메뉴 건너뛰기




Volumn 24, Issue 6, 2008, Pages 701-714

Cloning, characterization and expression analysis of SIMP (source of immunodominant MHC-associated peptides) in grass carp Ctenopharyngodon idella

Author keywords

cDNA; Gene organization; Grass carp; Organ; Promoter; SIMP

Indexed keywords

CTENOPHARYNGODON; CTENOPHARYNGODON IDELLA; CYPRINIDAE; ESCHERICHIA COLI; ORYCTOLAGUS CUNICULUS;

EID: 43049175012     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2007.11.019     Document Type: Article
Times cited : (5)

References (51)
  • 1
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • T.A. Rapoport B. Jungnickel U. Kutay Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes Annu Rev Biochem 65 1996 271 303
    • (1996) Annu Rev Biochem , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 2
    • 0032904470 scopus 로고    scopus 로고
    • The dolichol pathway of N-linked glycosylation
    • P. Burda M. Aebi The dolichol pathway of N-linked glycosylation Biochim Biophys Acta 1426 1999 239 257
    • (1999) Biochim Biophys Acta , vol.1426 , pp. 239-257
    • Burda, P.1    Aebi, M.2
  • 3
    • 0036909213 scopus 로고    scopus 로고
    • Control in the N-linked glycoprotein biosynthesis pathway
    • T.D. Butters Control in the N-linked glycoprotein biosynthesis pathway Chem Biol 9 2002 1266 1268
    • (2002) Chem Biol , vol.9 , pp. 1266-1268
    • Butters, T.D.1
  • 4
    • 0011928107 scopus 로고    scopus 로고
    • N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli
    • M. Wacker D. Linton P.G. Hitchen M. Nita-Lazar S.M. Haslam S.J. North N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli Science 298 2002 1790 1793
    • (2002) Science , vol.298 , pp. 1790-1793
    • Wacker, M.1    Linton, D.2    Hitchen, P.G.3    Nita-Lazar, M.4    Haslam, S.M.5    North, S.J.6
  • 5
    • 0031437891 scopus 로고    scopus 로고
    • The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p
    • D. Karaoglu D.J. Kelleher R. Gilmore The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p J Biol Chem 272 1997 32513 32520
    • (1997) J Biol Chem , vol.272 , pp. 32513-32520
    • Karaoglu, D.1    Kelleher, D.J.2    Gilmore, R.3
  • 6
    • 0030692762 scopus 로고    scopus 로고
    • The STT3 protein is a component of the yeast oligosaccharyltransferase complex
    • U. Spirig M. Glavas D. Bodmer G. Reiss P. Burda V. Lippuner The STT3 protein is a component of the yeast oligosaccharyltransferase complex Mol Gen Genet 256 1997 628 637
    • (1997) Mol Gen Genet , vol.256 , pp. 628-637
    • Spirig, U.1    Glavas, M.2    Bodmer, D.3    Reiss, G.4    Burda, P.5    Lippuner, V.6
  • 7
    • 0037033113 scopus 로고    scopus 로고
    • Studies on the function of oligosaccharyl transferase subunits: Stt3p is directly involved in the glycosylation process
    • Q. Yan W.J. Lennarz Studies on the function of oligosaccharyl transferase subunits: Stt3p is directly involved in the glycosylation process J Biol Chem 277 2002 47692 47700
    • (2002) J Biol Chem , vol.277 , pp. 47692-47700
    • Yan, Q.1    Lennarz, W.J.2
  • 8
    • 0037684809 scopus 로고    scopus 로고
    • Photocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complex
    • I. Nilsson D.J. Kelleher Y. Miao Y. Shao G. Kreibich R. Gilmore Photocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complex J Cell Biol 161 2003 715 725
    • (2003) J Cell Biol , vol.161 , pp. 715-725
    • Nilsson, I.1    Kelleher, D.J.2    Miao, Y.3    Shao, Y.4    Kreibich, G.5    Gilmore, R.6
  • 9
    • 0030024638 scopus 로고    scopus 로고
    • Molecular cloning of a highly conserved mouse and human integral membrane protein (Itm1) and genetic mapping to mouse chromosome 9
    • G. Hong W. Deleersnijder C.A. Kozak E. Van Marck P. Tylzanowski J. Merregaert Molecular cloning of a highly conserved mouse and human integral membrane protein ( Itm1 ) and genetic mapping to mouse chromosome 9 Genomics 31 1996 295 300
    • (1996) Genomics , vol.31 , pp. 295-300
    • Hong, G.1    Deleersnijder, W.2    Kozak, C.A.3    Van Marck, E.4    Tylzanowski, P.5    Merregaert, J.6
  • 11
    • 0038294237 scopus 로고    scopus 로고
    • Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties
    • D.J. Kelleher D. Karaoglu E.C. Mandon R. Gilmore Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties Mol Cell 12 2003 101 111
    • (2003) Mol Cell , vol.12 , pp. 101-111
    • Kelleher, D.J.1    Karaoglu, D.2    Mandon, E.C.3    Gilmore, R.4
  • 12
    • 0029988843 scopus 로고    scopus 로고
    • Isolation, characterization, and mapping to human chromosome 11q24-25 of a cDNA encoding a highly conserved putative transmembrane protein, TMC
    • N.A. Lissy A. Bellacosa G. Sonoda P.D. Miller S.C. Jhanwar J.R. Testa Isolation, characterization, and mapping to human chromosome 11q24-25 of a cDNA encoding a highly conserved putative transmembrane protein, TMC Biochim Biophys Acta 1306 1996 137 141
    • (1996) Biochim Biophys Acta , vol.1306 , pp. 137-141
    • Lissy, N.A.1    Bellacosa, A.2    Sonoda, G.3    Miller, P.D.4    Jhanwar, S.C.5    Testa, J.R.6
  • 13
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic oligosaccharyltransferase
    • D.J. Kelleher R. Gilmore An evolving view of the eukaryotic oligosaccharyltransferase Glycobiology 16 2006 47R 62R
    • (2006) Glycobiology , vol.16 , pp. 47R-62R
    • Kelleher, D.J.1    Gilmore, R.2
  • 14
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • E. Pamer P. Cresswell Mechanisms of MHC class I-restricted antigen processing Annu Rev Immunol 16 1998 323 358
    • (1998) Annu Rev Immunol , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 15
    • 0035142615 scopus 로고    scopus 로고
    • Cut and trim: generating MHC class I peptide ligands
    • J.W. Yewdell J.R. Bennink Cut and trim: generating MHC class I peptide ligands Curr Opin Immunol 13 2001 13 18
    • (2001) Curr Opin Immunol , vol.13 , pp. 13-18
    • Yewdell, J.W.1    Bennink, J.R.2
  • 16
    • 0036017391 scopus 로고    scopus 로고
    • Protein degradation and the generation of MHC class I-presented peptides
    • K.L. Rock I.A. York T. Saric A.L. Goldberg Protein degradation and the generation of MHC class I-presented peptides Adv Immunol 80 2002 1 70
    • (2002) Adv Immunol , vol.80 , pp. 1-70
    • Rock, K.L.1    York, I.A.2    Saric, T.3    Goldberg, A.L.4
  • 17
    • 0031045796 scopus 로고    scopus 로고
    • On the mechanisms of immunodominance in cytotoxic T lymphocyte responses to minor histocompatibility antigens
    • S. Pion P. Fontaine M. Desaulniers J. Jutras J.G. Filep C. Perreault On the mechanisms of immunodominance in cytotoxic T lymphocyte responses to minor histocompatibility antigens Eur J Immunol 27 1997 421 430
    • (1997) Eur J Immunol , vol.27 , pp. 421-430
    • Pion, S.1    Fontaine, P.2    Desaulniers, M.3    Jutras, J.4    Filep, J.G.5    Perreault, C.6
  • 18
    • 0032904671 scopus 로고    scopus 로고
    • Shaping the repertoire of cytotoxic T-lymphocyte responses: explanation for the immunodominance effect whereby cytotoxic T lymphocytes specific for immunodominant antigens prevent recognition of nondominant antigens
    • S. Pion G.J. Christianson P. Fontaine D.C. Roopenian C. Perreault Shaping the repertoire of cytotoxic T-lymphocyte responses: explanation for the immunodominance effect whereby cytotoxic T lymphocytes specific for immunodominant antigens prevent recognition of nondominant antigens Blood 93 1999 952 962
    • (1999) Blood , vol.93 , pp. 952-962
    • Pion, S.1    Christianson, G.J.2    Fontaine, P.3    Roopenian, D.C.4    Perreault, C.5
  • 19
    • 0034928716 scopus 로고    scopus 로고
    • Adoptive transfer of minor histocompatibility antigen-specific T lymphocytes eradicates leukemia cells without causing graft-versus-host disease
    • P. Fontaine G. Roy-Proulx L. Knafo C. Baron D.C. Roy C. Perreault Adoptive transfer of minor histocompatibility antigen-specific T lymphocytes eradicates leukemia cells without causing graft-versus-host disease Nat Med 7 2001 789 794
    • (2001) Nat Med , vol.7 , pp. 789-794
    • Fontaine, P.1    Roy-Proulx, G.2    Knafo, L.3    Baron, C.4    Roy, D.C.5    Perreault, C.6
  • 20
    • 28744440862 scopus 로고    scopus 로고
    • The structure and location of SIMP/STT3B account for its prominent imprint on the MHC I immunopeptidome
    • E. Caron R. Charbonneau G. Huppe S. Brochu C. Perreault The structure and location of SIMP/STT3B account for its prominent imprint on the MHC I immunopeptidome Int Immunol 17 2005 1583 1596
    • (2005) Int Immunol , vol.17 , pp. 1583-1596
    • Caron, E.1    Charbonneau, R.2    Huppe, G.3    Brochu, S.4    Perreault, C.5
  • 21
    • 29244462003 scopus 로고    scopus 로고
    • Identification of two distinct intracellular localization signals in STT3-B
    • E. Caron C. Cote M. Parisien F. Major C. Perreault Identification of two distinct intracellular localization signals in STT3-B Arch Biochem Biophys 445 2006 108 114
    • (2006) Arch Biochem Biophys , vol.445 , pp. 108-114
    • Caron, E.1    Cote, C.2    Parisien, M.3    Major, F.4    Perreault, C.5
  • 22
    • 21644480464 scopus 로고    scopus 로고
    • Identification of immune genes in grass carp Ctenopharyngodon idella in response to infection of the parasitic copepod Sinergasilus major
    • M.X. Chang P. Nie G.Y. Liu Y. Song Q. Gao Identification of immune genes in grass carp Ctenopharyngodon idella in response to infection of the parasitic copepod Sinergasilus major Parasitol Res 96 2005 224 229
    • (2005) Parasitol Res , vol.96 , pp. 224-229
    • Chang, M.X.1    Nie, P.2    Liu, G.Y.3    Song, Y.4    Gao, Q.5
  • 24
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: classification and secondary structure prediction system for membrane proteins
    • T. Hirokawa S. Boon-Chieng S. Mitaku SOSUI: classification and secondary structure prediction system for membrane proteins Bioinformatics 14 1998 378 379
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 25
    • 0034710821 scopus 로고    scopus 로고
    • Isolation and molecular characterization of the 5′-upstream region of the human TRAIL gene
    • Q. Wang Y. Ji X. Wang B.M. Evers Isolation and molecular characterization of the 5′-upstream region of the human TRAIL gene Biochem Biophys Res Commun 276 2000 466 471
    • (2000) Biochem Biophys Res Commun , vol.276 , pp. 466-471
    • Wang, Q.1    Ji, Y.2    Wang, X.3    Evers, B.M.4
  • 26
    • 33846670175 scopus 로고    scopus 로고
    • Identification of a putative oocyte-specific small nuclear ribonucleoprotein polypeptide C in gibel carp
    • H.Y. Wang L. Zhou J.F. Gui Identification of a putative oocyte-specific small nuclear ribonucleoprotein polypeptide C in gibel carp Comp Biochem Physiol B Biochem Mol Biol 146 2007 47 52
    • (2007) Comp Biochem Physiol B Biochem Mol Biol , vol.146 , pp. 47-52
    • Wang, H.Y.1    Zhou, L.2    Gui, J.F.3
  • 27
    • 0028834273 scopus 로고
    • STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo
    • R. Zufferey R. Knauer P. Burda I. Stagljar S. te Heesen L. Lehle STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo EMBO J 14 1995 4949 4960
    • (1995) EMBO J , vol.14 , pp. 4949-4960
    • Zufferey, R.1    Knauer, R.2    Burda, P.3    Stagljar, I.4    te Heesen, S.5    Lehle, L.6
  • 28
    • 10744227882 scopus 로고    scopus 로고
    • The STT3a subunit isoform of the Arabidopsis oligosaccharyltransferase controls adaptive responses to salt/osmotic stress
    • H. Koiwa F. Li M.G. McCully I. Mendoza N. Koizumi Y. Manabe The STT3a subunit isoform of the Arabidopsis oligosaccharyltransferase controls adaptive responses to salt/osmotic stress Plant Cell 15 2003 2273 2284
    • (2003) Plant Cell , vol.15 , pp. 2273-2284
    • Koiwa, H.1    Li, F.2    McCully, M.G.3    Mendoza, I.4    Koizumi, N.5    Manabe, Y.6
  • 29
    • 0028844407 scopus 로고
    • Cloning, expression, and characterization of the TATA-binding protein (TBP) promoter binding factor, a transcription activator of the Acanthamoeba TBP gene
    • W. Huang E. Bateman Cloning, expression, and characterization of the TATA-binding protein (TBP) promoter binding factor, a transcription activator of the Acanthamoeba TBP gene J Biol Chem 270 1995 28839 28847
    • (1995) J Biol Chem , vol.270 , pp. 28839-28847
    • Huang, W.1    Bateman, E.2
  • 30
    • 0033570899 scopus 로고    scopus 로고
    • CUG repeat binding protein (CUGBP1) interacts with the 5′ region of C/EBPbeta mRNA and regulates translation of C/EBPbeta isoforms
    • N.A. Timchenko A.L. Welm X. Lu L.T. Timchenko CUG repeat binding protein (CUGBP1) interacts with the 5′ region of C/EBPbeta mRNA and regulates translation of C/EBPbeta isoforms Nucleic Acids Res 27 1999 4517 4525
    • (1999) Nucleic Acids Res , vol.27 , pp. 4517-4525
    • Timchenko, N.A.1    Welm, A.L.2    Lu, X.3    Timchenko, L.T.4
  • 31
    • 0035971493 scopus 로고    scopus 로고
    • AP-1 in cell proliferation and survival
    • E. Shaulian M. Karin AP-1 in cell proliferation and survival Oncogene 20 2001 2390 2400
    • (2001) Oncogene , vol.20 , pp. 2390-2400
    • Shaulian, E.1    Karin, M.2
  • 32
    • 0035808355 scopus 로고    scopus 로고
    • YY1 as a regulator of replication-dependent hamster histone H3.2 promoter and an interactive partner of AP-2
    • F. Wu A.S. Lee YY1 as a regulator of replication-dependent hamster histone H3.2 promoter and an interactive partner of AP-2 J Biol Chem 276 2001 28 34
    • (2001) J Biol Chem , vol.276 , pp. 28-34
    • Wu, F.1    Lee, A.S.2
  • 34
    • 0842323782 scopus 로고    scopus 로고
    • The Yin Yang-1 (YY1) protein undergoes a DNA-replication-associated switch in localization from the cytoplasm to the nucleus at the onset of S phase
    • L. Palko H.W. Bass M.J. Beyrouthy M.M. Hurt The Yin Yang-1 (YY1) protein undergoes a DNA-replication-associated switch in localization from the cytoplasm to the nucleus at the onset of S phase J Cell Sci 117 2004 465 476
    • (2004) J Cell Sci , vol.117 , pp. 465-476
    • Palko, L.1    Bass, H.W.2    Beyrouthy, M.J.3    Hurt, M.M.4
  • 35
    • 30044432188 scopus 로고    scopus 로고
    • C/EBPbeta-2 confers EGF-independent growth and disrupts the normal acinar architecture of human mammary epithelial cells
    • L. Bundy S. Wells L. Sealy C/EBPbeta-2 confers EGF-independent growth and disrupts the normal acinar architecture of human mammary epithelial cells Mol Cancer 4 2005 43
    • (2005) Mol Cancer , vol.4 , pp. 43
    • Bundy, L.1    Wells, S.2    Sealy, L.3
  • 36
    • 28044437502 scopus 로고    scopus 로고
    • Chromatin domain activation via GATA-1 utilization of a small subset of dispersed GATA motifs within a broad chromosomal region
    • H. Im J.A. Grass K.D. Johnson S.I. Kim M.E. Boyer A.N. Imbalzano Chromatin domain activation via GATA-1 utilization of a small subset of dispersed GATA motifs within a broad chromosomal region Proc Natl Acad Sci USA 102 2005 17065 17070
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17065-17070
    • Im, H.1    Grass, J.A.2    Johnson, K.D.3    Kim, S.I.4    Boyer, M.E.5    Imbalzano, A.N.6
  • 37
    • 0028818693 scopus 로고
    • STT3, a novel essential gene related to the PKC1/STT1 protein kinase pathway, is involved in protein glycosylation in yeast
    • S. Yoshida Y. Ohya A. Nakano Y. Anraku STT3, a novel essential gene related to the PKC1/STT1 protein kinase pathway, is involved in protein glycosylation in yeast Gene 164 1995 167 172
    • (1995) Gene , vol.164 , pp. 167-172
    • Yoshida, S.1    Ohya, Y.2    Nakano, A.3    Anraku, Y.4
  • 38
    • 0032915136 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe stt3+ is a functional homologue of Saccharomyces cerevisiae STT3 which regulates oligosaccharyltransferase activity
    • S. Yoshida A. Matsuura J. Merregaert Y. Anraku Schizosaccharomyces pombe stt3+ is a functional homologue of Saccharomyces cerevisiae STT3 which regulates oligosaccharyltransferase activity Yeast 15 1999 497 505
    • (1999) Yeast , vol.15 , pp. 497-505
    • Yoshida, S.1    Matsuura, A.2    Merregaert, J.3    Anraku, Y.4
  • 39
    • 0026515866 scopus 로고
    • The Oct-1 POU domain mediates interactions between Oct-1 and other POU proteins
    • C.P. Verrijzer J.A. van Oosterhout P.C. van der Vliet The Oct-1 POU domain mediates interactions between Oct-1 and other POU proteins Mol Cell Biol 12 1992 542 551
    • (1992) Mol Cell Biol , vol.12 , pp. 542-551
    • Verrijzer, C.P.1    van Oosterhout, J.A.2    van der Vliet, P.C.3
  • 40
    • 0242268556 scopus 로고    scopus 로고
    • Oct-1 is posttranslationally modified and exhibits reduced capacity to bind cognate sites at late times after infection with herpes simplex virus 1
    • S.J. Advani L.O. Durand R.R. Weichselbaum B. Roizman Oct-1 is posttranslationally modified and exhibits reduced capacity to bind cognate sites at late times after infection with herpes simplex virus 1 J Virol 77 2003 11927 11932
    • (2003) J Virol , vol.77 , pp. 11927-11932
    • Advani, S.J.1    Durand, L.O.2    Weichselbaum, R.R.3    Roizman, B.4
  • 41
    • 0023663884 scopus 로고
    • Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain
    • J.T. Kadonaga K.R. Carner F.R. Masiarz R. Tjian Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain Cell 51 1987 1079 1090
    • (1987) Cell , vol.51 , pp. 1079-1090
    • Kadonaga, J.T.1    Carner, K.R.2    Masiarz, F.R.3    Tjian, R.4
  • 42
    • 0024331502 scopus 로고
    • Cognate DNA binding specificity retained after leucine zipper exchange between GCN4 and C/EBP
    • P. Agre P.F. Johnson S.L. McKnight Cognate DNA binding specificity retained after leucine zipper exchange between GCN4 and C/EBP Science 246 1989 922 926
    • (1989) Science , vol.246 , pp. 922-926
    • Agre, P.1    Johnson, P.F.2    McKnight, S.L.3
  • 43
    • 0025221436 scopus 로고
    • Transcriptional initiation is controlled by upstream GC-box interactions in a TATAA-less promoter
    • M.C. Blake R.C. Jambou A.G. Swick J.W. Kahn J.C. Azizkhan Transcriptional initiation is controlled by upstream GC-box interactions in a TATAA-less promoter Mol Cell Biol 10 1990 6632 6641
    • (1990) Mol Cell Biol , vol.10 , pp. 6632-6641
    • Blake, M.C.1    Jambou, R.C.2    Swick, A.G.3    Kahn, J.W.4    Azizkhan, J.C.5
  • 44
    • 0030765649 scopus 로고    scopus 로고
    • Disruption of the c/ebp alpha gene in adult mouse liver
    • Y.H. Lee B. Sauer P.F. Johnson F.J. Gonzalez Disruption of the c/ebp alpha gene in adult mouse liver Mol Cell Biol 17 1997 6014 6022
    • (1997) Mol Cell Biol , vol.17 , pp. 6014-6022
    • Lee, Y.H.1    Sauer, B.2    Johnson, P.F.3    Gonzalez, F.J.4
  • 45
    • 0033624014 scopus 로고    scopus 로고
    • C/EBPalpha inhibits cell growth via direct repression of E2F-DP-mediated transcription
    • B.A. Slomiany K.L. D'Arigo M.M. Kelly D.T. Kurtz C/EBPalpha inhibits cell growth via direct repression of E2F-DP-mediated transcription Mol Cell Biol 20 2000 5986 5997
    • (2000) Mol Cell Biol , vol.20 , pp. 5986-5997
    • Slomiany, B.A.1    D'Arigo, K.L.2    Kelly, M.M.3    Kurtz, D.T.4
  • 48
    • 0034013062 scopus 로고    scopus 로고
    • Class I and class II MHC bind self peptide sets that are strikingly different in their evolutionary characteristics
    • M. Yeager M. Carrington A.L. Hughes Class I and class II MHC bind self peptide sets that are strikingly different in their evolutionary characteristics Immunogenetics 51 2000 8 15
    • (2000) Immunogenetics , vol.51 , pp. 8-15
    • Yeager, M.1    Carrington, M.2    Hughes, A.L.3
  • 49
    • 0035060172 scopus 로고    scopus 로고
    • At the crossroads of cell biology and immunology: DRiPs and other sources of peptide ligands for MHC class I molecules
    • J.W. Yewdell U. Schubert J.R. Bennink At the crossroads of cell biology and immunology: DRiPs and other sources of peptide ligands for MHC class I molecules J Cell Sci 114 2001 845 851
    • (2001) J Cell Sci , vol.114 , pp. 845-851
    • Yewdell, J.W.1    Schubert, U.2    Bennink, J.R.3
  • 50
    • 0037072934 scopus 로고    scopus 로고
    • A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system
    • M.E. Illing R.S. Rajan N.F. Bence R.R. Kopito A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system J Biol Chem 277 2002 34150 34160
    • (2002) J Biol Chem , vol.277 , pp. 34150-34160
    • Illing, M.E.1    Rajan, R.S.2    Bence, N.F.3    Kopito, R.R.4
  • 51
    • 0346521283 scopus 로고    scopus 로고
    • Making sense of mass destruction: quantitating MHC class I antigen presentation
    • J.W. Yewdell E. Reits J. Neefjes Making sense of mass destruction: quantitating MHC class I antigen presentation Nat Rev Immunol 3 2003 952 961
    • (2003) Nat Rev Immunol , vol.3 , pp. 952-961
    • Yewdell, J.W.1    Reits, E.2    Neefjes, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.