References
Bodmer, J. G., Marsh, S. G. E., Albert, E. D., Bontrop, R. E., Charron, D., Bodmer, W. F., Dupont, B., Erlich, H., Mach, B., Mayr, W. R., Parham, P., Sasazuki, T., Schreuder, G. M. T., Strominger, J., Svejgaard, A., and Terasaki P. I. Nomenclature for factors of the HLA-System, 1995. Tissue Antigens 46: 1–18, 1995
Breur-Vriesendorp, B. S., Dekker-Saeys, A. J., and Ivanyi, P. Distribution of HLA-B27 subtypes in patients with ankylosing spondylitis: the disease is associated with a common determinant of the various B27 molecules. Ann Rheum Dis 46: 353–356, 1987
Chomczynski, P. and Sacchi, N. Single-step method of RNA isolation by acid guanidinium thiocyanate phenol chloroform extraction. Anal Biochem 162: 156–159, 1987
Chung, C. T., Niemela, S. L., and Miller, R. H. One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci USA 86: 2172–2175, 1989
Conolly, J. M., Hansen, T. H., Ingold, A. L., and Potter, T. A. Recognition by CD8 on cytotoxic T lymphocytes is ablated by several substitutions in the class I α3 domain: CD8 and the T-cell receptor recognize the same class I molecule. Proc Natl Acad Sci USA 87: 2137–2141, 1990
Lopez-Larrea, C., Sujirachato, K., Mehra, N. K., Chiewsilp, P., Isarangkura, D., Kanga, U., Dominguez, O., Coto, E., Pena, M., Setien, F., and Gonzalez-Roces, S. HLA-B27 subtypes in Asian patients with ankylosing spondylitis. Tissue antigens 45: 169–176, 1995
Potter, T. A., Rajan, T. V., Dick, R. F., and Bluestone, J. A. Substitution at residue 227 of H-2 class I molecules abrogates recognition by CD8-dependent, but not CD8-independent, cytotoxic T lymphocytes. Nature 337: 73–75, 1989
Salter, R. D., Norment, A. M., Chen, B. P., Clayberger, C., Krensky, A. M., Littman, D. R., and Parham, P. Polymorphism in the α3 domain of HLA-A molecules affects binding to CD8. Nature 338: 345–347, 1989
Saper, M. A., Bjorkman, P. J., and Wiley, D. C. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J Mol Biol 219: 277–319, 1991
Vega, M. A., Wallace, L., Rojo, S., Bragado, R., Aparicio, P., and Lopez de Castro, J. A. Delineation of functional sites in HLA-B27 antigens. Molecular analysis of a functional subtypes of HLA-B27 variant Wewak I defined by cytolytic T lymphocytes. J Immunol 135: 3323–3332, 1985
Vega, M. A., Bragado, R., Ivanyi, P., Pelaez, J. L., and Lopez de Castro, J. A. Molecular analysis of a functional subtype of HLA-B27. A possible evolutionary pathway for HLA-B27 polymorphism. J Immunol 137: 3557–3565, 1986
Vilches, C., de Pablo, R., and Kreisler, M. Nucleotide sequence of HLA-B2706. Immunogenetics 39: 219, 1994
Zemmour, J. and Parham, P. HLA class I nucleotide sequences, 1992. Hum Immunol 34: 225–241, 1992
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The names B * 2704 and B * 2706 were officially assigned by ythe WHO Nomenclature Committee in November 1987. This follows the agreed policy that, subject to the conditions stated in the most recent Nomenclature Report (Bodmer et al. 1995), names will be assigned to new sequences as they are identified. Lists of such new names will be published in the following WHO Nomenclature Report. The nucleotide sequences reported in this paper have been submitted to the GenBank nucleotide sequence database and have been a assigned the accession numbers U27608 and U35734
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Rudwaleit, M., Bowness, P. & Wordsworth, P. The nucleotide sequence of HLA-B * 2704 reveals a new amino acid substitution in exon 4 which is also present in HLA-B * 2706 . Immunogenetics 43, 160–162 (1996). https://doi.org/10.1007/BF00176678
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DOI: https://doi.org/10.1007/BF00176678