Rational library design by functional CDR resampling.
暂无分享,去创建一个
Qi Zhao | Diane Buhr | Courtney Gunter | Jenny Frenette | Mary Ferguson | Eric Sanford | Erika Holland | Chitra Rajagopal | Melissa Batonick | Margaret M Kiss | Michael P Weiner | M. Weiner | E. Sanford | Qi Zhao | M. Batonick | Chitra Rajagopal | C. Gunter | D. Buhr | Jenny Frenette | Mary Ferguson | E. Holland | M. M. Kiss | Eric M. Sanford | Mary R Ferguson | Courtney Gunter
[1] A. Pini,et al. Design and Use of a Phage Display Library , 1998, The Journal of Biological Chemistry.
[2] K D Wittrup,et al. Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[3] Myung-Shin Lee,et al. A pseudoknot improves selection efficiency in ribosome display , 2007, Molecular biotechnology.
[4] Frederic A. Fellouse,et al. Phage-displayed antibody libraries of synthetic heavy chain complementarity determining regions. , 2004, Journal of molecular biology.
[5] D. Cox,et al. Synthetic antibodies designed on natural sequence landscapes. , 2011, Journal of molecular biology.
[6] J. E. Chung,et al. Construction of a large synthetic human scFv library with six diversified CDRs and high functional diversity , 2009, Molecules and cells.
[7] A. Wu,et al. The crystal structure of an anti-CEA scFv diabody assembled from T84.66 scFvs in V(L)-to-V(H) orientation: implications for diabody flexibility. , 2003, Journal of molecular biology.
[8] Yatin R. Gokarn,et al. Characterization of antibody aggregation: role of buried, unpaired cysteines in particle formation. , 2010, Journal of pharmaceutical sciences.
[9] D. Rigden,et al. Employing in vitro directed molecular evolution for the selection of α-amylase variant inhibitors with activity toward cotton boll weevil enzyme. , 2013, Journal of biotechnology.
[10] R. Bhat,et al. Directed evolution of an anti-human red blood cell antibody , 2009, mAbs.
[11] Bartek Wilczynski,et al. Biopython: freely available Python tools for computational molecular biology and bioinformatics , 2009, Bioinform..
[12] I. Fujii. [Directed evolution of antibody molecules in phage-displayed combinatorial libraries]. , 2007, Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan.
[13] Jeong-Sun Kim,et al. Crystal structure of single‐domain VL of an anti‐DNA binding antibody 3D8 scFv and its active site revealed by complex structures of a small molecule and metals , 2008, Proteins.
[14] V. Quintero-Hernández,et al. Directed evolution, phage display and combination of evolved mutants: a strategy to recover the neutralization properties of the scFv version of BCF2 a neutralizing monoclonal antibody specific to scorpion toxin Cn2. , 2005, Journal of molecular biology.
[15] Paolo Marcatili,et al. PIGS: automatic prediction of antibody structures , 2008, Bioinform..
[16] S. Walsh,et al. Crystal structure of a 3B3 variant—A broadly neutralizing HIV‐1 scFv antibody , 2009, Protein science : a publication of the Protein Society.
[17] Xuelian Bai,et al. Construction of a scFv Library with Synthetic, Non-combinatorial CDR Diversity. , 2017, Methods in molecular biology.
[18] Daniele Sblattero,et al. Exploiting recombination in single bacteria to make large phage antibody libraries , 2000, Nature Biotechnology.
[19] Peter J. A. Cock,et al. Bio.Phylo: A unified toolkit for processing, analyzing and visualizing phylogenetic trees in Biopython , 2012, BMC Bioinformatics.
[20] Michele C. Kieke,et al. Directed evolution of a stable scaffold for T-cell receptor engineering , 2000, Nature Biotechnology.
[21] A. Lim,et al. Directed evolution of high-affinity antibody mimics using mRNA display. , 2002, Chemistry & biology.
[22] Baltazar Becerril,et al. A strategy for the generation of specific human antibodies by directed evolution and phage display , 2005, The FEBS journal.
[23] Melissa Batonick,et al. Platform for high-throughput antibody selection using synthetically-designed antibody libraries. , 2016, New biotechnology.
[24] A. Lesk,et al. Canonical structures for the hypervariable regions of immunoglobulins. , 1987, Journal of molecular biology.
[25] G. Winter,et al. Thermodynamically stable aggregation-resistant antibody domains through directed evolution. , 2008, Journal of molecular biology.