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 PDIp-Reference-Cited by-同舟云学术

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 PDIp

Published:2008-12-31 Issue:4 Volume:9 Page:758-764
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Ruddock Lloyd W.,Freedman Robert B.,Klappa Peter

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference41 articles.

1. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP;Blond-Elguindi;Cell,1993

2. Reconstitution of protein translocation from solubilized yeast membranes reveals topologically distinct roles for BiP and cytosolic Hsc70;Brodsky;J Cell Biol,1993

3. The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency;Darby;J Mol Biol,1998

4. Characterization and chromosomal localization of a new protein disulfide-isomerase, PDIp, highly expressed in human pancreas;DeSilva;DNA Cell Biol,1996

5. Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp;DeSilva;DNA Cell Biol,1997

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