Royal Society (fra 1983), European Molecular Biology Organization, National Academy of Sciences (fra 1993), Academia Europaea (fra 1989), American Academy of Arts and Sciences
^Jackson, S. E.; Fersht, A. R. (1991). "Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition". Biochemistry. 30 (43): 10428-10435. doi:10.1021/bi00107a010. PMID1931967.
^Fersht, A. R.; Shi, J. P.; Knill-Jones, J.; Lowe, D. M.; Wilkinson, A. J.; Blow, D. M.; Brick, P.; Carter, P.; Waye, M. M. Y.; Winter, G. (1985). "Hydrogen bonding and biological specificity analysed by protein engineering". Nature. 314 (6008): 235-238. Bibcode:1985Natur.314..235F. doi:10.1038/314235a0. PMID3845322. S2CID32388197.
^Fersht, A.; Matouschek, A.; Serrano, L. (1992). "The folding of an enzyme I. Theory of protein engineering analysis of stability and pathway of protein folding". Journal of Molecular Biology. 224 (3): 771-782. doi:10.1016/0022-2836(92)90561-W. PMID1569556.
^Fersht, Alan (1999). Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding. San Francisco: W.H. Freeman. ISBN0-7167-3268-8.