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Biochemistry|February 22, 1994
Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivoA Zapun, L Cooper, T E CreightonJournal of Quality in Clinical Practice|December 1, 1996
Medical general practice: influencing clients' levels of satisfactionD N DarbyBiochemistry|August 13, 1996
Identifying and characterizing a structural domain of protein disulfide isomeraseN J Darby, J Kemmink, T E CreightonBiochemistry|May 18, 1993
The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivoA Zapun, J C Bardwell, T E CreightonTrends in Biotechnology|January 1, 1995
Mechanisms and catalysts of disulfide bond formation in proteinsT E Creighton, A Zapun, N J DarbyBiochemistry|February 10, 1998
Contributions of substrate binding to the catalytic activity of DsbCN J Darby, S Raina, T E CreightonBiochemistry|November 19, 1996
Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomeraseT Kortemme, N J Darby, T E CreightonFASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology|January 1, 1996
The roles of partly folded intermediates in protein foldingT E Creighton, N J Darby, J KemminkBiochemistry|June 28, 1994
Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptideN J Darby, R B Freedman, T E CreightonBiochemistry|October 14, 1980
Ultraviolet difference spectroscopy of intermediates trapped in unfolding and refolding of bovine pancreatic trypsin inhibitorP A Kosen, T E Creighton, E R BloutPageof 9