Clarke, J; Fersht, A. R. (1993). «Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation». Biochemistry32 (16): 4322-9. PMID8476861. doi:10.1021/bi00067a022.
Fersht, A. R.; Dingwall, C. (1979). «Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases». Biochemistry18 (12): 2627-31. PMID375976. doi:10.1021/bi00579a030.
Fersht, A. R.; 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 Biology224 (3): 771-782. PMID1569556. doi:10.1016/0022-2836(92)90561-w.
Fersht, A. R. (2024). «From covalent transition states in chemistry to noncovalent in biology: from β- to Φ-value analysis of protein folding». Quarterly Reviews of Biophysics. 57 e4: e4. PMID38597675. doi:10.1017/S0033583523000045.
Itzhaki, L. S.; Otzen, D.E.; Fersht, A. R. (1995). «The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding». Journal of Molecular Biology254 (2): 260-88. PMID7490748. doi:10.1006/jmbi.1995.0616.
«Alan R. Fersht receives Bader Award / Corey Award to David W. C. Mac Millan / Breslow Award to Peter B. Dervan». Angewandte Chemie International Edition43 (41): 5430. 2004. PMID15484254. doi:10.1002/anie.200462026.
Clarke, J; Fersht, A. R. (1993). «Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation». Biochemistry32 (16): 4322-9. PMID8476861. doi:10.1021/bi00067a022.
Fersht, A. R.; Dingwall, C. (1979). «Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases». Biochemistry18 (12): 2627-31. PMID375976. doi:10.1021/bi00579a030.
Fersht, A. R.; 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 Biology224 (3): 771-782. PMID1569556. doi:10.1016/0022-2836(92)90561-w.
Fersht, A. R. (2024). «From covalent transition states in chemistry to noncovalent in biology: from β- to Φ-value analysis of protein folding». Quarterly Reviews of Biophysics. 57 e4: e4. PMID38597675. doi:10.1017/S0033583523000045.
Itzhaki, L. S.; Otzen, D.E.; Fersht, A. R. (1995). «The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding». Journal of Molecular Biology254 (2): 260-88. PMID7490748. doi:10.1006/jmbi.1995.0616.
«Alan R. Fersht receives Bader Award / Corey Award to David W. C. Mac Millan / Breslow Award to Peter B. Dervan». Angewandte Chemie International Edition43 (41): 5430. 2004. PMID15484254. doi:10.1002/anie.200462026.
«Alan Fersht. 2001 Stein and Moore Award». Protein Science10 (4): 905. 2001. PMID11345067.
Fersht, Alan (2017). Structure and mechanism in protein science : a guide to enzyme catalysis and protein folding. New Jersey. ISBN978-981-322-519-0. OCLC986523773.