Genetic Selection for Enhanced FoldingIn VivoTargets the Cys14-Cys38 Disulfide Bond in Bovine Pancreatic Trypsin Inhibitor-Reference-Cited by-同舟云学术

Genetic Selection for Enhanced FoldingIn VivoTargets the Cys14-Cys38 Disulfide Bond in Bovine Pancreatic Trypsin Inhibitor

Published:2011-03-15 Issue:6 Volume:14 Page:973-984
ISSN:1523-0864
Container-title:Antioxidants & Redox Signaling
language:en
Short-container-title:Antioxidants & Redox Signaling

Author:

Foit Linda¹,Mueller-Schickert Antje¹,Mamathambika Bharath S.¹,Gleiter Stefan¹,Klaska Caitlyn L.¹,Ren Guoping¹,Bardwell James C.A.¹

Affiliation:

1. Department of Molecular, Cellular and Developmental Biology, Howard Hughes Medical Institute, University of Michigan, Ann Arbor, Michigan.

Publisher

Mary Ann Liebert Inc

Subject

Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry,Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry

Link

http://www.liebertpub.com/doi/pdf/10.1089/ars.2010.3712

Reference50 articles.

1. Early events in the disulfide-coupled folding of BPTI

2. A genetic screen to identify variants of bovine pancreatic trypsin inhibitor with altered folding energetics

3. Expressing genes in different Escherichia coli compartments

4. Disulphide-coupled protein folding pathways

5. Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitor

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