메뉴 건너뛰기




Volumn 55, Issue 1, 2000, Pages 80-82

Identification of the novel allele HLA-B*1545: Assessment of alloreactivity in case of mismatch with other B*15 alleles

Author keywords

Bone marrow transplantation; HLA B*1545; Sequence analysis; Serological detection

Indexed keywords

HLA B ANTIGEN;

EID: 0033958648     PISSN: 00012815     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-0039.2000.550117.x     Document Type: Article
Times cited : (2)

References (17)
  • 1
    • 0030745410 scopus 로고    scopus 로고
    • Sequencing of HLA class I genes based on the conserved diversity of the noncoding regions: Sequencing-based typing of the HLA-A gene
    • 1. Kotsch K, Wehling J, Kohler S, Blasczyk R. Sequencing of HLA class I genes based on the conserved diversity of the noncoding regions: Sequencing-based typing of the HLA-A gene. Tissue Antigens 1997: 50: 178-91.
    • (1997) Tissue Antigens , vol.50 , pp. 178-191
    • Kotsch, K.1    Wehling, J.2    Kohler, S.3    Blasczyk, R.4
  • 3
    • 0023187442 scopus 로고
    • The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
    • 3. Bjorkman PJ, Saper MA, Samraoui B, Bennett WS, Strominger JL, Wiley DC. The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens. Nature 1987: 329: 512-8.
    • (1987) Nature , vol.329 , pp. 512-518
    • Bjorkman, P.J.1    Saper, M.A.2    Samraoui, B.3    Bennett, W.S.4    Strominger, J.L.5    Wiley, D.C.6
  • 5
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution
    • 5. Saper MA, Bjorkman PJ, Wiley DC. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J Mol Biol 1991: 219: 277-319.
    • (1991) J Mol Biol , vol.219 , pp. 277-319
    • Saper, M.A.1    Bjorkman, P.J.2    Wiley, D.C.3
  • 6
    • 0026794581 scopus 로고
    • The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
    • 6. Madden DR, Gorga JC, Strominger JL, Wiley DC. The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC. Cell 1992: 70: 1035-48.
    • (1992) Cell , vol.70 , pp. 1035-1048
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 7
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • 7. Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 1996: 384: 134-41.
    • (1996) Nature , vol.384 , pp. 134-141
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 8
    • 0029965954 scopus 로고    scopus 로고
    • An altered position of the α2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501
    • 8. Smith KJ, Reid SW, Stuart DI, McMichael AJ, Jones EY, Bell JI. An altered position of the α2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 1996: 4: 203-13.
    • (1996) Immunity , vol.4 , pp. 203-213
    • Smith, K.J.1    Reid, S.W.2    Stuart, D.I.3    McMichael, A.J.4    Jones, E.Y.5    Bell, J.I.6
  • 9
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • 9. Falk K, Rötzschke O, Stevanovic S, Jung G, Rammensee H-G. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 1991: 351: 290-6.
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rötzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.-G.5
  • 10
    • 0026495447 scopus 로고
    • Sequence motifs important for peptide binding to the human MHC class I molecule, HLA-A2
    • 10. Parker KC, Bednarek MA, Hull LK et al. Sequence motifs important for peptide binding to the human MHC class I molecule, HLA-A2. J Immunol 1992: 149: 3580-7.
    • (1992) J Immunol , vol.149 , pp. 3580-3587
    • Parker, K.C.1    Bednarek, M.A.2    Hull, L.K.3
  • 11
    • 0027311958 scopus 로고
    • Residues in pockets B and F of HLA-B27 are critical in the presentation of an influenza A virus nucleoprotein peptide and influence the stability of peptide-MHC complexes
    • 11. Carreno BM, Winter CC, Taurog JD, Hansen TH, Biddison WE. Residues in pockets B and F of HLA-B27 are critical in the presentation of an influenza A virus nucleoprotein peptide and influence the stability of peptide-MHC complexes, Int Immunol 1993: 5: 353-60.
    • (1993) Int Immunol , vol.5 , pp. 353-360
    • Carreno, B.M.1    Winter, C.C.2    Taurog, J.D.3    Hansen, T.H.4    Biddison, W.E.5
  • 13
    • 0030597348 scopus 로고    scopus 로고
    • A new approach to clustering the amino acids
    • 13. Stanfel LE. A new approach to clustering the amino acids. J Theor Biol 1996: 183: 195-205.
    • (1996) J Theor Biol , vol.183 , pp. 195-205
    • Stanfel, L.E.1
  • 14
    • 0027244254 scopus 로고
    • Characteristics of endogenous peptides eluted from the class I MHC molecule HLA-B7 determined by mass spectrometry and computer modeling
    • 14. Huczko EL, Bodnar WM, Benjamin D et al. Characteristics of endogenous peptides eluted from the class I MHC molecule HLA-B7 determined by mass spectrometry and computer modeling. J Immunol 1993: 151: 2572-87.
    • (1993) J Immunol , vol.151 , pp. 2572-2587
    • Huczko, E.L.1    Bodnar, W.M.2    Benjamin, D.3
  • 17
    • 0032735753 scopus 로고    scopus 로고
    • Nomenclature for factors of the HLA system, 1998
    • 17. Bodmer JG, Marsh SGE, Albert ED et al. Nomenclature for factors of the HLA system, 1998. Tissue Antigens 1999: 53: 407-46.
    • (1999) Tissue Antigens , vol.53 , pp. 407-446
    • Bodmer, J.G.1    Marsh, S.G.E.2    Albert, E.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.