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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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Reverse Transcriptase Mechanism of Somatic Hypermutation: 60 Years of Clonal Selection Theory
Steele, E. J. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01611 · Cited by 11
Lu, Z., Tallmadge, R. L., Callaway, H., Felippe, M. J. B., & Parker, J. S. L. (2017) · Scientific Reports · doi:10.1038/s41598-017-12725-5 · Cited by 11
Developmental progression of immunoglobulin heavy chain diversity in sheep
Gontier, É., Ayrault, O., Godet, I., Nau, F., & Ladevèze, V. (2004) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2004.08.013 · Cited by 11
Multiple major histocompatibility complex class I genes in Asian anurans: Ontogeny and phylogeny
Didinger, C., Eimes, J. A., Lillie, M., & Waldman, B. (2016) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2016.12.003 · Cited by 11
Direct Tie2 Agonists Stabilize Vasculature for the Treatment of Diabetic Macular Edema
Agard, N. J., Zhang, G., Ridgeway, J., DiCara, D. M., Chu, P. Y., Ohri, R. V., Sanowar, S., Vernes, J.-M., Chi, H. M., Zhang, J., et al. (2022) · Translational Vision Science & Technology · doi:10.1167/tvst.11.10.27 · Cited by 11
Stevens, F. J. (2007) · Journal of Molecular Recognition · doi:10.1002/jmr.861 · Cited by 11
Kabat, E. A., Wu, T. T., & Bilofsky, H. S. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.12.4471 · Cited by 11
Crystal Structure of NMC-4 Fab anti-von Willebrand Factor A1 Domain
Celikel, R., Madhusudan, Varughese, K. I., Shima, M., Yoshioka, A., Ware, J. L., & Ruggeri, Z. M. (1997) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.1997.0128 · Cited by 11
Phylogenetic Aspects of Immunoglobulin Variable Region Diversity
Kehoe, J. M., & Capra, J. D. (1974) · Springer eBooks · doi:10.1007/978-1-4684-2838-4_6 · Cited by 11
Diversity of expressed V and J regions of immunoglobulin light chains in Xenopus laevis
Stewart, S. E., Pasquier, L. D., & Steiner, L. A. (1993) · European Journal of Immunology · doi:10.1002/eji.1830230838 · Cited by 11
X-Ray Crystallographic Studies of Immunoglobulins
Poljak, R. J. (1973) · Springer eBooks · doi:10.1007/978-1-4684-7773-3_1 · Cited by 11
Structural Analysis of the Antibody Combining Site
Givol, D. (1973) · Springer eBooks · doi:10.1007/978-1-4684-7773-3_2 · Cited by 11
Sequence Variability of Rabbit Antibody Light Chains
Thunberg, A. L., & Kindt, T. J. (1975) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1975.tb02617.x · Cited by 11
Nathanson, N. M., & Schleif, R. F. (1975) · Journal of Molecular Biology · doi:10.1016/0022-2836(75)90190-4 · Cited by 11
Some mathematical problems in the initiation and regulation of the immune response
DeLisi, C. (1977) · Mathematical Biosciences · doi:10.1016/0025-5564(77)90083-9 · Cited by 11
Evaluation of the structural variation among light chain variable domains
PADLAN, E. A. (1979) · Molecular Immunology · doi:10.1016/0161-5890(79)90128-7 · Cited by 11
Fraser, B. A., Thunberg, A. L., & Kindt, T. J. (1978) · European Journal of Immunology · doi:10.1002/eji.1830080603 · Cited by 11
Structural and immunological studies of two IgGl-λ myeloma proteins from a single patient
Goldrosen, M. H., Pruzanski, W., & Freedman, M. H. (1972) · Immunochemistry · doi:10.1016/0019-2791(72)90309-6 · Cited by 11
Mann, D. W., McLaughlin-Taylor, E., Wallace, R. B., & Forman, J. (1988) · The Journal of Experimental Medicine · doi:10.1084/jem.168.1.307 · Cited by 11
Stanfield, R. L., & Wilson, I. A. (2009) · Wiley eBooks · doi:10.1002/9780470485408.ch2 · Cited by 13
Early Molecular Events in Antigen-Antibody Cell Activation
Metzger, H. P. (1979) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.19.040179.002235 · Cited by 11
Akbar, R., Robert, P. A., Pavlović, M., Jeliazkov, J. R., Snapkov, I., Slabodkin, A., Weber, C. R., Scheffer, L., Miho, E., Haff, I. H., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/759498 · Cited by 11
Antibody numbering schemes: advances, comparisons and tools for antibody engineering
Zhu, Z., Ashrafian, H., Mohammadian-Tabrizi, N., Matas, E. R., Girard, L., Ma, H., & Nice, E. C. (2025) · Protein Engineering Design and Selection · doi:10.1093/protein/gzaf005 · Cited by 15
Public antibodies: convergent signatures in human humoral immunity against pathogens
Rao, V. N., & Coelho, C. H. (2025) · mBio · doi:10.1128/mbio.02247-24 · Cited by 10
Neehus, A., Wistuba, J., Ladas, N., Eiz‐Vesper, B., Schlatt, S., & Müller, T. H. (2016) · Immunology · doi:10.1111/imm.12652 · Cited by 10
Naschberger, A., Fürnrohr, B. G., Roviš, T. L., Malić, S., Scheffzek, K., Dieplinger, H., & Rupp, B. (2016) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s205979831601723x · Cited by 10
Control of Malaria by Bio-Therapeutics and Drug Delivery Systems
Qaraghuli, M. M. A., Obeid, M. A., Aldulaimi, O., & Ferro, V. A. (2017) · Journal of Medical Microbiology & Diagnosis · doi:10.4172/2161-0703.1000260 · Cited by 10
Bjerregaard-Andersen, K., Johannesen, H., Abdel‐Rahman, N., Heggelund, J. E., Hoås, H. M., Abraha, F., Bousquet, P. A., Høydahl, L. S., Burschowsky, D., Rojas, G., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-28918-5 · Cited by 10
Divergent allele advantage in the MHC and amphibian emerging infectious disease
Fu, M., Eimes, J. A., & Waldman, B. (2023) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2023.105429 · Cited by 10
B Cell Receptor Structure and Effector Function
Mak, T. W., & Saunders, M. E. (2006) · Elsevier eBooks · doi:10.1016/b978-012088451-3.50007-7 · Cited by 10
Sunyer, J. O., & Boudinot, P. (2022) · Springer eBooks · doi:10.1007/978-3-030-85420-1_8 · Cited by 10
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
"SELF": STANDARD OF COMPARISON FOR IMMUNOLOGICAL RECOGNITION OF FOREIGNNESS
Tauber, J. W. (1976) · The Lancet · doi:10.1016/s0140-6736(76)90737-6 · Cited by 10
Structure and Properties of Human Immunoglobulin Light-Chain Dimers
Stevens, F. J., & Schiffer, M. (2003) · Humana Press eBooks · doi:10.1385/0-89603-275-2:51 · Cited by 10
Computational Biochemistry of Antibodies and T-Cell Receptors
Novotný, J., & Bajorath, J. (1996) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60490-8 · Cited by 10
Vargas‐Madrazo, E., Lara‐Ochoa, F., & Jim�nez-Monta�o, M. (1994) · Journal of Molecular Evolution · doi:10.1007/bf00175497 · Cited by 10
Collins, M. K., & Owen, M. J. (1985) · Biochemical Journal · doi:10.1042/bj2300281 · Cited by 10
The location and expression of idiotypic determinants in the immunoglobulin variable region—I
Rosenstein, R. W., Zeldis, J. B., Konigsberg, W. H., & Richards, F. F. (1979) · Molecular Immunology · doi:10.1016/0161-5890(79)90101-9 · Cited by 10
Bioinformatics Tools for Antibody Engineering
Martin, A. C. R., & Allen, J. (2007) · doi:10.1002/9783527619740.ch5 · Cited by 10
Expression of allelic and non‐allelic genes in immunoglobulin light chains from homozygous rabbits
Frangione, B., & Lamm, M. E. (1970) · FEBS Letters · doi:10.1016/0014-5793(70)80563-4 · Cited by 10
Friedenson, B., Hora, J., & Wang, L.-S. (1976) · Biochemistry · doi:10.1021/bi00667a019 · Cited by 10
MHCDB ? database of the human MHC
Newell, W. R., Trowsdale, J., & Beck, S. (1994) · Immunogenetics · doi:10.1007/bf00188173 · Cited by 10
Amino-Acid Sequences of Light Chains of a Rabbit Anti- p -Azobenzoate Antibody
Appella, E., Chersi, A., Roholt, O. A., & Pressman, D. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.10.2569 · Cited by 10
From the Structure of Antibodies to the Diversification of the Immune Responce (Noble Lecture)
Milstein, C. (1985) · Angewandte Chemie International Edition in English · doi:10.1002/anie.198508161 · Cited by 10
Mishra, S. K., Niranjan, S. K., Singh, R., Kumar, P., Kumar, S., Banerjee, B., & Kataria, R. S. (2020) · Genomics · doi:10.1016/j.ygeno.2020.07.041 · Cited by 9
García-Valiente, R., Tejero, E. M., Stratigopoulou, M., Balashova, D., Jongejan, A., Lashgari, D., Pélissier, A., Caniels, T. G., Claireaux, M. A. F., Musters, A., et al. (2023) · npj Systems Biology and Applications · doi:10.1038/s41540-023-00271-y · Cited by 9
Mishra, S. K., Niranjan, S. K., Banerjee, B., Dubey, P. K., Gonge, D. S., Mishra, B., & Kataria, R. S. (2016) · Immunogenetics · doi:10.1007/s00251-016-0915-0 · Cited by 9
Physicochemical determinants of antibody-protein interactions
Karadag, M., Arslan, M., Kaleli, N. E., & Kalyoncu, S. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.08.011 · Cited by 9
Frota, N., Rebouças, A., Fuzo, C. A., & Lourenzoni, M. R. (2021) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2021.107949 · Cited by 9
Vásquez, M., Krauland, E. M., Walker, L. M., Wittrup, K. D., & Gerngross, T. U. (2019) · mAbs · doi:10.1080/19420862.2019.1611172 · Cited by 9
Detection and analysis of recognition and selection in the immune response
DeLisi, C. (1977) · Bulletin of Mathematical Biology · doi:10.1007/bf02461779 · Cited by 9
Kramer, K., & Hock, B. (2004) · Springer series on chemical sensors and biosensors · doi:10.1007/978-3-662-05204-4_1 · Cited by 9
Thornton, J. M. (1990) · Nature · doi:10.1038/343411a0 · Cited by 9
SequenceEditingAligner: A multiple sequence editor and aligner
Barber, A. M., & Maizel, J. V. (1990) · Gene Analysis Techniques · doi:10.1016/0735-0651(90)90011-4 · Cited by 9
Structure of Class-I MHC Molecules: HLA-B27 and Disease
Parham, P. (1990) · Scandinavian Journal of Rheumatology · doi:10.3109/03009749009097053 · Cited by 9
Selection and characterisation of binders based on homodimerisation of immunoglobulin VH domains
Jin, H., Sepúlveda, J., & Burrone, Ó. R. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01182-7 · Cited by 9
Hendry, E. J., Taylor, G. L., Grennan-Jones, F., Sullivan, A., Liddy, N., Godfrey, J., Hayakawa, N., Powell, M., Sanders, J. F., Furmaniak, J., et al. (2001) · Thyroid · doi:10.1089/10507250152740920 · Cited by 9
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
Designing PCR Primers to Amplify Specific Members or Subgroups of Multigene Families
Horton, R. M., Raju, R. P., & Conti‐Fine, B. M. (2003) · Humana Press eBooks · doi:10.1385/0-89603-483-6:459 · Cited by 9
Kabat, E. A. (1988) · Advances in experimental medicine and biology · doi:10.1007/978-1-4613-1663-3_1 · Cited by 9
Ben‐Sasson, S. A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4598 · Cited by 9
Von der Antikörperstruktur zur Diversität der Immunantwort (Nobel‐Vortrag)
Milstein, C., & Borges, J. L. (1985) · Angewandte Chemie · doi:10.1002/ange.19850971006 · Cited by 9
Diversity in the human T cell receptor beta chain
LaRocque, R. C., & Robinson, M. A. (1996) · Human Immunology · doi:10.1016/0198-8859(96)00083-3 · Cited by 9
Gene activation during immune reaction
Jachertz, D. (1979) · Molecular and Cellular Biochemistry · doi:10.1007/bf00314890 · Cited by 9
The nature of ‘species-specific’ amino acid residues
Wang, A.-C., Fudenberg, H. H., & Bazin, H. (1975) · Immunochemistry · doi:10.1016/0019-2791(75)90075-0 · Cited by 9
Site-Directed Cross-Linking: A New Approach to Mapping Antibody Combining Sites
Hadler, N. M., & Metzger, H. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.7.1421 · Cited by 9
Subgroups of Tcr ? chains and correlation with T-cell function
Schiffer, M., Kabat, E. A., & Wu, T. T. (1992) · Immunogenetics · doi:10.1007/bf00166827 · Cited by 9
The V-region sequence of the H chain from a third rabbit anti-pneumococcal antibody
Jaton, J. (1976) · Biochemical Journal · doi:10.1042/bj1570449 · Cited by 9
Functional sites of human class I MHC molecules: Paradigms a dozen?
Parham, P. (1987) · Immunologic Research · doi:10.1007/bf02918089 · Cited by 9
The α and β Chains of the T-Cell Receptor
Caccia, N. C., Toyonaga, B., Kimura, N., & Mak, T. W. (1988) · Springer eBooks · doi:10.1007/978-1-4684-5406-2_2 · Cited by 9
The Structural Basis of Antibody Specificity
Kabat, E. A. (1976) · Springer eBooks · doi:10.1007/978-3-642-81083-1_1 · Cited by 9
ANARCII: A Generalised Language Model for Antigen Receptor NumberingPreprint
Greenshields‐Watson, A., Agarwal, P., Robinson, S. A., Williams, B. H., Gordon, G. L., Capel, H., Li, Y., Spoendlin, F. C., Aguilar-Sanjuan, B., Boyles, F., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.16.648720 · Cited by 9
A STUDY OF V REGION GENES USING ALLOTYPIC AND IDIOTYPIC MARKERS
Kindt, T. J., Thunberg, A. L., Mudgett, M., & Klapper, D. G. (1974) · Elsevier eBooks · doi:10.1016/b978-0-12-637150-5.50013-4 · Cited by 9
[4] Use of homologous sequences to improve protein secondary structure prediction
Niermann, T., & Kirschner, K. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)02006-u · Cited by 9
Adaptive Immune Receptor Repertoire (AIRR) Community Guide to TR and IG Gene Annotation
Babrak, L. M., Marquez, S., Busse, C. E., Lees, W., Miho, E., Ohlin, M., Rosenfeld, A. M., Stervbo, U., Watson, C. T., Schramm, C. A., et al. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2115-8_16 · Cited by 8
Larruskain, A., Minguijón, E., García‐Etxebarria, K., Aróstegui, I., Moreno, B., Juste, R. A., & Jugo, B. M. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.10.085 · Cited by 8
Non-random Codon Usage of Synonymous and Non-synonymous Mutations in the Human HLA-A Gene
Matsushita, T., & Kano‐Sueoka, T. (2023) · Journal of Molecular Evolution · doi:10.1007/s00239-023-10093-5 · Cited by 8
Structural basis of spike RBM-specific human antibodies counteracting broad SARS-CoV-2 variants
Shitaoka, K., Higashiura, A., Kawano, Y., Yamamoto, A., Mizoguchi, Y., Hashiguchi, T., Nishimichi, N., Huang, S., Ito, A., Ohki, S., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-04782-6 · Cited by 9
Non-major histocompatibility complex alloantigen genes affecting immunity
Briles, W. E. (2004) · Poultry Science · doi:10.1093/ps/83.4.606 · Cited by 8
Genetic Dynamic Analysis of the Influenza A H5N1 NS1 Gene in China
Wei, K., Chen, Y., Lin, Y., & Pan, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101384 · Cited by 8
Oberlin, M., Kroemer, R. T., Mikol, V., Minoux, H., Tastan, E., & Baurin, N. (2012) · Journal of Chemical Information and Modeling · doi:10.1021/ci3001474 · Cited by 8
Pearson, S. K., Bull, C. M., & Gardner, M. (2016) · Immunogenetics · doi:10.1007/s00251-016-0947-5 · Cited by 8
Goto, R. M., Warden, C., Shiina, T., Hosomichi, K., Zhang, J., Kang, T. H., Wu, X., Glass, M. C., Delany, M. E., & Miller, M. M. (2022) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkac218 · Cited by 8
Gowane, G. R., Sharma, P., Kumar, R., Misra, S. S., Alex, R., Vohra, V., Chhotaray, S., Dass, G., Chopra, A., Kandalkar, Y. B., et al. (2022) · Animal Biotechnology · doi:10.1080/10495398.2022.2125404 · Cited by 8
Vaisbourd, M., Ignatovich, O., Dremucheva, A., Karpas, A., & Winter, G. P. (2001) · Hybridoma and Hybridomics · doi:10.1089/15368590152740680 · Cited by 8
Synthesis of a Vpr-Binding Derivative for Use as a Novel HIV-1 Inhibitor
Hagiwara, K., Ishii, H., Murakami, T., Takeshima, S., Chutiwitoonchai, N., Kodama, E. N., Kawaji, K., Kondoh, Y., Honda, K., Osada, H., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145573 · Cited by 8
Bialon, M., Schellenberg, L., Herzog, N., Kraus, S., Jörißen, H., Fischer, R., Stein, C., Nähring, J. M., Barth, S., & Püttmann, C. (2014) · Monoclonal Antibodies in Immunodiagnosis and Immunotherapy · doi:10.1089/mab.2014.0044 · Cited by 8
Magadán, S., Mondot, S., Palti, Y., Gao, G., Lefranc, M., & Boudinot, P. (2021) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2021.103998 · Cited by 8
Overview of monoclonal antibodies
Kaur, H. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822318-5.00006-5 · Cited by 10
Preparation of a semisynthetic antibody
Gavish, M., Zakut, R., Wilchek, M., & Givol, D. (1978) · Biochemistry · doi:10.1021/bi00600a032 · Cited by 8
Population genetics of multigene families
Ohta, T. (1982) · Advances in Biophysics · doi:10.1016/0065-227x(82)90008-9 · Cited by 8
From esoteric theory to therapeutic antibodies
Wu, T. T. (1994) · Applied Biochemistry and Biotechnology · doi:10.1007/bf02787928 · Cited by 8
Haber, E., & Novotný, J. (1985) · Springer eBooks · doi:10.1007/978-1-4684-4964-8_3 · Cited by 8
Nordman, N., Valjakka, J., & Peräkylä, M. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10267 · Cited by 8
Oligonucleotide-Directed Mutagenesis of Antibody Combining Sites
Sharon, J., Kao, C.-Y. Y., & Sompuram, S. R. (1993) · International Reviews of Immunology · doi:10.3109/08830189309061689 · Cited by 8
Webster, D. M., Pedersen, J. T., Staunton, D., Jones, A., & Rees, A. R. (1994) · Applied Biochemistry and Biotechnology · doi:10.1007/bf02787929 · Cited by 8
Prospects for human monoclonal antibodies: a critical perspective.
Brown, N. A. (1982) · PubMed Central · Cited by 8
Immunoglobulins: Structure, Function, and Genes
Putnam, F. W. (1987) · Elsevier eBooks · doi:10.1016/b978-0-12-568405-7.50008-4 · Cited by 8
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PADLAN, E. A., Segal, D. M., Cohen, G. H., Davies, D. R., Rudikoff, S., & Potter, M. (1974) · Elsevier eBooks · doi:10.1016/b978-0-12-637150-5.50009-2 · Cited by 8
The Antigen-Binding Sites of Immunoglobulins
Porter, R. R. (1972) · Springer eBooks · doi:10.1007/978-1-4757-1343-5_6 · Cited by 8
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
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