A scFv Antibody Mutant Isolated in a Genetic Screen for Improved Export via the Twin Arginine Transporter Pathway Exhibits Faster Folding
- 8 June 2007
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 369 (3) , 631-639
- https://doi.org/10.1016/j.jmb.2007.03.068
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- Fresh embryo donation for human embryonic stem cell (hESC) research: the experiences and values of IVF couples asked to be embryo donorsHuman Reproduction, 2009
- The Bacterial Twin-Arginine Translocation PathwayAnnual Review of Microbiology, 2006
- Genetic selection for protein solubility enabled by the folding quality control feature of the twin‐arginine translocation pathwayProtein Science, 2006
- The DsbA Signal Sequence Directs Efficient, Cotranslational Export of Passenger Proteins to the Escherichia coli Periplasm via the Signal Recognition Particle PathwayJournal of Bacteriology, 2003
- The scFv fragment of the antibody hu4d5-8: evidence for early premature domain interaction in refoldingJournal of Molecular Biology, 2001
- In vitro folding and thermodynamic stability of an antibody fragment selected in Vivo for high expression levels in Escherichia coli cytoplasmJournal of Molecular Biology, 1999
- Folding and assembly of an antibody Fv fragment, a heterodimer stabilized by antigen 1 1Edited by P. E. WrightJournal of Molecular Biology, 1999
- Embryonic Stem Cell Lines Derived from Human BlastocystsScience, 1998
- Expression of an antibody fragment at high levels in the bacterial cytoplasmJournal of Molecular Biology, 1998
- Common Principles of Protein Translocation Across MembranesScience, 1996