Fitch, W. M. (1976) The molecular evolution of cytochrome c in eukaryotes. J. Mol. Evol. 8, 13–40.

Fitch, W. M. and Farris, J. S. (1974) Evolutionary trees with minimum nucleotide replacements from amino acid sequences. J. Mol. Evol. 3, 263–278.

Fitch, W. M. and Markowitz, E. (1970) An improved method for determining codon variability in a gene and its application to the rate of fixations of mutations in evolution. Biochem. Genet. 4, 579–593.

Fitch, W. M. and Ye, J. (1991) Weighted parsimony: Does it work? In Phylogenetic Analysis of DNA Sequences, eds. Miyamoto, M. and Cracraft, J. (Oxford Univ. Press, New York), pp. 147–154.

Fridovich, I. (1986) Superoxide dismutase. Adv. Enzymol. 58, 61–97.

Gaut, B. S., Muse, S. V. and Clegg, M. T. (1993) Relative rates of nucleotide substitution in the chloroplast genome. Mol. Phylogenet. Evol. 2, 89–96.

Getzoff, E. D., Tainer, J. A., Stempien, M. M., Bell, G. I. and Hallewell, R. A. (1989) Evolution of CuZn superoxide dismutase and the Greek key beta-barrel structural motif. Proteins 5, 322–336.

Jolles, J., Prager, E. M., Alnemri, E. S., Jolles, P., Ibrahimi, I. M. and Wilson, A. C. (1990) Amino acid sequences of stomach and nonstomach lysozymes of ruminants. J. Mol. Evol. 30, 370–382.

Jukes, T. H. and Cantor, C. R. (1969) Evolution of protein molecules In Mammalian Protein Metabolism, ed. Munro, H. N. (Academic, New York), pp. 21–132.

Kwiatowski, J., Hudson, R. R. and Ayala, F. J. (1991) The rate of Cu,Zn Superoxide dismutase evolution. Free Radical Res. Commun. 13, 363–370.

Kwiatowski, J., Skarecky, D. and Ayala, F. J. (1992) Structure and sequence of the Cu,Zn Sod gene in the Mediterranean fruit fly, Ceratitis capitata: Intron insertion/deletion and evolution of the gene. Mol. Phylogenet. Evol. 1, 72–82.

Li, W. H. and Graur, D. (1991) Fundamentals of Molecular Evolution (Sinauer, Sunderland, MA).

Margoliash, E. and Smith, E. (1965) Structural and functional aspects of cytochrome c in relation to evolution. In Evolving Genes and Proteins , eds. Bryson, V. and Vogel, H. J. (Academic, New York), pp. 221–242.

Shoemaker, J. S. and Fitch, W. M. (1989) Evidence from nuclear sequences that invariable sites should be considered when calculating sequence divergence. Mol. Biol. Evol. 6, 270–289.

Steinman, H. M. (1988) Bacterial superoxide dismutases. Basic Life Sci. 49, 641–646.

Stewart, C. B. & Wilson, A. C. (1987) Sequence convergence and functional adaptation of stomach lysozymes from foregut fermenters. Cold Spring Harbor Symposium. Quant. Biol. 52, 891–899.

Tainer, J. A., Getzoff, E. D., Beem, K. M., Richardson, J. S. and Richardson, D. C. (1982) Determination and analysis of the 2Å structure of copper, zinc superoxide dismutase. J. Mol. Biol. 160, 181–217.

Tainer, J. A., Getzoff, E. D., Richardson, J. S. and Richardson, D. C. (1983) Structure and mechanism of copper, zinc superoxide dismutase. Nature (London) 306, 284–287.

Zuckerkandl, E. and Pauling, L. (1962) Molecular disease, evolution and genetic heterogeneity. In Horizons in Biochemistry (Academic, New York), pp. 189–225.

The National Academies of Sciences, Engineering, and Medicine
500 Fifth St. N.W. | Washington, D.C. 20001

Copyright © National Academy of Sciences. All rights reserved.
Terms of Use and Privacy Statement