The folding and evolution of multidomain proteins. Nature Reviews Molecular Cell Biology. April 2007, 8 (4): 319–30. PMID 17356578. doi:10.1038/nrm2144.
The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. The Journal of Biological Chemistry. September 2001, 276 (36): 33293–6. PMID 11435447. doi:10.1074/jbc.R100016200.
Evolution of primate α and θ defensins revealed by analysis of genomes. Molecular Biology Reports. June 2014, 41 (6): 3859–66. PMID 24557891. doi:10.1007/s11033-014-3253-z.
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Efficient, crosswise catalytic promiscuity among enzymes that catalyze phosphoryl transfer. Biochimica et Biophysica Acta. January 2013, 1834 (1): 417–24. PMID 22885024. doi:10.1016/j.bbapap.2012.07.015.
Aplysia limacina myoglobin. Crystallographic analysis at 1.6 A resolution. Journal of Molecular Biology. February 1989, 205 (3): 529–44. PMID 2926816. doi:10.1016/0022-2836(89)90224-6.
The immunoglobulin fold. Structural classification, sequence patterns and common core. Journal of Molecular Biology. September 1994, 242 (4): 309–20. PMID 7932691. doi:10.1006/jmbi.1994.1582.
The folding and evolution of multidomain proteins. Nature Reviews Molecular Cell Biology. April 2007, 8 (4): 319–30. PMID 17356578. doi:10.1038/nrm2144.
The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. The Journal of Biological Chemistry. September 2001, 276 (36): 33293–6. PMID 11435447. doi:10.1074/jbc.R100016200.
Evolution of primate α and θ defensins revealed by analysis of genomes. Molecular Biology Reports. June 2014, 41 (6): 3859–66. PMID 24557891. doi:10.1007/s11033-014-3253-z.
Efficient, crosswise catalytic promiscuity among enzymes that catalyze phosphoryl transfer. Biochimica et Biophysica Acta. January 2013, 1834 (1): 417–24. PMID 22885024. doi:10.1016/j.bbapap.2012.07.015.
Aplysia limacina myoglobin. Crystallographic analysis at 1.6 A resolution. Journal of Molecular Biology. February 1989, 205 (3): 529–44. PMID 2926816. doi:10.1016/0022-2836(89)90224-6.
The immunoglobulin fold. Structural classification, sequence patterns and common core. Journal of Molecular Biology. September 1994, 242 (4): 309–20. PMID 7932691. doi:10.1006/jmbi.1994.1582.