Analysis of nanobody paratopes reveals greater diversity than classical antibodies
暂无分享,去创建一个
[1] B. Lee,et al. The interpretation of protein structures: estimation of static accessibility. , 1971, Journal of molecular biology.
[2] A. Lesk,et al. Conformations of immunoglobulin hypervariable regions , 1989, Nature.
[3] E. Kabat,et al. Identical V region amino acid sequences and segments of sequences in antibodies of different specificities. Relative contributions of VH and VL genes, minigenes, and complementarity-determining regions to binding of antibody-combining sites. , 1991, Journal of immunology.
[4] S. Muyldermans,et al. Naturally occurring antibodies devoid of light chains , 1993, Nature.
[5] M. Lawrence,et al. Shape complementarity at protein/protein interfaces. , 1993, Journal of molecular biology.
[6] Chantal Abergel,et al. Identification of specificity‐determining residues in antibodies , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[7] L. Wyns,et al. A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops. , 1999, Structure.
[8] T. N. Bhat,et al. The Protein Data Bank , 2000, Nucleic Acids Res..
[9] A. Plückthun,et al. Yet another numbering scheme for immunoglobulin variable domains: an automatic modeling and analysis tool. , 2001, Journal of molecular biology.
[10] C. Woo,et al. The generation of antibody diversity through somatic hypermutation and class switch recombination. , 2004, Genes & development.
[11] Fred Dyda,et al. Water molecules in the antibody-antigen interface of the structure of the Fab HyHEL-5-lysozyme complex at 1.7 A resolution: comparison with results from isothermal titration calorimetry. , 2005, Acta crystallographica. Section D, Biological crystallography.
[12] L. Wyns,et al. Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[13] Andrew C. R. Martin,et al. Analysis and improvements to Kabat and structurally correct numbering of antibody variable domains. , 2008, Molecular immunology.
[14] Jeffrey J. Gray,et al. Analysis and Modeling of the Variable Region of Camelid Single-Domain Antibodies , 2011, The Journal of Immunology.
[15] Randy J. Read,et al. Overview of the CCP4 suite and current developments , 2011, Acta crystallographica. Section D, Biological crystallography.
[16] S. Rasmussen,et al. Structure of a nanobody-stabilized active state of the β2 adrenoceptor , 2010, Nature.
[17] Yanay Ofran,et al. Paratome: an online tool for systematic identification of antigen-binding regions in antibodies based on sequence or structure , 2012, Nucleic Acids Res..
[18] H. Ewers,et al. A simple, versatile method for GFP-based super-resolution microscopy via nanobodies , 2012, Nature Methods.
[19] Michael Y. Galperin,et al. The 2012 Nucleic Acids Research Database Issue and the online Molecular Biology Database Collection , 2011, Nucleic Acids Res..
[20] B. Mumey,et al. Antigen-antibody interface properties: composition, residue interactions, and features of 53 non-redundant structures. , 2012, Biochimica et biophysica acta.
[21] Yanay Ofran,et al. Structural Consensus among Antibodies Defines the Antigen Binding Site , 2012, PLoS Comput. Biol..
[22] Serge Muyldermans,et al. Nanobodies: natural single-domain antibodies. , 2013, Annual review of biochemistry.
[23] N. Palaniyar,et al. NET balancing: a problem in inflammatory lung diseases , 2013, Front. Immun..
[24] Inbal Sela-Culang,et al. The Structural Basis of Antibody-Antigen Recognition , 2013, Front. Immunol..
[25] Paolo Marcatili,et al. Prediction of site-specific interactions in antibody-antigen complexes: the proABC method and server , 2013, Bioinform..
[26] P. Martineau,et al. Restricted diversity of antigen binding residues of antibodies revealed by computational alanine scanning of 227 antibody-antigen complexes. , 2014, Journal of molecular biology.
[27] S. Muyldermans,et al. Nanobody-based products as research and diagnostic tools. , 2014, Trends in biotechnology.
[28] A. Yang,et al. Origins of specificity and affinity in antibody–protein interactions , 2014, Proceedings of the National Academy of Sciences.
[29] Rubel Chakravarty,et al. Nanobody: The “Magic Bullet” for Molecular Imaging? , 2014, Theranostics.
[30] Jiye Shi,et al. SAbDab: the structural antibody database , 2013, Nucleic Acids Res..
[31] Qifang Xu,et al. PyIgClassify: a database of antibody CDR structural classifications , 2014, Nucleic Acids Res..
[32] E. Pelletier,et al. Abundant toxin-related genes in the genomes of beneficial symbionts from deep-sea hydrothermal vent mussels , 2015, eLife.
[33] A. Desmyter,et al. Camelid nanobodies: killing two birds with one stone. , 2015, Current opinion in structural biology.
[34] Mark Bates,et al. Nanobodies: site-specific labeling for super-resolution imaging, rapid epitope-mapping and native protein complex isolation , 2015, eLife.
[35] S. Oliveira,et al. Nanobody-based cancer therapy of solid tumors. , 2015, Nanomedicine.
[36] Charlotte M. Deane,et al. ANARCI: antigen receptor numbering and receptor classification , 2015, Bioinform..
[37] Simon Mitternacht,et al. FreeSASA: An open source C library for solvent accessible surface area calculations , 2016, F1000Research.
[38] Daisuke Kuroda,et al. Shape complementarity and hydrogen bond preferences in protein-protein interfaces: implications for antibody modeling and protein-protein docking , 2016, Bioinform..
[39] Lucy J. Colwell,et al. Comparative analysis of nanobody sequence and structure data , 2018, Proteins.