Kabat database and its applications: Future directions

An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity

Wu, T. T., & Kabat, E. A. (1970) · The Journal of Experimental Medicine · doi:10.1084/jem.132.2.211 · Cited by 1,340 · see citing works

Somatic hyperconversion diversifies the single VH gene of the chicken with a high incidence in the D region

Reynaud, C., Dahan, A., Anquez, V., & Weill, J. (1989) · Cell · doi:10.1016/0092-8674(89)90879-9 · Cited by 472 · see citing works

EVOLUTION OF ANTIGEN BINDING RECEPTORS

Litman, G. W., Anderson, M. K., & Rast, J. P. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.109 · Cited by 326 · see citing works

Kabat Database and its applications: 30 years after the first variability plot

Johnson, G. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.214 · Cited by 148 · see citing works

Antibodies of sharks: revolution and evolution

Marchalonis, J. J., Schluter, S. F., Bernstein, R. M., & Hohman, V. S. (1998) · Immunological Reviews · doi:10.1111/j.1600-065x.1998.tb01256.x · Cited by 88 · see citing works

A Method of Estimating the Numbers of Human and Mouse Immunoglobulin V-Genes

Johnson, G., & Wu, T. T. (1997) · Genetics · doi:10.1093/genetics/145.3.777 · Cited by 7 · see citing works

Profile of Numbers of Sequence Differences Among V-Genes Coding for the Variable Regions of T Cell Receptor for Antigen Alpha and Beta Chains

Johnson, G., & Wu, T. T. (1997) · Journal of Molecular Evolution · doi:10.1007/pl00006142 · Cited by 5 · see citing works

A method of estimating the numbers of human and mouse T cell receptors for antigen α and β chain V‐genes

Johnson, G., & Wu, T. T. (1997) · Immunology and Cell Biology · doi:10.1038/icb.1997.90 · Cited by 5 · see citing works

Possible Assortment of a1 and a2 Region Gene Segments in Human MHC Class I Molecules

Johnson, G., & Wu, T. T. (1998) · Genetics · doi:10.1093/genetics/149.2.1063 · Cited by 2 · see citing works

SAbDab: the structural antibody database

Dunbar, J., Krawczyk, K., Leem, J., Baker, T., Fuchs, A., Georges, G., Shi, J., & Deane, C. M. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt1043 · Cited by 674 · see citing works

A specific antidote for dabigatran: functional and structural characterization

Schiele, F., van Ryn, J., Canada, K. A., Newsome, C., Sepulveda, E., Park, J., Nar, H., & Litzenburger, T. (2013) · Blood · doi:10.1182/blood-2012-11-468207 · Cited by 561 · see citing works

Expressed Murine and Human CDR-H3 Intervals of Equal Length Exhibit Distinct Repertoires that Differ in their Amino Acid Composition and Predicted Range of Structures

Zemlin, M., Klinger, M., Link, J. M., Zemlin, C., Bauer, K., Engler, J. A., Schroeder, H. W., & Kirkham, P. M. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.007 · Cited by 327 · see citing works

Analysis and improvements to Kabat and structurally correct numbering of antibody variable domains

Abhinandan, K. R., & Martin, A. C. R. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.05.022 · Cited by 234 · see citing works

Nimotuzumab, an antitumor antibody that targets the epidermal growth factor receptor, blocks ligand binding while permitting the active receptor conformation.

Talavera, A., Friemann, R., Gómez-Puerta, S., Martínez-Fleites, C., Garrido, G., Rabasa, A., López-Requena, A., Pupo, A., Johansen, R. F., Sánchez, O., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4518 · Cited by 196 · see citing works

abYsis: integrated antibody sequence and structure-management, analysis, and prediction

Swindells, M. B., Porter, C. T., Couch, M., Hurst, J., Abhinandan, K. R., Nielsen, J. H., Macindoe, G., Hetherington, J., & Martin, A. C. R. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.019 · Cited by 184 · see citing works

VBASE2, an integrative V gene database

Retter, I. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki088 · Cited by 181 · see citing works

Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones

Levy, R., Weiss, R., Chen, G., Iverson, B. L., & Georgiou, G. (2001) · Protein Expression and Purification · doi:10.1006/prep.2001.1520 · Cited by 207 · see citing works

Generalized crystal-storing histiocytosis associated with monoclonal gammopathy: molecular analysis of a disorder with rapid clinical course and review of the literature

Lebeau, A., Zeindl‐Eberhart, E., Müller, E., Müller‐Höcker, J., Jungblut, P. R., Emmerich, B., & Löhrs, U. (2002) · Blood · doi:10.1182/blood.v100.5.1817.h81702001817_1817_1827 · Cited by 172 · see citing works

The major histocompatibility class I locus in Atlantic salmon ( Salmo salar L.): polymorphism, linkage analysis and protein modelling

Grimholt, U., Drabløs, F., Jørgensen, S., Høyheim, B., & Stet, R. J. M. (2002) · Immunogenetics · doi:10.1007/s00251-002-0499-8 · Cited by 155 · see citing works

Production of Functional Single-Chain Fv Antibodies in the Cytoplasm of Escherichia coli

Jurado, P., Ritz, D., Beckwith, J., de Lorenzo, V., & Fernández, L. Á. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00405-9 · Cited by 143 · see citing works

Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments

Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works

Generating conformation-specific synthetic antibodies to trap proteins in selected functional states

Paduch, M., Koide, A., Uysal, S., Rizk, S. S., Koide, S., & Kossiakoff, A. A. (2012) · Methods · doi:10.1016/j.ymeth.2012.12.010 · Cited by 102 · see citing works

Analyzing the ‘Degree of Humanness’ of antibody sequences

Abhinandan, K. R., & Martin, A. C. R. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.100 · Cited by 99 · see citing works

Antibody Epitopes on the Neuraminidase of a Recent H3N2 Influenza Virus (A/Memphis/31/98)

Gulati, U., Hwang, C., Venkatramani, L., Gulati, S., Stray, S. J., Lee, J. T., Laver, W. G., Bochkarev, A. V., Zlotnick, A., & Air, G. M. (2002) · Journal of Virology · doi:10.1128/jvi.76.23.12274-12280.2002 · Cited by 99 · see citing works

AbDb: antibody structure database-a database of PDB-derived antibody structures

Ferdous, S., & Martin, A. C. R. (2018) · Database · doi:10.1093/database/bay040 · Cited by 87 · see citing works

Clonal relation in a case of CLL, ALCL, and Hodgkin composite lymphoma

van den Berg, A., Maggio, E. M., Rust, R., Kooistra, K., Diepstra, A., & Poppema, S. (2002) · Blood · doi:10.1182/blood.v100.4.1425.h81602001425_1425_1429 · Cited by 91 · see citing works

Trends in Antibody Sequence Changes during the Somatic Hypermutation Process

Clark, L. A., Ganesan, S., Papp, S., & van Vlijmen, H. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.1.333 · Cited by 85 · see citing works

A generic approach to engineer antibody pH-switches using combinatorial histidine scanning libraries and yeast display

Schröter, C. J., Günther, R., Rhiel, L., Becker, S., Toleikis, L., Doerner, A., Becker, J., Schönemann, A., Nasu, D., Neuteboom, B., et al. (2014) · mAbs · doi:10.4161/19420862.2014.985993 · Cited by 80 · see citing works

Knowledge-based Design of Reagentless Fluorescent Biosensors from Recombinant Antibodies

Renard, M., Belkadi, L., Hugo, N., England, P., Altschuh, D., & Bedouelle, H. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00023-2 · Cited by 71 · see citing works

Germline VH/VL pairing in antibodies

Jayaram, N., Bhowmick, P., & Martin, A. C. R. (2012) · Protein Engineering Design and Selection · doi:10.1093/protein/gzs043 · Cited by 64 · see citing works

Computational immunology: The coming of age

Petrovsky, N., & Brusić, V. (2002) · Immunology and Cell Biology · doi:10.1046/j.1440-1711.2002.01093.x · Cited by 59 · see citing works

Phage Display on the Base of Filamentous Bacteriophages: Application for Recombinant Antibodies Selection

Викторовна, Т. Н., & Витальевна, М. В. (2009) · Acta Naturae · doi:10.32607/20758251-2009-1-3-20-28 · Cited by 57 · see citing works

Plasmodium-specific atypical memory B cells are short-lived activated B cells

Pérez‐Mazliah, D., Gardner, P. J., Schweighoffer, E., McLaughlin, S., Hosking, C., Tumwine, I., Davis, R. S., Potocnik, A. J., Tybulewicz, V. L. J., & Langhorne, J. (2018) · eLife · doi:10.7554/elife.39800 · Cited by 51 · see citing works

Length-independent structural similarities enrich the antibody CDR canonical class model

Nowak, J., BAKER, T. S., Georges, G. J., Kelm, S., Klostermann, S., Shi, J., Sridharan, S., & Deane, C. M. (2016) · mAbs · doi:10.1080/19420862.2016.1158370 · Cited by 54 · see citing works

Crystal structure of a cocaine-binding antibody

Larsen, N., Zhou, B., Heine, A., Wirsching, P., Janda, K. D., & Wilson, I. A. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4839 · Cited by 47 · see citing works

The outcome of Cryptococcus neoformansintracellular pathogenesis in human monocytes

Alvarez, M., Burn, T., Luo, Y., Pirofski, L., & Casadevall, A. (2009) · BMC Microbiology · doi:10.1186/1471-2180-9-51 · Cited by 46 · see citing works

Rigidity Emerges during Antibody Evolution in Three Distinct Antibody Systems: Evidence from QSFR Analysis of Fab Fragments

Li, T., Tracka, M. B., Uddin, S., Casas‐Finet, J. R., Jacobs, D. J., & Livesay, D. R. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004327 · Cited by 46 · see citing works

Sequence Plasticity in the Antigen-binding Site of a Therapeutic Anti-HER2 Antibody

Gerstner, R. B., Carter, P. M., & Lowman, H. B. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00677-0 · Cited by 46 · see citing works

Review: Prediction of in Vivo Fates of Proteins in the Era of Genomics and Proteomics

Nakai, K. (2001) · Journal of Structural Biology · doi:10.1006/jsbi.2001.4378 · Cited by 46 · see citing works

In Situ Diversification of the Antibody Repertoire in Chronic Lyme Arthritis Synovium

Ghosh, S., Steere, A. C., Stollar, B. D., & Huber, B. T. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.5.2860 · Cited by 43 · see citing works

Antibody Humanization by CDR Grafting

Lo, B. K. C. (2004) · Humana Press eBooks · doi:10.1385/1-59259-666-5:135 · Cited by 41 · see citing works

Structure and Molecular Interactions of a Unique Antitumor Antibody Specific for N-Glycolyl GM3

Krengel, U., Olsson, L., Martínez, C., Talavera, A., Rojas, G., Mier, E. S., Ångström, J., & Moreno, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311693200 · Cited by 41 · see citing works

A database of immunoglobulins with integrated tools: DIGIT

Chailyan, A., Tramontano, A. L., & Marcatili, P. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr806 · Cited by 39 · see citing works

The Humanness of Macaque Antibody Sequences

Thullier, P., Huish, O., Pelat, T., & Martin, A. C. R. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.12.041 · Cited by 38 · see citing works

Design and Activity of a Murine and Humanized Anti-CEACAM6 Single-Chain Variable Fragment in the Treatment of Pancreatic Cancer

Riley, C., Engelhardt, K. P., Saldanha, J. W., Qi, W., Cooke, L. S., Zhu, Y., Narayan, S., Shakalya, K., Croce, K. D., Georgiev, I. G., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2707 · Cited by 38 · see citing works

Diversity in Hapten Recognition: Structural Study of an Anti-cocaine Antibody M82G2

Pozharski, E. V., Moulin, A. G., Hewagama, A., Shanafelt, A. B., Petsko, G. A., & Ringe, D. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.03.080 · Cited by 37 · see citing works

Redistribution of Flexibility in Stabilizing Antibody Fragment Mutants Follows Le Châtelier’s Principle

Li, T., Tracka, M. B., Uddin, S., Casas‐Finet, J. R., Jacobs, D. J., & Livesay, D. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092870 · Cited by 36 · see citing works

Novel anti-CD30 recombinant immunotoxins containing disulfide-stabilized Fv fragments.

Nagata, S., Onda, M., Numata, Y., Santora, K., Beers, R., Kreitman, R. J., & Pastan, I. H. (2002) · PubMed · Cited by 36 · see citing works

Investigating the Properties of Bacillus thuringiensis Cry Proteins with Novel Loop Replacements Created Using Combinatorial Molecular Biology

Pigott, C. R., King, M. S., & Ellar, D. J. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.02844-07 · Cited by 35 · see citing works

Cofactor-containing antibodies: Crystal structure of the original yellow antibody

Zhu, X., Wentworth, P., Kyle, R. A., Lerner, R. A., & Wilson, I. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600251103 · Cited by 33 · see citing works

Highly Sensitive Immunoprecipitation Method for Extracting and Concentrating Low-Abundance Proteins from Human Serum

Michielsen, E. C. H. J., Diris, J. H. C., Hackeng, C. M., Wodzig, W. K. W. H., & van Dieijen‐Visser, M. P. (2004) · Clinical Chemistry · doi:10.1373/clinchem.2004.036251 · Cited by 32 · see citing works

A structural in silico analysis of the immunogenicity of l-asparaginase from Escherichia coli and Erwinia carotovora

Belén, L. H., Lissabet, J. F. B., Rangel‐Yagui, C. D. O., Effer, B. R., Monteiro, G., Pessoa, A., & Farías, J. G. (2019) · Biologicals · doi:10.1016/j.biologicals.2019.03.003 · Cited by 31 · see citing works

Anchoring a Cationic Ligand: The Structure of the Fab Fragment of the Anti-morphine Antibody 9B1 and its Complex with Morphine

Pozharski, E. V., Wilson, M. A., Hewagama, A., Shanafelt, A. B., Petsko, G. A., & Ringe, D. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.12.084 · Cited by 31 · see citing works

Immunogenicity of autologous IgG bearing the inflammation-associated marker 3-nitrotyrosine

Ohmori, H., Oka, M., Nishikawa, Y., Shigemitsu, H., Takeuchi, M., Magari, M., & Kanayama, N. (2004) · Immunology Letters · doi:10.1016/j.imlet.2004.07.004 · Cited by 31 · see citing works

V-gene amplification revisited – An optimised procedure for amplification of rearranged human antibody genes of different isotypes

Lim, T. S., Mollova, S., Rubelt, F., Sievert, V., Dübel, S., Lehrach, H. R., & Konthur, Z. (2010) · New Biotechnology · doi:10.1016/j.nbt.2010.01.001 · Cited by 30 · see citing works

Noncovalent scFv multimers of tumor‐targeting anti‐Lewisy hu3S193 humanized antibody

Power, B. E., Doughty, L., Shapira, D. R., Burns, J. E., Bayly, A. M., Caine, J. M., Liu, Z., Scott, A. M., Hudson, P. J., & Kortt, A. A. (2003) · Protein Science · doi:10.1110/ps.0228503 · Cited by 27 · see citing works

Mesenteric lymph nodes are critical for the induction of high-dose oral tolerance in the absence of Peyer's patches

Spahn, T. W., Weiner, H. L., Rennert, P. D., Lügering, N., Fontana, A., Domschke, W., & Kucharzik, T. F. (2002) · European Journal of Immunology · doi:10.1002/1521-4141(200204)32:4 · Cited by 194 · see citing works

Central Nervous System Delivery of Antibodies and Their Single-Domain Antibodies and Variable Fragment Derivatives with Focus on Intranasal Nose to Brain Administration

Soleimanizadeh, A., Dinter, H., & Schindowski, K. (2021) · Antibodies · doi:10.3390/antib10040047 · Cited by 25 · see citing works

Generation of Antibody Diversity

Backhaus, O. (2018) · InTech eBooks · doi:10.5772/intechopen.72818 · Cited by 25 · see citing works

Crystal structures of a therapeutic single chain antibody in complex with two drugs of abuse—Methamphetamine and 3,4‐methylenedioxymethamphetamine

Celikel, R., Peterson, E. C., Owens, S. M., & Varughese, K. I. (2009) · Protein Science · doi:10.1002/pro.244 · Cited by 23 · see citing works

B Cell Selection and Affinity Maturation During an Antibody Response in the Mouse with Limited B Cell Diversity

Kanayama, N., Kimoto, T., Todo, K., Nishikawa, Y., Hikida, M., Magari, M., Cascalho, M., & Ohmori, H. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.12.6865 · Cited by 22 · see citing works

Analysis of Single Chain Antibody Sequences Using the VBASE2 Fab Analysis Tool

Mollova, S., Retter, I., Hust, M., Dübel, S., & Müller, W. (2010) · Springer eBooks · doi:10.1007/978-3-642-01147-4_1 · Cited by 21 · see citing works

Consensus design of a NOD receptor leucine rich repeat domain with binding affinity for a muramyl dipeptide, a bacterial cell wall fragment

Parker, R. N., Mercedes-Camacho, A. Y., & Grove, T. Ž. (2014) · Protein Science · doi:10.1002/pro.2461 · Cited by 21 · see citing works

Expression and characterization of a humanized cocaine‐binding antibody

Redwan, E. M. M. M., Larsen, N., Zhou, B., Wirsching, P., Janda, K. D., & Wilson, I. A. (2003) · Biotechnology and Bioengineering · doi:10.1002/bit.10598 · Cited by 21 · see citing works

Dual isotype expressing B cells [κ(+)/λ(+)] arise during the ontogeny of B cells in the bone marrow of normal nontransgenic mice

Rezanka, L. J., Kenny, J. J., & Longo, D. L. (2005) · Cellular Immunology · doi:10.1016/j.cellimm.2005.12.004 · Cited by 21 · see citing works

Structural Basis for Antibody Catalysis of a Cationic Cyclization Reaction

Zhu, X., Heine, A., Monnat, F., Houk, K. N., Janda, K. D., & Wilson, I. A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00406-6 · Cited by 21 · see citing works

Unraveling the mysteries of γδ T cell recognition

Wilson, I. A., & Stanfield, R. L. (2001) · Nature Immunology · doi:10.1038/89718 · Cited by 21 · see citing works

An Anti-urokinase Plasminogen Activator Receptor (uPAR) Antibody: Crystal Structure and Binding Epitope

Li, Y., Parry, G. C., Chen, L., Callahan, J. A., Shaw, D. E., Meehan, E. J., Mazar, A. P., & Huang, M. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.059 · Cited by 20 · see citing works

Generating Conformation and Complex-Specific Synthetic Antibodies

Paduch, M., & Kossiakoff, A. A. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6857-2_6 · Cited by 20 · see citing works

Targeting hemoglobin receptors IsdH and IsdB of Staphylococcus aureus with a single VHH antibody inhibits bacterial growth

Valenciano-Bellido, S., Caaveiro, J. M. M., Nakakido, M., Kuroda, D., Aikawa, C., Nakagawa, I., & Tsumoto, K. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104927 · Cited by 18 · see citing works

Elongation of the C-terminal domain of an anti-amyloid β single-chain variable fragment increases its thermodynamic stability and decreases its aggregation tendency

Rivera-Hernández, G., Marin‐Argany, M., Blasco-Moreno, B., Bonet, J., Oliva, B., & Villegas, S. (2013) · mAbs · doi:10.4161/mabs.25382 · Cited by 17 · see citing works

Four different clones of mouse anti-acetyllysine monoclonal antibodies having different recognition properties share a common immunoglobulin framework structure

Komatsu, Y., Yukutake, Y., & Yoshida, M. (2003) · Journal of Immunological Methods · doi:10.1016/s0022-1759(02)00500-8 · Cited by 14 · see citing works

Generation of “LYmph Node Derived Antibody Libraries” (LYNDAL) for selecting fully human antibody fragments with therapeutic potential

Diebolder, P., Keller, A., Haase, S., Schlegelmilch, A., Kiefer, J. D., Karimi, T., Weber, T., Moldenhauer, G., Kehm, R., Eis‐Hübinger, A. M., et al. (2013) · mAbs · doi:10.4161/mabs.27236 · Cited by 13 · see citing works

Characterization of 11-dehydro-thromboxane B2 recombinant antibody obtained by phage display technology

Tsuruta, L. R., Tomioka, Y., Hishinuma, T., Katō, Y., Itoh, K., Suzuki, T., Oguri, H., Hirama, M., Goto, J., & Mizugaki, M. (2003) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/s0952-3278(03)00006-1 · Cited by 13 · see citing works

Immunogenicity assessment of fungal l-asparaginases: an in silico approach

Belén, L. H., Lissabet, J. F. B., Rangel‐Yagui, C. D. O., Monteiro, G., Pessoa, A., & Farías, J. G. (2020) · SN Applied Sciences · doi:10.1007/s42452-020-2021-z · Cited by 12 · see citing works

CDR Repair: A Novel Approach to Antibody Humanization

Dennis, M. S. (2009) · Springer eBooks · doi:10.1007/978-0-387-76643-0_2 · Cited by 10 · see citing works

Functional humanization of an anti-CD16 Fab fragment: obstacles of switching from murine to human or light chains

Schlapschy, M., Fogarasi, M., Gruber, H., Gresch, O., Schafer, C., Aguib, Y., & Skerra, A. (2008) · Protein Engineering Design and Selection · doi:10.1093/protein/gzn066 · Cited by 10 · see citing works

Construction and characterization of a Fab recombinant protein for Japanese encephalitis virus neutralization

WU, S., Lin, Y., CHOU, J., & Lin, C. (2004) · Vaccine · doi:10.1016/j.vaccine.2004.05.016 · Cited by 10 · see citing works

Monoclonal Antibody 667 Recognizes the Variable Region A Motif of the Ecotropic Retrovirus CasBrE Envelope Glycoprotein and Inhibits Env Binding to the Viral Receptor

Dreja, H. S., Gros, L., Villard, S., Bachrach, E., Oates, A., Granier, C., Chardès, T., Mani, J. C., Piechaczyk, M., & Pelegrín, M. (2003) · Journal of Virology · doi:10.1128/jvi.77.20.10984-10993.2003 · Cited by 9 · see citing works

The Kabat Database and a Bioinformatics Example

Johnson, G., & Wu, T. T. (2004) · Humana Press eBooks · doi:10.1385/1-59259-666-5:11 · Cited by 9 · see citing works

Construction of a humanized antibody to hepatitis B surface antigen by specificity-determining residues (SDR)-grafting and de-immunization

Kim, K., Kim, H., Han, B. W., Myung, P.-K., & Hong, H. J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.04.071 · Cited by 8 · see citing works

Structural basis for a disfavored elimination reaction in catalytic antibody 1D4

Larsen, N., Heine, A., Crane, L. E., Cravatt, B. F., Lerner, R. A., & Wilson, I. A. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5112 · Cited by 8 · see citing works

Immunoglobulin κ Genes of Human and Mouse

Zachau, H. G. (2004) · Elsevier eBooks · doi:10.1016/b978-012053641-2/50004-6 · Cited by 8 · see citing works

Structural biology of moonlighting: lessons from antibodies

Martin, A. C. R. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140211 · Cited by 7 · see citing works

Structural Characterization of a Therapeutic Anti-Methamphetamine Antibody Fragment: Oligomerization and Binding of Active Metabolites

Peterson, E. C., Celikel, R., Gokulan, K., & Varughese, K. I. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082690 · Cited by 7 · see citing works

Web-Based Tools for Vaccine Design

Lund, O., Nielsen, M., Keşmir, C., Christensen, J. K., Lundegaard, C., Worning, P., & Brunak, S. (2005) · The MIT Press eBooks · doi:10.7551/mitpress/3679.003.0013 · Cited by 7 · see citing works

The Bcl6 locus is not mutated in mouse B-cell lineage lymphomas

Hori, M., Qi, C., Torrey, T. A., Huppi, K. E., & Morse, H. C. (2002) · Leukemia Research · doi:10.1016/s0145-2126(01)00200-4 · Cited by 6 · see citing works

Generation, characterization, and docking studies of DNA‐hydrolyzing recombinant Fab antibodies

Zein, H. S., El‐Sehemy, A., Fares, M., ElHefnawi, M., da Silva, J. A. T., & Miyatake, K. (2011) · Journal of Molecular Recognition · doi:10.1002/jmr.1129 · Cited by 3 · see citing works

Clonal diversification in OspA-specific antibodies from peripheral circulation of a chronic Lyme arthritis patient

Ghosh, S., & Huber, B. T. (2007) · Journal of Immunological Methods · doi:10.1016/j.jim.2007.01.007 · Cited by 3 · see citing works

Apparent structural differences at the tetramerization region of erythroid and nonerythroid beta spectrin as discriminated by phage displayed scFvs

Song, Y., Antoniou, C., Memić, A., Kay, B. K., & Fung, L. W. ‐. (2011) · Protein Science · doi:10.1002/pro.617 · Cited by 3 · see citing works

Sensitization to food or inhalant allergens in pediatric patients. Clinical usefulness of first-level panel tests for specific IgE.

Altrinetti, V., Salmaso, C., Montagna, P., Castellano, E., Cosentino, C., Pesce, G., & Bagnasco, M. (2003) · PubMed · Cited by 3 · see citing works

Cloning and sequence analysis of cDNAs encoding the heavy and light chain variable regions of an Ab2β anti-idiotypic monoclonal antibody possessing an internal image of cocaine

Ho, M., & Segre, M. (2001) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(01)00253-6 · Cited by 1 · see citing works

Production and characterization of a recombinant single-chain antibody (scFv) for tracing the σ54 factor of Pseudomonas putida

Jurado, P., Fernández, L. Á., & de Lorenzo, V. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2011.12.011 · Cited by 1 · see citing works

Correction: Structural Characterization of a Therapeutic Anti-Methamphetamine Antibody Fragment: Oligomerization and Binding of Active Metabolites

Peterson, E. C., Celikel, R., Gokulan, K., & Varughese, K. I. (2014) · PLoS ONE · doi:10.1371/annotation/f92e9067-daee-45af-b5da-5779273225ed · Cited by 1 · see citing works

Shared ligand-blocking mechanism but distinct conformational modulation by α5-targeting antibodies BIIG2 and MINT1526APreprint

Nguyen, A., Heim, J. B., Cordara, G., Chan, M. C., Johannesen, H., Charlesworth, C. M., Li, M., Azumaya, C. M., Madden, B. J., Krengel, U., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.08.631572 · Cited by 1 · see citing works

Sequence and structural analysis of antibodies

Raghavan, A. (2009) · OpenGrey (Institut de l'Information Scientifique et Technique) · Cited by 1 · see citing works

Pathological and therapeutic antibodies: new tools for autoimmunity diagnosis and anticancer therapy

Tedesco, A. (2008) · Università degli Studi di Napoli Federico II · doi:10.6092/unina/fedoa/1959

Structural Basis for a Disfavored Elimination Reaction in Catalytic Antibody 1D4

sHeine, A. (2001)

An Index for Deviation Distance Among Amino Acid Sequences of Antibody Complementarity Determining RegionsPreprint

Hoshino, T., Yalikun, Y., & Qiao, X. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5118517

An index for deviation distance among amino acid sequences of antibody complementarity determining regions

Yalikun, Y., Qiao, X., & Hoshino, T. (2025) · Journal of Immunological Methods · doi:10.1016/j.jim.2025.114005

Shared ligand-blocking mechanism but distinct conformational modulation by α5-targeting antibodies BIIG2 and MINT1526A

Nguyen, A., Heim, J. B., Cordara, G., Chan, M. C., Johannesen, H., Charlesworth, C., Li, M., Azumaya, C. M., Madden, B. J., Krengel, U., et al. (2026) · Structure · doi:10.1016/j.str.2026.08.001 · Cited by 1 · see citing works

Implications of cardiac troponin T degradation

Michielsen, E. C. H. J. (2008) · doi:10.26481/dis.20080229em

Kabat Database and its applications: 30 years after the first variability plot

Johnson, G. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.214 · Cited by 148 · see citing works

The Kabat Database and a Bioinformatics Example

Johnson, G., & Wu, T. T. (2004) · Humana Press eBooks · doi:10.1385/1-59259-666-5:11 · Cited by 9 · see citing works

The three-dimensional structure ofEscherichia coliporphobilinogen deaminase at 1.76-Å resolution

Louie, G. V., Brownlie, P. D., Lambert, R., Cooper, J. B., Blundell, T. L., Wood, S., Malashkevich, V. N., Hädener, A., Warren, M. J., & Shoolingin‐Jordan, P. M. (1996) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(199605)25:1 · Cited by 43 · see citing works

Analysis and improvements to Kabat and structurally correct numbering of antibody variable domains

Abhinandan, K. R., & Martin, A. C. R. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.05.022 · Cited by 234 · see citing works

VIR.II: a new interface with the antibody sequences in the Kabat database

Ramirez-Benitez, M. D. C., Moreno‐Hagelsieb, G., & Almagro, J. C. (2001) · Biosystems · doi:10.1016/s0303-2647(01)00166-6 · Cited by 6 · see citing works