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Bioscience Reports|October 1, 1985
Conformation and processing of cathepsin DR H Pain, T Lah, V Turk
The Biochemical Journal|June 1, 1970
Dissociation of catalase. A correlation between changes in sedimentation and spectroscopic properties accompanying dissociation of bacterial catalase in alkaline solutionP Jones, R H Pain, A Suggett
The Biochemical Journal|September 1, 1974
Conformational changes in gastric mucoproteins induced by caesium chloride and guanidinium chlorideD Snary, A Allen, R H Pain
FEBS Letters|January 26, 1987
Tumour necrosis factor is a compact trimerP Wingfield, R H Pain, S Craig
Cellular and Molecular Life Sciences : CMLS|June 6, 1998
Beta-lactamases as models for protein-folding studiesM Vanhove, A Lejeune, R H Pain
The Biochemical Journal|August 1, 1986
Reversible deactivation of beta-lactamase by quinacillin. Extent of the conformational change in the isolated transitory complexK C Persaud, R H Pain, R Virden
Biochemistry|October 4, 2000
The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzymeB Cigić, S W Dahl, R H Pain
The Biochemical Journal|August 1, 1975
The active site of penicillinase from Staphylococcus aureus PC1. Isolation of a specific covalent complex with the substrate quinacillinR Virden, A F Bristow, R H Pain
Biochimica Et Biophysica Acta|March 29, 1984
The reversible deactivation of beta-lactamase from Staphylococcus aureus by quinacillin and cephaloridine and its modification by antibodiesE A Carrey, R Virden, R H Pain
European Journal of Biochemistry|November 4, 1985
The folding and mutual interaction of the domains of yeast 3-phosphoglycerate kinaseB Adams, R J Burgess, R H Pain
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