메뉴 건너뛰기




Volumn 175, Issue 4, 2005, Pages 2252-2260

Insertion of the dibasic motif in the flanking region of a cryptic self-determinant leads to activation of the epitope-specific T cells

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; LYSOZYME; PROTEINASE;

EID: 23444450284     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.175.4.2252     Document Type: Article
Times cited : (17)

References (60)
  • 1
    • 0024428816 scopus 로고
    • How some T cells escape tolerance induction
    • Gammon, G., and E. Sercarz. 1989. How some T cells escape tolerance induction. Nature 342: 183-185.
    • (1989) Nature , vol.342 , pp. 183-185
    • Gammon, G.1    Sercarz, E.2
  • 3
    • 0027524738 scopus 로고
    • Dominant determinants in hen eggwhite lysozyme correspond to the cryptic determinants within its self-homologue, mouse lysozyme: Implications in shaping of the T cell repertoire and autoimmunity
    • Moudgil, K. D., and E. E. Sercarz. 1993. Dominant determinants in hen eggwhite lysozyme correspond to the cryptic determinants within its self-homologue, mouse lysozyme: implications in shaping of the T cell repertoire and autoimmunity. J. Exp. Med. 178: 2131-2138.
    • (1993) J. Exp. Med. , vol.178 , pp. 2131-2138
    • Moudgil, K.D.1    Sercarz, E.E.2
  • 4
    • 3242790763 scopus 로고    scopus 로고
    • Mouse lysozyme-M knockout mice reveal how the self determinant hierarchy shapes the T cell repertoire against this circulating self antigen in wild-type mice
    • Sinha, P., H. H. Chi, H. R. Kim, B. E. Clausen, B. Pederson, E. E. Sercarz, I. Forster, and K. D. Moudgil. 2004. Mouse lysozyme-M knockout mice reveal how the self determinant hierarchy shapes the T cell repertoire against this circulating self antigen in wild-type mice. J. Immunol. 173: 1763-1771.
    • (2004) J. Immunol. , vol.173 , pp. 1763-1771
    • Sinha, P.1    Chi, H.H.2    Kim, H.R.3    Clausen, B.E.4    Pederson, B.5    Sercarz, E.E.6    Forster, I.7    Moudgil, K.D.8
  • 6
    • 0036172037 scopus 로고    scopus 로고
    • Influence of a dominant cryptic epitope on autoimmune T cell tolerance
    • Anderton, S. M., N. J. Viner, P. Matharu, P. A. Lowrey, and D. C. Wraith. 2002. Influence of a dominant cryptic epitope on autoimmune T cell tolerance. Nat. Immunol. 3: 175-181.
    • (2002) Nat. Immunol. , vol.3 , pp. 175-181
    • Anderton, S.M.1    Viner, N.J.2    Matharu, P.3    Lowrey, P.A.4    Wraith, D.C.5
  • 7
    • 0025738012 scopus 로고
    • T cells that recognize peptide sequences of self MHC class II molecules exist in syngeneic mice
    • Agrawal, B., M. Manickasundari, E. Fraga, and B. Singh. 1991. T cells that recognize peptide sequences of self MHC class II molecules exist in syngeneic mice. J. Immunol. 147: 383-390.
    • (1991) J. Immunol. , vol.147 , pp. 383-390
    • Agrawal, B.1    Manickasundari, M.2    Fraga, E.3    Singh, B.4
  • 8
    • 0027479452 scopus 로고
    • The inability to process a self-peptide allows autoreactive T cells to escape tolerance
    • Mamula, M. J. 1993. The inability to process a self-peptide allows autoreactive T cells to escape tolerance. J. Exp. Med. 177: 567-571.
    • (1993) J. Exp. Med. , vol.177 , pp. 567-571
    • Mamula, M.J.1
  • 9
    • 0026664422 scopus 로고
    • Spreading of T-cell autoimmunity to cryptic determinants of an autoantigen
    • Lehmann, P. V., T. Forsthuber, A. Miller, and E. E. Sercarz. 1992. Spreading of T-cell autoimmunity to cryptic determinants of an autoantigen. Nature 358: 155-157.
    • (1992) Nature , vol.358 , pp. 155-157
    • Lehmann, P.V.1    Forsthuber, T.2    Miller, A.3    Sercarz, E.E.4
  • 10
    • 0036229420 scopus 로고    scopus 로고
    • Cryptic determinants and promiscuous sequences on human acetylcholine receptor: HLA-dependent dichotomy in T-cell function
    • Raju, R., E. Marietta, J. Vinasco, B. M. Conti-Fine, A. J. Infante, and C. S. David. 2002. Cryptic determinants and promiscuous sequences on human acetylcholine receptor: HLA-dependent dichotomy in T-cell function. Hum. Immunol. 63: 237-247.
    • (2002) Hum. Immunol. , vol.63 , pp. 237-247
    • Raju, R.1    Marietta, E.2    Vinasco, J.3    Conti-Fine, B.M.4    Infante, A.J.5    David, C.S.6
  • 11
    • 0032858439 scopus 로고    scopus 로고
    • Reversal of immunodominance among autoantigenic T-cell epitopes
    • Fairchild, P. J. 1999. Reversal of immunodominance among autoantigenic T-cell epitopes. Autoimmunity 30: 209-221.
    • (1999) Autoimmunity , vol.30 , pp. 209-221
    • Fairchild, P.J.1
  • 13
    • 0032526853 scopus 로고    scopus 로고
    • Endogenous myelin basic protein inactivates the high avidity T cell repertoire
    • Targoni, O. S., and P. V. Lehmann. 1998. Endogenous myelin basic protein inactivates the high avidity T cell repertoire. J. Exp. Med. 187: 2055-2063.
    • (1998) J. Exp. Med. , vol.187 , pp. 2055-2063
    • Targoni, O.S.1    Lehmann, P.V.2
  • 14
  • 15
    • 0032845223 scopus 로고    scopus 로고
    • The self-directed T cell repertoire against mouse lysozyme reflects the influence of the hierarchy of its own determinants and can be engaged by a foreign lysozyme
    • Moudgil, K. D., S. Southwood, A. Ametani, K. Kim, A. Sette, and E. E. Sercarz. 1999. The self-directed T cell repertoire against mouse lysozyme reflects the influence of the hierarchy of its own determinants and can be engaged by a foreign lysozyme. J. Immunol. 163: 4232-4237.
    • (1999) J. Immunol. , vol.163 , pp. 4232-4237
    • Moudgil, K.D.1    Southwood, S.2    Ametani, A.3    Kim, K.4    Sette, A.5    Sercarz, E.E.6
  • 16
    • 0025797161 scopus 로고
    • Recognition of peptides that are immunopathogenic but cryptic: Mechanisms that allow lymphocytes sensitized against cryptic peptides to initiate pathogenic autoimmune processes
    • Lipham, W. J., T. M. Redmond, H. Takahashi, J. A. Berzofsky, B. Wiggert, G. J. Chader, and I. Gery. 1991. Recognition of peptides that are immunopathogenic but cryptic: mechanisms that allow lymphocytes sensitized against cryptic peptides to initiate pathogenic autoimmune processes. J. Immunol. 146: 3757-3762.
    • (1991) J. Immunol. , vol.146 , pp. 3757-3762
    • Lipham, W.J.1    Redmond, T.M.2    Takahashi, H.3    Berzofsky, J.A.4    Wiggert, B.5    Chader, G.J.6    Gery, I.7
  • 17
    • 0036533552 scopus 로고    scopus 로고
    • Autoreactive T cells revealed in the normal repertoire: Escape from negative selection and peripheral tolerance
    • Yan, J., and M. J. Mamula. 2002. Autoreactive T cells revealed in the normal repertoire: escape from negative selection and peripheral tolerance. J. Immunol. 168: 3188-3194.
    • (2002) J. Immunol. , vol.168 , pp. 3188-3194
    • Yan, J.1    Mamula, M.J.2
  • 18
    • 0027943292 scopus 로고
    • The T cell repertoire against cryptic self determinants and its involvement in autoimmunity and cancer
    • Moudgil, K. D., and E. E. Sercarz. 1994. The T cell repertoire against cryptic self determinants and its involvement in autoimmunity and cancer. Clin. Immunol. Immunopathol. 73: 283-289.
    • (1994) Clin. Immunol. Immunopathol. , vol.73 , pp. 283-289
    • Moudgil, K.D.1    Sercarz, E.E.2
  • 19
    • 0029006389 scopus 로고
    • How can cryptic epitopes trigger autoimmunity?
    • Lanzavecchia, A. 1995. How can cryptic epitopes trigger autoimmunity? J. Exp. Med. 181: 1945-1948.
    • (1995) J. Exp. Med. , vol.181 , pp. 1945-1948
    • Lanzavecchia, A.1
  • 20
    • 0036481263 scopus 로고    scopus 로고
    • Epitope spreading in immune-mediated diseases: Implications for immunotherapy
    • Vanderlugt, C. L., and S. D. Miller. 2002. Epitope spreading in immune-mediated diseases: implications for immunotherapy. Nat. Rev. Immunol. 2: 85-95.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 85-95
    • Vanderlugt, C.L.1    Miller, S.D.2
  • 21
    • 0029069499 scopus 로고
    • T cell determinants from autoantibodies to DNA can up-regulate autoimmunity in murine systemic lupus erythematosus
    • Singh, R. R., V. Kumar, F. M. Ebling, S. Southwood, A. Sette, E. E. Sercarz, and B. H. Hahn. 1995. T cell determinants from autoantibodies to DNA can up-regulate autoimmunity in murine systemic lupus erythematosus. J. Exp. Med. 181: 2017-2027.
    • (1995) J. Exp. Med. , vol.181 , pp. 2017-2027
    • Singh, R.R.1    Kumar, V.2    Ebling, F.M.3    Southwood, S.4    Sette, A.5    Sercarz, E.E.6    Hahn, B.H.7
  • 22
    • 0031595750 scopus 로고    scopus 로고
    • Modulation of the immunogenicity of antigenic determinants by their flanking residues
    • Moudgil, K. D., E. E. Sercarz, and I. S. Grewal. 1998. Modulation of the immunogenicity of antigenic determinants by their flanking residues. Immunol. Today 19: 217-220.
    • (1998) Immunol. Today , vol.19 , pp. 217-220
    • Moudgil, K.D.1    Sercarz, E.E.2    Grewal, I.S.3
  • 23
    • 0029035307 scopus 로고
    • Modulation of antigen processing by bound antibodies can boost or suppress class II major histocompatibility complex presentation of different T cell determinants
    • Simitsek, P. D., D. G. Campbell, A. Lanzavecchia, N. Fairweather, and C. Watts. 1995. Modulation of antigen processing by bound antibodies can boost or suppress class II major histocompatibility complex presentation of different T cell determinants. J. Exp. Med. 181: 1957-1963.
    • (1995) J. Exp. Med. , vol.181 , pp. 1957-1963
    • Simitsek, P.D.1    Campbell, D.G.2    Lanzavecchia, A.3    Fairweather, N.4    Watts, C.5
  • 24
    • 0029069507 scopus 로고
    • HIVgp120 activates autoreactive CD4-specific T cell responses by unveiling of hidden CD4 peptides during processing
    • Salemi, S., A. P. Caporossi, L. Boffa, M. G. Longobardi, and V. Barnaba. 1995. HIVgp120 activates autoreactive CD4-specific T cell responses by unveiling of hidden CD4 peptides during processing. J. Exp. Med. 181: 2253-2257.
    • (1995) J. Exp. Med. , vol.181 , pp. 2253-2257
    • Salemi, S.1    Caporossi, A.P.2    Boffa, L.3    Longobardi, M.G.4    Barnaba, V.5
  • 25
    • 0033980525 scopus 로고    scopus 로고
    • Increasing the frequency of T-cell precursors specific for a cryptic epitope of hen-egg lysozyme converts it to an immunodominant epitope
    • Thatcher, T. H., D. P. O'Brien, S. Altuwaijri, and R. K. Barth. 2000. Increasing the frequency of T-cell precursors specific for a cryptic epitope of hen-egg lysozyme converts it to an immunodominant epitope. Immunology 99: 235-242.
    • (2000) Immunology , vol.99 , pp. 235-242
    • Thatcher, T.H.1    O'Brien, D.P.2    Altuwaijri, S.3    Barth, R.K.4
  • 26
    • 0030712935 scopus 로고    scopus 로고
    • Antigen-presenting cells and the selection of immunodominant epitopes
    • Blum, J. S., C. Ma, and S. Kovats. 1997. Antigen-presenting cells and the selection of immunodominant epitopes. Crit. Rev. Immunol. 17: 411-417.
    • (1997) Crit. Rev. Immunol. , vol.17 , pp. 411-417
    • Blum, J.S.1    Ma, C.2    Kovats, S.3
  • 27
    • 0033807322 scopus 로고    scopus 로고
    • DM determines the cryptic and immunodominant fate of T cell epitopes
    • Nanda, N. K., and A. J. Sant. 2000. DM determines the cryptic and immunodominant fate of T cell epitopes. J. Exp. Med. 192: 781-788.
    • (2000) J. Exp. Med. , vol.192 , pp. 781-788
    • Nanda, N.K.1    Sant, A.J.2
  • 28
    • 0023772346 scopus 로고
    • Influences of antigen processing on the expression of the T cell repertoire: Evidence for MHC-specific hindering structures on the products of processing
    • Brett, S. J., K. B. Cease, and J. A. Berzofsky. 1988. Influences of antigen processing on the expression of the T cell repertoire: evidence for MHC-specific hindering structures on the products of processing. J. Exp. Med. 168: 357-373.
    • (1988) J. Exp. Med. , vol.168 , pp. 357-373
    • Brett, S.J.1    Cease, K.B.2    Berzofsky, J.A.3
  • 30
    • 43949158638 scopus 로고
    • Can antitumor immune responses discriminate between self and nonself?
    • Moudgil, K. D., and E. E. Sercarz. 1994. Can antitumor immune responses discriminate between self and nonself? Immunol. Today 15: 353-355.
    • (1994) Immunol. Today , vol.15 , pp. 353-355
    • Moudgil, K.D.1    Sercarz, E.E.2
  • 31
    • 0036605567 scopus 로고    scopus 로고
    • Generation of T-cell immunity to the HER-2/neu protein after active immunization with HER-2/neu peptide-based vaccines
    • Disis, M. L., T. A. Gooley, K. Rinn, D. Davis, M. Piepkorn, M. A. Cheever, K. L. Knutson, and K. Schiffman. 2002. Generation of T-cell immunity to the HER-2/neu protein after active immunization with HER-2/neu peptide-based vaccines. J. Clin. Oncol. 20: 2624-2632.
    • (2002) J. Clin. Oncol. , vol.20 , pp. 2624-2632
    • Disis, M.L.1    Gooley, T.A.2    Rinn, K.3    Davis, D.4    Piepkorn, M.5    Cheever, M.A.6    Knutson, K.L.7    Schiffman, K.8
  • 33
    • 0020008342 scopus 로고
    • Post-translational proteolysis in polypeptide hormone biosynthesis
    • Docherty, K., and D. F. Steiner. 1982. Post-translational proteolysis in polypeptide hormone biosynthesis. Annu. Rev. Physiol. 44: 625-638.
    • (1982) Annu. Rev. Physiol. , vol.44 , pp. 625-638
    • Docherty, K.1    Steiner, D.F.2
  • 34
    • 0023947194 scopus 로고
    • Peptide hormones and neuropeptides: Proteolytic processing of the precursor regulatory peptides
    • Burger, E. 1988. Peptide hormones and neuropeptides: proteolytic processing of the precursor regulatory peptides. Arzneimittelforschung 38: 754-761.
    • (1988) Arzneimittelforschung , vol.38 , pp. 754-761
    • Burger, E.1
  • 35
    • 0025368575 scopus 로고
    • An in vivo characterization of the cleavage site specificity of the insulin cell prohormone processing enzymes
    • Thorne, B. A., and G. Thomas. 1990. An in vivo characterization of the cleavage site specificity of the insulin cell prohormone processing enzymes. J. Biol. Chem. 265: 8436-8443.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8436-8443
    • Thorne, B.A.1    Thomas, G.2
  • 36
    • 0026750606 scopus 로고
    • Prohormone thiol protease and enkephalin precursor processing: Cleavage at dibasic and monobasic sites
    • Krieger, T. J., L. Mende-Mueller, and V. Y. Hook. 1992. Prohormone thiol protease and enkephalin precursor processing: cleavage at dibasic and monobasic sites. J. Neurochem. 59: 26-31.
    • (1992) J. Neurochem. , vol.59 , pp. 26-31
    • Krieger, T.J.1    Mende-Mueller, L.2    Hook, V.Y.3
  • 37
    • 0033548650 scopus 로고    scopus 로고
    • Analysis of the relationship between enzyme activity and its internal motion using nuclear magnetic resonance: 15N relaxation studies of wild-type and mutant lysozyme
    • Mine, S., S. Tate, T. Ueda, M. Kainosho, and T. Imoto. 1999. Analysis of the relationship between enzyme activity and its internal motion using nuclear magnetic resonance: 15N relaxation studies of wild-type and mutant lysozyme. J. Mol. Biol. 286: 1547-1565.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1547-1565
    • Mine, S.1    Tate, S.2    Ueda, T.3    Kainosho, M.4    Imoto, T.5
  • 38
    • 0013967156 scopus 로고
    • Serum and urinary lysozyme (muramidase) in monocytic and monomyelocytic leukemia
    • Osserman, E. F., and D. P. Lawlor. 1966. Serum and urinary lysozyme (muramidase) in monocytic and monomyelocytic leukemia. J. Exp. Med. 124: 921-952.
    • (1966) J. Exp. Med. , vol.124 , pp. 921-952
    • Osserman, E.F.1    Lawlor, D.P.2
  • 39
    • 0037278025 scopus 로고    scopus 로고
    • Solution structure and activity of mouse lysozyme M
    • Obita, T., T. Ueda, and T. Imoto. 2003. Solution structure and activity of mouse lysozyme M. Cell Mol Life Sci. 60: 176-184.
    • (2003) Cell Mol Life Sci. , vol.60 , pp. 176-184
    • Obita, T.1    Ueda, T.2    Imoto, T.3
  • 40
    • 0005077914 scopus 로고    scopus 로고
    • Antigen processing and presentation
    • A. M. K. J. E. Coligan, D. H. Margulies, E. M. Shevach, and W. Strober, eds. John Wiley & Sons, Hoboken
    • Harding, C. V. 1997. Antigen processing and presentation. In Current Protocols in Immunology. A. M. K. J. E. Coligan, D. H. Margulies, E. M. Shevach, and W. Strober, eds. John Wiley & Sons, Hoboken, pp. 16.0.1.-16.0.20.
    • (1997) Current Protocols in Immunology
    • Harding, C.V.1
  • 41
    • 0015821893 scopus 로고
    • A rapid method for the isolation of functional thymus-derived murine lymphocytes
    • Julius, M. H., E. Simpson, and L. A. Herzenberg. 1973. A rapid method for the isolation of functional thymus-derived murine lymphocytes. Eur. J. Immunol. 3: 645-649.
    • (1973) Eur. J. Immunol. , vol.3 , pp. 645-649
    • Julius, M.H.1    Simpson, E.2    Herzenberg, L.A.3
  • 42
    • 0029937756 scopus 로고    scopus 로고
    • Complexes generated by the binding of free peptides to class II MHC molecules are antigenically diverse compared with those generated by intracellular processing
    • Viner, N. J., C. A. Nelson, B. Deck, and E. R. Unanue. 1996. Complexes generated by the binding of free peptides to class II MHC molecules are antigenically diverse compared with those generated by intracellular processing. J. Immunol. 156: 2365-2368.
    • (1996) J. Immunol. , vol.156 , pp. 2365-2368
    • Viner, N.J.1    Nelson, C.A.2    Deck, B.3    Unanue, E.R.4
  • 43
    • 0027220178 scopus 로고
    • Minute quantities of a single immunodominant foreign epitope are presented as large nested sets by major histocompatibility complex class II molecules
    • Vignali, D. A., R. G. Urban, R. M. Chicz, and J. L. Strominger. 1993. Minute quantities of a single immunodominant foreign epitope are presented as large nested sets by major histocompatibility complex class II molecules. Eur. J. Immunol. 23: 1602-1607.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 1602-1607
    • Vignali, D.A.1    Urban, R.G.2    Chicz, R.M.3    Strominger, J.L.4
  • 44
    • 0026553120 scopus 로고
    • Constraints in antigen processing result in unresponsiveness to a T cell epitope of hen egg lysozyme in C57BL/6 mice
    • Kim, B. S., and Y. S. Jang. 1992. Constraints in antigen processing result in unresponsiveness to a T cell epitope of hen egg lysozyme in C57BL/6 mice. Eur. J. Immunol. 22: 775-782.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 775-782
    • Kim, B.S.1    Jang, Y.S.2
  • 45
    • 0029739249 scopus 로고    scopus 로고
    • Overcoming the crypticity of a viral T cell determinant by insertion into a chimeric bacterial protein
    • Lo-Man, R., P. Martineau, B. Manoury-Schwartz, M. Hofnung, and C. Leclerc. 1996. Overcoming the crypticity of a viral T cell determinant by insertion into a chimeric bacterial protein. Int. Immunol. 8: 1245-1255.
    • (1996) Int. Immunol. , vol.8 , pp. 1245-1255
    • Lo-Man, R.1    Martineau, P.2    Manoury-Schwartz, B.3    Hofnung, M.4    Leclerc, C.5
  • 46
    • 0030802693 scopus 로고    scopus 로고
    • T cell receptor recognition of MHC class II-bound peptide flanking residues enhances immunogenicity and results in altered TCR V region usage
    • Carson, R. T., K. M. Vignali, D. L. Woodland, and D. A. Vignali. 1997. T cell receptor recognition of MHC class II-bound peptide flanking residues enhances immunogenicity and results in altered TCR V region usage. Immunity 7: 387-399.
    • (1997) Immunity , vol.7 , pp. 387-399
    • Carson, R.T.1    Vignali, K.M.2    Woodland, D.L.3    Vignali, D.A.4
  • 47
    • 0026768974 scopus 로고
    • Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs
    • Rudensky, A., P. Preston-Hurlburt, B. K. al-Ramadi, J. Rothbard, and C. A. Janeway, Jr. 1992. Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs. Nature 359: 429-431.
    • (1992) Nature , vol.359 , pp. 429-431
    • Rudensky, A.1    Preston-Hurlburt, P.2    Al-Ramadi, B.K.3    Rothbard, J.4    Janeway Jr., C.A.5
  • 48
    • 0034235311 scopus 로고    scopus 로고
    • Cutting edge: Introduction of an endopeptidase cleavage motif into a determinant flanking region of hen egg lysozyme results in enhanced T cell determinant display
    • Schneider, S. C., J. Ohmen, L. Fosdick, B. Gladstone, J. Guo, A. Ametani, E. E. Sercarz, and H. Deng. 2000. Cutting edge: introduction of an endopeptidase cleavage motif into a determinant flanking region of hen egg lysozyme results in enhanced T cell determinant display. J. Immunol. 165: 20-23.
    • (2000) J. Immunol. , vol.165 , pp. 20-23
    • Schneider, S.C.1    Ohmen, J.2    Fosdick, L.3    Gladstone, B.4    Guo, J.5    Ametani, A.6    Sercarz, E.E.7    Deng, H.8
  • 49
    • 0343307146 scopus 로고    scopus 로고
    • Eukaryotic protein processing: Endoproteolysis of precursor proteins
    • Seidah, N. G., and M. Chretien. 1997. Eukaryotic protein processing: endoproteolysis of precursor proteins. Curr. Opin. Biotechnol. 8: 602-607.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 602-607
    • Seidah, N.G.1    Chretien, M.2
  • 50
  • 51
    • 0036083664 scopus 로고    scopus 로고
    • Proprotein convertases in tumor progression and malignancy: Novel targets in cancer therapy
    • Khatib, A. M., G. Siegfried, M. Chretien, P. Metrakos, and N. G. Seidah. 2002. Proprotein convertases in tumor progression and malignancy: novel targets in cancer therapy. Am. J. Pathol. 160: 1921-1935.
    • (2002) Am. J. Pathol. , vol.160 , pp. 1921-1935
    • Khatib, A.M.1    Siegfried, G.2    Chretien, M.3    Metrakos, P.4    Seidah, N.G.5
  • 53
    • 0040142226 scopus 로고    scopus 로고
    • Sorting of furin at the rrans-Golgi network: Interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins
    • Teuchert, M., W. Schafer, S. Berghofer, B. Hoflack, H. D. Klenk, and W. Garten. 1999. Sorting of furin at the rrans-Golgi network: interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins. J. Biol. Chem. 274: 8199-8207.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8199-8207
    • Teuchert, M.1    Schafer, W.2    Berghofer, S.3    Hoflack, B.4    Klenk, H.D.5    Garten, W.6
  • 54
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas, G. 2002. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell Biol. 3: 753-766.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 753-766
    • Thomas, G.1
  • 55
    • 2542466750 scopus 로고    scopus 로고
    • Role of cytoplasmic domain serines in intracellular trafficking of furin
    • Schapiro, F. B., T. T. Soe, W. G. Mallet, and F. R. Maxfield. 2004. Role of cytoplasmic domain serines in intracellular trafficking of furin. Mol. Biol. Cell 15: 2884-2894.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2884-2894
    • Schapiro, F.B.1    Soe, T.T.2    Mallet, W.G.3    Maxfield, F.R.4
  • 56
    • 0031665409 scopus 로고    scopus 로고
    • The phenotype of H-2M-deficient mice is dependent on the MHC class II molecules expressed
    • Wolf, P. R., S. Tourne, T. Miyazaki, C. Benoist, D. Mathis, and H. L. Ploegh. 1998. The phenotype of H-2M-deficient mice is dependent on the MHC class II molecules expressed. Eur. J. Immunol. 28: 2605-2618.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 2605-2618
    • Wolf, P.R.1    Tourne, S.2    Miyazaki, T.3    Benoist, C.4    Mathis, D.5    Ploegh, H.L.6
  • 57
    • 0029921609 scopus 로고    scopus 로고
    • Variation in HLA-DM expression influences conversion of MHC class II αβ:class II-associated invariant chain peptide complexes to mature peptide-bound class II αβ dimers in a normal B cell line
    • Ramachandra, L., S. Kovats, S. Eastman, and A. Y. Rudensky. 1996. Variation in HLA-DM expression influences conversion of MHC class II αβ:class II-associated invariant chain peptide complexes to mature peptide-bound class II αβ dimers in a normal B cell line. J. Immunol. 156: 2196-2204.
    • (1996) J. Immunol. , vol.156 , pp. 2196-2204
    • Ramachandra, L.1    Kovats, S.2    Eastman, S.3    Rudensky, A.Y.4
  • 60
    • 2942741160 scopus 로고    scopus 로고
    • The regulatory C-terminal determinants within mycobacterial heat shock protein 65 are cryptic and cross-reactive with the dominant self homologs: Implications for the pathogenesis of autoimmune arthritis
    • Durai, M., H. R. Kim, and K. D. Moudgil. 2004. The regulatory C-terminal determinants within mycobacterial heat shock protein 65 are cryptic and cross-reactive with the dominant self homologs: implications for the pathogenesis of autoimmune arthritis. J. Immunol. 173: 181-188.
    • (2004) J. Immunol. , vol.173 , pp. 181-188
    • Durai, M.1    Kim, H.R.2    Moudgil, K.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.