Emergence and evolution of functional heavy-chain antibodies in Camelidae.
暂无分享,去创建一个
S. Muyldermans | U. Wernery | K. Conrath | V. Nguyen | Serge Muyldermans | Katja Conrath | Ulrich Wernery | Viet Khong Nguyen
[1] R. Jacobs,et al. Exceptionally long CDR3H region with multiple cysteine residues in functional bovine IgM antibodies , 1999, European journal of immunology.
[2] Jean-Claude Weill,et al. Somatic hyperconversion diversifies the single VH gene of the chicken with a high incidence in the D region , 1989, Cell.
[3] E. Hsu. Mutation, selection, and memory in B lymphocytes of exothermic vertebrates , 1998, Immunological reviews.
[4] A. Langaney,et al. The IGHG3 gene shows a structural polymorphism characterized by different hinge lengths: sequence of a new 2-exon hinge gene , 1996, Human Genetics.
[5] L. Wyns,et al. Selection and identification of single domain antibody fragments from camel heavy‐chain antibodies , 1997, FEBS letters.
[6] S. Muyldermans,et al. Heavy-chain antibodies in Camelidae; a case of evolutionary innovation , 2002, Immunogenetics.
[7] L. Hendershot. Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition , 1990, The Journal of cell biology.
[8] N. Okada,et al. Molecular evidence from retroposons that whales form a clade within even-toed ungulates , 1997, Nature.
[9] Toshiro Matsuda,et al. Somatic mutation hotspots correlate with DNA polymerase η error spectrum , 2001, Nature Immunology.
[10] A. Garen,et al. Comparison of fusion phage libraries displaying VH or single-chain Fv antibody fragments derived from the antibody repertoire of a vaccinated melanoma patient as a source of melanoma-specific targeting molecules. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[11] J. C. Almagro,et al. The differences between the structural repertoires of VH germ-line gene segments of mice and humans: implication for the molecular mechanism of the immune response. , 1997, Molecular immunology.
[12] A. Desmyter,et al. Functional heavy-chain antibodies in Camelidae. , 2001, Advances in immunology.
[13] L. Wyns,et al. LOSS OF SPLICE CONSENSUS SIGNAL IS RESPONSIBLE FOR THE REMOVAL OF THE ENTIRE CH1 DOMAIN OF THE FUNCTIONAL CAMEL IGG2A HEAVY-CHAIN ANTIBODIES' , 1999 .
[14] M. Cogné,et al. Immunoglobulin gene alterations in human heavy chain diseases. , 1989, Research in immunology.
[15] C. Amemiya,et al. Distinct patterns of IgH structure and organization in a divergent lineage of chrondrichthyan fishes , 1998, Immunogenetics.
[16] F. Alt,et al. Ordered rearrangement of immunoglobulin heavy chain variable region segments. , 1984, The EMBO journal.
[17] Lode Wyns,et al. Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme , 1996, Nature Structural Biology.
[18] S. Muyldermans,et al. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. , 1994, Protein engineering.
[19] M. Meltzer,et al. Heavy chain disease—A new disorder of serum γ-globulins: Report of the first case , 1964 .
[20] C. Alberini,et al. Developmental regulation of IgM secretion: The role of the carboxy-terminal cysteine , 1990, Cell.
[21] L. Wyns,et al. Comparison of llama VH sequences from conventional and heavy chain antibodies. , 1997, Molecular immunology.
[22] K. Bernstein,et al. Kappa-chain allotypes and isotypes in the rabbit: cDNA sequences of clones encoding b9 suggest an evolutionary pathway and possible role of the interdomain disulfide bond in quantitative allotype expression. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[23] L. Hellman,et al. Evidence for an early appearance of modern post‐switch isotypes in mammalian evolution; cloning of IgE, IgG and IgA from the marsupial Monodelphis domestica , 1998, European journal of immunology.
[24] M. Wabl,et al. A theory of allelic and isotypic exclusion for immunoglobulin genes. , 1982, Proceedings of the National Academy of Sciences of the United States of America.
[25] B. de Geus,et al. Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features. , 2000, Molecular immunology.
[26] J. Frère,et al. β-Lactamase Inhibitors Derived from Single-Domain Antibody Fragments Elicited in the Camelidae , 2001, Antimicrobial Agents and Chemotherapy.
[27] I. Tomlinson,et al. Somatic insertions and deletions shape the human antibody repertoire. , 1999, Journal of molecular biology.
[28] S. Webb. Locomotor evolution in camels , 1972 .
[29] N. Carter,et al. A map of the human immunoglobulin VH locus completed by analysis of the telomeric region of chromosome 14q , 1994, Nature Genetics.
[30] L. Wyns,et al. Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology. , 2002, The Journal of biological chemistry.
[31] E. Kabat,et al. Sequences of proteins of immunological interest , 1991 .
[32] J Deisenhofer,et al. Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 A and 1.0 A resolution. , 1980, Journal of molecular biology.
[33] S. Muyldermans,et al. The specific variable domain of camel heavy-chain antibodies is encoded in the germline. , 1998, Journal of molecular biology.
[34] L. Wyns,et al. A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops. , 1999, Structure.
[35] Lode Wyns,et al. Potent enzyme inhibitors derived from dromedary heavy‐chain antibodies , 1998, The EMBO journal.
[36] S. Muyldermans,et al. Unique single‐domain antigen binding fragments derived from naturally occurring camel heavy‐chain antibodies , 1999, Journal of molecular recognition : JMR.
[37] Andrew J. Martin,et al. Structural families in loops of homologous proteins: automatic classification, modelling and application to antibodies. , 1996, Journal of molecular biology.
[38] G. Köhler. Immunoglobulin chain loss in hybridoma lines. , 1980, Proceedings of the National Academy of Sciences of the United States of America.
[39] B. Bertocci,et al. Formation of the chicken B-cell repertoire: ontogenesis, regulation of Ig gene rearrangement, and diversification by gene conversion. , 1994, Advances in immunology.
[40] I. Shimada,et al. Effector functions of a mouse IgG that lacks the entire CH1 domain. C1q binding and complement fixation in the absence of antigen. , 1993, Journal of immunology.
[41] I. Tomlinson,et al. The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops. , 1992, Journal of molecular biology.
[42] R. Becker,et al. Molecular basis of the allelic inheritance of rabbit immunoglobulin VH allotypes: Implications for the generation of antibody diversity , 1990, Cell.
[43] H. Jäck,et al. Ig mu heavy chains with VH81X variable regions do not associate with lambda 5. , 1995, Annals of the New York Academy of Sciences.
[44] K. Knight. Restricted VH gene usage and generation of antibody diversity in rabbit. , 1992, Annual review of immunology.
[45] N. Klinman,et al. Predominance of nonproductive rearrangements of VH81X gene segments evidences a dependence of B cell clonal maturation on the structure of nascent H chains. , 1991, Journal of immunology.
[46] J. Sun,et al. Antibody repertoire development in fetal and neonatal piglets. I. Four VH genes account for 80 percent of VH usage during 84 days of fetal life. , 1998, Journal of immunology.
[47] M. Flajnik,et al. Somatic hypermutation of the new antigen receptor gene (NAR) in the nurse shark does not generate the repertoire: possible role in antigen-driven reactions in the absence of germinal centers. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[48] S. Muyldermans,et al. Naturally occurring antibodies devoid of light chains , 1993, Nature.
[49] C. Milstein,et al. Regulation of membrane IgM expression in secretory B cells: translational and post‐translational events. , 1987, The EMBO journal.
[50] C. Mackay,et al. Somatic generation of diversity in a mammalian primary lymphoid organ: The sheep ileal Peyer's patches , 1991, Cell.
[51] L. Wyns,et al. Degenerate interfaces in antigen-antibody complexes. , 2001, Journal of molecular biology.
[52] A. Khamlichi,et al. Structure of abnormal heavy chains in human heavy-chain-deposition disease. , 1995, European journal of biochemistry.
[53] R. Bell. Marsupial immunoglobulins: the distribution and evolution of macropod IgG2, IgG1, IgM and light chain antigenic markers within the sub-class Metatheria. , 1977, Immunology.
[54] C. Milstein,et al. Codon bias targets mutation , 1995, Nature.
[55] Jamshid Tanha,et al. Selection by phage display of llama conventional V(H) fragments with heavy chain antibody V(H)H properties. , 2002, Journal of immunological methods.
[56] N. M. Brooke,et al. A molecular timescale for vertebrate evolution , 1998, Nature.
[57] C. Schiff,et al. The Ig germline gene repertoire: economy or wastage? , 1988, Immunology today.
[58] S. Saini,et al. A single predominantly expressed polymorphic immunoglobulin VH gene family, related to mammalian group, I, clan, II, is identified in cattle. , 1997, Molecular immunology.
[59] L. Riechmann,et al. Single antibody domains as small recognition units: design and in vitro antigen selection of camelized, human VH domains with improved protein stability. , 1996, Protein engineering.
[60] S. Tonegawa,et al. Somatic generation of antibody diversity. , 1976, Nature.
[61] L. Wyns,et al. Camel heavy‐chain antibodies: diverse germline VHH and specific mechanisms enlarge the antigen‐binding repertoire , 2000, The EMBO journal.
[62] M. Milili,et al. The VDJ repertoire expressed in human preB cells reflects the selection of bona fide heavy chains , 1996, European journal of immunology.
[63] A single diversified VH gene family dominates the bovine immunoglobulin repertoire. , 1997, Biochemical Society transactions.
[64] K. Knight,et al. Development of the Antibody Repertoire in Rabbits , 1995, Annals of the New York Academy of Sciences.
[65] A M Lesk,et al. Structural repertoire of the human VH segments. , 1992, Journal of molecular biology.
[66] A. Lesk,et al. Conformations of immunoglobulin hypervariable regions , 1989, Nature.
[67] P. Lang,et al. Antigen binding and effector functions of a chimeric antibody with a deletion of the CH1 domain and non-covalently associated kappa chains. , 1993, Biological chemistry Hoppe-Seyler.
[68] L. Wyns,et al. Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes? , 2000, Journal of molecular biology.
[69] E. Padlan,et al. Anatomy of the antibody molecule. , 1994, Molecular immunology.
[70] J. Brouet,et al. Heavy Chain Diseases: Current Findings and Concepts , 1979, Immunological reviews.
[71] H. Jäck,et al. Ig μ Heavy Chains with VH81X Variable Regions Do Not Associate with λ5 a , 1995 .
[72] M. Gething,et al. BiP Binding Sequences in Antibodies (*) , 1995, The Journal of Biological Chemistry.
[73] W. Frankel,et al. Isotype switching of an immunoglobulin heavy chain transgene occurs by DNA recombination between different chromosomes , 1990, Cell.
[74] L. Frenken,et al. The structure of the llama heavy chain constant genes reveals a mechanism for heavy-chain antibody formation , 1999, Immunogenetics.
[75] C. Pérez,et al. A single VH family and long CDR3s are the targets for hypermutation in bovine immunoglobulin heavy chains , 1998, Immunological reviews.
[76] L. Wyns,et al. Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains. , 2001, Trends in biochemical sciences.
[77] T. T. Wu,et al. Generation of the primary antibody repertoire in rabbits: expression of a diverse set of Igk-V genes may compensate for limited combinatorial diversity at the heavy chain locus , 1999, Immunogenetics.
[78] J. Rast,et al. Evolution of antigen binding receptors. , 1999, Annual review of immunology.
[79] B. Stollar,et al. VH‐Gene Representation in Autoantibodies Reflects the Normal Human B‐Cell Repertoire , 1992, Immunological reviews.
[80] Austin Hughes,et al. A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks , 1995, Nature.
[81] A. Garen,et al. A melanoma-specific VH antibody cloned from a fusion phage library of a vaccinated melanoma patient. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[82] M. Flajnik,et al. Structural analysis of the nurse shark (new) antigen receptor (NAR): molecular convergence of NAR and unusual mammalian immunoglobulins. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[83] L. Wyns,et al. Antigen Specificity and High Affinity Binding Provided by One Single Loop of a Camel Single-domain Antibody* , 2001, The Journal of Biological Chemistry.
[84] R. Staden,et al. Both DNA strands of antibody genes are hypermutation targets. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[85] J. Kearney,et al. Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein , 1987, The Journal of cell biology.
[86] R. Schwartz,et al. Heavy-chain directed B-cell maturation: continuous clonal selection beginning at the pre-B cell stage. , 1994, Immunology today.
[87] D. Nemazee. Receptor editing in B cells. , 2000, Advances in immunology.
[88] P. Brodeur,et al. The organization of the mouse Igh-V locus. Dispersion, interspersion, and the evolution of VH gene family clusters , 1988, The Journal of experimental medicine.