메뉴 건너뛰기




Volumn 160, Issue 10, 1998, Pages 4859-4868

Dissociation of proteasomal degradation of biosynthesized viral proteins from generation of MHC class I-associated antigenic peptides

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEASOME; VIRUS PROTEIN;

EID: 0032524940     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (55)

References (75)
  • 1
    • 0026484826 scopus 로고
    • Cell biology of antigen processing and presentation to MHC class I molecule-restricted T lymphocytes
    • Yewdell, J. W., and J. R. Bennink. 1992. Cell biology of antigen processing and presentation to MHC class I molecule-restricted T lymphocytes. Adv. Immunol. 52:1.
    • (1992) Adv. Immunol. , vol.52 , pp. 1
    • Yewdell, J.W.1    Bennink, J.R.2
  • 2
    • 0027468145 scopus 로고
    • The biochemistry and cell biology of antigen processing and presentation
    • Germain, R. N., and D. H. Margulies. 1993. The biochemistry and cell biology of antigen processing and presentation. Annu. Rev. Immunol. 11:403.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 403
    • Germain, R.N.1    Margulies, D.H.2
  • 3
    • 0029001515 scopus 로고
    • Generation, translocation, and presentation of MHC class-I restricted peptides
    • Heemels, M.-T., and H. Ploegh. 1995. Generation, translocation, and presentation of MHC class-I restricted peptides. Annu. Rev. Biochem. 64:463.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 463
    • Heemels, M.-T.1    Ploegh, H.2
  • 4
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., K. Tanaka, and A. L. Goldberg. 1996. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:801.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 5
    • 0030248766 scopus 로고    scopus 로고
    • Peptide antigen production by the proteasome: Complexity provides efficiency
    • Groettrup, M., A. Soza, U. Kuckelkorn, and P.-M. Kloetzel. 1996. Peptide antigen production by the proteasome: complexity provides efficiency. Immunol. Today 17:429.
    • (1996) Immunol. Today , vol.17 , pp. 429
    • Groettrup, M.1    Soza, A.2    Kuckelkorn, U.3    Kloetzel, P.-M.4
  • 6
    • 0025123346 scopus 로고
    • The multicatalytic proteinase complex, a major extralysosomal proteolytic system
    • Orlowski, M. 1990. The multicatalytic proteinase complex, a major extralysosomal proteolytic system. Biochemistry 29:70259.
    • (1990) Biochemistry , vol.29 , pp. 70259
    • Orlowski, M.1
  • 7
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the Archaeon T. acidophilum at 3.4 Å resolution
    • Löwe, J., D. Stock, B. Jap, P. Zwickl, W. Baumeister, and R. Huber. 1995. Crystal structure of the 20S proteasome from the Archaeon T. acidophilum at 3.4 Å resolution. Science 268:533.
    • (1995) Science , vol.268 , pp. 533
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 9
    • 0027410433 scopus 로고
    • Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex: Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids
    • Orlowski, M., C. Cardozo, and C. Michaud. 1993. Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex: properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids. Biochemistry 32:1563.
    • (1993) Biochemistry , vol.32 , pp. 1563
    • Orlowski, M.1    Cardozo, C.2    Michaud, C.3
  • 10
    • 0031570893 scopus 로고    scopus 로고
    • The generation of MHC class I-associated peptides is only partially inhibited by proteasome inhibitors: Involvement of nonproteasomal cytosolic proteases in antigen processing?
    • Vinitsky, A., L. C. Antón, H. L. Snyder, M. Orlowski, J. R. Bennink, and J. W. Yewdell. 1997. The generation of MHC class I-associated peptides is only partially inhibited by proteasome inhibitors: involvement of nonproteasomal cytosolic proteases in antigen processing? J. Immunol. 159:554.
    • (1997) J. Immunol. , vol.159 , pp. 554
    • Vinitsky, A.1    Antón, L.C.2    Snyder, H.L.3    Orlowski, M.4    Bennink, J.R.5    Yewdell, J.W.6
  • 11
    • 0028180516 scopus 로고
    • A β-lactone related to lactacystin induces neunte outgrowth in a neuroblastoma cell line and inhibits cell cycle progression in an osteosarcoma cell line
    • Fenteany, G., R. F. Standaert, G. A. Reichard, E. J. Corey, and S. L. Schreiber. 1994. A β-lactone related to lactacystin induces neunte outgrowth in a neuroblastoma cell line and inhibits cell cycle progression in an osteosarcoma cell line. Proc. Natl. Acad. Sci. USA 91:3358.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3358
    • Fenteany, G.1    Standaert, R.F.2    Reichard, G.A.3    Corey, E.J.4    Schreiber, S.L.5
  • 12
    • 0026764311 scopus 로고
    • Proteolysis, proteasomes and antigen processing
    • Goldberg, A. L., and K. L. Rock. 1992. Proteolysis, proteasomes and antigen processing. Nature 357:375.
    • (1992) Nature , vol.357 , pp. 375
    • Goldberg, A.L.1    Rock, K.L.2
  • 13
    • 0022621891 scopus 로고
    • The LMP antigens: A stable MHC-controlled multisubunit protein complex
    • Monaco, J. J., and H. O. McDevitt. 1986. The LMP antigens: a stable MHC-controlled multisubunit protein complex. Hum. Immunol. 15:416.
    • (1986) Hum. Immunol. , vol.15 , pp. 416
    • Monaco, J.J.1    McDevitt, H.O.2
  • 14
    • 0027223877 scopus 로고
    • MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
    • Driscoll, J., M. G. Brown, D. Finley, and J. J. Monaco. 1993. MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature 365:262.
    • (1993) Nature , vol.365 , pp. 262
    • Driscoll, J.1    Brown, M.G.2    Finley, D.3    Monaco, J.J.4
  • 15
    • 0027214605 scopus 로고
    • Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • Gaczynska, M., K. L. Rock, and A. L. Goldberg. 1993. Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 365:264.
    • (1993) Nature , vol.365 , pp. 264
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 16
    • 0028097823 scopus 로고
    • Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasome
    • Boes, B., H. Hengel, T. Ruppert, G. Multhaup, U. H. Koszinowski, and P. M. Koetzel. 1994. Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasome. J. Exp. Med. 179:901.
    • (1994) J. Exp. Med. , vol.179 , pp. 901
    • Boes, B.1    Hengel, H.2    Ruppert, T.3    Multhaup, G.4    Koszinowski, U.H.5    Koetzel, P.M.6
  • 17
    • 0028890880 scopus 로고
    • Effects of Interferon gamma and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic proteases
    • Ustrell, V., G. Pratt, and M. Rechsteiner. 1995. Effects of Interferon gamma and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic proteases. Proc. Natl. Acad. Sci. USA 92:584.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 584
    • Ustrell, V.1    Pratt, G.2    Rechsteiner, M.3
  • 20
    • 0024095276 scopus 로고
    • Defective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen
    • Townsend, A., J. Bastin, K. Gould, G. Brownlee, M. Andrew, B. Coupar, D. Boyle, S. Chan, and G. Smith. 1988. Defective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen. J. Exp. Med. 168:1211.
    • (1988) J. Exp. Med. , vol.168 , pp. 1211
    • Townsend, A.1    Bastin, J.2    Gould, K.3    Brownlee, G.4    Andrew, M.5    Coupar, B.6    Boyle, D.7    Chan, S.8    Smith, G.9
  • 21
    • 0030977234 scopus 로고    scopus 로고
    • Targeting of HIV-1 antigens for rapid intracellular degradation enhances cytotoxic T lymphocyte (CTL) recognition and the induction of de novo CTL responses in vivo after immunization
    • Tobery, T. W., and R. F. Siliciano. 1997. Targeting of HIV-1 antigens for rapid intracellular degradation enhances cytotoxic T lymphocyte (CTL) recognition and the induction of de novo CTL responses in vivo after immunization. J. Exp. Med. 185:909.
    • (1997) J. Exp. Med. , vol.185 , pp. 909
    • Tobery, T.W.1    Siliciano, R.F.2
  • 22
    • 0029120173 scopus 로고
    • Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation
    • Grant, E. P., M. T. Michalek, A. L. Goldberg, and K. L. Rock. 1995. Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation. J. Immunol. 155:3750.
    • (1995) J. Immunol. , vol.155 , pp. 3750
    • Grant, E.P.1    Michalek, M.T.2    Goldberg, A.L.3    Rock, K.L.4
  • 23
    • 0030240571 scopus 로고    scopus 로고
    • Generation of naturally processed peptide/MHC class I complexes is independent of the stability of endogenously synthesized precursors
    • Goth, S., V. Nguyen, and N. Shastri. 1996. Generation of naturally processed peptide/MHC class I complexes is independent of the stability of endogenously synthesized precursors. J. Immunol. 157:1894.
    • (1996) J. Immunol. , vol.157 , pp. 1894
    • Goth, S.1    Nguyen, V.2    Shastri, N.3
  • 24
    • 0027263157 scopus 로고
    • A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation
    • Michalek, M. T., E. P. Grant, C. Gramm, A. L. Goldberg, and K. L. Rock. 1993. A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation. Nature 363:552.
    • (1993) Nature , vol.363 , pp. 552
    • Michalek, M.T.1    Grant, E.P.2    Gramm, C.3    Goldberg, A.L.4    Rock, K.L.5
  • 26
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K. L., C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A. L. Goldberg. 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761.
    • (1994) Cell , vol.78 , pp. 761
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 27
    • 0029966286 scopus 로고    scopus 로고
    • The requirement for proteasome activity in class I major histocompatibility complex antigen presentation is dictated by the length of preprocessed antigen
    • Yang, B., Y. S. Hahn, C. S. Hahn, and T. J. Braciale. 1996. The requirement for proteasome activity in class I major histocompatibility complex antigen presentation is dictated by the length of preprocessed antigen. J. Exp. Med. 183:1545.
    • (1996) J. Exp. Med. , vol.183 , pp. 1545
    • Yang, B.1    Hahn, Y.S.2    Hahn, C.S.3    Braciale, T.J.4
  • 28
    • 0028123031 scopus 로고
    • Injection of detergent-denatured ovalbumin primes murine class I-restricted cytotoxic T cells in vivo
    • Schirmbeck, R., W. Böhm, and J. Reimann. 1994. Injection of detergent-denatured ovalbumin primes murine class I-restricted cytotoxic T cells in vivo. Eur. J. Immunol. 24:2068.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 2068
    • Schirmbeck, R.1    Böhm, W.2    Reimann, J.3
  • 29
  • 30
    • 0028968217 scopus 로고
    • Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I molecules
    • Niedermann, G., S. Butz, H. G. Ihlenfeldt, R. Grimm, M. Lucchiari, H. Hoschützky, G. Jung, B. Maier, and K. Eichmann. 1995. Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I molecules. Immunity 2:289.
    • (1995) Immunity , vol.2 , pp. 289
    • Niedermann, G.1    Butz, S.2    Ihlenfeldt, H.G.3    Grimm, R.4    Lucchiari, M.5    Hoschützky, H.6    Jung, G.7    Maier, B.8    Eichmann, K.9
  • 32
    • 0027983803 scopus 로고
    • Molecular cloning and expression of gamma interferon-inducible activator of multicatalytic protease
    • Realini, C., W. Dubiel, G. Pratt, K. Ferrell, and M. Rechsteiner. 1994. Molecular cloning and expression of gamma interferon-inducible activator of multicatalytic protease. J. Biol. Chem. 269:20727.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20727
    • Realini, C.1    Dubiel, W.2    Pratt, G.3    Ferrell, K.4    Rechsteiner, M.5
  • 33
    • 0028970626 scopus 로고
    • The interferon-gamma-inducible 11S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20S proteasome in vitro
    • Groettrup, M., T. Ruppert, L. Kuehn, L. Seeger, S. Standera, U. Koszinowski, and P. M. Kloetzel. 1995. The interferon-gamma-inducible 11S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20S proteasome in vitro. J. Biol. Chem, 270:23808.
    • (1995) J. Biol. Chem , vol.270 , pp. 23808
    • Groettrup, M.1    Ruppert, T.2    Kuehn, L.3    Seeger, L.4    Standera, S.5    Koszinowski, U.6    Kloetzel, P.M.7
  • 35
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky, A., C. Michaud, J. C. Powers, and M. Orlowski. 1992. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 31:9421.
    • (1992) Biochemistry , vol.31 , pp. 9421
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 36
    • 0026758135 scopus 로고
    • A transient transfection system for identifying biosynthesized proteins processed and presented to class I MHC restricted T lymphocytes
    • Eisenlohr, L. C., J. W. Yewdell, and J. R. Bennink. 1992. A transient transfection system for identifying biosynthesized proteins processed and presented to class I MHC restricted T lymphocytes. J. Immunol. Methods 154:131.
    • (1992) J. Immunol. Methods , vol.154 , pp. 131
    • Eisenlohr, L.C.1    Yewdell, J.W.2    Bennink, J.R.3
  • 38
    • 1842290406 scopus 로고    scopus 로고
    • Introduction of a glycosylation site into a secreted protein provides evidence for a novel antigen processing pathway: Transport of precursors of MHC class I restricted peptides from the endoplasmic reticulum to the cytosol
    • Bacik, I., H. Link-Snyder, L. C. Antón, G. Russ, W. Chen, J. R. Bennink, L. Urge, L. Otvos, B. Dudkowska, L. Eisenlohr, and J. W. Yewdell. 1997. Introduction of a glycosylation site into a secreted protein provides evidence for a novel antigen processing pathway: transport of precursors of MHC class I restricted peptides from the endoplasmic reticulum to the cytosol. J. Exp. Med. 186.-479.
    • (1997) J. Exp. Med. , vol.186 , pp. 479
    • Bacik, I.1    Link-Snyder, H.2    Antón, L.C.3    Russ, G.4    Chen, W.5    Bennink, J.R.6    Urge, L.7    Otvos, L.8    Dudkowska, B.9    Eisenlohr, L.10    Yewdell, J.W.11
  • 39
    • 0021917922 scopus 로고
    • Vaccinia virus recombinants: Expression of VSV genes and protective immunization of mice and cattle
    • Mackett, M., J. K. Yilma, and B. Moss. 1985. Vaccinia virus recombinants: expression of VSV genes and protective immunization of mice and cattle. Science 227:433.
    • (1985) Science , vol.227 , pp. 433
    • Mackett, M.1    Yilma, J.K.2    Moss, B.3
  • 40
    • 0026455159 scopus 로고
    • Expression of a membrane protease enhances presentation of endogenous antigens to MHC class I-restricted T lymphocytes
    • Eisenlohr, L. C., I. Bacik, J. R. Bennink, K. Bernstein, and J. W. Yewdell. 1992. Expression of a membrane protease enhances presentation of endogenous antigens to MHC class I-restricted T lymphocytes. Cell 71:963.
    • (1992) Cell , vol.71 , pp. 963
    • Eisenlohr, L.C.1    Bacik, I.2    Bennink, J.R.3    Bernstein, K.4    Yewdell, J.W.5
  • 41
    • 0028208970 scopus 로고
    • TAP-independent presentation of endogenously synthesized peptides is enhanced by endoplasmic reticulum insertion sequences located at the amino but not carboxy terminus of the peptide
    • Bacik, I., J. H. Cox, R. Anderson, J. W. Yewdell, and J. R. Bennink. 1994. TAP-independent presentation of endogenously synthesized peptides is enhanced by endoplasmic reticulum insertion sequences located at the amino but not carboxy terminus of the peptide. J. Immunol. 152:381.
    • (1994) J. Immunol. , vol.152 , pp. 381
    • Bacik, I.1    Cox, J.H.2    Anderson, R.3    Yewdell, J.W.4    Bennink, J.R.5
  • 42
    • 0030849769 scopus 로고    scopus 로고
    • Localization, quantitation, and in situ detection of specific peplide-MHC class I complexes using a monoclonal antibody
    • Porgador, A., J. W. Yewdell, Y. Deng, J. R. Bennink, and R. N. Germain. 1997. Localization, quantitation, and in situ detection of specific peplide-MHC class I complexes using a monoclonal antibody. Immunity 6:715.
    • (1997) Immunity , vol.6 , pp. 715
    • Porgador, A.1    Yewdell, J.W.2    Deng, Y.3    Bennink, J.R.4    Germain, R.N.5
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 44
    • 0022246296 scopus 로고
    • Intracellular transport of membrane glycoproteins: Two closely related histocompatibility antigens differ in their rates of transit to the cell surface
    • Williams, D. B., S. J. Sweidler, and G. W. Hart. 1985. Intracellular transport of membrane glycoproteins: two closely related histocompatibility antigens differ in their rates of transit to the cell surface. J. Cell Biol. 101:725.
    • (1985) J. Cell Biol. , vol.101 , pp. 725
    • Williams, D.B.1    Sweidler, S.J.2    Hart, G.W.3
  • 45
    • 0025949447 scopus 로고
    • A 50-kDa cytosolic protein complexed with the 90-kDa heat shock protein (hsp90) is the same protein complexed with pp60 v-src hsp90 in cells transformed by the Rous sarcoma virus
    • Whitelaw, M. L., K. Hutchison, and G. H. Perdew. 1991. A 50-kDa cytosolic protein complexed with the 90-kDa heat shock protein (hsp90) is the same protein complexed with pp60 v-src hsp90 in cells transformed by the Rous sarcoma virus. J. Biol. Chem. 266:16436.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16436
    • Whitelaw, M.L.1    Hutchison, K.2    Perdew, G.H.3
  • 46
    • 0031569179 scopus 로고    scopus 로고
    • MHC class I-associated peptides produced from endogenous gene products with vastly different efficiencies
    • Antón, L. C., J. W. Yewdell, and J. R. Bennink. 1997. MHC class I-associated peptides produced from endogenous gene products with vastly different efficiencies. J. Immunol. 158:2535.
    • (1997) J. Immunol. , vol.158 , pp. 2535
    • Antón, L.C.1    Yewdell, J.W.2    Bennink, J.R.3
  • 47
    • 0028096715 scopus 로고
    • Trimming of antigenic peptides in an early secretory compartment
    • Snyder, H. L., J. W. Yewdell, and J. R. Bennink. 1994. Trimming of antigenic peptides in an early secretory compartment. J. Exp. Med. 180:2389.
    • (1994) J. Exp. Med. , vol.180 , pp. 2389
    • Snyder, H.L.1    Yewdell, J.W.2    Bennink, J.R.3
  • 48
    • 0022337375 scopus 로고
    • Structure and expression of genes encoding murine Qa-2 class I antigens
    • Mellor, A. L., J. Antoniou, and P. J. Robinson. 1985. Structure and expression of genes encoding murine Qa-2 class I antigens. Proc. Natl. Acad. Sci. USA 82:5920.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5920
    • Mellor, A.L.1    Antoniou, J.2    Robinson, P.J.3
  • 49
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., D. Finley, and A. Varshavsky. 1986. In vivo half-life of a protein is a function of its amino-terminal residue. Science 234:179.
    • (1986) Science , vol.234 , pp. 179
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 50
    • 0028150688 scopus 로고
    • Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes
    • Vinitsky, A., C. Cardozo, L. Sepp-Lorenzino, C. Michaud, and M. Orlowski. 1994. Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes. J. Biol. Chem. 269:29860.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29860
    • Vinitsky, A.1    Cardozo, C.2    Sepp-Lorenzino, L.3    Michaud, C.4    Orlowski, M.5
  • 51
    • 0028136875 scopus 로고
    • A new inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S proteasome) induces accumulation of ubiquitin-protein conjugates in a neuronal cell
    • Figueiredo-Pereira, M. E., K. A. Berg, and S. Wilk. 1994. A new inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S proteasome) induces accumulation of ubiquitin-protein conjugates in a neuronal cell. J. Neurochem. 63:1578.
    • (1994) J. Neurochem. , vol.63 , pp. 1578
    • Figueiredo-Pereira, M.E.1    Berg, K.A.2    Wilk, S.3
  • 52
    • 0025200973 scopus 로고
    • The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo: Processing of altered iso-1-cytochromes c created by oligonucleotide transformation
    • Moerschell, R. P., Y. Hosokawa, S. Tsunasawa, and F. Sherman. 1990. The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo: processing of altered iso-1-cytochromes c created by oligonucleotide transformation. J. Biol. Chem. 265:19638.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19638
    • Moerschell, R.P.1    Hosokawa, Y.2    Tsunasawa, S.3    Sherman, F.4
  • 53
    • 0025740521 scopus 로고
    • Identification of naturally processed viral nonapeptides allows their quantification in infected cells and suggests an allele-specific T cell epitope forecast
    • Falk, K., O. Rötzschke, K. Deres, J. Metzger, G. Jung, and H.-G. Rammensee. 1991. Identification of naturally processed viral nonapeptides allows their quantification in infected cells and suggests an allele-specific T cell epitope forecast. J. Exp. Med. 174:425.
    • (1991) J. Exp. Med. , vol.174 , pp. 425
    • Falk, K.1    Rötzschke, O.2    Deres, K.3    Metzger, J.4    Jung, G.5    Rammensee, H.-G.6
  • 54
    • 0026014942 scopus 로고
    • k-restricted T cell epitopes within the influenza A/PR/8/34 virus hemagglutinin
    • k-restricted T cell epitopes within the influenza A/PR/8/34 virus hemagglutinin. J. Virol. 65:5401.
    • (1991) J. Virol. , vol.65 , pp. 5401
    • Gould, K.G.1    Scotney, H.2    Brownlee, G.G.3
  • 55
    • 0024500652 scopus 로고
    • Brefeldin A implicates egress from endoplasmic reticulum in class I restricted antigen presentation
    • Nuchtern, J. G., J. S. Bonifacino, W. E. Biddison, and R. D. Klausner. 1989. Brefeldin A implicates egress from endoplasmic reticulum in class I restricted antigen presentation. Nature 339:223.
    • (1989) Nature , vol.339 , pp. 223
    • Nuchtern, J.G.1    Bonifacino, J.S.2    Biddison, W.E.3    Klausner, R.D.4
  • 56
    • 0024338401 scopus 로고
    • Brefeldin A specifically inhibits presentation of protein antigens to cytotoxic T lymphocytes
    • Yewdell, J. W., and J. R. Bennink. 1989. Brefeldin A specifically inhibits presentation of protein antigens to cytotoxic T lymphocytes. Science 244:1072.
    • (1989) Science , vol.244 , pp. 1072
    • Yewdell, J.W.1    Bennink, J.R.2
  • 58
    • 0027260585 scopus 로고
    • Heat shock protein 70-associated peptides elicit specific cancer immunity
    • Udono, H., and P. K. Srivastava. 1993. Heat shock protein 70-associated peptides elicit specific cancer immunity. J. Exp. Med. 178:1391.
    • (1993) J. Exp. Med. , vol.178 , pp. 1391
    • Udono, H.1    Srivastava, P.K.2
  • 59
    • 0027527563 scopus 로고
    • Peptide-binding heat shock proteins in the endoplasmic reticulum: Role in immune response to cancer and in antigen presentation
    • Srivastava, P. K. 1993. Peptide-binding heat shock proteins in the endoplasmic reticulum: role in immune response to cancer and in antigen presentation. Adv. Cancer Res. 62:153.
    • (1993) Adv. Cancer Res. , vol.62 , pp. 153
    • Srivastava, P.K.1
  • 61
    • 0031114456 scopus 로고    scopus 로고
    • Point mutation flanking a CTL epitope ablates in vitro and in vivo recognition of a full-length viral protein
    • Yellen-Shaw, A. J., E. J. Wherry, G. C. Dubois, and L. C. Eisenlohr. 1997. Point mutation flanking a CTL epitope ablates in vitro and in vivo recognition of a full-length viral protein. J. Immunol. 158:3227.
    • (1997) J. Immunol. , vol.158 , pp. 3227
    • Yellen-Shaw, A.J.1    Wherry, E.J.2    Dubois, G.C.3    Eisenlohr, L.C.4
  • 62
    • 0031568385 scopus 로고    scopus 로고
    • Regulation of class-I restricted epitope processing by local or distal flanking sequence
    • Yellen-Shaw, A. J., and L. C. Eisenlohr. 1997. Regulation of class-I restricted epitope processing by local or distal flanking sequence. J. Immunol. 158:1727.
    • (1997) J. Immunol. , vol.158 , pp. 1727
    • Yellen-Shaw, A.J.1    Eisenlohr, L.C.2
  • 63
    • 0031032422 scopus 로고    scopus 로고
    • The proteasome-specinc inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells
    • Cerundolo, V., A. Benham, V. Braud, S. Mukherjee, K. Gould, B. Macino, J. Neefjes, and A. Townsend. 1997. The proteasome-specinc inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells, Eur. J. Immunol. 27:336.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 336
    • Cerundolo, V.1    Benham, A.2    Braud, V.3    Mukherjee, S.4    Gould, K.5    Macino, B.6    Neefjes, J.7    Townsend, A.8
  • 64
    • 0028907938 scopus 로고
    • Genes encoded in the major histocompatibility complex aifecting the generation of peptides for TAP transport
    • Cerundolo, V., A. Kelly, T. Elliot, J. Trowsdale, and A. Townsend. 1995. Genes encoded in the major histocompatibility complex aifecting the generation of peptides for TAP transport. Eur. J. Immunol. 25:554.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 554
    • Cerundolo, V.1    Kelly, A.2    Elliot, T.3    Trowsdale, J.4    Townsend, A.5
  • 65
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey, and S. L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726.
    • (1995) Science , vol.268 , pp. 726
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 66
    • 0030926777 scopus 로고    scopus 로고
    • Lactacystin and clato-iactacystin betalactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation
    • Craiu, A., M. Gaczynska, T. Akopian, C. F. Gramm, G. Fenteany, A. L. Goldberg, and K. L. Rock. 1997. Lactacystin and clato-iactacystin betalactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation. J. Blol. Chem. 272:13437.
    • (1997) J. Blol. Chem. , vol.272 , pp. 13437
    • Craiu, A.1    Gaczynska, M.2    Akopian, T.3    Gramm, C.F.4    Fenteany, G.5    Goldberg, A.L.6    Rock, K.L.7
  • 67
    • 18744428952 scopus 로고    scopus 로고
    • Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme
    • Ostrowska, H., C. Wojcik, S. Omura, and K. Woroowski. 1997. Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme. Biochem. Biophys. Res. Commun. 234:729.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 729
    • Ostrowska, H.1    Wojcik, C.2    Omura, S.3    Woroowski, K.4
  • 68
    • 0029965803 scopus 로고    scopus 로고
    • The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-L-norlcucinal. decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum
    • Hughes, E. A., B. Ortmann, M. Surman, and P. Cresswell. 1996. The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-L-norlcucinal. decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum. J. Exp. Med. 183:1569.
    • (1996) J. Exp. Med. , vol.183 , pp. 1569
    • Hughes, E.A.1    Ortmann, B.2    Surman, M.3    Cresswell, P.4
  • 69
    • 2642607007 scopus 로고    scopus 로고
    • An endoplasmic reticulum-targeting signal sequence enhances the immunogenicity of an immunorecessive simian virus 40 large T antigen cytotoxic T-lymphocyte epitope
    • Fu, T.-M., L. M. Mylin, T. D. Schell, I. Bacik, G. Russ, J. W. Yewdell, J. R. Bennink, and S. Tevethia. 1998. An endoplasmic reticulum-targeting signal sequence enhances the immunogenicity of an immunorecessive simian virus 40 large T antigen cytotoxic T-lymphocyte epitope. J. Virol. 72:1469.
    • (1998) J. Virol. , vol.72 , pp. 1469
    • Fu, T.-M.1    Mylin, L.M.2    Schell, T.D.3    Bacik, I.4    Russ, G.5    Yewdell, J.W.6    Bennink, J.R.7    Tevethia, S.8
  • 70
    • 0030239693 scopus 로고    scopus 로고
    • Defective ribosomal products (DRiPs): A major source of antigenic peptides for MHC class I molecules?
    • Yewdell, J. W., L. C. Antón, and J. R. Bennink. 1996. Defective ribosomal products (DRiPs): a major source of antigenic peptides for MHC class I molecules? J. Immunol. 157:1823.
    • (1996) J. Immunol. , vol.157 , pp. 1823
    • Yewdell, J.W.1    Antón, L.C.2    Bennink, J.R.3
  • 71
    • 0029780370 scopus 로고    scopus 로고
    • Evidence that a rapidly turning over protein, normally degraded by proteasomes, regulates hsp72 gene transcription in HepG2 cells
    • Zhou, M., X. Wu, and H. N. Ginsberg. 1996. Evidence that a rapidly turning over protein, normally degraded by proteasomes, regulates hsp72 gene transcription in HepG2 cells. J. Biol. Chem. 271:24769.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24769
    • Zhou, M.1    Wu, X.2    Ginsberg, H.N.3
  • 72
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • Bush, K. T., A. L. Goldberg, and S. K. Nigam. 1997. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J. Biol. Chem. 272:9086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9086
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 73
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox, J. S., and P. Walter. 1996. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87:391.
    • (1996) Cell , vol.87 , pp. 391
    • Cox, J.S.1    Walter, P.2
  • 75
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • Srivastava, P. K., H. Udono, N. E. Blachere, and Z. Li. 1994. Heat shock proteins transfer peptides during antigen processing and CTL priming, Immunogenetics 39:93.
    • (1994) Immunogenetics , vol.39 , pp. 93
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.