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Current Biology : CB|July 4, 1998
Protein folding: a missing redox link in the endoplasmic reticulumR B Freedman, A D Dunn, L W Ruddock
Biochemistry|February 11, 2004
The disassembly and reassembly of mutants of Escherichia coli heat-labile enterotoxin: replacement of proline 93 does not abolish the reassembly-competent and reassembly-incompetent statesC Cheesman, R B Freedman, L W Ruddock
Protein Science : a Publication of the Protein Society|May 4, 2000
Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIpL W Ruddock, R B Freedman, P Klappa
Biochemistry|February 11, 2004
The refolding and reassembly of Escherichia coli heat-labile enterotoxin B-subunit: analysis of reassembly-competent and reassembly-incompetent unfolded statesC Cheesman, L W Ruddock, R B Freedman
The Biochemical Journal|May 1, 1996
pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrateL W Ruddock, T R Hirst, R B Freedman
The EMBO Journal|March 28, 1998
The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteinsP Klappa, L W Ruddock, N J Darby, et al.
European Journal of Biochemistry|July 4, 1998
A pancreas-specific glycosylated protein disulphide-isomerase binds to misfolded proteins and peptides with an interaction inhibited by oestrogensP Klappa, T Stromer, R Zimmermann, et al.
The Journal of Biological Chemistry|August 9, 1996
Assembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. Kinetics and molecular basis of rate-limiting steps in vitroL W Ruddock, J J Coen, C Cheesman, et al.
Antioxidants & Redox Signaling|September 19, 2003
The influence of His94 and Pro149 in modulating the activity of V. cholerae DsbAJ Blank, T Kupke, E Lowe, et al.
The Journal of Biological Chemistry|January 13, 2001
Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57A Pirneskoski, L W Ruddock, P Klappa, et al.
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