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AN ANALYSIS OF THE SEQUENCES OF THE VARIABLE REGIONS OF BENCE JONES PROTEINS AND MYELOMA LIGHT CHAINS AND THEIR IMPLICATIONS FOR ANTIBODY COMPLEMENTARITY
Open accessAbstract
In an attempt to account for antibody specificity and complementarity in terms of structure, human kappa-, human lambda-, and mouse kappa-Bence Jones proteins and light chains are considered as a single population and the variable and constant regions are compared using the sequence data available. Statistical criteria are used in evaluating each position in the sequence as to whether it is essentially invariant or group-specific, subgroup-specific, species-specific, etc. Examination of the invariant residues of the variable and constant regions confirms the existence of a large number of invariant glycines, no invariant valine, lysine, and histidine, and only one invariant leucine and alanine in the variable region, as compared with the absence of invariant glycines and presence of three each of invariant alanine, leucine, and valine and two each of invariant lysine and histidine in the constant region. The unique role of glycine in the variable region is emphasized. Hydrophobicity of the invariant residues of the two regions is also evaluated. A parameter termed variability is defined and plotted against the position for the 107 residues of the variable region. Three stretches of unusually high variability are noted at residues 24-34, 50-56, and 89-97; variations in length have been found in the first and third of these. It is hypothesized that positions 24-34 and 89-97 contain the complementarity-determining residues of the light chain-those which make contact with the antigenic determinant. The heavy chain also has been reported to have a similar region of very high variability which would also participate in forming the antibody-combining site. It is postulated that the information for site complementarity is contained in some extrachromosomal DNA such as an episome and is incorporated by insertion into the DNA of the structural genes for the variable region of short linear sequences of nucleotides. The advantages and disadvantages of this hypothesis are discussed.
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“Kabat and IMGT definitions are based on sequence alignments identifying conserved positions in the variable region [152, 153] whereas Chothia takes into account the 3D structure of the CDR loops.”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [152]
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“Since the seminal work to define a standard numbering scheme for antibodies was carried out by Kabat in 1970 [152], the Chothia [32] and IMGT [153] schemes have been adopted as the main alternatives.”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [152]
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Cites
Construction of Phylogenetic Trees
Fitch, W. M., & Margoliash, E. (1967) · Science · doi:10.1126/science.155.3760.279 · Cited by 3,611
Conformation of Polypeptides and Proteins
Ramachandran, G. N., & Sasisekharan, V. (1968) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60402-7 · Cited by 2,950
Transduction of linked genetic characters of the host by bacteriophage P1
Lennox, E. S. (1955) · Virology · doi:10.1016/0042-6822(55)90016-7 · Cited by 2,604
On the average hydrophobicity of proteins and the relation between it and protein structure
Bigelow, C. C. (1967) · Journal of Theoretical Biology · doi:10.1016/0022-5193(67)90004-5 · Cited by 793
CELL TO CELL INTERACTION IN THE IMMUNE RESPONSE
Mitchell, G. F., & MILLER, J. F. A. P. (1968) · The Journal of Experimental Medicine · doi:10.1084/jem.128.4.821 · Cited by 680
Lederberg, J. (1959) · Science · doi:10.1126/science.129.3364.1649 · Cited by 676
CELL TO CELL INTERACTION IN THE IMMUNE RESPONSE
MILLER, J. F. A. P., & Mitchell, G. F. (1968) · The Journal of Experimental Medicine · doi:10.1084/jem.128.4.801 · Cited by 645
THE HEN EGG-WHITE LYSOZYME MOLECULE
Phillips, D. C. (1967) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.57.3.483 · Cited by 514
Individual Antigenic Specificity of Isolated Antibodies
Kunkel, H. G., Mannik, M., & Williams, R. C. (1963) · Science · doi:10.1126/science.140.3572.1218 · Cited by 489
On the conformation of the hen egg-white lysozyme molecule
Blake, C. C. F., Mair, G. A., North, A. C. T., Phillips, D. C., & Sarma, V. R. (1967) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1967.0034 · Cited by 430
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Items 901–1,000 of 1,001
Structural Studies in Solution on the Combining Site of the Myeloma Protein MOPC 315
Dwek, R. A. (1977) · Springer eBooks · doi:10.1007/978-1-4684-2841-4_1 · Cited by 8
Mapping of the full profile of T cell allorecognition regions on HLA‐DR2β subunit
Ulrich, R. G., & Atassi, M. Z. (1990) · European Journal of Immunology · doi:10.1002/eji.1830200402 · Cited by 8
Wang, A.-C., Fudenberg, H. H., & Bazin, H. (1976) · Biochemical Genetics · doi:10.1007/bf00484761 · Cited by 8
Amino acid sequence of the first hypervariable region of 2κ and Aλ Bence Jones cryoglobulin
Meinke, G. C., & Spiegelberg, H. L. (1976) · Immunochemistry · doi:10.1016/0019-2791(76)90235-4 · Cited by 8
Immunoglobulin Structure, Synthesis, Secretion, and Relation to Neoplasms of B Cells
Franklin, E. C., & Buxbaum, J. N. (1977) · Clinics in Haematology · doi:10.1016/s0308-2261(21)00274-5 · Cited by 8
Blake-Hedges, J. M., Groff, D., Foo, W. L., Hanson, J., Castillo, E., Wen, M., Cheung, D., Masikat, M. R., Lu, J. G., Park, Y. J., et al. (2024) · mAbs · doi:10.1080/19420862.2024.2316872 · Cited by 7
Zhu, Z., Olson, K. S., & Magliery, T. J. (2024) · Antibodies · doi:10.3390/antib13040099 · Cited by 7
Tsai, C.-Y., & Chiu, C.-C. (2007) · Pattern Recognition Letters · doi:10.1016/j.patrec.2007.11.013 · Cited by 7
Evolution of MHC IIB Diversity Across Cichlid Fish Radiations
Lozano-Martín, C., Bracamonte, S. E., & Barluenga, M. (2023) · Genome Biology and Evolution · doi:10.1093/gbe/evad110 · Cited by 7
A Novel Dual-Fc Bispecific Antibody with Enhanced Fc Effector Function
Zhou, F., Ben, Y., Jiang, H., Tan, S., Mu, G., Zha, Z., Dong, S., Huang, S., Zhou, Y., Jin, Y., et al. (2024) · Biochemistry · doi:10.1021/acs.biochem.3c00481 · Cited by 7
A single-domain antibody library based on a stability-engineered human VH3 scaffold
Lee, N. J., Jung, M., Yang, H. Y., & Shim, H. (2024) · Scientific Reports · doi:10.1038/s41598-024-68680-5 · Cited by 10
Monoclonal antibodies – A repertoire of therapeutics
Tapryal, S. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.11.001 · Cited by 6
Zimering, M. B., MORITZ, T. E., & DONNELLY, R. J. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00058 · Cited by 7
Tian, C., Ding, Y., Ao, J., & Chen, X. (2011) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2011.03.024 · Cited by 7
Robustness of the residue conservation score reflecting both frequencies and physicochemistries
Liu, X.-S., & Guo, W. (2008) · Amino Acids · doi:10.1007/s00726-007-0017-2 · Cited by 7
Nonnative Intermediate State of Acid-Stable β-Sheet Protein
Yang, J. J., Carroll, A. R., Yang, W., Ye, Y., & Nguyen, C. N. (2000) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:33:3:253 · Cited by 7
From the structure of antibodies to the diversification of the immune response
Milstein, C. (1985) · Bioscience Reports · doi:10.1007/bf01116899 · Cited by 7
On the domain pairing in chimeric antibodies
Teplyakov, A., Obmolova, G., Carton, J. M., Gao, W., Zhao, Y., & Gilliland, G. L. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.05.002 · Cited by 7
Functional Versatility of AGY Serine Codons in Immunoglobulin Variable Region Genes
Detanico, T., Phillips, M., & Wysocki, L. J. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00525 · Cited by 7
Giles, I., Lambrianides, A., & Rahman, A. (2008) · Lupus · doi:10.1177/0961203308091541 · Cited by 7
Gene rearrangement can extinguish as well as activate and diversify immunoglobulin genes
Gough, N. M. (1981) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(81)90107-9 · Cited by 7
Antibody Diversification: the Somatic Mutation Model Revisited
Cohn, M. (1973) · Springer eBooks · doi:10.1007/978-94-010-2550-8_35 · Cited by 7
Self-Incompatibility in Flowering Plants
Thompson, R. D., Kaufmann, H., Kirch, H., & Salamini, F. (1991) · Current plant science and biotechnology in agriculture · doi:10.1007/978-94-011-3296-1_19 · Cited by 7
Chapter 3 Genes encoding the immunoglobulin variable regions
Brodeur, P. H. (1987) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60155-6 · Cited by 7
Molecular Engineering I: Humanization
Saldanha, J. W. (2007) · Wiley eBooks · doi:10.1002/9783527619740.ch6 · Cited by 7
Antibody Engineering: Humanization, Affinity Maturation, and Selection Techniques
Almagro, J. C., & Strohl, W. R. (2009) · Wiley eBooks · doi:10.1002/9780470485408.ch13 · Cited by 8
Distributions of the use frequencies of amino acids in the hypervariable regions of immunoglobulins
Lara‐Ochoa, F., Vargas‐Madrazo, E., & Almagro, J. C. (1995) · Journal of Molecular Evolution · doi:10.1007/bf00174045 · Cited by 7
Aasted, B., & Kindt, T. J. (1976) · European Journal of Immunology · doi:10.1002/eji.1830061013 · Cited by 7
Conformational flexibility of an antibody combining site composed of two identical V regions
Gavish, M., Dwek, R. A., & Givol, D. (1978) · European Journal of Immunology · doi:10.1002/eji.1830080109 · Cited by 7
Riesen, W. F., & Jaton, J. C. (1976) · Biochemistry · doi:10.1021/bi00662a028 · Cited by 7
Amino acid sequence of the pFc′ fragment of guinea-pig IgG1
Melamed, M. D. (1976) · Immunochemistry · doi:10.1016/0019-2791(76)90226-3 · Cited by 7
Friedenson, B., Tung, A. S., & Nisonoff, A. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.9.3676 · Cited by 7
ANTIBODY DIVERSITY: AN ASSESSMENT
Hood, L., Barstad, P. A., Loh, E. Y., & Nottenburg, C. (1974) · Elsevier eBooks · doi:10.1016/b978-0-12-637150-5.50015-8 · Cited by 7
Loat, S., Kumari, N., Saini, S., Dige, M. S., Kumar, A., Dhilor, N., Dang, A. K., Lathwal, S. S., Sodhi, M., & Kataria, R. S. (2021) · Animal Biotechnology · doi:10.1080/10495398.2021.2010088 · Cited by 6
Rodarte, J. V., Baehr, C., Hicks, D. M., McGovern, M., Zhang, Y., Silva-Ortiz, P., Hannon, B., Duddu, S., Pancera, M., & Pravetoni, M. (2024) · ACS Omega · doi:10.1021/acsomega.4c06617 · Cited by 6
DeLaitsch, A. T., Keeffe, J. R., Gristick, H. B., Lee, J. A., Ding, W., Liu, W., Skelly, A. N., Shaw, G. M., Hahn, B. H., & Björkman, P. J. (2024) · npj Vaccines · doi:10.1038/s41541-024-01038-0 · Cited by 6
Gearhart, P. J., Mock, B. A., Casellas, R. C., & Cancro, M. P. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1701516 · Cited by 6
Almanza, G., Clark, A. E., Kouznetsova, V. L., Olmedillas, E., Castro, A., Tsigelny, I. F., Wu, Y., Gao, G. F., Leibel, S. L., Bray, W. A., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010686 · Cited by 5
Candon, S., & Margulies, D. H. (2004) · Springer eBooks · doi:10.1007/978-1-4419-8999-4_3 · Cited by 6
Zylstra, P., Franklin, A., Hassan, K. A., Powell, K. L., Steele, E. J., & Blanden, R. V. (2003) · Immunogenetics · doi:10.1007/s00251-003-0565-x · Cited by 6
Xi, D., Hao, T., He, Y., Leng, J., Sun, Y., Yang, Y., Mao, H., & Deng, W. (2014) · International Journal of Immunogenetics · doi:10.1111/iji.12109 · Cited by 6
From subgenome analysis to protein structure
Man, O., Atarot, T., Sadot, A., Olender, T., & Lancet, D. (2003) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(03)00071-x · Cited by 6
Calvanico, N. J., & Tomasi, T. B. (1979) · Springer eBooks · doi:10.1007/978-1-4613-2922-0_1 · Cited by 6
The physiology of anti-idiotypic interactions: From clonal to paratopic selection
Greally, J. M. (1991) · Clinical Immunology and Immunopathology · doi:10.1016/0090-1229(91)90107-l · Cited by 6
Song, S.-C., Czerwiński, M., Wójczyk, B. S., & Spitalnik, S. L. (2004) · Transfusion · doi:10.1111/j.1537-2995.2004.00625.x · Cited by 6
From the Structure of Antibodies to the Diversification of the Immune Response
Milstein, C. (2004) · Bioscience Reports · doi:10.1007/s10540-005-2735-6 · Cited by 6
Immunoglobulin evolution, 30 years on
Steiner, L. A. (1996) · Glycobiology · doi:10.1093/glycob/6.7.649 · Cited by 6
Genetic characterization of MHC class II DQB exon 2 variants in gayal (Bos frontalis)
Sun, Y., Xi, D., Li, G., Hao, T., Chen, Y., & Yang, Y. (2014) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2014.960787 · Cited by 6
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
Straub, R. H. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-803321-0.00004-5 · Cited by 6
Inhibition of phosphorylcholine binding to antibodies using synthetic peptides
Lai, E., Rabat, E. A., Meienhofer, J., Heimer, E. P., Olson, A. J., & Lerner, R. A. (1987) · Nature · doi:10.1038/325168a0 · Cited by 6
Localization of rabbit kappa light chain allotypic determinants
McCartney-Francis, N. L., PADLAN, E. A., Cohen, G. H., & Mage, R. G. (1986) · Molecular Immunology · doi:10.1016/0161-5890(86)90111-2 · Cited by 6
Appella, E. (1980) · Molecular Immunology · doi:10.1016/0161-5890(80)90140-6 · Cited by 6
The specification of the immune response: A general selective model
Danchin, A. (1979) · Molecular Immunology · doi:10.1016/0161-5890(79)90079-8 · Cited by 6
Gex‐Fabry, M., Marchetti, F., Kotoko, N., & DeLisi, C. (1989) · Molecular Immunology · doi:10.1016/0161-5890(89)90061-8 · Cited by 6
The molecular biology of the T cell antigen receptor
OWEN, M., & Collins, M. K. (1985) · Immunology Letters · doi:10.1016/0165-2478(85)90030-6 · Cited by 6
Wuilmart, C., & Urbain, J. (1991) · Molecular Immunology · doi:10.1016/0161-5890(91)90178-m · Cited by 6
The Identification of Somatic Mutations in Immunoglobulin Expression and Structure
Zack, D. J., & Scharff, M. D. (1984) · Springer eBooks · doi:10.1007/978-1-4684-4664-7_10 · Cited by 6
Lawton, A. R., Kearney, J. F., & Cooper, M. D. (1980) · Springer eBooks · doi:10.1007/978-1-4684-9933-9_9 · Cited by 6
Pashov, A. D., Puente, C. V. H., Ibrahim, S. M., Monzavi‐Karbassi, B., Makhoul, I., & Kieber‐Emmons, T. (2018) · Monoclonal Antibodies in Immunodiagnosis and Immunotherapy · doi:10.1089/mab.2018.0014 · Cited by 6
Dorraji, E., Borgen, E., Segura-Peña, D., Rawat, P., Smorodina, E., Dunn, C., Greiff, V., Sekulić, N., Russnes, H. G., & Kyte, J. A. (2022) · Cancers · doi:10.3390/cancers14194859 · Cited by 4
A Brief Chronicle of Antibody Research and Technological Advances
Araki, K., & Maeda, R. (2024) · Antibodies · doi:10.3390/antib13040090 · Cited by 9
Building immunoglobulin and T cell receptor gene databases for the future
Watson, C. T., Collins, A. M., Ohlin, M., Heather, J., Peres, A., Lees, W., & Yaari, G. (2025) · ImmunoInformatics · doi:10.1016/j.immuno.2025.100059 · Cited by 5
Antibodies: A History of Their Discovery and Properties
Rees, A. R. (2020) · Learning materials in biosciences · doi:10.1007/978-3-030-54630-4_2 · Cited by 5
Language model-accelerated deep symbolic optimization
da Silva, F. L., Gonçalves, A. R., Nguyen, S., Vashchenko, D., Glatt, R., Desautels, T., Landajuela, M., Faissol, D., & Petersen, B. K. (2023) · Neural Computing and Applications · doi:10.1007/s00521-023-08802-8 · Cited by 5
Evaluation of the Potential Impact of In Silico Humanization on VHH Dynamics
Martins, C., Diharce, J., Nadaradjane, A. A., & de Brevern, A. G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914586 · Cited by 5
Exploiting the Fc base of IgG antibodies to create functional nanoparticle conjugates
Qaraghuli, M. M. A., Kubiak-Ossowska, K., Ferro, V. A., & Mulheran, P. A. (2024) · Scientific Reports · doi:10.1038/s41598-024-65822-7 · Cited by 5
Shimmon, G. L., Kotecha, A., Ren, J., Asfor, A. S., Newman, J., Berryman, S., Cottam, E. M., Gold, S., Tuthill, T. J., King, D. P., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0201853 · Cited by 5
Homology Modeling of Antibody Variable Regions: Methods and Applications
Bansia, H., & Ramakumar, S. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-2974-1_16 · Cited by 5
Liu, C., HongMei, L., Ran, X., & Wang, J. (2020) · PeerJ · doi:10.7717/peerj.9889 · Cited by 5
Holmes, J. C., Scholl, E. H., Dickey, A. N., & Hess, P. R. (2021) · Immunogenetics · doi:10.1007/s00251-021-01221-w · Cited by 5
Crystallographic analysis of the NNA7 Fab and proposal for the mode of human blood-group recognition
Xie, K., Song, S., Spitalnik, S. L., & Wedekind, J. E. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905023851 · Cited by 5
LIU, & Wolf (1998) · Immunology · doi:10.1046/j.1365-2567.1998.00590.x · Cited by 5
Substitution patterns in alleles of immunoglobulin V genes in humans and mice
Romo‐González, T., & Vargas‐Madrazo, E. (2005) · Molecular Immunology · doi:10.1016/j.molimm.2005.03.018 · Cited by 5
Liu, X., Li, J., Guo, W., & Wang, W. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.157 · Cited by 5
A possible basis for major histocompatibility complex-restricted T-cell recognition
Davis, M. M., Chien, Y., Björkman, P. J., Elliott, J. F., Iwashima, M., Rock, E. P., & Patten, P. A. (1989) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1989.0030 · Cited by 5
Jarasch, A., & Skerra, A. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25193 · Cited by 5
Primary structure of the variable regions of two canine immunoglobulin heavy chains
Wasserman, R. L., & Capra, J. D. (1977) · Biochemistry · doi:10.1021/bi00633a019 · Cited by 5
A human kappa Bence Jones protein (subgroup I) showing new amino acid substitutions
Matthews, J. B., & Jefferis, R. (1977) · Immunochemistry · doi:10.1016/0019-2791(77)90349-4 · Cited by 5
Affinity-labeling of anti-lactose antibody
Gopalakrishnan, P., & Karush, F. (1975) · Immunochemistry · doi:10.1016/0019-2791(75)90063-4 · Cited by 5
Aspects of vertebrate immunoglobulin evolution. Constancy in light chain electrophoretic behavior
Merz, D. C., Finstad, C. L., Litman, G. W., & Good, R. A. (1975) · Immunochemistry · doi:10.1016/0019-2791(75)90074-9 · Cited by 5
Jackson, W. R. C., Leatherbarrow, R. J., Gavish, M., Givol, D., & Dwek, R. A. (1981) · Biochemistry · doi:10.1021/bi00511a041 · Cited by 5
Molecular Evolution and the Immunoglobulin Gene Superfamily
Hood, L., & Hunkapiller, T. (1991) · Springer eBooks · doi:10.1007/978-4-431-68302-5_9 · Cited by 5
[23] Use of anti-idiotypic antibodies to treat lymphoid tumors
Stevenson, G. T. (1989) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(89)78025-3 · Cited by 5
Abraham, G. N., Brown, P. M., Johnston, S. L., Nellis, L., Marks, S., & Welch, E. H. (1978) · PubMed · Cited by 5
Wang, D., & Kabat, E. A. (1998) · Elsevier eBooks · doi:10.1006/rwei.1999.0042 · Cited by 5
Grandguillaume, I., da Silva, F. L. B., & Etchebest, C. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c01599 · Cited by 4
Moreno‐Cugnon, L., Esparza-Baquer, A., Larruskain, A., García‐Etxebarria, K., Menne, S., González‐Aseguinolaza, G., & Jugo, B. M. (2014) · Molecular Immunology · doi:10.1016/j.molimm.2014.10.011 · Cited by 4
Systematic evaluation of B-cell clonal family inference approaches
Balashova, D., van Schaik, B. D. C., Stratigopoulou, M., Guikema, J. E. J., Caniels, T. G., Claireaux, M. A. F., van Gils, M. J., Musters, A., Anang, D. C., de Vries, N., et al. (2024) · BMC Immunology · doi:10.1186/s12865-024-00600-8 · Cited by 4
The development of single-domain VHH nanobodies that target the Candida albicans cell surface
Cesare, G. B. D., Sauer, F. M., Kolecka, A., Stavrou, A. A., Verrips, T. C., Boekhout, T., Dolk, E., & Munro, C. A. (2024) · Microbiology Spectrum · doi:10.1128/spectrum.04269-23 · Cited by 4
Capturing Degeneracy in the Immune System
Tieri, P., Castellani, G., Remondini, D., Valensin, S., Loroni, J., Salvioli, S., & Franceschi, C. (2007) · Springer eBooks · doi:10.1007/978-0-387-39241-7_7 · Cited by 4
Ranieri, D. I., Hofstetter, H., & Hofstetter, O. (2009) · Journal of Separation Science · doi:10.1002/jssc.200800694 · Cited by 4
Zhao, L., & Li, J. (2009) · IEEE International Conference on Bioinformatics and Biomedicine Workshops (BIBMW) · doi:10.1109/bibmw.2009.5332121 · Cited by 4
Yasukochi, Y., Naka, I., Patarapotikul, J., Hananantachai, H., & Ohashi, J. (2015) · Malaria Journal · doi:10.1186/s12936-015-0820-2 · Cited by 4
Codon information value and codon transition-probability distributions in short-term evolution
Jiménez-Montaño, M. A., Coronel-Brizio, H. F., Hernández-Montoya, R., & Ramos, A. (2016) · Physica A Statistical Mechanics and its Applications · doi:10.1016/j.physa.2016.02.043 · Cited by 4
Kwon, Y. D., Wang, X. E., Bender, M. F., Yang, R. S., Li, Y., McKee, K., Rawi, R., O'Dell, S. J., Schneck, N. A., Shaddeau, A., et al. (2021) · Antibodies · doi:10.3390/antib10020023 · Cited by 4
Cohen, S. (1975) · Journal of Clinical Pathology · doi:10.1136/jcp.s1-6.1.1 · Cited by 4
Higher Affinity Antibodies Bind With Lower Hydration and Flexibility in Large Scale Simulations
Wong, M. T. Y., Kelm, S., Liu, X., Taylor, R. D., BAKER, T. S., & Essex, J. W. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.884110 · Cited by 4
Arslan, M., Uluçay, T., Kale, S., & Kalyoncu, S. (2023) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2023.140915 · Cited by 4
Information-driven modelling of antibody–antigen complexes
Ambrosetti, F., Jiménez-García, B., Roel-Touris, J., & Bonvin, A. M. J. J. (2019) · SSRN Electronic Journal · doi:10.2139/ssrn.3362436 · Cited by 2
Metadata
- Authors
- Wu, T. T., & Kabat, E. A.
- Affiliations
- NewYork–Presbyterian Hospital (US)
- Venue
- The Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 1970-08-01
- Volume
- 132
- Issue
- 2
- Pages
- 211-250
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2138737
- OpenAlex
- W2127552260
- Cited by
- 1,340
- References
- 72
- Citations by year
- 2026: 18 · 2025: 17 · 2024: 33 · 2023: 22 · 2022: 24 · 2021: 28 · 2020: 28 · 2019: 30 · 2018: 21 · 2017: 25 · 2016: 31 · 2015: 32 · 2014: 34 · 2013: 35 · 2012: 28
- FWCI
- 65.83
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (GB-8341)
- National Cancer Institute (CA08748)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Health Sciences › Medicine › Hematology › Multiple Myeloma Research and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- Bence Jones protein, immunoglobulin variable region, hypervariable region, invariant residues, glycine, hydrophobicity, sequence variation, kappa light chain, lambda light chain, episomes, antibody combining site, antigenic determinants
- MeSH terms
- Alanine, Amino Acid Sequence, Analysis of Variance, Animals, Antibodies, Antibody Specificity, Bence Jones Protein, Binding Sites, Genes, Glycine, Histidine, Humans, Immunoglobulin G, Immunoglobulin M, Leucine, Lysine, Models, Chemical, Multiple Myeloma, Rabbits, Species Specificity, Valine, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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