberts TH, Hejgaard J., Funct Integr Genomics 8(1), 2008
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Yampolsky LY, Stoltzfus A., Genetics 170(4), 2005
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The heparin binding properties of heparin cofactor II suggest an antithrombin-like activation mechanism.
O'Keeffe D, Olson ST, Gasiunas N, Gallagher J, Baglin TP, Huntington JA., J Biol Chem 279(48), 2004
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van Gent D, Sharp P, Morgan K, Kalsheker N., Int J Biochem Cell Biol 35(11), 2003
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