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

P Klappa

Showing results (11-20 of 21) with videos related to

Pageof 3
Sort By:
Biotechnology and Bioengineering|November 3, 2009
Protein disulfide isomerase does not control recombinant IgG4 productivity in mammalian cell linesN V L Hayes, C M Smales, P Klappa
The EMBO Journal|October 1, 1991
A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomesP Klappa, P Mayinger, R Pipkorn, et al.
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.
The Biochemical Journal|June 21, 2001
Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein foldingB Kramer, D M Ferrari, P Klappa, 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|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.
FEBS Letters|April 14, 1997
Pancreas specific protein disulfide isomerase, PDIp, is in transient contact with secretory proteins during late stages of translocationJ Volkmer, S Guth, W Nastainczyk, 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.
Pageof 3

Showing results (11-20 of 21) with videos related to

Sort By:
Pageof 3
Biotechnology and Bioengineering|November 3, 2009
Protein disulfide isomerase does not control recombinant IgG4 productivity in mammalian cell linesN V L Hayes, C M Smales, P Klappa
The EMBO Journal|October 1, 1991
A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomesP Klappa, P Mayinger, R Pipkorn, et al.
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.
The Biochemical Journal|June 21, 2001
Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein foldingB Kramer, D M Ferrari, P Klappa, 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|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.
FEBS Letters|April 14, 1997
Pancreas specific protein disulfide isomerase, PDIp, is in transient contact with secretory proteins during late stages of translocationJ Volkmer, S Guth, W Nastainczyk, 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.
Pageof 3