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Mabs|November 23, 2022
A computational method for predicting the aggregation propensity of IgG1 and IgG4(P) mAbs in common storage buffersJames T Heads, Sebastian Kelm, Kerry Tyson, et al.
Acta Neuropathologica|January 1, 1991
Sensory nerve pathology in amyotrophic lateral sclerosisT Heads, M Pollock, A Robertson, et al.
Protein Engineering, Design & Selection : PEDS|May 16, 2012
Towards a universal disulphide stabilised single chain Fv format: importance of interchain disulphide bond location and vL-vH orientationEve E Weatherill, Katharine L Cain, Sam P Heywood, et al.
Acta Crystallographica. Section F, Structural Biology Communications|March 6, 2020
Engineering the Fab fragment of the anti-IgE omalizumab to prevent Fab crystallization and permit IgE-Fc complex crystallizationAlkistis N Mitropoulou, Tom Ceska, James T Heads, et al.
Protein Science : a Publication of the Protein Society|July 5, 2012
Relative stabilities of IgG1 and IgG4 Fab domains: influence of the light-heavy interchain disulfide bond architectureJames T Heads, Ralph Adams, Lena E D'Hooghe, et al.
Protein Engineering, Design & Selection : PEDS|December 24, 2019
Electrostatic interactions modulate the differential aggregation propensities of IgG1 and IgG4P antibodies and inform charged residue substitutions for improved developabilityJames T Heads, Richard Lamb, Sebastian Kelm, et al.
Clinical and Vaccine Immunology : CVI|January 18, 2013
A mixture of functionally oligoclonal humanized monoclonal antibodies that neutralize Clostridium difficile TcdA and TcdB with high levels of in vitro potency shows in vivo protection in a hamster infection modelNicola L Davies, Joanne E Compson, Brendon Mackenzie, et al.
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