Cited by 1,340Monoclonal and Polyclonal Antibodies ResearchMultiple Myeloma Research and TreatmentsProtein Structure and Dynamics

The DOI matches its Crossref record; 70 of the 72 references it cites were found in a registry or an index.

AN ANALYSIS OF THE SEQUENCES OF THE VARIABLE REGIONS OF BENCE JONES PROTEINS AND MYELOMA LIGHT CHAINS AND THEIR IMPLICATIONS FOR ANTIBODY COMPLEMENTARITY

Open access

Wu, Tai Te, Kabat, Elvin A.·1970·The Journal of Experimental Medicine

DOI 10.1084/jem.132.2.211PMC PMC2138737

Open this paper in CoChat — free account Open PDF

Abstract

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1084/jem.132.2.211

Cites

70 of 70 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
Genes and Antibodies
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

Show all 72 references

Sorted by citations

Items 301–400 of 1,001

Amino acid sequences at constant and variable regions of heavy chains of monotypic immunoglobulins G and M of a single patient
Wang, A. C., Gergely, J., & Fudenberg, H. H. (1973) · Biochemistry · doi:10.1021/bi00727a027 · Cited by 60
The INNs and outs of antibody nonproprietary names
Jones, T. D., Carter, P. J., Plückthun, A., Vásquez, M., Holgate, R., Hötzel, I., Popplewell, A. G., Parren, P. W. H. I., Enzelberger, M. M., Rademaker, H. J., et al. (2015) · mAbs · doi:10.1080/19420862.2015.1114320 · Cited by 60
AbRSA: A robust tool for antibody numbering
Li, L., Chen, S., Miao, Z., Liu, Y., Liu, X., Xiao, Z. J., & Cao, Y. (2019) · Protein Science · doi:10.1002/pro.3633 · Cited by 62
The genetic engineering of monoclonal antibodies
Owens, R. J., & Young, R. J. (1994) · Journal of Immunological Methods · doi:10.1016/0022-1759(94)90051-5 · Cited by 60
Antibody modeling using the Prediction of ImmunoGlobulin Structure (PIGS) web server
Marcatili, P., Olimpieri, P. P., Chailyan, A., & Tramontano, A. L. (2014) · Nature Protocols · doi:10.1038/nprot.2014.189 · Cited by 60
The binding of opioid peptides to the Mcg light chain dimer: Flexible keys and adjustable locks
Edmundson, A. B., Ely, K. R., Herron, J. N., & Cheson, B. D. (1987) · Molecular Immunology · doi:10.1016/0161-5890(87)90003-4 · Cited by 59
Partial amino acid sequences of chicken and turkey immunoglobulin light chains. Homology with mammalian .lambda. chains
Grant, J., Sanders, B. G., & Hood, L. (1971) · Biochemistry · doi:10.1021/bi00792a022 · Cited by 58
Variable region framework differences result in decreased or increased affinity of variant anti-digoxin antibodies.
Panka, D. J., Mudgett-Hunter, M., Parks, D. R., Peterson, L. L., Herzenberg, L. A., Haber, E., & Margolies, M. N. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.9.3080 · Cited by 58
Amyloidosis
Cohen, A. S., Cathcart, E. S., & Skinner, M. M. (1978) · Arthritis & Rheumatism · doi:10.1002/art.1780210126 · Cited by 58
DETECTION OF IDIOTYPIC CROSS-REACTIONS AMONG STREPTOCOCCAL ANTISERA FROM RELATED RABBITS
Kindt, T. J., Seide, R. K., Bokisch, V. A., & Krause, R. M. (1973) · The Journal of Experimental Medicine · doi:10.1084/jem.138.3.522 · Cited by 58
The role of antibodies to DNA in systemic lupus erythematosus— A review and introduction to an international workshop on DNA antibodies held in London, May 1996
Isenberg, D. A., Ravirajan, C. T., Rahman, A., & Kalsi, J. (1997) · Lupus · doi:10.1177/096120339700600316 · Cited by 57
[1] Basic principles of antigen-antibody reactions
Kabat, E. A. (1980) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(80)70040-x · Cited by 57
[6] Molecular modeling of antibody combining sites
Martin, A. C. R., Cheetham, J. C., & Rees, A. R. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)03008-5 · Cited by 57
A hypothetical space-filling model of the V-regions of the galactan-binding myeloma immunoglobulin J539☆
Feldmann, R. J., POTTER, M., & Glaudemans, C. P. J. (1981) · Molecular Immunology · doi:10.1016/0161-5890(81)90060-2 · Cited by 57
Frequency of occurrence of idiotypes associated with anti-p-azophenylarsonate antibodies arising in mice immunologically suppressed with respect to a cross-reactive idiotype.
Ju, S., Gray, A. B., & Nisonoff, A. (1977) · The Journal of Experimental Medicine · doi:10.1084/jem.145.3.540 · Cited by 57
Amino acid sequence diversity within the family of antibodies bearing the major antiarsonate cross-reactive idiotype of the A strain mouse.
Slaughter, C. A., & Capra, J. D. (1983) · The Journal of Experimental Medicine · doi:10.1084/jem.158.5.1615 · Cited by 57
Humanization of chicken monoclonal antibody using phage-display system
Nishibori, N., Horiuchi, H., Furusawa, S., & Matsuda, H. (2005) · Molecular Immunology · doi:10.1016/j.molimm.2005.04.002 · Cited by 57
Evolution of Vertebrate Immunoglobulin Variable Gene Segments
Ota, T., Sitnikova, T. Y., & Nei, M. (2000) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-59674-2_10 · Cited by 56
STRUCTURE‐FUNCTION RELATIONSHIPS AMONG ANTI‐GAMMA GLOBULIN ANTIBODIES*
Capra, J. D., Kehoe, J. M., WINCHESTER, R. J., & Kunkel, H. G. (1971) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1971.tb13549.x · Cited by 56
Evolutionary relationships among the primate Mhc-DQA1 and DQA2 alleles
Kenter, M. J. H., Otting, Ń., Anholts, J. D. H., Leunissen, J. A. M., Jonker, M., & Bontrop, R. E. (1992) · Immunogenetics · doi:10.1007/bf00215282 · Cited by 56
Computer models of the human immunoglobulins
Pumphrey, R. S. H. (1986) · Immunology Today · doi:10.1016/0167-5699(86)90106-4 · Cited by 56
Variability of three-dimensional structure in immunoglobulins.
PADLAN, E. A., & Davies, D. R. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.3.819 · Cited by 56
Mining for the antibody-antigen interacting associations that predict the B cell epitopes
Zhao, L., & Li, J. (2010) · BMC Structural Biology · doi:10.1186/1472-6807-10-s1-s6 · Cited by 55
Fatal amyloid formation in a patient’s antibody light chain is caused by a single point mutation
Kazman, P., Vielberg, M.-T., Cendales, M. D. P., Hunziger, L., Weber, B., Hegenbart, U., Zacharias, M., Köhler, R., Schönland, S. O., Groll, M., et al. (2020) · eLife · doi:10.7554/elife.52300 · Cited by 54
Reflections on the clonal-selection theory
Cohn, M., Mitchison, N. A., Paul, W. E., Silverstein, A. M., Talmage, D. W., & WEIGERT, M. G. (2007) · Nature reviews. Immunology · doi:10.1038/nri2177 · Cited by 54
On Near-Optimal Alignments of Biological Sequences
Naor, D., & Brutlag, D. L. (1994) · Journal of Computational Biology · doi:10.1089/cmb.1994.1.349 · Cited by 54
Efficient Isolation of Soluble Intracellular Single-chain Antibodies using the Twin-arginine Translocation Machinery
Fisher, A. C., & DeLisa, M. P. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.10.051 · Cited by 54
Sequence and diversity of MHC DQA and DQB genes of the owl monkey Aotus nancymaae
Diaz, D., Martin, N., Rodríguez, R., Nino-Vasquez, J. J., Moreno, A., Patarroyo, M. E., Pluschke, G., & Daubenberger, C. (2000) · Immunogenetics · doi:10.1007/s002510000189 · Cited by 54
Structural differences between the repertoires of mouse and human germline genes and their evolutionary implications
Almagro, J. C., Hernández, I., Ramírez, M. C., & Vargas‐Madrazo, E. (1998) · Immunogenetics · doi:10.1007/s002510050370 · Cited by 54
Novel arrangement of immunoglobulin variable domains: x-ray crystallographic analysis of the .lambda.-chain dimer Bence-Jones protein Loc
Chang, C. H., Short, M., Westholm, F. A., Stevens, F. J., Wang, B. C., Furey, W. F., Solomon, A., & Schiffer, M. (1985) · Biochemistry · doi:10.1021/bi00339a025 · Cited by 54
Diversity and locus specificity of chicken MHC B class I sequences
Livant, E. J., Brigati, J. R., & Ewald, S. J. (2004) · Animal Genetics · doi:10.1111/j.1365-2052.2003.01078.x · Cited by 53
Prediction of methionine oxidation risk in monoclonal antibodies using a machine learning method
Sankar, K., Hoi, K. H., Yin, Y., Ramachandran, P., Andersen, N., Hilderbrand, A. E., McDonald, P., Spiess, C., & Zhang, Q. (2018) · mAbs · doi:10.1080/19420862.2018.1518887 · Cited by 51
Genetic polymorphism of the swine major histocompatibility complex (SLA) class�I genes, SLA-1, -2 and -3
Ando, A., Kawata, H., Shigenari, A., Anzai, T., Ôta, M., Katsuyama, Y., Sada, M., Goto, R., Takeshima, S., Aida, Y., et al. (2003) · Immunogenetics · doi:10.1007/s00251-003-0619-0 · Cited by 53
An improved model of association for VH–VL immunoglobulin domains: Asymmetries between VH and VL in the packing of some interface residues
Vargas‐Madrazo, E., & Paz‐García, E. (2003) · Journal of Molecular Recognition · doi:10.1002/jmr.613 · Cited by 53
Evolution of major histocompatibility complex class II allelic diversity: direct descent in mice and humans.
Lundberg, A. S., & McDevitt, H. O. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.14.6545 · Cited by 53
Mouse Immunoglobulin Heavy Chains Are Coded by Multiple Germ Line Variable Region Genes
Barstad, P. A., Farnsworth, V., WEIGERT, M. G., Cohn, M., & Hood, L. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.10.4096 · Cited by 53
Organization of kappa light chain genes in germ-line and somatic tissue.
Joho, R. H., Weissman, I. L., Early, P. W., Cole, J., & Hood, L. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.2.1106 · Cited by 53
Skewed Primary Igκ Repertoire and V–J Joining in C57BL/6 Mice: Implications for Recombination Accessibility and Receptor Editing
Aoki-Ota, M., Torkamani, A., Ota, T., Schork, N. J., & Nemazee, D. A. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103484 · Cited by 52
Screening Libraries To Identify Proteins with Desired Binding Activities Using a Split-GFP Reassembly Assay
Jackrel, M. E., Cortajarena, A. L., Liu, T. Y., & Regan, L. (2009) · ACS Chemical Biology · doi:10.1021/cb900272j · Cited by 52
Oxidation in the complementarity-determining regions differentially influences the properties of therapeutic antibodies
Dashivets, T., Stracke, J. O., Dengl, S., Knaupp, A., Pollmann, J., Büchner, J., & Schlothauer, T. (2016) · mAbs · doi:10.1080/19420862.2016.1231277 · Cited by 52
An arthritogenic alphavirus uses the α1β1 integrin collagen receptor
Linn, M. L., Eble, J. A., Lübken, C., Slade, R., Heino, J., Davies, J. M., & Suhrbier, A. (2005) · Virology · doi:10.1016/j.virol.2005.03.015 · Cited by 52
Analysis of MHC class I genes across horse MHC haplotypes
Tallmadge, R. L., Campbell, J. A., Miller, D. C., & Antczak, D. F. (2010) · Immunogenetics · doi:10.1007/s00251-009-0420-9 · Cited by 52
Gene duplications and sequence polymorphism of bovine class II DQB genes
Sigurdard�ttir, S., Borsch, C., Gustafsson, K. T., & Andersson, L. (1992) · Immunogenetics · doi:10.1007/bf00185115 · Cited by 52
Crystal structure of the anti-(carcinoembryonic antigen) single-chain Fv antibody MFE-23 and a model for antigen binding based on intermolecular contacts
Boehm, M. K., Corper, A. L., Wan, T., Sohi, M. K., Sutton, B. J., Thornton, J. D., Keep, P. A., Chester, K. A., Beǵent, R. H. J., & Perkins, S. J. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3460519 · Cited by 52
Chemical Analyses of Variable Regions of Heavy and Light Chains of Cold Agglutinins1
Gergely, J., Wang, A. C., & Fudenberg, H. H. (1973) · Vox Sanguinis · doi:10.1111/j.1423-0410.1973.tb03484.x · Cited by 52
From Antibody Structure to Immunological Diversification of Immune Response
Milstein, C. (1986) · Science · doi:10.1126/science.3080810 · Cited by 52
Towards a Unified Theory of Immunoglobulin Structure‐Function Relations
Kieder‐Emmons, T., & Köhler, H. (1986) · Immunological Reviews · doi:10.1111/j.1600-065x.1986.tb01476.x · Cited by 52
Probing antibody diversity by 2D NMR: comparison of amino acid sequences, predicted structures, and observed antibody-antigen interactions in complexes of two antipeptide antibodies
Levy, R., Assulin, O., Scherf, T., Levitt, M., & Anglister, J. (1989) · Biochemistry · doi:10.1021/bi00444a006 · Cited by 52
The Interaction of Homogeneous, Murine Myeloma Immunoglobulins with Polysaccharide Antigens
Glaudemans, C. P. J. (1975) · Advances in carbohydrate chemistry and biochemistry · doi:10.1016/s0065-2318(08)60299-1 · Cited by 52
Identification of Igσ and Igλ in channel catfish, Ictalurus punctatus, and Igλ in Atlantic cod, Gadus morhua
Edholm, E., Wilson, M., Sahoo, M., Miller, N. W., Pilström, L., Wermenstam, N. E., & Bengtén, E. (2009) · Immunogenetics · doi:10.1007/s00251-009-0365-z · Cited by 51
Conserved amino acid networks involved in antibody variable domain interactions
Wang, N. C., Smith, W. F., Miller, B., Aivazian, D., Lugovskoy, A. A., Reff, M. E., Glaser, S., Croner, L. J., & Demarest, S. J. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22319 · Cited by 53
Conformational Plasticity in the HIV-1 Fusion Peptide Facilitates Recognition by Broadly Neutralizing Antibodies
Yuan, M., Cottrell, C. A., Ozorowski, G., van Gils, M. J., Kumar, S., Wu, N. C., Sarkar, A., Torres, J. L., de Val, N., Copps, J., et al. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2019.04.011 · Cited by 54
Clone: A Monte-Carlo Computer Simulation of B Cell Clonal Expansion, Somatic Mutation, and Antigen-Driven Selection
Shlomchik, M. J., Watts, P., WEIGERT, M. G., & Litwin, S. (1998) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-71984-4_13 · Cited by 51
Amino acid sequence of the light chain derived from a rabbit anti-p-azobenzoate antibody of restricted heterogeneity
Appella, E., Roholt, O. A., Chersi, A., Radzimski, G., & Pressman, D. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(73)90581-0 · Cited by 51
Terminal Deoxynucleotidyl Transferase: Biological Studies
Bollum, F. J. (1979) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122921.ch6 · Cited by 51
Homogeneous Antibodies: Induction and Value as Probe for the Antibody Problem
Braun, D. G., & Jaton, J. (1974) · Modern aspects of electrochemistry · doi:10.1007/978-3-642-65908-9_2 · Cited by 51
Protein Engineering of Antibodies
Sandhu, J. (1992) · Critical Reviews in Biotechnology · doi:10.3109/07388559209114235 · Cited by 50
Immunoglobulin with complementary paratope and idiotope.
Kang, C., & Köhler, H. (1986) · The Journal of Experimental Medicine · doi:10.1084/jem.163.4.787 · Cited by 50
Generation of immunoglobulin variable gene diversity
Gearhart, P. J. (1982) · Immunology Today · doi:10.1016/s0167-5699(82)80026-1 · Cited by 50
The influence of nearest‐neighboring amino acid residues on aspects of secondary structure of proteins. Attempts to locate α‐helices and β‐sheets
Kabat, E. A., & Wu, T. (1973) · Biopolymers · doi:10.1002/bip.1973.360120406 · Cited by 50
Immunoglobulins with hapten‐binding activity: structure‐function correlations and genetic implications
Barstad, P. A., Hubert, J. J., Hunkapiller, M. W., Goetze, A. M., Schilling, J., Black, B., Eaton, B., Richards, J. H., Weigert, M., & Hood, L. (1978) · European Journal of Immunology · doi:10.1002/eji.1830080709 · Cited by 50
Immunoglobulin Structure: Amino Terminal Sequences of Kappa Chains from Genetically Similar Mice (BALB/c)
Hood, L., Potter, M., & McKEAN, D. J. (1970) · Science · doi:10.1126/science.170.3963.1207 · Cited by 50
A Structure-Based Database of Antibody Variable Domain Diversity
Bond, C. J., Wiesmann, C., Marsters, J. C., & Sidhu, S. S. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.063 · Cited by 49
Amino Acid Sequence of the Light Chain from a Mouse Myeloma Protein with Anti-Hapten Activity: Evidence for a Third Type of Light Chain
Schulenburg, E. P., Simms, E. S., Lynch, R. G., Bradshaw, R. A., & Eisen, H. N. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.11.2623 · Cited by 49
Development of Norwalk Virus-Specific Monoclonal Antibodies with Therapeutic Potential for the Treatment of Norwalk Virus Gastroenteritis
Chen, Z., Sosnovtsev, S. V., Bok, K., Parra, G. I., Makiya, M. A., Agulto, L., Green, K. Y., & Purcell, R. H. (2013) · Journal of Virology · doi:10.1128/jvi.01376-13 · Cited by 48
Monoclonal Antibodies Directed toward the Hepatitis C Virus Glycoprotein E2 Detect Antigenic Differences Modulated by the N-Terminal Hypervariable Region 1 (HVR1), HVR2, and Intergenotypic Variable Region
Alhammad, Y. M. O., Gu, J., Boo, I., Harrison, D. J., McCaffrey, K., Vietheer, P. T., Edwards, S. J., Quinn, C. T., Coulibaly, F., Poumbourios, P., et al. (2015) · Journal of Virology · doi:10.1128/jvi.02070-15 · Cited by 48
How B-Cell Receptor Repertoire Sequencing Can Be Enriched with Structural Antibody Data
Kovaltsuk, A., Krawczyk, K., Galson, J. D., Kelly, D. F., Deane, C. M., & Trück, J. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01753 · Cited by 49
The contrasting properties of conservation and correlated phylogeny in protein functional residue prediction
Manning, J. R., Jefferson, E., & Barton, G. J. (2008) · BMC Bioinformatics · doi:10.1186/1471-2105-9-51 · Cited by 48
The Generation and Maintenance of MHC Class II Gene Polymorphism in Rodents
Wakeland, E. K., Boehme, S. A., & She, J. (1990) · Immunological Reviews · doi:10.1111/j.1600-065x.1990.tb00042.x · Cited by 48
[4] Construction of single-chain Fv derivatives of monoclonal antibodies and their production in Escherichia coli
Johnson, S., & Bird, R. E. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)03006-3 · Cited by 48
Complex intrapatient sequence variation in the V1 and V2 hypervariable regions of the HIV-1 gp120 envelope sequence
Pedroza-Martins, L., Chenciner, N., & Wain–Hobson, S. (1992) · Virology · doi:10.1016/0042-6822(92)90259-r · Cited by 48
The Electron Transfer Function of Cytochrome c
Ferguson-Miller, S. M., Brautigan, D. L., & Margoliash, E. (1979) · Elsevier eBooks · doi:10.1016/b978-0-12-220107-3.50011-6 · Cited by 48
HLA-A,B,C: Patterns of Polymorphism in Peptide-Binding Proteins
Parham, P., Lawlor, D. A., Salter, R. D., Lomen, C. E., Björkman, P. J., & Ennis, P. D. (1989) · Springer eBooks · doi:10.1007/978-3-662-39946-0_2 · Cited by 49
ANTIBODY STRUCTURE AND MOLECULAR IMMUNOLOGY*
Edelman, G. M. (1971) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1971.tb13520.x · Cited by 47
AN IDIOTYPIC CROSS-REACTION BETWEEN ALLOTYPE a3 AND ALLOTYPE a NEGATIVE RABBIT ANTIBODIES TO STREPTOCOCCAL CARBOHYDRATE
Kindt, T. J., Klapper, D. G., & Waterfield, M. D. (1973) · The Journal of Experimental Medicine · doi:10.1084/jem.137.3.636 · Cited by 47
Affinity maturation of antibody fragments: A review encompassing the development from random approaches to computational rational optimization
Li, J., Kang, G., Wang, J., Yuan, H., Wu, Y., Meng, S., Wang, P., Zhang, M., Wang, Y., Feng, Y., et al. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.125733 · Cited by 50
A comparative study of conservation and variation scores
Johansson, F., & Toh, H. (2010) · BMC Bioinformatics · doi:10.1186/1471-2105-11-388 · Cited by 46
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
Amino-Acid Sequence of an Allotype b4 Light Chain from a Rabbit Antibody to Streptococcal Carbohydrate
Chen, K. C. S., Kindt, T. J., & Krause, R. M. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.5.1995 · Cited by 46
Mechanisms of antibody diversity: Multiple genes encode structurally related mouse κ variable regions
McKEAN, D. J., Bell, M., & Potter, M. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.8.3913 · Cited by 46
The Distribution of Variation in Regulatory Gene Segments, as Present in MHC Class II PromotersPreprint
Cowell, L. G., Kepler, T. B., Janitz, M., Lauster, R., & Mitchison, N. A. (1998) · Genome Research · doi:10.1101/gr.8.2.124 · Cited by 46
Antibody-Specified B-Cell Epitope Prediction in Line with the Principle of Context-Awareness
Zhao, L., Wong, L., & Li, J. (2011) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2011.49 · Cited by 45
Structural Basis of Antibody–Antigen Interactions
Sundberg, E. J. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-450-6_2 · Cited by 45
Organization, complexity and allelic diversity of the porcine (Sus scrofa domestica) immunoglobulin lambda locus
Schwartz, J. C., Lefranc, M., & Murtaugh, M. P. (2011) · Immunogenetics · doi:10.1007/s00251-011-0594-9 · Cited by 45
Molecular characterization of major histocompatibility complex class II alleles in wild tiger salamanders (Ambystoma tigrinum)
Bos, D. H., & DeWoody, J. A. (2005) · Immunogenetics · doi:10.1007/s00251-005-0038-5 · Cited by 45
Evolution of V genes: DNA sequence structure of functional germline genes and pseudogenes
Rothenfluh, H. S., Blanden, R., & Steele, E. (1995) · Immunogenetics · doi:10.1007/bf00191221 · Cited by 45
Subgroups of variable region genes of beta chains of T-cell receptors for antigen.
Schiffer, M., Wu, T. T., & Kabat, E. A. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.12.4461 · Cited by 45
Marked hydrophobicity of the NH2-terminal extra piece of immunoglobulin light-chain precursors: possible physiological functions of the extra piece.
Schechter, I., & Burstein, Y. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.9.3273 · Cited by 45
Structural trends in antibody-antigen binding interfaces: a computational analysis of 1833 experimentally determined 3D structures
Madsen, A. V., Mejias-Gomez, O., Pedersen, L. E., Morth, J. P., Kristensen, P. K., Jenkins, T. P., & Goletz, S. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.11.056 · Cited by 46
Site-Specific Photoconjugation of Antibodies Using Chemically Synthesized IgG-Binding Domains
Perols, A., & Karlström, A. E. (2014) · Bioconjugate Chemistry · doi:10.1021/bc400440u · Cited by 44
Molecular mechanism of amyloidogenic mutations in hypervariable regions of antibody light chains
Rottenaicher, G. J., Weber, B., Rührnößl, F., Kazman, P., Absmeier, R. M., Hitzenberger, M., Zacharias, M., & Büchner, J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100334 · Cited by 45
Evolution of the porcine (Sus scrofa domestica) immunoglobulin kappa locus through germline gene conversion
Schwartz, J. C., Lefranc, M., & Murtaugh, M. P. (2011) · Immunogenetics · doi:10.1007/s00251-011-0589-6 · Cited by 44
T-cell clones and T-cell receptors
Fitch, F. W. (1986) · Microbiological Reviews · doi:10.1128/mmbr.50.1.50-69.1986 · Cited by 44
FIRST ORDER CONSIDERATIONS IN ANALYZING THE GENERATOR OF DIVERSITY
Cohn, M., Blomberg, B. B., Geckeler, W. R., Raschke, W. C., Riblet, R. J., & Weigert, M. (1974) · Elsevier eBooks · doi:10.1016/b978-0-12-637150-5.50014-6 · Cited by 44
Recombinant antibodies for environmental analysis
Kramer, K., & Hock, B. (2003) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-003-2161-1 · Cited by 43
Structural basis of broad HIV neutralization by a vaccine-induced cow antibody
Stanfield, R. L., Berndsen, Z. T., Huang, R., Sok, D., Jenkins, G. W., Torres, J. L., Burton, D. R., Ward, A. B., Wilson, I. A., & Smider, V. V. (2020) · Science Advances · doi:10.1126/sciadv.aba0468 · Cited by 41
A systematic analysis of sequences of human antiphospholipid and anti–β2-glycoprotein I antibodies: The importance of somatic mutations and certain sequence motifs
Giles, I., Haley, J., Nagl, S., Isenberg, D. A., Latchman, D. S., & Rahman, A. (2003) · Seminars in Arthritis and Rheumatism · doi:10.1053/sarh.2003.49994 · Cited by 43
Allelic diversity at the Mhc-DP locus in rhesus macaques (Macaca mulatta)
Slierendregt, B. L., Otting, Ń., Kenter, M. J. H., & Bontrop, R. E. (1995) · Immunogenetics · doi:10.1007/bf00188429 · Cited by 43
Analysis of the antibody structure based on high-resolution crystallographic studies
Narciso, J. E. T., Uy, I. D., Cabang, A. B., Chavez, J. F. C., Pablo, J. L., Padilla-Concepcion, G., & PADLAN, E. A. (2011) · New Biotechnology · doi:10.1016/j.nbt.2011.03.012 · Cited by 44
A genetic approach for identifying critical residues in the fingers and palm subdomains of HIV-1 reverse transcriptase
Wrobel, J. A., Chao, S.-F., Conrad, M. J., Merker, J. D., Swanstrom, R. I., Pielak, G. J., & Hutchison, C. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.2.638 · Cited by 43

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
DOI: 10.1084/jem.132.2.211
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 ›

Are you an author, or do you see a problem with this page? Request a review

AN ANALYSIS OF THE SEQUENCES OF THE VARIABLE REGIONS OF BENCE JONES PROTEINS AND MYELOMA LIGHT CHAINS AND THEIR IMPLICATIONS FOR ANTIBODY COMPLEMENTARITY

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks