Mapping time dependent disulfide bond formation during in-vitro refolding of recombinant peptibody: A Fc-fusion protein
- 24 May 2023
- journal article
- research article
- Published by Elsevier in Biochemical Engineering Journal
- Vol. 197, 108969
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- The folding cooperativity of a protein is controlled by its chain topologyNature, 2010
- Identification of the Unpaired Cysteine Status and Complete Mapping of the 17 Disulfides of Recombinant Tissue Plasminogen Activator Using LC−MS with Electron Transfer Dissociation/Collision Induced DissociationAnalytical Chemistry, 2010
- Identification and prevention of antibody disulfide bond reduction during cell culture manufacturingBiotechnology and Bioengineering, 2010
- Disulfide-Linked Protein Folding PathwaysAnnual Review of Cell and Developmental Biology, 2008
- Atomic force microscopy reveals parallel mechanical unfolding pathways of T4 lysozyme: Evidence for a kinetic partitioning mechanismProceedings of the National Academy of Sciences, 2008
- Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domainProtein Science, 2008
- The folding and evolution of multidomain proteinsNature Reviews Molecular Cell Biology, 2007
- Mapping of Protein Disulfide Bonds Using Negative Ion Fragmentation with a Broadband Precursor SelectionAnalytical Chemistry, 2006
- Evolution of the Protein RepertoireScience, 2003
- Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulationsAAPS PharmSci, 2003