N‐terminal or signal peptide sequence engineering prevents truncation of human monoclonal antibody light chains
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S. Milne | S. Gibson | D. Hatton | N. Bond | G. Pettman | N J Bond | S Milne | D. Higazi | S J Gibson | A Lewis | A Sheriff | G Pettman | R Pradhan | D R Higazi | D Hatton | R. Pradhan | A. Lewis | A. Sheriff
[1] A. Balland,et al. Rapid identification of an antibody DNA construct rearrangement sequence variant by mass spectrometry , 2014, mAbs.
[2] Stian Knappskog,et al. The level of synthesis and secretion of Gaussia princeps luciferase in transfected CHO cells is heavily dependent on the choice of signal peptide. , 2007, Journal of biotechnology.
[3] J. Gordon,et al. Deletion of the propeptide from human preproapolipoprotein A-II redirects cotranslational processing by signal peptidase. , 1986, The Journal of biological chemistry.
[4] G von Heijne,et al. Signal sequences. The limits of variation. , 1985, Journal of molecular biology.
[5] B. Li,et al. Optimization of Heavy Chain and Light Chain Signal Peptides for High Level Expression of Therapeutic Antibodies in CHO Cells , 2015, PloS one.
[6] S. Cianférani,et al. Characterization of the N-terminal heterogeneities of monoclonal antibodies using in-gel charge derivatization of α-amines and LC-MS/MS. , 2015, Analytical chemistry.
[7] B. Wilkinson,et al. Co-translational targeting and translocation of proteins to the endoplasmic reticulum. , 2013, Biochimica et biophysica acta.
[8] S. Salzberg,et al. GeneSplicer: a new computational method for splice site prediction. , 2001, Nucleic acids research.
[9] G. Winter,et al. Cloning immunoglobulin variable domains for expression by the polymerase chain reaction. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[10] A. Cattaneo,et al. An integrated vector system for the eukaryotic expression of antibodies or their fragments after selection from phage display libraries. , 1997, Gene.
[11] Identification of an alternative signal peptide cleavage site of mouse monoclonal antibodies by mass spectrometry. , 2007, Immunology letters.
[12] Z. Konthur,et al. Secretory signal peptide modification for optimized antibody-fragment expression-secretion in Leishmania tarentolae , 2012, Microbial Cell Factories.
[13] A. Ambrogelly,et al. Characterization of antibody variants during process development: The tale of incomplete processing of N-terminal secretion peptide , 2012, mAbs.
[14] G von Heijne,et al. Patterns of amino acids near signal-sequence cleavage sites. , 1983, European journal of biochemistry.
[15] D. Hatton,et al. A high‐yielding CHO transient system: Coexpression of genes encoding EBNA‐1 and GS enhances transient protein expression , 2014, Biotechnology progress.
[16] Shoba Ranganathan,et al. Flanking signal and mature peptide residues influence signal peptide cleavage , 2008, BMC Bioinformatics.
[17] A. J. Mixson,et al. Alteration in the IL‐2 signal peptide affects secretion of proteins in vitro and in vivo , 2005, The journal of gene medicine.
[18] D Perlman,et al. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. , 1983, Journal of molecular biology.
[19] A. Raghani,et al. Analysis of monoclonal antibody product heterogeneity resulting from alternate cleavage sites of signal peptide. , 2010, Analytical biochemistry.
[20] Christoph Zehe,et al. Optimized signal peptides for the development of high expressing CHO cell lines , 2013, Biotechnology and bioengineering.
[21] G von Heijne,et al. How signal sequences maintain cleavage specificity. , 1984, Journal of molecular biology.
[22] M. N. Margolies,et al. A spontaneous variant of an antidigoxin hybridoma antibody with increased affinity arises from a heavy chain signal peptide mutation. , 1992, Molecular immunology.
[23] S. Brunak,et al. SignalP 4.0: discriminating signal peptides from transmembrane regions , 2011, Nature Methods.
[24] Kazuhiro Masuda,et al. Establishment of a signal peptide with cross-species compatibility for functional antibody expression in both Escherichia coli and Chinese hamster ovary cells. , 2014, Biochemical and biophysical research communications.
[25] Thomas Noll. Cells and Culture , 2010 .
[26] W. Xu,et al. Developability studies before initiation of process development , 2013, mAbs.
[27] J. Gordon,et al. Substrate specificity of eukaryotic signal peptidase. Site-saturation mutagenesis at position -1 regulates cleavage between multiple sites in human pre (delta pro) apolipoprotein A-II. , 1988, The Journal of biological chemistry.
[28] Alain Van Dorsselaer,et al. Characterization of therapeutic antibodies and related products. , 2013, Analytical chemistry.
[29] J I Gordon,et al. Residues flanking the COOH-terminal C-region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase and the extent of coupling of its co-translational translocation and proteolytic processing in vitro. , 1990, The Journal of biological chemistry.
[30] G. von Heijne,et al. The code for directing proteins for translocation across ER membrane: SRP cotranslationally recognizes specific features of a signal sequence. , 2015, Journal of molecular biology.
[31] Yelena Lyubarskaya,et al. Analysis of recombinant monoclonal antibody isoforms by electrospray ionization mass spectrometry as a strategy for streamlining characterization of recombinant monoclonal antibody charge heterogeneity. , 2006, Analytical biochemistry.