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Volumn 158, Issue 9, 1997, Pages 4341-4350

Heat Shock Protein 72 on Tumor Cells: A Recognition Structure for Natural Killer Cells

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 72; MEMBRANE ANTIGEN;

EID: 0031132876     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (342)

References (56)
  • 1
    • 0026460892 scopus 로고
    • Mammalian stress response: Cell physiology, structure/function of stress proteins, and implications for medicine and disease
    • Welch, W. J. 1992. Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease. Physiol. Rev. 72:1063.
    • (1992) Physiol. Rev. , vol.72 , pp. 1063
    • Welch, W.J.1
  • 2
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402.
    • (1993) Microbiol. Rev. , vol.57 , pp. 402
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 3
    • 0021259444 scopus 로고
    • Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells
    • Welch, W. J., and J. R. Feramisco. 1984. Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells. J. Biol. Chem. 259:4501.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4501
    • Welch, W.J.1    Feramisco, J.R.2
  • 4
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • Ferrarini, M., S. Heltai, M. R. Zocchi, and C. Rugarli. 1992. Unusual expression and localization of heat-shock proteins in human tumor cells. Int. J. Cancer 51:613.
    • (1992) Int. J. Cancer , vol.51 , pp. 613
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 5
    • 0028953056 scopus 로고
    • A stress-inducible 72 kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells
    • Multhoff, G., C. Botzler, M. Wiesnet, E. Müller, T. Meier, W. Wilmanns, and R. D. Issels. 1995. A stress-inducible 72 kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells. Int. J. Cancer 61:272.
    • (1995) Int. J. Cancer , vol.61 , pp. 272
    • Multhoff, G.1    Botzler, C.2    Wiesnet, M.3    Müller, E.4    Meier, T.5    Wilmanns, W.6    Issels, R.D.7
  • 6
    • 0024674842 scopus 로고
    • The mycobacterial GroEL stress protein: A common target of T-cell recognition in infection and autoimmunity
    • Lamb, J. R., V. Bal, J. B. Rothbard, A. Mehlert, P. Mendez-Samperio, and D. B. Young. 1989. The mycobacterial GroEL stress protein: a common target of T-cell recognition in infection and autoimmunity. J. Autoimmun. 2(Suppl.):93.
    • (1989) J. Autoimmun. , vol.2 , Issue.SUPPL. , pp. 93
    • Lamb, J.R.1    Bal, V.2    Rothbard, J.B.3    Mehlert, A.4    Mendez-Samperio, P.5    Young, D.B.6
  • 7
    • 0026535812 scopus 로고
    • Cell surface localization of a 72 kilodalton heat shock protein in retroocular fibroblasts from patients with Graves' ophthalmopathy
    • Heufelder, A. E., B. E. Wenzel, and R. S. Bahn. 1992. Cell surface localization of a 72 kilodalton heat shock protein in retroocular fibroblasts from patients with Graves' ophthalmopathy. J. Clin. Endocrinol. Metab. 74:732.
    • (1992) J. Clin. Endocrinol. Metab. , vol.74 , pp. 732
    • Heufelder, A.E.1    Wenzel, B.E.2    Bahn, R.S.3
  • 9
    • 0027154993 scopus 로고
    • Spontaneous heat shock protein synthesis by alveolar macrophages in interstitial lung disease associated with phagocytosis of eosinophils
    • Polla, B. S., S. Kantengwa, G. J. Gleich, M. Kondo, C. M. Reimert, and A. F. Junod. 1993. Spontaneous heat shock protein synthesis by alveolar macrophages in interstitial lung disease associated with phagocytosis of eosinophils. Eur. Respir. J. 6:483.
    • (1993) Eur. Respir. J. , vol.6 , pp. 483
    • Polla, B.S.1    Kantengwa, S.2    Gleich, G.J.3    Kondo, M.4    Reimert, C.M.5    Junod, A.F.6
  • 11
    • 0029079390 scopus 로고
    • Co-segregation of tumor immunogenicity with expression of inducible but not constitutive hsp70 in rat colon carcinomas
    • Menoret, A., Y. Patry, C. Burg, and J. Le-Pendu. 1995. Co-segregation of tumor immunogenicity with expression of inducible but not constitutive hsp70 in rat colon carcinomas. J. Immunol. 155:740.
    • (1995) J. Immunol. , vol.155 , pp. 740
    • Menoret, A.1    Patry, Y.2    Burg, C.3    Le-Pendu, J.4
  • 12
    • 0021339151 scopus 로고
    • The serologically unique cell surface antigen of Zajdela ascitic hepatoma is also its tumor-associated transplantation antigen
    • Srivastava, P. K., and M. R. Das. 1984. The serologically unique cell surface antigen of Zajdela ascitic hepatoma is also its tumor-associated transplantation antigen. Int. J. Cancer 33:417.
    • (1984) Int. J. Cancer , vol.33 , pp. 417
    • Srivastava, P.K.1    Das, M.R.2
  • 15
    • 0028301079 scopus 로고
    • Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90. and hsp70
    • Udono, H., and P. K. Srivastava. 1994. Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90. and hsp70. J. Immunol. 152: 5398.
    • (1994) J. Immunol. , vol.152 , pp. 5398
    • Udono, H.1    Srivastava, P.K.2
  • 16
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • Suto, R., and P. K. Srivastava. 1995. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 269:1585.
    • (1995) Science , vol.269 , pp. 1585
    • Suto, R.1    Srivastava, P.K.2
  • 17
    • 0028000105 scopus 로고
    • Heat shock proteins in immune response to cancer: The Fourth Paradigm
    • Srivastava, P. K. 1994. Heat shock proteins in immune response to cancer: the Fourth Paradigm. Experientia 50:1054.
    • (1994) Experientia , vol.50 , pp. 1054
    • Srivastava, P.K.1
  • 18
    • 0027379256 scopus 로고
    • The primary signal in the biological perception of temperature: Pd-catalyzed hydrogenation of membrane lipids stimulated the expression of the desA gene in Synechocystis PCC6803
    • Vigh, L., D. A. Los, I. Horvath, and N. Murata. 1993. The primary signal in the biological perception of temperature: Pd-catalyzed hydrogenation of membrane lipids stimulated the expression of the desA gene in Synechocystis PCC6803. Proc. Natl. Acad. Sci. USA 90:9090.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9090
    • Vigh, L.1    Los, D.A.2    Horvath, I.3    Murata, N.4
  • 19
    • 0027056047 scopus 로고
    • A molecular model for membrane fusion based on solution studies of an amphiphilic peptide from HIV gp41
    • Fujii, G., S. Horvath, S. Woodward, F. Eiserling, and D. Eisenberg. 1992. A molecular model for membrane fusion based on solution studies of an amphiphilic peptide from HIV gp41. Protein Sci. 1:1454.
    • (1992) Protein Sci. , vol.1 , pp. 1454
    • Fujii, G.1    Horvath, S.2    Woodward, S.3    Eiserling, F.4    Eisenberg, D.5
  • 20
    • 0027381473 scopus 로고
    • Distinct phenotypic and functional characteristics of human natural killer cells obtained by rapid interleukin 2-induced adherence to plastic
    • Vujanovic, N. L., H. Rabinovich, Y. J. Lee, R. B. Herberman, and T. L. Whiteside. 1993. Distinct phenotypic and functional characteristics of human natural killer cells obtained by rapid interleukin 2-induced adherence to plastic. Cell. Immunol. 151:133.
    • (1993) Cell. Immunol. , vol.151 , pp. 133
    • Vujanovic, N.L.1    Rabinovich, H.2    Lee, Y.J.3    Herberman, R.B.4    Whiteside, T.L.5
  • 21
    • 0028978682 scopus 로고
    • CD3-large granular lymphocytes recognize a heat-inducible immunogenic determinant associated with the 72 kDa heat shock protein on human sarcoma cells
    • Multhoff, G., C. Botzler, M. Wiesnet, G. Eissner, and R. Issels. 1995. CD3-large granular lymphocytes recognize a heat-inducible immunogenic determinant associated with the 72 kDa heat shock protein on human sarcoma cells. Blood 86:1374.
    • (1995) Blood , vol.86 , pp. 1374
    • Multhoff, G.1    Botzler, C.2    Wiesnet, M.3    Eissner, G.4    Issels, R.5
  • 22
    • 0018701862 scopus 로고
    • Monoclonal antibodies defining distinctive human T cell surface antigens
    • Kung, P., G. Goldstein, E. L. Reinherz, and S. F. Schlossman. 1979. Monoclonal antibodies defining distinctive human T cell surface antigens. Science 206:347.
    • (1979) Science , vol.206 , pp. 347
    • Kung, P.1    Goldstein, G.2    Reinherz, E.L.3    Schlossman, S.F.4
  • 23
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide and flow cytometry
    • Nicoletti, I., Migliorati, G., Pagliacci, M. C., Grignani, F., and Riccardi, C. 1991. A rapid and simple method for measuring thymocyte apoptosis by propidium iodide and flow cytometry. J. Immunol. Methods 139:271.
    • (1991) J. Immunol. Methods , vol.139 , pp. 271
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 24
    • 0019830409 scopus 로고
    • Localization of gold in biological tissue: A photochemical method for light and electronmicroscopy
    • Danscher, G. 1981. Localization of gold in biological tissue: a photochemical method for light and electronmicroscopy. Histochemistry 71:81.
    • (1981) Histochemistry , vol.71 , pp. 81
    • Danscher, G.1
  • 25
    • 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
  • 26
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 28
    • 0020326047 scopus 로고
    • Monoclonal antibodies: Purification, fragmentation and application to structural and functional studies of class I MHC antigens
    • Parham, P., M. J. Androlewicz, F. M. Brodsky, N. J. Holmes, and J. P. Ways. 1982. Monoclonal antibodies: purification, fragmentation and application to structural and functional studies of class I MHC antigens. J. Immunol. Methods 53:133.
    • (1982) J. Immunol. Methods , vol.53 , pp. 133
    • Parham, P.1    Androlewicz, M.J.2    Brodsky, F.M.3    Holmes, N.J.4    Ways, J.P.5
  • 29
    • 0642311927 scopus 로고
    • Stress proteins, arthritis and autoimmunity
    • Winfield, J. B. 1989. Stress proteins, arthritis and autoimmunity. Arthritis Rheum. 31:1221.
    • (1989) Arthritis Rheum. , vol.31 , pp. 1221
    • Winfield, J.B.1
  • 30
    • 0028138250 scopus 로고
    • T cells reactive to an inducible heat shock protein induce disease in toxin-induced interstitial nephritis
    • Weiss, R. A., M. P. Madaio, J. E. Tomaszewski, and C. J. Kelly. 1994. T cells reactive to an inducible heat shock protein induce disease in toxin-induced interstitial nephritis. J. Exp. Med. 180:2239.
    • (1994) J. Exp. Med. , vol.180 , pp. 2239
    • Weiss, R.A.1    Madaio, M.P.2    Tomaszewski, J.E.3    Kelly, C.J.4
  • 32
    • 0027397058 scopus 로고
    • The roles of heat shock proteins and immediate early genes in central nervous system normal function and pathology
    • Chopp, M. 1993. The roles of heat shock proteins and immediate early genes in central nervous system normal function and pathology. Curr. Opin. Neurol. Neurosurg. 6:6.
    • (1993) Curr. Opin. Neurol. Neurosurg. , vol.6 , pp. 6
    • Chopp, M.1
  • 33
    • 0028912572 scopus 로고
    • Heat shock protein reactivity of lymphocytes isolated from heterotopic rat cardiac allografts
    • Moliterno, R., L. Valdivia, F. Pan, and R. J. Duquesnoy. 1995. Heat shock protein reactivity of lymphocytes isolated from heterotopic rat cardiac allografts. Transplantation 59:598.
    • (1995) Transplantation , vol.59 , pp. 598
    • Moliterno, R.1    Valdivia, L.2    Pan, F.3    Duquesnoy, R.J.4
  • 34
    • 0026793232 scopus 로고
    • Recognition and killing of tumour cells expressing heat shock protein 65 kDa with immunotoxins containing saporin
    • Poccia, F., P. Piselli, S. Di-Cesare, S. Bach, V. Colizzi, M. Mattei, A. Bolognesi, and F. Stirpe. 1992. Recognition and killing of tumour cells expressing heat shock protein 65 kDa with immunotoxins containing saporin. Br. J. Cancer 66: 427.
    • (1992) Br. J. Cancer , vol.66 , pp. 427
    • Poccia, F.1    Piselli, P.2    Di-Cesare, S.3    Bach, S.4    Colizzi, V.5    Mattei, M.6    Bolognesi, A.7    Stirpe, F.8
  • 35
    • 0026690529 scopus 로고
    • Surface expressed heat-shock proteins by stressed or human immunodeficiency virus (HIV)-infected lymphoid cells represent the target for antibody-dependent cellular cytotoxicity
    • Di-Cesare, S., F. Poccia, A. Mastino, and V. Colizzi. 1992. Surface expressed heat-shock proteins by stressed or human immunodeficiency virus (HIV)-infected lymphoid cells represent the target for antibody-dependent cellular cytotoxicity. Immunology 76:341.
    • (1992) Immunology , vol.76 , pp. 341
    • Di-Cesare, S.1    Poccia, F.2    Mastino, A.3    Colizzi, V.4
  • 36
    • 0025894722 scopus 로고
    • Heat shock proteins in host-parasite interactions
    • Polla, B. S. 1991. Heat shock proteins in host-parasite interactions. Immunol. Today 12:38.
    • (1991) Immunol. Today , vol.12 , pp. 38
    • Polla, B.S.1
  • 37
    • 0026068780 scopus 로고
    • Heat shock proteins as antigens of bacterial and parasitic pathogens
    • Shinnick, T. M. 1991. Heat shock proteins as antigens of bacterial and parasitic pathogens. Curr. Top. Microbiol. Immunol. 167:145.
    • (1991) Curr. Top. Microbiol. Immunol. , vol.167 , pp. 145
    • Shinnick, T.M.1
  • 38
    • 0025294233 scopus 로고
    • Human humoral immunity to hsp70 during Trypanosoma cruzi infection
    • Engman, D. M., E. A. Dragon, and J. E. Donelson. 1990. Human humoral immunity to hsp70 during Trypanosoma cruzi infection. J. Immunol. 144:3987.
    • (1990) J. Immunol. , vol.144 , pp. 3987
    • Engman, D.M.1    Dragon, E.A.2    Donelson, J.E.3
  • 39
    • 0028228822 scopus 로고
    • Distribution of HSP72 and monomeric laminin receptor expression in human liung cancers infiltrated hy gamma delta T lymphocytes
    • Ferrarini, M., S. M. Pupa, M. R. Zocchi, C. Rgarli, and S. Menard. 1994. Distribution of HSP72 and monomeric laminin receptor expression in human liung cancers infiltrated hy gamma delta T lymphocytes. Int. J. Cancer 57:486.
    • (1994) Int. J. Cancer , vol.57 , pp. 486
    • Ferrarini, M.1    Pupa, S.M.2    Zocchi, M.R.3    Rgarli, C.4    Menard, S.5
  • 40
    • 0027385461 scopus 로고
    • 70 kDa heat shock cognate protein is a transformation-associated antigen and a possible target for the host's anti-tumor immunity
    • Tamura, Y., N. Tsuboi, N. Sato, and K. Kikuchi. 1993. 70 kDa heat shock cognate protein is a transformation-associated antigen and a possible target for the host's anti-tumor immunity. J. Immunol. 151:5516.
    • (1993) J. Immunol. , vol.151 , pp. 5516
    • Tamura, Y.1    Tsuboi, N.2    Sato, N.3    Kikuchi, K.4
  • 41
  • 42
    • 0030224714 scopus 로고    scopus 로고
    • Cell surface expression of heat shock proteins and the immune response
    • Multhoff, G., and L. Hightower. 1996. Cell surface expression of heat shock proteins and the immune response. Cell Stress Chaperones 1:167.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 167
    • Multhoff, G.1    Hightower, L.2
  • 43
    • 0027955522 scopus 로고
    • Heat shock proteins expressed on the surface of human T cell leukemia virus type I-infected cell lines induce autoantibodies in rabbits
    • Chouchane, L., S. Bowers, S. Sawasdikosol, R. M. Simpson, and T. J. Kindt. 1994. Heat shock proteins expressed on the surface of human T cell leukemia virus type I-infected cell lines induce autoantibodies in rabbits. J. Infect. Dis. 169:253.
    • (1994) J. Infect. Dis. , vol.169 , pp. 253
    • Chouchane, L.1    Bowers, S.2    Sawasdikosol, S.3    Simpson, R.M.4    Kindt, T.J.5
  • 44
    • 0026548976 scopus 로고
    • Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmatic reticulum-Golgi complex
    • Mignatti, P., T. Morimoto, and D. B. Rifkin. 1992. Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmatic reticulum-Golgi complex. J. Cell. Physiol. 151: 81.
    • (1992) J. Cell. Physiol. , vol.151 , pp. 81
    • Mignatti, P.1    Morimoto, T.2    Rifkin, D.B.3
  • 45
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1β, a protein lacking a signal sequence
    • Rubartelli, A., F. Cozzolino, M. Talio, and R. Sitia. 1990. A novel secretory pathway for interleukin-1β, a protein lacking a signal sequence. EMBO J. 9:1503.
    • (1990) EMBO J. , vol.9 , pp. 1503
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 46
    • 0028135554 scopus 로고
    • HSP70s and lysosomal proteolysis
    • Terleckey, S. R. 1994. HSP70s and lysosomal proteolysis. Experientia 50:1021.
    • (1994) Experientia , vol.50 , pp. 1021
    • Terleckey, S.R.1
  • 47
    • 0028857636 scopus 로고
    • Expression of hsp70 induced in CHO cells by 45.0 degrees C hyperthermia is cell cycle associated and DNA synthesis dependent
    • Hang, H., and M. H. Fox. 1995. Expression of hsp70 induced in CHO cells by 45.0 degrees C hyperthermia is cell cycle associated and DNA synthesis dependent. Cytometry 19:119.
    • (1995) Cytometry , vol.19 , pp. 119
    • Hang, H.1    Fox, M.H.2
  • 48
    • 0024587611 scopus 로고
    • Cell cycle-dependent association of HSP70 with specific cellular proteins
    • Milarski, K. L., W. J. Welch, and R. I. Morimoto. 1989. Cell cycle-dependent association of HSP70 with specific cellular proteins. J. Cell Biol. 108:413.
    • (1989) J. Cell Biol. , vol.108 , pp. 413
    • Milarski, K.L.1    Welch, W.J.2    Morimoto, R.I.3
  • 49
    • 0026692820 scopus 로고
    • An 80-kilodalton antigen from Histoplasma capsulatum that has homology to heat shock protein 70 induces cell-mediated immune responses and protection in mice
    • Gomez, F. J., A. M. Gomez, and G. S. J. Deepe. 1992. An 80-kilodalton antigen from Histoplasma capsulatum that has homology to heat shock protein 70 induces cell-mediated immune responses and protection in mice. Infect. Immun. 60:2565.
    • (1992) Infect. Immun. , vol.60 , pp. 2565
    • Gomez, F.J.1    Gomez, A.M.2    Deepe, G.S.J.3
  • 50
    • 0029925942 scopus 로고    scopus 로고
    • Noncytotoxic alkyl-lysophospholipid treatment increases sensitivity of leukemic K562 cells to lysis by natural killer (NK) cells
    • Botzler, C., H. J. Kolb, R. D. Issels, and G. Multhoff. 1996. Noncytotoxic alkyl-lysophospholipid treatment increases sensitivity of leukemic K562 cells to lysis by natural killer (NK) cells. Int. J. Cancer 65:633.
    • (1996) Int. J. Cancer , vol.65 , pp. 633
    • Botzler, C.1    Kolb, H.J.2    Issels, R.D.3    Multhoff, G.4
  • 51
    • 0028337687 scopus 로고
    • Ontogeny, specific functions and receptors of human natural killer cells
    • Moretta, L., E. Ciccone, A. Poggi, M. C. Mingari, and A. Moretta. 1994. Ontogeny, specific functions and receptors of human natural killer cells. Immunol. Lett. 40:83.
    • (1994) Immunol. Lett. , vol.40 , pp. 83
    • Moretta, L.1    Ciccone, E.2    Poggi, A.3    Mingari, M.C.4    Moretta, A.5
  • 52
    • 0028982812 scopus 로고
    • Tiazofurin induces a down-modulation of ICAM-1 expression on K562 target cells impairing NK adhesion and killing
    • Zamai, L., G. Zauli, A. Bavelloni, S. Marmiroli, A. Cataldi, G. Weber, and M. Vitale. 1995. Tiazofurin induces a down-modulation of ICAM-1 expression on K562 target cells impairing NK adhesion and killing. Cell. Immunol. 164:100.
    • (1995) Cell. Immunol. , vol.164 , pp. 100
    • Zamai, L.1    Zauli, G.2    Bavelloni, A.3    Marmiroli, S.4    Cataldi, A.5    Weber, G.6    Vitale, M.7
  • 53
    • 0025966856 scopus 로고
    • Target lysis hy human LAK cells is critically dependent upon target binding properties, but LFA-1, LFA-3 and ICAM-1 are not the major adhesion ligands on targets
    • Quillet-Mary, A., L. Cavarec, N. Kermarrec, C. Marchiol-Fournigault, M. L. Gil, H. Conjeaud, and D. Fradelizi. 1991. Target lysis hy human LAK cells is critically dependent upon target binding properties, but LFA-1, LFA-3 and ICAM-1 are not the major adhesion ligands on targets. Int. J. Cancer 47:473.
    • (1991) Int. J. Cancer , vol.47 , pp. 473
    • Quillet-Mary, A.1    Cavarec, L.2    Kermarrec, N.3    Marchiol-Fournigault, C.4    Gil, M.L.5    Conjeaud, H.6    Fradelizi, D.7
  • 54
    • 0026516255 scopus 로고
    • Expression of the adhesion molecules ICAM-1 and ICAM-2 on tumor cell lines does not correlate with their susceptibility to natural killer cell-mediated cytolysis: Evidence for additional ligands for effector cell beta integrins
    • Akella, R., and R. E. Hall. 1992. Expression of the adhesion molecules ICAM-1 and ICAM-2 on tumor cell lines does not correlate with their susceptibility to natural killer cell-mediated cytolysis: evidence for additional ligands for effector cell beta integrins. Eur. J. Immunol. 22:1069.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1069
    • Akella, R.1    Hall, R.E.2
  • 55
    • 0028947936 scopus 로고
    • Coexpression of two functionally independent p58 inhibitory receptors in human natural killer cell clones results in the inability to kill all normal allogeneic target cells
    • Vitale, M., S. Sivori, D. Pende, L. Moretta, and A. Moretta. 1995. Coexpression of two functionally independent p58 inhibitory receptors in human natural killer cell clones results in the inability to kill all normal allogeneic target cells. Proc. Natl. Accad. Sci. USA 92:3536.
    • (1995) Proc. Natl. Accad. Sci. USA , vol.92 , pp. 3536
    • Vitale, M.1    Sivori, S.2    Pende, D.3    Moretta, L.4    Moretta, A.5
  • 56
    • 0028920183 scopus 로고
    • Carbohydrate recognition by a natural killer cell receptor, Ly-49C
    • Brennan, J., F. Takei, S. Wong, and D. L. Mager. 1995. Carbohydrate recognition by a natural killer cell receptor, Ly-49C. J. Biol. Chem. 270:9691.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9691
    • Brennan, J.1    Takei, F.2    Wong, S.3    Mager, D.L.4


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