메뉴 건너뛰기




Volumn 85, Issue 3, 2015, Pages 155-166

TAPBPR: A new player in the MHC class I presentation pathway

Author keywords

Antigen processing and presentation; Disease association; Human; Major histocompatibility complex (MHC); Tapasin; TAPBPR TAPBPL

Indexed keywords

AMINOPEPTIDASE; CALNEXIN; CALRETICULIN; CHAPERONE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; TAPASIN; TAPASIN RELATED PROTEIN TAPBPR; UDP GLUCOSE GLYCOPROTEIN GLUCOSYLTRANSFERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE; CARRIER PROTEIN; HLA ANTIGEN CLASS 1; IMMUNOGLOBULIN; MEMBRANE PROTEIN; PEPTIDE; TAPBPL PROTEIN, HUMAN;

EID: 84923376447     PISSN: 00012815     EISSN: 13990039     Source Type: Journal    
DOI: 10.1111/tan.12538     Document Type: Review
Times cited : (21)

References (107)
  • 1
    • 77956297939 scopus 로고    scopus 로고
    • The cell biology of major histocompatibility complex class I assembly: towards a molecular understanding
    • Van Hateren A, James E, Bailey A, Phillips A, Dalchau N, Elliott T. The cell biology of major histocompatibility complex class I assembly: towards a molecular understanding. Tissue Antigens 2010: 76: 259-75.
    • (2010) Tissue Antigens , vol.76 , pp. 259-275
    • Van Hateren, A.1    James, E.2    Bailey, A.3    Phillips, A.4    Dalchau, N.5    Elliott, T.6
  • 2
    • 0030239693 scopus 로고    scopus 로고
    • Defective ribosomal products (DRiPs): a major source of antigenic peptides for MHC class I molecules?
    • Yewdell JW, Anton LC, Bennink JR. Defective ribosomal products (DRiPs): a major source of antigenic peptides for MHC class I molecules? J Immunol 1996: 157: 1823-6.
    • (1996) J Immunol , vol.157 , pp. 1823-1826
    • Yewdell, J.W.1    Anton, L.C.2    Bennink, J.R.3
  • 3
    • 34247585533 scopus 로고    scopus 로고
    • Rethinking peptide supply to MHC class I molecules
    • Eisenlohr LC, Huang L, Golovina TN. Rethinking peptide supply to MHC class I molecules. Nat Rev Immunol 2007: 7: 403-10.
    • (2007) Nat Rev Immunol , vol.7 , pp. 403-410
    • Eisenlohr, L.C.1    Huang, L.2    Golovina, T.N.3
  • 4
    • 79961013520 scopus 로고    scopus 로고
    • Running the gauntlet: from peptide generation to antigen presentation by MHC class I
    • Saunders PM, van Endert P. Running the gauntlet: from peptide generation to antigen presentation by MHC class I. Tissue Antigens 2011: 78: 161-70.
    • (2011) Tissue Antigens , vol.78 , pp. 161-170
    • Saunders, P.M.1    van Endert, P.2
  • 5
    • 79961016996 scopus 로고    scopus 로고
    • Major source of antigenic peptides for the MHC class I pathway is produced during the pioneer round of mRNA translation
    • Apcher S, Daskalogianni C, Lejeune F et al. Major source of antigenic peptides for the MHC class I pathway is produced during the pioneer round of mRNA translation. Proc Natl Acad Sci U S A 2011: 108: 11572-7.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 11572-11577
    • Apcher, S.1    Daskalogianni, C.2    Lejeune, F.3
  • 6
    • 84887046208 scopus 로고    scopus 로고
    • Translation of pre-spliced RNAs in the nuclear compartment generates peptides for the MHC class I pathway
    • Apcher S, Millot G, Daskalogianni C, Scherl A, Manoury B, Fahraeus R. Translation of pre-spliced RNAs in the nuclear compartment generates peptides for the MHC class I pathway. Proc Natl Acad Sci U S A 2013: 110: 17951-6.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 17951-17956
    • Apcher, S.1    Millot, G.2    Daskalogianni, C.3    Scherl, A.4    Manoury, B.5    Fahraeus, R.6
  • 7
    • 84862991256 scopus 로고    scopus 로고
    • Leucine-tRNA initiates at CUG start codons for protein synthesis and presentation by MHC class I
    • Starck SR, Jiang V, Pavon-Eternod M et al. Leucine-tRNA initiates at CUG start codons for protein synthesis and presentation by MHC class I. Science 2012: 336: 1719-23.
    • (2012) Science , vol.336 , pp. 1719-1723
    • Starck, S.R.1    Jiang, V.2    Pavon-Eternod, M.3
  • 8
    • 0025633562 scopus 로고
    • MHC class II region encoding proteins related to the multidrug resistance family of transmembrane transporters
    • Deverson EV, Gow IR, Coadwell WJ, Monaco JJ, Butcher GW, Howard JC. MHC class II region encoding proteins related to the multidrug resistance family of transmembrane transporters. Nature 1990: 348: 738-41.
    • (1990) Nature , vol.348 , pp. 738-741
    • Deverson, E.V.1    Gow, I.R.2    Coadwell, W.J.3    Monaco, J.J.4    Butcher, G.W.5    Howard, J.C.6
  • 9
    • 0025688348 scopus 로고
    • Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters
    • Trowsdale J, Hanson I, Mockridge I, Beck S, Townsend A, Kelly A. Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters. Nature 1990: 348: 741-4.
    • (1990) Nature , vol.348 , pp. 741-744
    • Trowsdale, J.1    Hanson, I.2    Mockridge, I.3    Beck, S.4    Townsend, A.5    Kelly, A.6
  • 10
    • 0025604835 scopus 로고
    • A gene in the human major histocompatibility complex class II region controlling the class I antigen presentation pathway
    • Spies T, Bresnahan M, Bahram S et al. A gene in the human major histocompatibility complex class II region controlling the class I antigen presentation pathway. Nature 1990: 348: 744-7.
    • (1990) Nature , vol.348 , pp. 744-747
    • Spies, T.1    Bresnahan, M.2    Bahram, S.3
  • 11
    • 0022718930 scopus 로고
    • Impaired assembly and transport of HLA-A and -B antigens in a mutant TxB cell hybrid
    • Salter RD, Cresswell P. Impaired assembly and transport of HLA-A and -B antigens in a mutant TxB cell hybrid. EMBO J 1986: 5: 943-9.
    • (1986) EMBO J , vol.5 , pp. 943-949
    • Salter, R.D.1    Cresswell, P.2
  • 12
    • 0025845432 scopus 로고
    • Restored expression of major histocompatibility class I molecules by gene transfer of a putative peptide transporter
    • Spies T, DeMars R. Restored expression of major histocompatibility class I molecules by gene transfer of a putative peptide transporter. Nature 1991: 351: 323-4.
    • (1991) Nature , vol.351 , pp. 323-324
    • Spies, T.1    DeMars, R.2
  • 13
    • 0026500826 scopus 로고
    • Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer
    • Spies T, Cerundolo V, Colonna M, Cresswell P, Townsend A, DeMars R. Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. Nature 1992: 355: 644-6.
    • (1992) Nature , vol.355 , pp. 644-646
    • Spies, T.1    Cerundolo, V.2    Colonna, M.3    Cresswell, P.4    Townsend, A.5    DeMars, R.6
  • 14
    • 0036902105 scopus 로고    scopus 로고
    • An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides
    • Saric T, Chang SC, Hattori A et al. An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat Immunol 2002: 3: 1169-76.
    • (2002) Nat Immunol , vol.3 , pp. 1169-1176
    • Saric, T.1    Chang, S.C.2    Hattori, A.3
  • 15
    • 0037015624 scopus 로고    scopus 로고
    • ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum
    • Serwold T, Gonzalez F, Kim J, Jacob R, Shastri N. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 2002: 419: 480-3.
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 16
  • 17
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • York IA, Chang SC, Saric T et al. The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat Immunol 2002: 3: 1177-84.
    • (2002) Nat Immunol , vol.3 , pp. 1177-1184
    • York, I.A.1    Chang, S.C.2    Saric, T.3
  • 18
    • 84881396597 scopus 로고    scopus 로고
    • ERAAP and tapasin independently edit the amino and carboxyl termini of MHC class I peptides
    • Kanaseki T, Lind KC, Escobar H et al. ERAAP and tapasin independently edit the amino and carboxyl termini of MHC class I peptides. J Immunol 2013: 191: 1547-55.
    • (2013) J Immunol , vol.191 , pp. 1547-1555
    • Kanaseki, T.1    Lind, K.C.2    Escobar, H.3
  • 19
    • 0036387164 scopus 로고    scopus 로고
    • NMR structures of 36 and 73-residue fragments of the calreticulin P-domain
    • Ellgaard L, Bettendorff P, Braun D et al. NMR structures of 36 and 73-residue fragments of the calreticulin P-domain. J Mol Biol 2002: 322: 773-84.
    • (2002) J Mol Biol , vol.322 , pp. 773-784
    • Ellgaard, L.1    Bettendorff, P.2    Braun, D.3
  • 21
    • 0037119465 scopus 로고    scopus 로고
    • Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    • Leach MR, Cohen-Doyle MF, Thomas DY, Williams DB. Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. J Biol Chem 2002: 277: 29686-97.
    • (2002) J Biol Chem , vol.277 , pp. 29686-29697
    • Leach, M.R.1    Cohen-Doyle, M.F.2    Thomas, D.Y.3    Williams, D.B.4
  • 22
    • 33744961082 scopus 로고    scopus 로고
    • Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules
    • Zhang Y, Baig E, Williams DB. Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules. J Biol Chem 2006: 281: 14622-31.
    • (2006) J Biol Chem , vol.281 , pp. 14622-14631
    • Zhang, Y.1    Baig, E.2    Williams, D.B.3
  • 23
    • 0026528005 scopus 로고
    • Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide
    • Degen E, Cohen-Doyle MF, Williams DB. Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide. J Exp Med 1992: 175: 1653-61.
    • (1992) J Exp Med , vol.175 , pp. 1653-1661
    • Degen, E.1    Cohen-Doyle, M.F.2    Williams, D.B.3
  • 24
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • Sadasivan B, Lehner PJ, Ortmann B, Spies T, Cresswell P. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 1996: 5: 103-14.
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 25
    • 33750002010 scopus 로고    scopus 로고
    • Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing
    • Park B, Lee S, Kim E et al. Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 2006: 127: 369-82.
    • (2006) Cell , vol.127 , pp. 369-382
    • Park, B.1    Lee, S.2    Kim, E.3
  • 26
    • 27144497781 scopus 로고    scopus 로고
    • Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
    • Peaper DR, Wearsch PA, Cresswell P. Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex. EMBO J 2005: 24: 3613-23.
    • (2005) EMBO J , vol.24 , pp. 3613-3623
    • Peaper, D.R.1    Wearsch, P.A.2    Cresswell, P.3
  • 27
    • 34547092165 scopus 로고    scopus 로고
    • Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin
    • Kienast A, Preuss M, Winkler M, Dick TP. Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin. Nat Immunol 2007: 8: 864-72.
    • (2007) Nat Immunol , vol.8 , pp. 864-872
    • Kienast, A.1    Preuss, M.2    Winkler, M.3    Dick, T.P.4
  • 28
    • 38449098111 scopus 로고    scopus 로고
    • Molecular architecture of the TAP-associated MHC class I peptide-loading complex
    • Rufer E, Leonhardt RM, Knittler MR. Molecular architecture of the TAP-associated MHC class I peptide-loading complex. J Immunol 2007: 179: 5717-27.
    • (2007) J Immunol , vol.179 , pp. 5717-5727
    • Rufer, E.1    Leonhardt, R.M.2    Knittler, M.R.3
  • 29
    • 84888350706 scopus 로고    scopus 로고
    • The binding of TAPBPR and Tapasin to MHC class I is mutually exclusive
    • Hermann C, Strittmatter LM, Deane JE, Boyle LH. The binding of TAPBPR and Tapasin to MHC class I is mutually exclusive. J Immunol 2013: 191: 5743-50.
    • (2013) J Immunol , vol.191 , pp. 5743-5750
    • Hermann, C.1    Strittmatter, L.M.2    Deane, J.E.3    Boyle, L.H.4
  • 30
    • 0030865333 scopus 로고    scopus 로고
    • A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes
    • Ortmann B, Copeman J, Lehner PJ et al. A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes. Science 1997: 277: 1306-9.
    • (1997) Science , vol.277 , pp. 1306-1309
    • Ortmann, B.1    Copeman, J.2    Lehner, P.J.3
  • 31
    • 11844249995 scopus 로고    scopus 로고
    • A charged amino acid residue in the transmembrane/cytoplasmic region of tapasin influences MHC class I assembly and maturation
    • Petersen JL, Hickman-Miller HD, McIlhaney MM et al. A charged amino acid residue in the transmembrane/cytoplasmic region of tapasin influences MHC class I assembly and maturation. J Immunol 2005: 174: 962-9.
    • (2005) J Immunol , vol.174 , pp. 962-969
    • Petersen, J.L.1    Hickman-Miller, H.D.2    McIlhaney, M.M.3
  • 32
    • 0032005348 scopus 로고    scopus 로고
    • Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line .220
    • Lehner PJ, Surman MJ, Cresswell P. Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line .220. Immunity 1998: 8: 221-31.
    • (1998) Immunity , vol.8 , pp. 221-231
    • Lehner, P.J.1    Surman, M.J.2    Cresswell, P.3
  • 33
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick TP, Bangia N, Peaper DR, Cresswell P. Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 2002: 16: 87-98.
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 34
    • 48749105947 scopus 로고    scopus 로고
    • The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading
    • Peaper DR, Cresswell P. The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading. Proc Natl Acad Sci U S A 2008: 105: 10477-82.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 10477-10482
    • Peaper, D.R.1    Cresswell, P.2
  • 35
    • 2942620134 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status
    • Wearsch PA, Jakob CA, Vallin A, Dwek RA, Rudd PM, Cresswell P. Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status. J Biol Chem 2004: 279: 25112-21.
    • (2004) J Biol Chem , vol.279 , pp. 25112-25121
    • Wearsch, P.A.1    Jakob, C.A.2    Vallin, A.3    Dwek, R.A.4    Rudd, P.M.5    Cresswell, P.6
  • 36
    • 79953194818 scopus 로고    scopus 로고
    • Essential glycan-dependent interactions optimize MHC class I peptide loading
    • Wearsch PA, Peaper DR, Cresswell P. Essential glycan-dependent interactions optimize MHC class I peptide loading. Proc Natl Acad Sci U S A 2011: 108: 4950-5.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 4950-4955
    • Wearsch, P.A.1    Peaper, D.R.2    Cresswell, P.3
  • 37
    • 0036169941 scopus 로고    scopus 로고
    • Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin
    • Gao B, Adhikari R, Howarth M et al. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 2002: 16: 99-109.
    • (2002) Immunity , vol.16 , pp. 99-109
    • Gao, B.1    Adhikari, R.2    Howarth, M.3
  • 38
    • 0034279712 scopus 로고    scopus 로고
    • Impaired immune responses and altered peptide repertoire in tapasin-deficient mice
    • Garbi N, Tan P, Diehl AD et al. Impaired immune responses and altered peptide repertoire in tapasin-deficient mice. Nat Immunol 2000: 1: 234-8.
    • (2000) Nat Immunol , vol.1 , pp. 234-238
    • Garbi, N.1    Tan, P.2    Diehl, A.D.3
  • 39
    • 0033681184 scopus 로고    scopus 로고
    • Impaired assembly yet normal trafficking of MHC class I molecules in Tapasin mutant mice
    • Grandea AG 3rd, Golovina TN, Hamilton SE et al. Impaired assembly yet normal trafficking of MHC class I molecules in Tapasin mutant mice. Immunity 2000: 13: 213-22.
    • (2000) Immunity , vol.13 , pp. 213-222
    • Grandea 3rd, A.G.1    Golovina, T.N.2    Hamilton, S.E.3
  • 40
  • 41
    • 4143051423 scopus 로고    scopus 로고
    • Tapasin enhances MHC class I peptide presentation according to peptide half-life
    • Howarth M, Williams A, Tolstrup AB, Elliott T. Tapasin enhances MHC class I peptide presentation according to peptide half-life. Proc Natl Acad Sci U S A 2004: 101: 11737-42.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 11737-11742
    • Howarth, M.1    Williams, A.2    Tolstrup, A.B.3    Elliott, T.4
  • 42
    • 0035863732 scopus 로고    scopus 로고
    • Quantitative and qualitative influences of tapasin on the class I peptide repertoire
    • Purcell AW, Gorman JJ, Garcia-Peydro M et al. Quantitative and qualitative influences of tapasin on the class I peptide repertoire. J Immunol 2001: 166: 1016-27.
    • (2001) J Immunol , vol.166 , pp. 1016-1027
    • Purcell, A.W.1    Gorman, J.J.2    Garcia-Peydro, M.3
  • 43
    • 0036467491 scopus 로고    scopus 로고
    • HLA-DM, HLA-DO and tapasin: functional similarities and differences
    • Brocke P, Garbi N, Momburg F, Hammerling GJ. HLA-DM, HLA-DO and tapasin: functional similarities and differences. Curr Opin Immunol 2002: 14: 22-9.
    • (2002) Curr Opin Immunol , vol.14 , pp. 22-29
    • Brocke, P.1    Garbi, N.2    Momburg, F.3    Hammerling, G.J.4
  • 44
    • 0029974597 scopus 로고    scopus 로고
    • Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing
    • Neisig A, Wubbolts R, Zang X, Melief C, Neefjes J. Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing. J Immunol 1996: 156: 3196-206.
    • (1996) J Immunol , vol.156 , pp. 3196-3206
    • Neisig, A.1    Wubbolts, R.2    Zang, X.3    Melief, C.4    Neefjes, J.5
  • 47
    • 0031595997 scopus 로고    scopus 로고
    • HLA-A*0201 presents TAP-dependent peptide epitopes to cytotoxic T lymphocytes in the absence of tapasin
    • Lewis JW, Sewell A, Price D, Elliott T. HLA-A*0201 presents TAP-dependent peptide epitopes to cytotoxic T lymphocytes in the absence of tapasin. Eur J Immunol 1998: 28: 3214-20.
    • (1998) Eur J Immunol , vol.28 , pp. 3214-3220
    • Lewis, J.W.1    Sewell, A.2    Price, D.3    Elliott, T.4
  • 48
    • 0027988164 scopus 로고
    • Novel allele-specific, post-translational reduction in HLA class I surface expression in a mutant human B cell line
    • Greenwood R, Shimizu Y, Sekhon GS, DeMars R. Novel allele-specific, post-translational reduction in HLA class I surface expression in a mutant human B cell line. J Immunol 1994: 153: 5525-36.
    • (1994) J Immunol , vol.153 , pp. 5525-5536
    • Greenwood, R.1    Shimizu, Y.2    Sekhon, G.S.3    DeMars, R.4
  • 49
    • 0028817950 scopus 로고
    • Dependence of peptide binding by MHC class I molecules on their interaction with TAP
    • Grandea AG 3rd, Androlewicz MJ, Athwal RS, Geraghty DE, Spies T. Dependence of peptide binding by MHC class I molecules on their interaction with TAP. Science 1995: 270: 105-8.
    • (1995) Science , vol.270 , pp. 105-108
    • Grandea 3rd, A.G.1    Androlewicz, M.J.2    Athwal, R.S.3    Geraghty, D.E.4    Spies, T.5
  • 50
    • 0032076171 scopus 로고    scopus 로고
    • HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading
    • Peh CA, Burrows SR, Barnden M et al. HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity 1998: 8: 531-42.
    • (1998) Immunity , vol.8 , pp. 531-542
    • Peh, C.A.1    Burrows, S.R.2    Barnden, M.3
  • 51
    • 84901290106 scopus 로고    scopus 로고
    • Distinct assembly profiles of HLA-B molecules
    • Rizvi SM, Salam N, Geng J et al. Distinct assembly profiles of HLA-B molecules. J Immunol 2014: 192: 4967-76.
    • (2014) J Immunol , vol.192 , pp. 4967-4976
    • Rizvi, S.M.1    Salam, N.2    Geng, J.3
  • 52
    • 2942753075 scopus 로고    scopus 로고
    • Natural HLA class I polymorphism controls the pathway of antigen presentation and susceptibility to viral evasion
    • Zernich D, Purcell AW, Macdonald WA et al. Natural HLA class I polymorphism controls the pathway of antigen presentation and susceptibility to viral evasion. J Exp Med 2004: 200: 13-24.
    • (2004) J Exp Med , vol.200 , pp. 13-24
    • Zernich, D.1    Purcell, A.W.2    Macdonald, W.A.3
  • 53
    • 0037438347 scopus 로고    scopus 로고
    • A single polymorphic residue within the peptide-binding cleft of MHC class I molecules determines spectrum of tapasin dependence
    • Park B, Lee S, Kim E, Ahn K. A single polymorphic residue within the peptide-binding cleft of MHC class I molecules determines spectrum of tapasin dependence. J Immunol 2003: 170: 961-8.
    • (2003) J Immunol , vol.170 , pp. 961-968
    • Park, B.1    Lee, S.2    Kim, E.3    Ahn, K.4
  • 54
    • 26244451375 scopus 로고    scopus 로고
    • The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex
    • Elliott T, Williams A. The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex. Immunol Rev 2005: 207: 89-99.
    • (2005) Immunol Rev , vol.207 , pp. 89-99
    • Elliott, T.1    Williams, A.2
  • 55
    • 80355148422 scopus 로고    scopus 로고
    • Tapasin dependence of major histocompatibility complex class I molecules correlates with their conformational flexibility
    • Garstka MA, Fritzsche S, Lenart I et al. Tapasin dependence of major histocompatibility complex class I molecules correlates with their conformational flexibility. FASEB J 2011: 25: 3989-98.
    • (2011) FASEB J , vol.25 , pp. 3989-3998
    • Garstka, M.A.1    Fritzsche, S.2    Lenart, I.3
  • 56
    • 80055080759 scopus 로고    scopus 로고
    • A peptide filtering relation quantifies MHC class I peptide optimization
    • Dalchau N, Phillips A, Goldstein LD et al. A peptide filtering relation quantifies MHC class I peptide optimization. PLoS Comput Biol 2011: 7: e1002144.
    • (2011) PLoS Comput Biol , vol.7 , pp. e1002144
    • Dalchau, N.1    Phillips, A.2    Goldstein, L.D.3
  • 57
    • 58149215628 scopus 로고    scopus 로고
    • Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer
    • Dong G, Wearsch PA, Peaper DR, Cresswell P, Reinisch KM. Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity 2009: 30: 21-32.
    • (2009) Immunity , vol.30 , pp. 21-32
    • Dong, G.1    Wearsch, P.A.2    Peaper, D.R.3    Cresswell, P.4    Reinisch, K.M.5
  • 58
    • 33947606283 scopus 로고    scopus 로고
    • Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection
    • Chen M, Bouvier M. Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection. EMBO J 2007: 26: 1681-90.
    • (2007) EMBO J , vol.26 , pp. 1681-1690
    • Chen, M.1    Bouvier, M.2
  • 59
    • 0029813510 scopus 로고    scopus 로고
    • MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains
    • Suh WK, Mitchell EK, Yang Y, Peterson PA, Waneck GL, Williams DB. MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains. J Exp Med 1996: 184: 337-48.
    • (1996) J Exp Med , vol.184 , pp. 337-348
    • Suh, W.K.1    Mitchell, E.K.2    Yang, Y.3    Peterson, P.A.4    Waneck, G.L.5    Williams, D.B.6
  • 60
    • 0033180470 scopus 로고    scopus 로고
    • Lateral diffusion of GFP-tagged H2Ld molecules and of GFP-TAP1 reports on the assembly and retention of these molecules in the endoplasmic reticulum
    • Marguet D, Spiliotis ET, Pentcheva T, Lebowitz M, Schneck J, Edidin M. Lateral diffusion of GFP-tagged H2Ld molecules and of GFP-TAP1 reports on the assembly and retention of these molecules in the endoplasmic reticulum. Immunity 1999: 11: 231-40.
    • (1999) Immunity , vol.11 , pp. 231-240
    • Marguet, D.1    Spiliotis, E.T.2    Pentcheva, T.3    Lebowitz, M.4    Schneck, J.5    Edidin, M.6
  • 61
    • 0034517368 scopus 로고    scopus 로고
    • Selective export of MHC class I molecules from the ER after their dissociation from TAP
    • Spiliotis ET, Manley H, Osorio M, Zuniga MC, Edidin M. Selective export of MHC class I molecules from the ER after their dissociation from TAP. Immunity 2000: 13: 841-51.
    • (2000) Immunity , vol.13 , pp. 841-851
    • Spiliotis, E.T.1    Manley, H.2    Osorio, M.3    Zuniga, M.C.4    Edidin, M.5
  • 62
    • 79953194126 scopus 로고    scopus 로고
    • A role for UDP-glucose glycoprotein glucosyltransferase in expression and quality control of MHC class I molecules
    • Zhang W, Wearsch PA, Zhu Y, Leonhardt RM, Cresswell P. A role for UDP-glucose glycoprotein glucosyltransferase in expression and quality control of MHC class I molecules. Proc Natl Acad Sci U S A 2011: 108: 4956-61.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 4956-4961
    • Zhang, W.1    Wearsch, P.A.2    Zhu, Y.3    Leonhardt, R.M.4    Cresswell, P.5
  • 63
    • 77952583769 scopus 로고    scopus 로고
    • UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control
    • D'Alessio C, Caramelo JJ, Parodi AJ. UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control. Semin Cell Dev Biol 2010: 21: 491-9.
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 491-499
    • D'Alessio, C.1    Caramelo, J.J.2    Parodi, A.J.3
  • 64
    • 84878750391 scopus 로고    scopus 로고
    • Endoplasmic reticulum glycoprotein quality control regulates CD1d assembly and CD1d-mediated antigen presentation
    • Kunte A, Zhang W, Paduraru C et al. Endoplasmic reticulum glycoprotein quality control regulates CD1d assembly and CD1d-mediated antigen presentation. J Biol Chem 2013: 288: 16391-402.
    • (2013) J Biol Chem , vol.288 , pp. 16391-16402
    • Kunte, A.1    Zhang, W.2    Paduraru, C.3
  • 66
    • 35648938644 scopus 로고    scopus 로고
    • Peptide-receptive major histocompatibility complex class I molecules cycle between endoplasmic reticulum and cis-Golgi in wild-type lymphocytes
    • Garstka M, Borchert B, Al-Balushi M et al. Peptide-receptive major histocompatibility complex class I molecules cycle between endoplasmic reticulum and cis-Golgi in wild-type lymphocytes. J Biol Chem 2007: 282: 30680-90.
    • (2007) J Biol Chem , vol.282 , pp. 30680-30690
    • Garstka, M.1    Borchert, B.2    Al-Balushi, M.3
  • 67
    • 78650035575 scopus 로고    scopus 로고
    • Receptor-mediated ER export of human MHC class I molecules is regulated by the C-terminal single amino acid
    • Cho S, Ryoo J, Jun Y, Ahn K. Receptor-mediated ER export of human MHC class I molecules is regulated by the C-terminal single amino acid. Traffic 2011: 12: 42-55.
    • (2011) Traffic , vol.12 , pp. 42-55
    • Cho, S.1    Ryoo, J.2    Jun, Y.3    Ahn, K.4
  • 68
    • 2942596020 scopus 로고    scopus 로고
    • Bap29/31 influences the intracellular traffic of MHC class I molecules
    • Paquet ME, Cohen-Doyle M, Shore GC, Williams DB. Bap29/31 influences the intracellular traffic of MHC class I molecules. J Immunol 2004: 172: 7548-55.
    • (2004) J Immunol , vol.172 , pp. 7548-7555
    • Paquet, M.E.1    Cohen-Doyle, M.2    Shore, G.C.3    Williams, D.B.4
  • 69
    • 33750320380 scopus 로고    scopus 로고
    • Bap31 enhances the endoplasmic reticulum export and quality control of human class I MHC molecules
    • Ladasky JJ, Boyle S, Seth M et al. Bap31 enhances the endoplasmic reticulum export and quality control of human class I MHC molecules. J Immunol 2006: 177: 6172-81.
    • (2006) J Immunol , vol.177 , pp. 6172-6181
    • Ladasky, J.J.1    Boyle, S.2    Seth, M.3
  • 70
    • 65249103521 scopus 로고    scopus 로고
    • Interaction of Bap31 and MHC class I molecules and their traffic out of the endoplasmic reticulum
    • Abe F, Van Prooyen N, Ladasky JJ, Edidin M. Interaction of Bap31 and MHC class I molecules and their traffic out of the endoplasmic reticulum. J Immunol 2009: 182: 4776-83.
    • (2009) J Immunol , vol.182 , pp. 4776-4783
    • Abe, F.1    Van Prooyen, N.2    Ladasky, J.J.3    Edidin, M.4
  • 71
    • 0034866115 scopus 로고    scopus 로고
    • The truncated cytoplasmic tail of HLA-G serves a quality-control function in post-ER compartments
    • Park B, Lee S, Kim E, Chang S, Jin M, Ahn K. The truncated cytoplasmic tail of HLA-G serves a quality-control function in post-ER compartments. Immunity 2001: 15: 213-24.
    • (2001) Immunity , vol.15 , pp. 213-224
    • Park, B.1    Lee, S.2    Kim, E.3    Chang, S.4    Jin, M.5    Ahn, K.6
  • 72
    • 33645749031 scopus 로고    scopus 로고
    • Selective cytotoxic T-lymphocyte targeting of tumor immune escape variants
    • van Hall T, Wolpert EZ, van Veelen P et al. Selective cytotoxic T-lymphocyte targeting of tumor immune escape variants. Nat Med 2006: 12: 417-24.
    • (2006) Nat Med , vol.12 , pp. 417-424
    • van Hall, T.1    Wolpert, E.Z.2    van Veelen, P.3
  • 73
    • 84864936907 scopus 로고    scopus 로고
    • Alternative peptide repertoire of HLA-E reveals a binding motif that is strikingly similar to HLA-A2
    • Lampen MH, Hassan C, Sluijter M et al. Alternative peptide repertoire of HLA-E reveals a binding motif that is strikingly similar to HLA-A2. Mol Immunol 2013: 53: 126-31.
    • (2013) Mol Immunol , vol.53 , pp. 126-131
    • Lampen, M.H.1    Hassan, C.2    Sluijter, M.3
  • 74
    • 84875635224 scopus 로고    scopus 로고
    • Importance of TAP-independent processing pathways
    • Oliveira CC, van Hall T. Importance of TAP-independent processing pathways. Mol Immunol 2013: 55: 113-6.
    • (2013) Mol Immunol , vol.55 , pp. 113-116
    • Oliveira, C.C.1    van Hall, T.2
  • 75
    • 84875614010 scopus 로고    scopus 로고
    • Are membrane proteins favored over cytosolic proteins in TAP-independent processing pathways?
    • Del Val M, Lazaro S, Ramos M, Anton LC. Are membrane proteins favored over cytosolic proteins in TAP-independent processing pathways? Mol Immunol 2013: 55: 117-9.
    • (2013) Mol Immunol , vol.55 , pp. 117-119
    • Del Val, M.1    Lazaro, S.2    Ramos, M.3    Anton, L.C.4
  • 76
    • 0026576422 scopus 로고
    • HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides
    • Wei ML, Cresswell P. HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. Nature 1992: 356: 443-6.
    • (1992) Nature , vol.356 , pp. 443-446
    • Wei, M.L.1    Cresswell, P.2
  • 77
    • 0028876773 scopus 로고
    • Association of the invariant chain with major histocompatibility complex class I molecules directs trafficking to endocytic compartments
    • Sugita M, Brenner MB. Association of the invariant chain with major histocompatibility complex class I molecules directs trafficking to endocytic compartments. J Biol Chem 1995: 270: 1443-8.
    • (1995) J Biol Chem , vol.270 , pp. 1443-1448
    • Sugita, M.1    Brenner, M.B.2
  • 78
    • 0030588711 scopus 로고    scopus 로고
    • Invariant chain association with MHC class I: preference for HLA class I/beta 2-microglobulin heterodimers, specificity, and influence of the MHC peptide-binding groove
    • Vigna JL, Smith KD, Lutz CT. Invariant chain association with MHC class I: preference for HLA class I/beta 2-microglobulin heterodimers, specificity, and influence of the MHC peptide-binding groove. J Immunol 1996: 157: 4503-10.
    • (1996) J Immunol , vol.157 , pp. 4503-4510
    • Vigna, J.L.1    Smith, K.D.2    Lutz, C.T.3
  • 79
    • 0017126775 scopus 로고
    • Cross-priming for a secondary cytotoxic response to minor H antigens with H-2 congenic cells which do not cross-react in the cytotoxic assay
    • Bevan MJ. Cross-priming for a secondary cytotoxic response to minor H antigens with H-2 congenic cells which do not cross-react in the cytotoxic assay. J Exp Med 1976: 143: 1283-8.
    • (1976) J Exp Med , vol.143 , pp. 1283-1288
    • Bevan, M.J.1
  • 81
    • 0035109189 scopus 로고    scopus 로고
    • Antigen loading of MHC class I molecules in the endocytic tract
    • Kleijmeer MJ, Escola JM, UytdeHaag FG et al. Antigen loading of MHC class I molecules in the endocytic tract. Traffic 2001: 2: 124-37.
    • (2001) Traffic , vol.2 , pp. 124-137
    • Kleijmeer, M.J.1    Escola, J.M.2    UytdeHaag, F.G.3
  • 82
    • 84857171607 scopus 로고    scopus 로고
    • A CD74-dependent MHC class I endolysosomal cross-presentation pathway
    • Basha G, Omilusik K, Chavez-Steenbock A et al. A CD74-dependent MHC class I endolysosomal cross-presentation pathway. Nat Immunol 2012: 13: 237-45.
    • (2012) Nat Immunol , vol.13 , pp. 237-245
    • Basha, G.1    Omilusik, K.2    Chavez-Steenbock, A.3
  • 83
    • 0033649486 scopus 로고    scopus 로고
    • The phylogenetic origin of antigen-specific receptors
    • Du Pasquier L. The phylogenetic origin of antigen-specific receptors. Curr Top Microbiol Immunol 2000: 248: 160-85.
    • (2000) Curr Top Microbiol Immunol , vol.248 , pp. 160-185
    • Du Pasquier, L.1
  • 85
  • 86
    • 84874459064 scopus 로고    scopus 로고
    • Tapasin-related protein TAPBPR is an additional component of the MHC class I presentation pathway
    • Boyle LH, Hermann C, Boname JM et al. Tapasin-related protein TAPBPR is an additional component of the MHC class I presentation pathway. Proc Natl Acad Sci U S A 2013: 110: 3465-70.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 3465-3470
    • Boyle, L.H.1    Hermann, C.2    Boname, J.M.3
  • 87
    • 33744936808 scopus 로고    scopus 로고
    • The double lysine motif of tapasin is a retrieval signal for retention of unstable MHC class I molecules in the endoplasmic reticulum
    • Paulsson KM, Jevon M, Wang JW, Li S, Wang P. The double lysine motif of tapasin is a retrieval signal for retention of unstable MHC class I molecules in the endoplasmic reticulum. J Immunol 2006: 176: 7482-8.
    • (2006) J Immunol , vol.176 , pp. 7482-7488
    • Paulsson, K.M.1    Jevon, M.2    Wang, J.W.3    Li, S.4    Wang, P.5
  • 88
    • 78650089607 scopus 로고    scopus 로고
    • The leukocyte nuclear envelope proteome varies with cell activation and contains novel transmembrane proteins that affect genome architecture
    • Korfali N, Wilkie GS, Swanson SK et al. The leukocyte nuclear envelope proteome varies with cell activation and contains novel transmembrane proteins that affect genome architecture. Mol Cell Proteomics 2010: 9: 2571-85.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 2571-2585
    • Korfali, N.1    Wilkie, G.S.2    Swanson, S.K.3
  • 89
  • 90
    • 13144255735 scopus 로고    scopus 로고
    • HLA-DO is a negative modulator of HLA-DM-mediated MHC class II peptide loading
    • van Ham SM, Tjin EP, Lillemeier BF et al. HLA-DO is a negative modulator of HLA-DM-mediated MHC class II peptide loading. Curr Biol 1997: 7: 950-7.
    • (1997) Curr Biol , vol.7 , pp. 950-957
    • van Ham, S.M.1    Tjin, E.P.2    Lillemeier, B.F.3
  • 91
    • 26244441527 scopus 로고    scopus 로고
    • Right place, right time, right peptide: DO keeps DM focused
    • Denzin LK, Fallas JL, Prendes M, Yi W. Right place, right time, right peptide: DO keeps DM focused. Immunol Rev 2005: 207: 279-92.
    • (2005) Immunol Rev , vol.207 , pp. 279-292
    • Denzin, L.K.1    Fallas, J.L.2    Prendes, M.3    Yi, W.4
  • 92
    • 0025331726 scopus 로고
    • Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding
    • Roche PA, Cresswell P. Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding. Nature 1990: 345: 615-8.
    • (1990) Nature , vol.345 , pp. 615-618
    • Roche, P.A.1    Cresswell, P.2
  • 93
    • 0026440236 scopus 로고
    • HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides
    • Riberdy JM, Newcomb JR, Surman MJ, Barbosa JA, Cresswell P. HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides. Nature 1992: 360: 474-7.
    • (1992) Nature , vol.360 , pp. 474-477
    • Riberdy, J.M.1    Newcomb, J.R.2    Surman, M.J.3    Barbosa, J.A.4    Cresswell, P.5
  • 94
    • 0025202076 scopus 로고
    • MHC class II-associated invariant chain contains a sorting signal for endosomal compartments
    • Bakke O, Dobberstein B. MHC class II-associated invariant chain contains a sorting signal for endosomal compartments. Cell 1990: 63: 707-16.
    • (1990) Cell , vol.63 , pp. 707-716
    • Bakke, O.1    Dobberstein, B.2
  • 95
    • 0025602116 scopus 로고
    • Intracellular transport of class II MHC molecules directed by invariant chain
    • Lotteau V, Teyton L, Peleraux A et al. Intracellular transport of class II MHC molecules directed by invariant chain. Nature 1990: 348: 600-5.
    • (1990) Nature , vol.348 , pp. 600-605
    • Lotteau, V.1    Teyton, L.2    Peleraux, A.3
  • 96
    • 0027498929 scopus 로고
    • Relationship between invariant chain expression and major histocompatibility complex class II transport into early and late endocytic compartments
    • Romagnoli P, Layet C, Yewdell J, Bakke O, Germain RN. Relationship between invariant chain expression and major histocompatibility complex class II transport into early and late endocytic compartments. J Exp Med 1993: 177: 583-96.
    • (1993) J Exp Med , vol.177 , pp. 583-596
    • Romagnoli, P.1    Layet, C.2    Yewdell, J.3    Bakke, O.4    Germain, R.N.5
  • 97
    • 0026353496 scopus 로고
    • Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules
    • Roche PA, Cresswell P. Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules. Proc Natl Acad Sci U S A 1991: 88: 3150-4.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3150-3154
    • Roche, P.A.1    Cresswell, P.2
  • 98
    • 0028344898 scopus 로고
    • Endosomal aspartic proteinases are required for invariant-chain processing
    • Maric MA, Taylor MD, Blum JS. Endosomal aspartic proteinases are required for invariant-chain processing. Proc Natl Acad Sci U S A 1994: 91: 2171-5.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 2171-2175
    • Maric, M.A.1    Taylor, M.D.2    Blum, J.S.3
  • 100
    • 84899092221 scopus 로고    scopus 로고
    • TAPBPR isoforms exhibit altered association with MHC class I
    • Porter KM, Hermann C, Traherne JA, Boyle LH. TAPBPR isoforms exhibit altered association with MHC class I. Immunology 2014: 142: 289-99.
    • (2014) Immunology , vol.142 , pp. 289-299
    • Porter, K.M.1    Hermann, C.2    Traherne, J.A.3    Boyle, L.H.4
  • 101
    • 84923338219 scopus 로고    scopus 로고
    • Systematic genetic analysis identifies Cis-eQTL target genes associated with glioblastoma patient survival
    • Chen QR, Hu Y, Yan C, Buetow K, Meerzaman D. Systematic genetic analysis identifies Cis-eQTL target genes associated with glioblastoma patient survival. PLoS One 2014: 9: e105393.
    • (2014) PLoS One , vol.9 , pp. e105393
    • Chen, Q.R.1    Hu, Y.2    Yan, C.3    Buetow, K.4    Meerzaman, D.5
  • 103
  • 104
    • 35748981184 scopus 로고    scopus 로고
    • Association scan of 14,500 nonsynonymous SNPs in four diseases identifies autoimmunity variants
    • Wellcome Trust Case Control Consortium, Australo-Anglo-American Spondylitis Consortium
    • Wellcome Trust Case Control Consortium, Australo-Anglo-American Spondylitis Consortium, Burton PR et al. Association scan of 14, 500 nonsynonymous SNPs in four diseases identifies autoimmunity variants. Nat Genet 2007: 39: 1329-37.
    • (2007) Nat Genet , vol.39 , pp. 1329-1337
    • Burton, P.R.1
  • 105
    • 79960899377 scopus 로고    scopus 로고
    • Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility
    • Evans DM, Spencer CC, Pointon JJ et al. Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility. Nat Genet 2011: 43: 761-7.
    • (2011) Nat Genet , vol.43 , pp. 761-767
    • Evans, D.M.1    Spencer, C.C.2    Pointon, J.J.3
  • 106
    • 84879663069 scopus 로고    scopus 로고
    • Naturally occurring ERAP1 haplotypes encode functionally distinct alleles with fine substrate specificity
    • Reeves E, Edwards CJ, Elliott T, James E. Naturally occurring ERAP1 haplotypes encode functionally distinct alleles with fine substrate specificity. J Immunol 2013: 191: 35-43.
    • (2013) J Immunol , vol.191 , pp. 35-43
    • Reeves, E.1    Edwards, C.J.2    Elliott, T.3    James, E.4
  • 107
    • 84866490075 scopus 로고    scopus 로고
    • HIV and HLA class I: an evolving relationship
    • Goulder PJ, Walker BD. HIV and HLA class I: an evolving relationship. Immunity 2012: 37: 426-40.
    • (2012) Immunity , vol.37 , pp. 426-440
    • Goulder, P.J.1    Walker, B.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.