Localization of the conformational alteration of MHC molecules induced by the association of mouse class I heavy chain with a xenogeneic beta 2-microglobulin.

[1]  G. Ogg,et al.  Anti-HLA-A2 antibody-enhancement of peptide association with HLA-A2 as detected by cytotoxic T lymphocytes , 1989, Nature.

[2]  David B. Williams,et al.  Role of beta 2-microglobulin in the intracellular transport and surface expression of murine class I histocompatibility molecules. , 1989, Journal of immunology.

[3]  P. Iványi,et al.  H-2-dependent binding of xenogeneic beta 2-microglobulin from culture media. , 1988, Journal of immunology.

[4]  D. R. Lee,et al.  Studies of two antigenic forms of Ld with disparate beta 2-microglobulin (beta 2m) associations suggest that beta 2m facilitate the folding of the alpha 1 and alpha 2 domains during de novo synthesis. , 1988, Journal of immunology.

[5]  M. A. Saper,et al.  Structure of the human class I histocompatibility antigen, HLA-A2 , 1987, Nature.

[6]  P. Iványi,et al.  Monomorphic anti-HLA monoclonal antibody (W6/32) recognizes polymorphic H-2 heavy-chain determinants exposed by association with bovine or human but not murine beta 2-microglobulin. , 1987, Human immunology.

[7]  H. Ploegh,et al.  Crosses of two independently derived transgenic mice demonstrate functional complementation of the genes encoding heavy (HLA‐B27) and light (beta 2‐microglobulin) chains of HLA class I antigens. , 1987, The EMBO journal.

[8]  F. Lemonnier,et al.  Acquisition of HLA class I W6/32 defined antigenic determinant by heavy chains from different species following association with bovine beta 2-microglobulin. , 1987, Journal of immunology.

[9]  W. Jefferies,et al.  Expression of the W6/32 HLA epitope by cells of rat, mouse, human and other species: critical dependence on the interaction of specific MHC heavy chains with human or bovine β2‐microglobulin , 1987, European journal of immunology.

[10]  F. Lemonnier,et al.  The association between murine beta 2-microglobulin and HLA class I heavy chains results in serologically detectable conformational changes of both chains. , 1985, Journal of immunology.

[11]  K. Kubota.  Association of serum beta 2-microglobulin with H-2 class I heavy chains on the surface of mouse cells in culture. , 1984, Journal of immunology.

[12]  P. Pala,et al.  Domain interactions of H–2 class I antigens alter cytotoxic T-cell recognition sites , 1984, Nature.

[13]  M. Rijn,et al.  β2-Microglobulin from serum associates with MHC class I antigens on the surface of cultured cells , 1984, Nature.

[14]  K. Ozato,et al.  Monoclonal antibodies to mouse MHC antigens. III. Hybridoma antibodies reacting to antigens of the H-2b haplotype reveal genetic control of isotype expression. , 1981, Journal of immunology.

[15]  K. Ozato,et al.  Monoclonal antibodies to mouse MHC antigens. II. Antibodies to the H-2Ld antigen, the products of a third polymorphic locus of the mouse major histocompatibility complex. , 1980, Journal of immunology.

[16]  H. Lodish,et al.  Biosynthesis of HLA-A and HLA-B antigens in vivo. , 1980, The Journal of biological chemistry.

[17]  H. Lemke,et al.  Fine Specificity Analysis with Monoclonal Antibodies of Antigens Controlled by the Major Histocompatibility Complex and by the Qa/TL Region in Mice , 1979, Immunological reviews.

[18]  D. Lancet,et al.  Heavy chain of HLA-A and HLA-B antigens is conformationally labile: a possible role for beta 2-microglobulin. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[19]  H. Ploegh,et al.  Cell-free translation of the mRNAs for the heavy and light chains of HLA-A and HLA-B antigens. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[20]  C. Barnstable,et al.  Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens-new tools for genetic analysis , 1978, Cell.

[21]  J. Frelinger,et al.  New lymphocyte antigen system (Lna) controlled by the Ir region of the mouse H-2 complex. , 1973, Proceedings of the National Academy of Sciences of the United States of America.