Harvey JA, Itzhaki LS, Main ERG(2018). Programmed Protein Self-Assembly Driven by Genetically Encoded Intein-Mediated Native Chemical Ligation. ACS Synth Biol vol. 7, (4) 1067-1074.
Lowe AR, Perez-Riba A, Itzhaki LS et al.(2018). PyFolding: Open-Source Graphing, Simulation, and Analysis of the Biophysical Properties of Proteins. Biophysical Journal
Perez-Riba A, Lowe A, Main E et al. (2017). Entropically-Challenged Tandem-repeat Proteins: Breakdown of Nearest-Neighbour Cooperativity. PROTEIN SCIENCE. vol. 26, 108-108.
Millership C, Phillips JJ, Main ERG(2016). Ising Model Reprogramming of a Repeat Protein's Equilibrium Unfolding Pathway. Journal of Molecular Biology vol. 428, (9 Pt A) 1804-1817.
Perez-Riba A, Main ER, Itzhaki LS (2016). The Effect of Loop Insertions on the Folding of Tandem-Repeat Proteins. BIOPHYSICAL JOURNAL. vol. 110, 181A-181A.
Rowling PJE, Sivertsson EM, Perez-Riba A et al.(2015). Dissecting and reprogramming the folding and assembly of tandem-repeat proteins. Biochem Soc Trans vol. 43, (5) 881-888.
Main ERG, Phillips JJ, Millership C(2013). Repeat protein engineering: creating functional nanostructures/biomaterials from modular building blocks. Biochem Soc Trans vol. 41, (5) 1152-1158.
Singh SK, Boyle AL, Main ERG(2013). LcrH, a class II chaperone from the type three secretion system, has a highly flexible native structure. J Biol Chem vol. 288, (6) 4048-4055.
Phillips JJ, Millership C, Main ERG(2012). Fibrous nanostructures from the self-assembly of designed repeat protein modules. Angew Chem Int Ed Engl vol. 51, (52) 13132-13135.
Phillips JJ, Javadi Y, Millership C et al.(2012). Modulation of the multistate folding of designed TPR proteins through intrinsic and extrinsic factors. Protein Sci vol. 21, (3) 327-338.
Mahendrarajah K, Dalby PA, Wilkinson B et al.(2011). A high-throughput fluorescence chemical denaturation assay as a general screen for protein-ligand binding. Anal Biochem vol. 411, (1) 155-157.
Boyd LK, Mercer B, Thompson D et al.(2010). Characterisation of the SUMO-like domains of Schizosaccharomyces pombe Rad60. PLoS One vol. 5, (9)
Gaudet M, Remtulla N, Jackson SE et al.(2010). Protein denaturation and protein:drugs interactions from intrinsic protein fluorescence measurements at the nanolitre scale. PROTEIN SCI vol. 19, (8) 1544-1554.
Javadi Y, Main ERG(2009). Exploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins. P NATL ACAD SCI USA vol. 106, (41) 17383-17388.
Main ERG, Lowe AR, Mochrie SGJ et al.(2005). A recurring theme in protein engineering: the design, stability and folding of repeat proteins. CURR OPIN STRUC BIOL vol. 15, (4) 464-471.
Kajander T, Cortajarena AL, Main ERG et al.(2005). A new folding paradigm for repeat proteins. J AM CHEM SOC vol. 127, (29) 10188-10190.
Main ERG, Stott K, Jackson SE et al.(2005). Local and long-range stability in tandemly arrayed tetratricopeptide repeats. P NATL ACAD SCI USA vol. 102, (16) 5721-5726.
Maxwell KL, Wildes D, Zarrine-Afsar A et al.(2005). Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. PROTEIN SCI vol. 14, (3) 602-616.
Main ERG, Jackson SE, Regan L(2003). The folding and design of repeat proteins: reaching a consensus. CURR OPIN STRUC BIOL vol. 13, (4) 482-489.
Main ERG, Xiong Y, Cocco MJ et al.(2003). Design of stable alpha-helical arrays from an idealized TPR motif. STRUCTURE vol. 11, (5) 497-508.
Main ERG, Fulton KF, Daggett V et al.(2001). A comparison of experimental and computational methods for mapping the interactions present in the transition state for folding of FKBP12. J BIOL PHYS vol. 27, (2) 99-117.
Main ERG, Jackson SE(1999). Does trifluoroethanol affect folding pathways and can it be used as a probe of structure in transition states?. NAT STRUCT BIOL vol. 6, (9) 831-835.
Main ERG, Fulton KF, Jackson SE(1999). Folding pathway of FKBP12 and characterisation of the transition state. J MOL BIOL vol. 291, (2) 429-444.
Fulton KF, Main ERG, Daggett V et al.(1999). Mapping the interactions present in the transition state for unfolding/folding of FKBP12. J MOL BIOL vol. 291, (2) 445-461.
Main ERG, Fulton KF, Jackson SE(1998). Context-dependent nature of destabilizing mutations on the stability of FKBP12. BIOCHEMISTRY-US vol. 37, (17) 6145-6153.