메뉴 건너뛰기




Volumn 91, Issue 4, 2012, Pages 274-286

HLA class I-associated diseases with a suspected autoimmune etiology: HLA-B27 subtypes as a model system

Author keywords

Ankylosing Spondylitis; Autoimmunity; Heavy chain flexibility; HLA B27 subtypes; Infrared spectroscopy; Micropolymorphisms; Multiple Sclerosis; Peptide binding modes; T cell selection; X ray crystallography

Indexed keywords

BETA 2 MICROGLOBULIN; HLA ANTIGEN CLASS 1; HLA B27 ANTIGEN;

EID: 84855809682     PISSN: 01719335     EISSN: 16181298     Source Type: Journal    
DOI: 10.1016/j.ejcb.2011.03.003     Document Type: Short Survey
Times cited : (23)

References (138)
  • 1
    • 79960325833 scopus 로고    scopus 로고
    • The autoimmune tautology
    • Anaya J.-M. The autoimmune tautology. Arthritis Res. Ther. 2010, 12:147.
    • (2010) Arthritis Res. Ther. , vol.12 , pp. 147
    • Anaya, J.-M.1
  • 2
    • 70349577810 scopus 로고    scopus 로고
    • 3D presentation of structural and image data
    • Anon.
    • Anon. 3D presentation of structural and image data. J. Biol. Chem. 2009, 284:21101.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21101
  • 5
    • 0025881471 scopus 로고
    • Peptide binding to empty HLA-B27 molecules of viable human cells
    • Benjamin R.J., Madrigal J.A., Parham P. Peptide binding to empty HLA-B27 molecules of viable human cells. Nature 1991, 351:74-77.
    • (1991) Nature , vol.351 , pp. 74-77
    • Benjamin, R.J.1    Madrigal, J.A.2    Parham, P.3
  • 6
    • 0023903525 scopus 로고
    • High prevalence of the haplotype HLA-A11. B27 in arthritis patients from the highlands of Papua New Guinea
    • Bhatia K., Richens J., Prasad M.L., Koki G. High prevalence of the haplotype HLA-A11. B27 in arthritis patients from the highlands of Papua New Guinea. Tissue Antigens 1988, 31:103-106.
    • (1988) Tissue Antigens , vol.31 , pp. 103-106
    • Bhatia, K.1    Richens, J.2    Prasad, M.L.3    Koki, G.4
  • 7
    • 25144457511 scopus 로고    scopus 로고
    • High-resolution structure of HLA-A*1101 in complex with SARS nucleocapsid peptide
    • Blicher T., Kastrup J.S., Buus S., Gajhede M. High-resolution structure of HLA-A*1101 in complex with SARS nucleocapsid peptide. Acta Crystallogr. D 2005, 61:1031-1040.
    • (2005) Acta Crystallogr. D , vol.61 , pp. 1031-1040
    • Blicher, T.1    Kastrup, J.S.2    Buus, S.3    Gajhede, M.4
  • 10
    • 0034608939 scopus 로고    scopus 로고
    • Direct selection of a human antibody fragment directed against the tumor T-cell epitope HLA-A1-MAGE-A1 from a nonimmunized phage-Fab library
    • Chames P., Hufton S.E., Coulie P.G., Uchanska-Ziegler B., Hoogenboom H.R. Direct selection of a human antibody fragment directed against the tumor T-cell epitope HLA-A1-MAGE-A1 from a nonimmunized phage-Fab library. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:7969-7974.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7969-7974
    • Chames, P.1    Hufton, S.E.2    Coulie, P.G.3    Uchanska-Ziegler, B.4    Hoogenboom, H.R.5
  • 11
    • 0036514392 scopus 로고    scopus 로고
    • Increased HLA-A*11 in Chinese children with steroid-responsive nephrotic syndrome
    • Cheung W., Ren E.C., Chan S.H., Gong W.K., Yap H.K. Increased HLA-A*11 in Chinese children with steroid-responsive nephrotic syndrome. Pediatr. Nephrol. 2002, 17:212-216.
    • (2002) Pediatr. Nephrol. , vol.17 , pp. 212-216
    • Cheung, W.1    Ren, E.C.2    Chan, S.H.3    Gong, W.K.4    Yap, H.K.5
  • 12
    • 77956275082 scopus 로고    scopus 로고
    • On the issue of peptide recognition in T cell development
    • Crites T.J., Varma R. On the issue of peptide recognition in T cell development. Self/Nonself 2010, 1:55-61.
    • (2010) Self/Nonself , vol.1 , pp. 55-61
    • Crites, T.J.1    Varma, R.2
  • 14
    • 0037189545 scopus 로고    scopus 로고
    • HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum
    • Dangoria N.S., DeLay M., Kingsbury D.J., Mear J.P., Uchanska-Ziegler B., Ziegler A., Colbert R.A. HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum. J. Biol. Chem. 2002, 277:23459-23468.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23459-23468
    • Dangoria, N.S.1    DeLay, M.2    Kingsbury, D.J.3    Mear, J.P.4    Uchanska-Ziegler, B.5    Ziegler, A.6    Colbert, R.A.7
  • 16
    • 0034523282 scopus 로고    scopus 로고
    • MHC-linked olfactory receptor loci exhibit polymorphism and contribute to extended HLA/OR haplotypes
    • Ehlers A., Beck S., Forbes S., Trowsdale J., Volz A., Younger R., Ziegler A. MHC-linked olfactory receptor loci exhibit polymorphism and contribute to extended HLA/OR haplotypes. Genome Res. 2000, 10:1968-1978.
    • (2000) Genome Res. , vol.10 , pp. 1968-1978
    • Ehlers, A.1    Beck, S.2    Forbes, S.3    Trowsdale, J.4    Volz, A.5    Younger, R.6    Ziegler, A.7
  • 18
  • 19
    • 79955611721 scopus 로고    scopus 로고
    • Influence of inflammation-related changes on conformational characteristics of HLA-B27 subtypes as detected by IR spectroscopy
    • FEBS J.,in press
    • Fabian, H., Loll, B., Huser, H., Uchanska-Ziegler, B., Naumann, D., Ziegler, A. Influence of inflammation-related changes on conformational characteristics of HLA-B27 subtypes as detected by IR spectroscopy. FEBS J.,in press 2011.
    • (2011)
    • Fabian, H.1    Loll, B.2    Huser, H.3    Uchanska-Ziegler, B.4    Naumann, D.5    Ziegler, A.6
  • 20
    • 0027074320 scopus 로고
    • Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule
    • Fahnestock M.L., Tamir I., Narhi L., Bjorkman P.J. Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule. Science 1992, 258:1658-1662.
    • (1992) Science , vol.258 , pp. 1658-1662
    • Fahnestock, M.L.1    Tamir, I.2    Narhi, L.3    Bjorkman, P.J.4
  • 23
    • 0033935853 scopus 로고    scopus 로고
    • CD8(+) T-cell autoreactivity to an HLA-B27-restricted self-epitope correlates with ankylosing spondylitis
    • Fiorillo M.T., Maragno M., Butler R., Dupuis M.L., Sorrentino R. CD8(+) T-cell autoreactivity to an HLA-B27-restricted self-epitope correlates with ankylosing spondylitis. J. Clin. Invest. 2000, 106:47-53.
    • (2000) J. Clin. Invest. , vol.106 , pp. 47-53
    • Fiorillo, M.T.1    Maragno, M.2    Butler, R.3    Dupuis, M.L.4    Sorrentino, R.5
  • 25
    • 70349575011 scopus 로고    scopus 로고
    • T-cell responses against viral and self-epitopes and HLA-B27 subtypes differentially associated with ankylosing spondylitis
    • Fiorillo M.T., Sorrentino R. T-cell responses against viral and self-epitopes and HLA-B27 subtypes differentially associated with ankylosing spondylitis. Adv. Exp. Med. Biol. 2009, 649:255-262.
    • (2009) Adv. Exp. Med. Biol. , vol.649 , pp. 255-262
    • Fiorillo, M.T.1    Sorrentino, R.2
  • 26
    • 0033975139 scopus 로고    scopus 로고
    • Multiple sclerosis: a modifying influence of HLA class I genes in an HLA class II associated autoimmune disease
    • Fogdell-Hahn A., Ligers A., Grønning M., Hillert J., Olerup O. Multiple sclerosis: a modifying influence of HLA class I genes in an HLA class II associated autoimmune disease. Tissue Antigens 2000, 55:140-148.
    • (2000) Tissue Antigens , vol.55 , pp. 140-148
    • Fogdell-Hahn, A.1    Ligers, A.2    Grønning, M.3    Hillert, J.4    Olerup, O.5
  • 28
    • 78649810797 scopus 로고    scopus 로고
    • Mutational analysis reveals a complex interplay of peptide binding and multiple biological features of HLA-B27
    • Galocha B., López de Castro J.A. Mutational analysis reveals a complex interplay of peptide binding and multiple biological features of HLA-B27. J. Biol. Chem. 2010, 285:39180-39190.
    • (2010) J. Biol. Chem. , vol.285 , pp. 39180-39190
    • Galocha, B.1    López de Castro, J.A.2
  • 29
    • 0026529908 scopus 로고
    • HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides
    • Garboczi D.N., Hung D.T., Wiley D.C. HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:3429-3433.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 3429-3433
    • Garboczi, D.N.1    Hung, D.T.2    Wiley, D.C.3
  • 33
    • 64149127259 scopus 로고    scopus 로고
    • Expression, purification and preliminary X-ray crystallographic analysis of the chicken MHC class I molecule YF1*7.1
    • Hee C.S., Gao S., Miller M.M., Goto R., Ziegler A., Daumke O., Uchanska-Ziegler B. Expression, purification and preliminary X-ray crystallographic analysis of the chicken MHC class I molecule YF1*7.1. Acta Cryst. F 2009, 65:422-425.
    • (2009) Acta Cryst. F , vol.65 , pp. 422-425
    • Hee, C.S.1    Gao, S.2    Miller, M.M.3    Goto, R.4    Ziegler, A.5    Daumke, O.6    Uchanska-Ziegler, B.7
  • 35
    • 0019290163 scopus 로고
    • Expression of major histocompatibility antigens on human thymocytes studied using monoclonal antibodies
    • Heinrichs H., Wernet P., Ziegler A. Expression of major histocompatibility antigens on human thymocytes studied using monoclonal antibodies. Immunogenetics 1980, 11:629-635.
    • (1980) Immunogenetics , vol.11 , pp. 629-635
    • Heinrichs, H.1    Wernet, P.2    Ziegler, A.3
  • 38
    • 62849108693 scopus 로고    scopus 로고
    • An encyclopedic effort to make 3D structures easier to understand
    • Hodis E., Sussman J.L. An encyclopedic effort to make 3D structures easier to understand. Trends Biochem. Sci. 2009, 34:100-101.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 100-101
    • Hodis, E.1    Sussman, J.L.2
  • 39
    • 74549185929 scopus 로고    scopus 로고
    • Why CD8+ T cells need diversity when growing up
    • Hogquist K.A., Xing Y. Why CD8+ T cells need diversity when growing up. Immunity 2010, 32:5-6.
    • (2010) Immunity , vol.32 , pp. 5-6
    • Hogquist, K.A.1    Xing, Y.2
  • 41
    • 0034671891 scopus 로고    scopus 로고
    • Functional requirement for class I MHC in CNS development and plasticity
    • Huh G.S., Boulanger L.M., Du H., Riquelme P.A., Brotz T.M., Shatz C.J. Functional requirement for class I MHC in CNS development and plasticity. Science 2000, 290:2155-2159.
    • (2000) Science , vol.290 , pp. 2155-2159
    • Huh, G.S.1    Boulanger, L.M.2    Du, H.3    Riquelme, P.A.4    Brotz, T.M.5    Shatz, C.J.6
  • 44
    • 19944430890 scopus 로고    scopus 로고
    • A major histocompatibility complex:peptide-restricted antibody and T cell receptor molecules recognize their target by distinct binding modes. Crystal structure of human leukocyte antigen (HLA)-A1:MAGE-A1 in complex with Fab-Hyb3
    • Hülsmeyer M., Chames P., Hillig R.C., Stanfield R.L., Held G., Coulie P.G., Alings C., Wille G., Saenger W., Uchanska-Ziegler B., Hoogenboom H.R., Ziegler A. A major histocompatibility complex:peptide-restricted antibody and T cell receptor molecules recognize their target by distinct binding modes. Crystal structure of human leukocyte antigen (HLA)-A1:MAGE-A1 in complex with Fab-Hyb3. J. Biol. Chem. 2005, 280:2972-2980.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2972-2980
    • Hülsmeyer, M.1    Chames, P.2    Hillig, R.C.3    Stanfield, R.L.4    Held, G.5    Coulie, P.G.6    Alings, C.7    Wille, G.8    Saenger, W.9    Uchanska-Ziegler, B.10    Hoogenboom, H.R.11    Ziegler, A.12
  • 46
    • 34848813147 scopus 로고    scopus 로고
    • Thymic selection stifles TCR reactivity with the main chain structure of MHC and forces interactions with the peptide side chains
    • Huseby E.S., Kappler J.W., Marrack P. Thymic selection stifles TCR reactivity with the main chain structure of MHC and forces interactions with the peptide side chains. Mol. Immunol. 2008, 45:599-606.
    • (2008) Mol. Immunol. , vol.45 , pp. 599-606
    • Huseby, E.S.1    Kappler, J.W.2    Marrack, P.3
  • 47
    • 12944320844 scopus 로고    scopus 로고
    • Comparative genomics of major histocompatibility complexes
    • Kelley J., Walter L., Trowsdale J. Comparative genomics of major histocompatibility complexes. Immunogenetics 2005, 56:683-695.
    • (2005) Immunogenetics , vol.56 , pp. 683-695
    • Kelley, J.1    Walter, L.2    Trowsdale, J.3
  • 49
    • 72949104779 scopus 로고    scopus 로고
    • Antigen presentation in the thymus for positive selection and central tolerance induction
    • Klein L., Hinterberger M., Wirnsberger G., Kyewski B. Antigen presentation in the thymus for positive selection and central tolerance induction. Nat. Rev. Immunol. 2009, 9:833-844.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 833-844
    • Klein, L.1    Hinterberger, M.2    Wirnsberger, G.3    Kyewski, B.4
  • 52
    • 34447345931 scopus 로고    scopus 로고
    • Expression, purification and preliminary X-ray crystallographic analysis of the human major histocompatibility antigen HLA-B*1402 in complex with a viral and with a self-peptide
    • Kumar P., Vahedi-Farid A., Merino E., López de Castro J.A., Volz A., Ziegler A., Saenger W., Uchanska-Ziegler B. Expression, purification and preliminary X-ray crystallographic analysis of the human major histocompatibility antigen HLA-B*1402 in complex with a viral and with a self-peptide. Acta Cryst. F 2007, 63:631-634.
    • (2007) Acta Cryst. F , vol.63 , pp. 631-634
    • Kumar, P.1    Vahedi-Farid, A.2    Merino, E.3    López de Castro, J.A.4    Volz, A.5    Ziegler, A.6    Saenger, W.7    Uchanska-Ziegler, B.8
  • 55
    • 58149477056 scopus 로고    scopus 로고
    • Conformational changes within the HLA-A1:MAGE-A1 complex induced by binding of a recombinant antibody fragment with TCR-like specificity
    • Kumar P., Vahedi-Faridi A., Saenger W., Ziegler A., Uchanska-Ziegler B. Conformational changes within the HLA-A1:MAGE-A1 complex induced by binding of a recombinant antibody fragment with TCR-like specificity. Prot. Sci. 2009, 18:37-49.
    • (2009) Prot. Sci. , vol.18 , pp. 37-49
    • Kumar, P.1    Vahedi-Faridi, A.2    Saenger, W.3    Ziegler, A.4    Uchanska-Ziegler, B.5
  • 58
    • 2442489882 scopus 로고    scopus 로고
    • Structures of HLA-A*1101 complexed with immunodominant nonamer and decamer HIV-1 epitopes clearly reveal the presence of a middle, secondary anchor residue
    • Li L., Bouvier M. Structures of HLA-A*1101 complexed with immunodominant nonamer and decamer HIV-1 epitopes clearly reveal the presence of a middle, secondary anchor residue. J. Immunol. 2004, 172:6175-6184.
    • (2004) J. Immunol. , vol.172 , pp. 6175-6184
    • Li, L.1    Bouvier, M.2
  • 59
    • 21344470461 scopus 로고    scopus 로고
    • A biochemical and structural analysis of genetic diversity within the HLA-A*11 subtype
    • Li L., Chen W., Bouvier M. A biochemical and structural analysis of genetic diversity within the HLA-A*11 subtype. Immunogenetics 2005, 57:315-325.
    • (2005) Immunogenetics , vol.57 , pp. 315-325
    • Li, L.1    Chen, W.2    Bouvier, M.3
  • 60
    • 33744496810 scopus 로고    scopus 로고
    • Preliminary X-ray diffraction analysis of crystals from the recombinantly expressed human major histocompatibility antigen HLA-B*2704 in complex with a viral peptide and with a self-peptide
    • Loll B., Zawacka A., Biesiadka J., Petter C., Rückert C., Saenger W., Uchanska-Ziegler B., Ziegler A. Preliminary X-ray diffraction analysis of crystals from the recombinantly expressed human major histocompatibility antigen HLA-B*2704 in complex with a viral peptide and with a self-peptide. Acta Cryst. F 2004, 61:939-941.
    • (2004) Acta Cryst. F , vol.61 , pp. 939-941
    • Loll, B.1    Zawacka, A.2    Biesiadka, J.3    Petter, C.4    Rückert, C.5    Saenger, W.6    Uchanska-Ziegler, B.7    Ziegler, A.8
  • 61
    • 79251588410 scopus 로고    scopus 로고
    • Loss of recognition by cross-reactive T cells and its relation to C-terminus-induced conformational reorientation of an HLA-B*2705-bound peptide
    • Loll B., Rückert C., Hee C.S., Saenger W., Uchanska-Ziegler B., Ziegler A. Loss of recognition by cross-reactive T cells and its relation to C-terminus-induced conformational reorientation of an HLA-B*2705-bound peptide. Prot. Sci. 2011, 20:278-290.
    • (2011) Prot. Sci. , vol.20 , pp. 278-290
    • Loll, B.1    Rückert, C.2    Hee, C.S.3    Saenger, W.4    Uchanska-Ziegler, B.5    Ziegler, A.6
  • 62
    • 43849110108 scopus 로고    scopus 로고
    • Peptides: the cornerstone of HLA-B27 biology and pathogenetic role in spondyloarthritis
    • López de Castro J.A. Peptides: the cornerstone of HLA-B27 biology and pathogenetic role in spondyloarthritis. Tissue Antigens 2007, 71:495-506.
    • (2007) Tissue Antigens , vol.71 , pp. 495-506
    • de López, C.J.A.1
  • 66
    • 0028943275 scopus 로고
    • The three-dimensional structure of peptide-MHC complexes
    • Madden D.R. The three-dimensional structure of peptide-MHC complexes. Annu. Rev. Immunol. 1995, 13:587-622.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 587-622
    • Madden, D.R.1
  • 67
    • 0026794581 scopus 로고
    • The three-dimensional structure of HLA-B27 at 2.1A resolution suggests a general mechanism for tight peptide binding to MHC
    • Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C. The three-dimensional structure of HLA-B27 at 2.1A resolution suggests a general mechanism for tight peptide binding to MHC. Cell 1992, 70:1035-1048.
    • (1992) Cell , vol.70 , pp. 1035-1048
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 68
    • 0028944083 scopus 로고
    • Strong association between major histocompatibility complex class I antigens and immune aberrations among healthy Venezuelans
    • Makhatadze N.J., Sanches-Llamozas P., Franco M.T., Layrisse Z. Strong association between major histocompatibility complex class I antigens and immune aberrations among healthy Venezuelans. Hum. Immunol. 1995, 42:189-194.
    • (1995) Hum. Immunol. , vol.42 , pp. 189-194
    • Makhatadze, N.J.1    Sanches-Llamozas, P.2    Franco, M.T.3    Layrisse, Z.4
  • 70
    • 0031571122 scopus 로고    scopus 로고
    • Heterogeneity in rates of recombination in the 6 Mb region telomeric to the human major histocompatibility complex
    • Malfroy L., Roth M., Borot N., Carrington M., Volz A., Ziegler A., Coppin H. Heterogeneity in rates of recombination in the 6 Mb region telomeric to the human major histocompatibility complex. Genomics 1997, 43:226-231.
    • (1997) Genomics , vol.43 , pp. 226-231
    • Malfroy, L.1    Roth, M.2    Borot, N.3    Carrington, M.4    Volz, A.5    Ziegler, A.6    Coppin, H.7
  • 71
    • 0032171644 scopus 로고    scopus 로고
    • A very high level of crossreactivity is an essential feature of the T-cell receptor
    • Mason D. A very high level of crossreactivity is an essential feature of the T-cell receptor. Immunol. Today. 1998, 19:395-404.
    • (1998) Immunol. Today. , vol.19 , pp. 395-404
    • Mason, D.1
  • 72
    • 53649100391 scopus 로고    scopus 로고
    • Tasmanian devil facial tumour disease: lessons for conservation biology
    • McCallum H. Tasmanian devil facial tumour disease: lessons for conservation biology. Trends Ecol. Evol. 2008, 23:631-637.
    • (2008) Trends Ecol. Evol. , vol.23 , pp. 631-637
    • McCallum, H.1
  • 73
    • 66149136493 scopus 로고    scopus 로고
    • H2-Kb and H2-Db regulate cerebellar long-term depression and limit motor learning
    • McConnell M.J., Huang Y.H., Datwani A., Shatz C.J. H2-Kb and H2-Db regulate cerebellar long-term depression and limit motor learning. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:6784-6789.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 6784-6789
    • McConnell, M.J.1    Huang, Y.H.2    Datwani, A.3    Shatz, C.J.4
  • 75
    • 33845416108 scopus 로고    scopus 로고
    • The major histocompatibility complex, sexual selection and mate choice
    • Milinski M. The major histocompatibility complex, sexual selection and mate choice. Annu. Rev. Ecol. Evol. Syst. 2006, 37:159-186.
    • (2006) Annu. Rev. Ecol. Evol. Syst. , vol.37 , pp. 159-186
    • Milinski, M.1
  • 77
    • 0020570403 scopus 로고
    • Quantitative and qualitative differences in the distribution of HLA class I antigenic determinants in the human thymic compartments
    • Müller C., Stein H., Ziegler A., Wernet P. Quantitative and qualitative differences in the distribution of HLA class I antigenic determinants in the human thymic compartments. Eur. J. Immunol. 1983, 13:414-418.
    • (1983) Eur. J. Immunol. , vol.13 , pp. 414-418
    • Müller, C.1    Stein, H.2    Ziegler, A.3    Wernet, P.4
  • 80
    • 53149153573 scopus 로고    scopus 로고
    • Molecular determinants of major histocompatibility complex class I complex stability: shaping antigenic features through short range and long range electrostatic interactions
    • Narzi D., Winkler K., Saidowsky J., Misselwitz R., Ziegler A., Böckmann R.A., Alexiev U. Molecular determinants of major histocompatibility complex class I complex stability: shaping antigenic features through short range and long range electrostatic interactions. J. Biol. Chem. 2008, 283:23093-23103.
    • (2008) J. Biol. Chem. , vol.283 , pp. 23093-23103
    • Narzi, D.1    Winkler, K.2    Saidowsky, J.3    Misselwitz, R.4    Ziegler, A.5    Böckmann, R.A.6    Alexiev, U.7
  • 81
    • 0028151819 scopus 로고
    • Negative selection of lymphocytes
    • Nossal G.J. Negative selection of lymphocytes. Cell 1994, 76:229-239.
    • (1994) Cell , vol.76 , pp. 229-239
    • Nossal, G.J.1
  • 82
    • 0026447431 scopus 로고
    • The optimal number of major histocompatibility complex molecules in an individual
    • Nowak M.A., Tarczy-Hornoch K., Austyn J.M. The optimal number of major histocompatibility complex molecules in an individual. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:10896-10899.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10896-10899
    • Nowak, M.A.1    Tarczy-Hornoch, K.2    Austyn, J.M.3
  • 85
    • 0031841345 scopus 로고    scopus 로고
    • How do major histocompatibility complex genes influence odor and mating preferences?
    • Penn D., Potts W.K. How do major histocompatibility complex genes influence odor and mating preferences?. Adv. Immunol. 1998, 69:411-436.
    • (1998) Adv. Immunol. , vol.69 , pp. 411-436
    • Penn, D.1    Potts, W.K.2
  • 86
    • 33644998297 scopus 로고    scopus 로고
    • The evolutionary ecology of the major histocompatibility complex
    • Piertney S.B., Oliver M.K. The evolutionary ecology of the major histocompatibility complex. Heredity 2006, 96:7-21.
    • (2006) Heredity , vol.96 , pp. 7-21
    • Piertney, S.B.1    Oliver, M.K.2
  • 88
    • 0042665284 scopus 로고    scopus 로고
    • Sequence variability analysis of human class I and class II MHC molecules: functional and structural correlates of amino acid polymorphisms
    • Reche P.A., Reinherz E.L. Sequence variability analysis of human class I and class II MHC molecules: functional and structural correlates of amino acid polymorphisms. J. Mol. Biol. 2003, 331:623-641.
    • (2003) J. Mol. Biol. , vol.331 , pp. 623-641
    • Reche, P.A.1    Reinherz, E.L.2
  • 89
    • 18744368784 scopus 로고    scopus 로고
    • EPIMHC: a curated database of MHC-binding peptides for customized computational vaccinology
    • Reche P.A., Zhang H., Glutting J.P., Reinherz E.L. EPIMHC: a curated database of MHC-binding peptides for customized computational vaccinology. Bioinformatics 2005, 21:2140-2141.
    • (2005) Bioinformatics , vol.21 , pp. 2140-2141
    • Reche, P.A.1    Zhang, H.2    Glutting, J.P.3    Reinherz, E.L.4
  • 90
    • 0034023796 scopus 로고    scopus 로고
    • Structurally diverse forms of HLA-B27 molecules are displayed in vivo in a cell type-dependent manner
    • Rehm A., Rohr A., Seitz C., Wonigeit K., Ziegler A., Uchanska-Ziegler B. Structurally diverse forms of HLA-B27 molecules are displayed in vivo in a cell type-dependent manner. Hum. Immunol. 2000, 61:408-418.
    • (2000) Hum. Immunol. , vol.61 , pp. 408-418
    • Rehm, A.1    Rohr, A.2    Seitz, C.3    Wonigeit, K.4    Ziegler, A.5    Uchanska-Ziegler, B.6
  • 96
    • 77956011249 scopus 로고    scopus 로고
    • Variation and linkage disequilibrium within odorant receptor gene clusters linked to the human major histocompatibility complex
    • Santos P.S.C., Uehara C.J.S., Ziegler A., Uchanska-Ziegler B., Bicalho M.G. Variation and linkage disequilibrium within odorant receptor gene clusters linked to the human major histocompatibility complex. Hum. Immunol. 2010, 71:843-850.
    • (2010) Hum. Immunol. , vol.71 , pp. 843-850
    • Santos, P.S.C.1    Uehara, C.J.S.2    Ziegler, A.3    Uchanska-Ziegler, B.4    Bicalho, M.G.5
  • 98
    • 0028675018 scopus 로고
    • Are MHC-bound peptides a nuisance for positive selection?
    • Schumacher T.N., Ploegh H.L. Are MHC-bound peptides a nuisance for positive selection?. Immunity 1994, 1:721-723.
    • (1994) Immunity , vol.1 , pp. 721-723
    • Schumacher, T.N.1    Ploegh, H.L.2
  • 100
    • 77955355152 scopus 로고    scopus 로고
    • MHC gene copy number variation in Tasmanian devils: implications for the spread of a contagious cancer
    • Siddle H.V., Marzec J., Cheng Y., Jones M., Belov K. MHC gene copy number variation in Tasmanian devils: implications for the spread of a contagious cancer. Proc. Biol. Sci. 2010, 277:2001-2006.
    • (2010) Proc. Biol. Sci. , vol.277 , pp. 2001-2006
    • Siddle, H.V.1    Marzec, J.2    Cheng, Y.3    Jones, M.4    Belov, K.5
  • 101
    • 0026621224 scopus 로고
    • Atomic structure of a human MHC molecule presenting an influenza virus peptide
    • Silver M.L., Guo H.C., Strominger J.L., Wiley D.C. Atomic structure of a human MHC molecule presenting an influenza virus peptide. Nature 1992, 360:367-369.
    • (1992) Nature , vol.360 , pp. 367-369
    • Silver, M.L.1    Guo, H.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 104
    • 0029775278 scopus 로고    scopus 로고
    • The obese strain chicken as a model for human Hashimoto's thyroiditis
    • Sundick R.S., Bagchi N., Brown T.R. The obese strain chicken as a model for human Hashimoto's thyroiditis. Exp. Clin. Endocrinol. Diabetes 1996, 104(Suppl. 3):4-6.
    • (1996) Exp. Clin. Endocrinol. Diabetes , vol.104 , Issue.SUPPL. 3 , pp. 4-6
    • Sundick, R.S.1    Bagchi, N.2    Brown, T.R.3
  • 106
    • 70349573919 scopus 로고    scopus 로고
    • Animal models of spondyloarthritis
    • Taurog J.D. Animal models of spondyloarthritis. Adv. Exp. Med. Biol. 2009, 649:245-254.
    • (2009) Adv. Exp. Med. Biol. , vol.649 , pp. 245-254
    • Taurog, J.D.1
  • 107
    • 78649751253 scopus 로고    scopus 로고
    • The role of HLA-B27 in spondyloarthritis
    • Taurog J.D. The role of HLA-B27 in spondyloarthritis. J. Rheumatol. 2010, 37:2006-2016.
    • (2010) J. Rheumatol. , vol.37 , pp. 2006-2016
    • Taurog, J.D.1
  • 108
    • 73249129708 scopus 로고    scopus 로고
    • Genetics and genomics of ankylosing spondylitis
    • Thomas G.P., Brown M.A. Genetics and genomics of ankylosing spondylitis. Immunol. Rev. 2010, 233:162-180.
    • (2010) Immunol. Rev. , vol.233 , pp. 162-180
    • Thomas, G.P.1    Brown, M.A.2
  • 109
    • 33645852216 scopus 로고    scopus 로고
    • Additional human beta2-microglobulin curbs HLA-B27 misfolding and promotes arthritis and spondylitis without colitis in male HLA-B27-transgenic rats
    • Tran T.M., Dorris M.L., Satumtira N., Richardson J.A., Hammer R.E., Shang J., Taurog J.D. Additional human beta2-microglobulin curbs HLA-B27 misfolding and promotes arthritis and spondylitis without colitis in male HLA-B27-transgenic rats. Arthritis Rheum. 2006, 54:1317-1327.
    • (2006) Arthritis Rheum. , vol.54 , pp. 1317-1327
    • Tran, T.M.1    Dorris, M.L.2    Satumtira, N.3    Richardson, J.A.4    Hammer, R.E.5    Shang, J.6    Taurog, J.D.7
  • 110
    • 0035725583 scopus 로고    scopus 로고
    • Combination of HLA-A and HLA class II alleles controls the susceptibility to rheumatoid arthritis
    • Tsuchiya K., Kimura A., Kondo M., Nishimura Y., Sasazuki T. Combination of HLA-A and HLA class II alleles controls the susceptibility to rheumatoid arthritis. Tissue Antigens 2001, 58:395-401.
    • (2001) Tissue Antigens , vol.58 , pp. 395-401
    • Tsuchiya, K.1    Kimura, A.2    Kondo, M.3    Nishimura, Y.4    Sasazuki, T.5
  • 111
    • 50849117543 scopus 로고    scopus 로고
    • Dragging (and zooming and rotating) publication of 3D molecular structures into the 21st century
    • Tyzack J.K. Dragging (and zooming and rotating) publication of 3D molecular structures into the 21st century. Trends Biochem. Sci. 2008, 33:405-407.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 405-407
    • Tyzack, J.K.1
  • 114
    • 33847399185 scopus 로고    scopus 로고
    • On the reactivity of monoclonal antibodies specific for different forms of HLA class I molecules
    • Uchanska-Ziegler B., Ziegler A. On the reactivity of monoclonal antibodies specific for different forms of HLA class I molecules. Rheumatology (Oxford) 2007, 46:555-556.
    • (2007) Rheumatology (Oxford) , vol.46 , pp. 555-556
    • Uchanska-Ziegler, B.1    Ziegler, A.2
  • 115
    • 49149094592 scopus 로고    scopus 로고
    • HLA-B27 transgenic rats, amyloid deposits, and spondyloarthropathies
    • Uchanska-Ziegler B., Ziegler A. HLA-B27 transgenic rats, amyloid deposits, and spondyloarthropathies. Mod. Rheumatol. 2008, 18:425-426.
    • (2008) Mod. Rheumatol. , vol.18 , pp. 425-426
    • Uchanska-Ziegler, B.1    Ziegler, A.2
  • 118
    • 0028032155 scopus 로고
    • Positive selection of lymphocytes
    • von Boehmer H. Positive selection of lymphocytes. Cell 1994, 76:219-228.
    • (1994) Cell , vol.76 , pp. 219-228
    • von Boehmer, H.1
  • 121
    • 35348937601 scopus 로고    scopus 로고
    • Natural MHC class I polymorphism controls the pathway of peptide dissociation from HLA-B27 complexes
    • Winkler K., Winter A., Rueckert C., Uchanska-Ziegler B., Alexiev U. Natural MHC class I polymorphism controls the pathway of peptide dissociation from HLA-B27 complexes. Biophys. J. 2007, 93:2743-2755.
    • (2007) Biophys. J. , vol.93 , pp. 2743-2755
    • Winkler, K.1    Winter, A.2    Rueckert, C.3    Uchanska-Ziegler, B.4    Alexiev, U.5
  • 122
    • 58249091800 scopus 로고    scopus 로고
    • Does intra-individual major histocompatibility complex diversity keep a golden mean?
    • Woelfing B., Traulsen A., Milinski M., Boehm T. Does intra-individual major histocompatibility complex diversity keep a golden mean?. Phil. Trans. R. Soc. B 2009, 364:117-128.
    • (2009) Phil. Trans. R. Soc. B , vol.364 , pp. 117-128
    • Woelfing, B.1    Traulsen, A.2    Milinski, M.3    Boehm, T.4
  • 124
    • 0031543892 scopus 로고    scopus 로고
    • Biology of chromosome 6
    • Ziegler A. Biology of chromosome 6. DNA Sequence 1997, 8:189-202.
    • (1997) DNA Sequence , vol.8 , pp. 189-202
    • Ziegler, A.1
  • 125
    • 0345491351 scopus 로고    scopus 로고
    • Moleküle des MHC und olfaktorische Rezeptoren: Mögliche Bedeutung im Rahmen der Reproduktion
    • Ziegler A. Moleküle des MHC und olfaktorische Rezeptoren: Mögliche Bedeutung im Rahmen der Reproduktion. J. Fertil. Reprod. 2003, 13:14-18.
    • (2003) J. Fertil. Reprod. , vol.13 , pp. 14-18
    • Ziegler, A.1
  • 126
    • 0017125539 scopus 로고
    • Chemical properties of two antigens controlled by the major histocompatibility complex of the chicken
    • Ziegler A., Pink J.R.L. Chemical properties of two antigens controlled by the major histocompatibility complex of the chicken. J. Biol. Chem. 1976, 251:5391-5396.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5391-5396
    • Ziegler, A.1    Pink, J.R.L.2
  • 128
    • 0036019002 scopus 로고    scopus 로고
    • Possible roles for products of polymorphic MHC and linked olfactory receptor genes during selection processes in reproduction
    • Ziegler A., Dohr G., Uchanska-Ziegler B. Possible roles for products of polymorphic MHC and linked olfactory receptor genes during selection processes in reproduction. Am. J. Reprod. Immunol. 2002, 48:34-42.
    • (2002) Am. J. Reprod. Immunol. , vol.48 , pp. 34-42
    • Ziegler, A.1    Dohr, G.2    Uchanska-Ziegler, B.3
  • 132
    • 49249122114 scopus 로고    scopus 로고
    • Systematic comparison and reconstruction of sea urchin (Echinoidea) internal anatomy: a novel approach using magnetic resonance imaging
    • Ziegler A., Faber C., Mueller S., Bartolomaeus T. Systematic comparison and reconstruction of sea urchin (Echinoidea) internal anatomy: a novel approach using magnetic resonance imaging. BMC Biol. 2008, 6:33.
    • (2008) BMC Biol. , vol.6 , pp. 33
    • Ziegler, A.1    Faber, C.2    Mueller, S.3    Bartolomaeus, T.4
  • 134
    • 70349567381 scopus 로고    scopus 로고
    • Implications of structural and thermodynamic studies of HLA-B27 subtypes exhibiting differential association with ankylosing spondylitis
    • Ziegler A., Loll B., Misselwitz R., Uchanska-Ziegler B. Implications of structural and thermodynamic studies of HLA-B27 subtypes exhibiting differential association with ankylosing spondylitis. Adv. Exp. Med. Biol. 2009, 649:177-195.
    • (2009) Adv. Exp. Med. Biol. , vol.649 , pp. 177-195
    • Ziegler, A.1    Loll, B.2    Misselwitz, R.3    Uchanska-Ziegler, B.4
  • 137
    • 77957923458 scopus 로고    scopus 로고
    • Origin and evolutionary plasticity of the gastric caecum in sea urchins (Echinodermata: Echinoidea)
    • Ziegler A., Mooi R., Rolet G., de Ridder C. Origin and evolutionary plasticity of the gastric caecum in sea urchins (Echinodermata: Echinoidea). BMC Evol. Biol. 2010, 10:313.
    • (2010) BMC Evol. Biol. , vol.10 , pp. 313
    • Ziegler, A.1    Mooi, R.2    Rolet, G.3    de Ridder, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.