Pages that link to "Q42988858"

The following pages link to Dependence of the anti-chaperone activity of protein disulphide isomerase on its chaperone activity (Q42988858):

Displaying 13 items.

• FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock-inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteins (Q28343586) (← links)
• Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding (Q30746401) (← links)
• Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (Q31072248) (← links)
• The protein disulphide-isomerase family: unravelling a string of folds (Q33543247) (← links)
• Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor (Q36282102) (← links)
• Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor (Q36519464) (← links)
• Molecular cloning, expression and characterization of protein disulfide isomerase from Conus marmoreus (Q42628946) (← links)
• Chaperone and antichaperone activities of trigger factor (Q44138637) (← links)
• The acidic C-terminal domain stabilizes the chaperone function of protein disulfide isomerase. (Q45052895) (← links)
• Catalysis of creatine kinase refolding by protein disulfide isomerase involves disulfide cross-link and dimer to tetramer switch (Q45254051) (← links)
• Mutations that destabilize the a' domain of human protein-disulfide isomerase indirectly affect peptide binding. (Q52539029) (← links)
• Contributions of protein disulfide isomerase domains to its chaperone activity (Q72999583) (← links)
• Chaperone activity of DsbC (Q77955138) (← links)