Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

L W Ruddock

Showing results (11-20 of 22) with videos related to

Pageof 3
Sort By:
Proceedings of the National Academy of Sciences of the United States of America|January 5, 2000
Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiaeS S Eaglestone, L W Ruddock, B S Cox, et al.
Antioxidants & Redox Signaling|May 9, 2006
pH dependence of the peptide thiol-disulfide oxidase activity of six members of the human protein disulfide isomerase familyH I Alanen, K E H Salo, A Pirneskoski, et al.
The Journal of Biological Chemistry|September 8, 2001
Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id essential and sufficient for peptide bindingH M Webb, L W Ruddock, R J Marchant, 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.
The Biochemical Journal|March 10, 2001
The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligandsP Klappa, R B Freedman, M Langenbuch, et al.
The Journal of Biological Chemistry|May 2, 2000
Mutations that destabilize the a' domain of human protein-disulfide isomerase indirectly affect peptide bindingP Klappa, P Koivunen, A Pirneskoski, et al.
Biochemistry|December 17, 1996
A pH-dependent conformational change in the B-subunit pentamer of Escherichia coli heat-labile enterotoxin: structural basis and possible functional role for a conserved feature of the AB5 toxin familyL W Ruddock, H M Webb, S P Ruston, et al.
Antioxidants & Redox Signaling|September 19, 2003
Defining the domain boundaries of the human protein disulfide isomerasesH I Alanen, K E H Salo, M Pekkala, et al.
Pageof 3

Showing results (11-20 of 22) with videos related to

Sort By:
Pageof 3
Proceedings of the National Academy of Sciences of the United States of America|January 5, 2000
Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiaeS S Eaglestone, L W Ruddock, B S Cox, et al.
Antioxidants & Redox Signaling|May 9, 2006
pH dependence of the peptide thiol-disulfide oxidase activity of six members of the human protein disulfide isomerase familyH I Alanen, K E H Salo, A Pirneskoski, et al.
The Journal of Biological Chemistry|September 8, 2001
Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id essential and sufficient for peptide bindingH M Webb, L W Ruddock, R J Marchant, 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.
The Biochemical Journal|March 10, 2001
The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligandsP Klappa, R B Freedman, M Langenbuch, et al.
The Journal of Biological Chemistry|May 2, 2000
Mutations that destabilize the a' domain of human protein-disulfide isomerase indirectly affect peptide bindingP Klappa, P Koivunen, A Pirneskoski, et al.
Biochemistry|December 17, 1996
A pH-dependent conformational change in the B-subunit pentamer of Escherichia coli heat-labile enterotoxin: structural basis and possible functional role for a conserved feature of the AB5 toxin familyL W Ruddock, H M Webb, S P Ruston, et al.
Antioxidants & Redox Signaling|September 19, 2003
Defining the domain boundaries of the human protein disulfide isomerasesH I Alanen, K E H Salo, M Pekkala, et al.
Pageof 3