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L W Ruddock

Showing results (1-10 of 22) with videos related to

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Current Biology : CB|June 9, 1999
Oxidative stress: Protein folding with a novel redox switchL W Ruddock, P Klappa
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
Current Biology : CB|July 4, 1998
Protein folding: a missing redox link in the endoplasmic reticulumR B Freedman, A D Dunn, L W Ruddock
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
Biometrics|November 7, 2003
Models for yeast prionsB J T Morgan, M S Ridout, L W Ruddock
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.
Biochemical Society Transactions|November 1, 1995
Translocation of folded proteins across bacterial outer membranes: a novel secretory phenomenonT R Hirst, J B Hillary, L W Ruddock, 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.
Pageof 3

Showing results (1-10 of 22) with videos related to

Sort By:
Pageof 3
Current Biology : CB|June 9, 1999
Oxidative stress: Protein folding with a novel redox switchL W Ruddock, P Klappa
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
Current Biology : CB|July 4, 1998
Protein folding: a missing redox link in the endoplasmic reticulumR B Freedman, A D Dunn, L W Ruddock
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
Biometrics|November 7, 2003
Models for yeast prionsB J T Morgan, M S Ridout, L W Ruddock
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.
Biochemical Society Transactions|November 1, 1995
Translocation of folded proteins across bacterial outer membranes: a novel secretory phenomenonT R Hirst, J B Hillary, L W Ruddock, 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.
Pageof 3