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Volumn 23, Issue 3, 1998, Pages 153-158

Localization of pNT22 70 kDa heat shock cognate-like protein in the plasma membrane

Author keywords

Cell surface expression; Epitope mapping; hsc73; Triton X 114 phase separation

Indexed keywords

CELL MEMBRANE PROTEIN; HEAT SHOCK PROTEIN 70; MONOCLONAL ANTIBODY;

EID: 0031665599     PISSN: 03867196     EISSN: None     Source Type: Journal    
DOI: 10.1247/csf.23.153     Document Type: Article
Times cited : (15)

References (27)
  • 2
  • 3
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • BORDIER, C. 1981. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol Chem., 256: 1604-1607.
    • (1981) J. Biol Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 4
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: Functional principles of molecular chaperones
    • BUCHNER, J. 1996. Supervising the fold: functional principles of molecular chaperones. FASEB J., 10: 10-19.
    • (1996) FASEB J. , vol.10 , pp. 10-19
    • Buchner, J.1
  • 5
    • 0002237472 scopus 로고
    • Cytosolic hsp70 of Saccharomyces cerevisiae: Roles in protein synthesis, protein translocation, proteolysis, and regulation
    • (R.I. Morimoto, A. Tissieres and C. Georgopoulos, Eds.), Cold Spring Harbor Press, Cold Spring Harbor, NY
    • CRAIG, E.A., BAXTER, B.K., BECKER, J., HALLADAY, J., and ZIEGELHOFFER, T. 1994. Cytosolic hsp70 of Saccharomyces cerevisiae: roles in protein synthesis, protein translocation, proteolysis, and regulation. In "The Biology of Heat Shock Proteins and Molecular Chaperones." (R.I. Morimoto, A. Tissieres and C. Georgopoulos, Eds.), Cold Spring Harbor Press, Cold Spring Harbor, NY.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones
    • Craig, E.A.1    Baxter, B.K.2    Becker, J.3    Halladay, J.4    Ziegelhoffer, T.5
  • 6
    • 0023649886 scopus 로고
    • Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein
    • DWORNICZAK, B. and MIRAULT, M.E. 1987. Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein. Nucleic Acids Res., 15: 5181-5197.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 5181-5197
    • Dworniczak, B.1    Mirault, M.E.2
  • 7
    • 0027294030 scopus 로고
    • The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors
    • ENGLUND, P.T. 1993. The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors. Annu. Rev. Biochem., 62: 121-138.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 121-138
    • Englund, P.T.1
  • 8
    • 0027181575 scopus 로고
    • Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5
    • FATHALLAH, D.M., CHELIF, D., DELLAGI, K., and ARNAOUT, M.A. 1993. Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5. J. Immunol., 151: 810-813.
    • (1993) J. Immunol. , vol.151 , pp. 810-813
    • Fathallah, D.M.1    Chelif, D.2    Dellagi, K.3    Arnaout, M.A.4
  • 9
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • FREEMAN, B.C., MYERS, M., P., SCHUMACHER, R., and MORIMOTO, R.I. 1995. Identification of a regulatory motif in hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J., 14: 2281-2292.
    • (1995) EMBO J. , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 10
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • FRYDMAN, J. and HÖHFELD, J. 1997. Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci., 22: 87-92.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Höhfeld, J.2
  • 11
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • HARTL, F.U. 1996. Molecular chaperones in cellular protein folding. Nature, 381: 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 12
    • 0023176996 scopus 로고
    • A major immunogen in Schistoma mansoni infections is homologous to the heat-shock protein hsp70
    • HEDSTROM, R., CULPEPPER, J., HARRISON, R.A., ADABIAN, N., and NEWPORT, G. 1987. A major immunogen in Schistoma mansoni infections is homologous to the heat-shock protein hsp70. J. Exp. Med., 165: 1430-1435.
    • (1987) J. Exp. Med. , vol.165 , pp. 1430-1435
    • Hedstrom, R.1    Culpepper, J.2    Harrison, R.A.3    Adabian, N.4    Newport, G.5
  • 13
    • 0002664005 scopus 로고
    • Interactions of vertebrate hsc70 and hsp70 with unfold proteins and peptides
    • (R.I. Morimoto, A. Tissieres and C. Georgopoulos, Eds.), Cold Spring Harbor Press, Cold Spring Harbor, NY
    • HIGHTOWER, L.E., SADIS, S.E., and TAKENAKA, I.M. 1994. Interactions of vertebrate hsc70 and hsp70 with unfold proteins and peptides. In "The Biology of Heat Shock Proteins and Molecular Chaperones." (R.I. Morimoto, A. Tissieres and C. Georgopoulos, Eds.), Cold Spring Harbor Press, Cold Spring Harbor, NY.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones
    • Hightower, L.E.1    Sadis, S.E.2    Takenaka, I.M.3
  • 14
    • 0000097632 scopus 로고
    • Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70
    • HUNT, C. and MORIMOTO, R.I. 1985. Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc. Natl. Acad. Sci. USA., 82: 6455-6459.
    • (1985) Proc. Natl. Acad. Sci. USA. , vol.82 , pp. 6455-6459
    • Hunt, C.1    Morimoto, R.I.2
  • 15
    • 0018974586 scopus 로고
    • Sequence of three copies of the gene for the major Drosophila heat shock induced protein and their flanking regions
    • INGOLIA, T.D., GRAIG, E.A., and MCCARTHY, B.J. 1980. Sequence of three copies of the gene for the major Drosophila heat shock induced protein and their flanking regions. Cell, 21: 669-679.
    • (1980) Cell , vol.21 , pp. 669-679
    • Ingolia, T.D.1    Graig, E.A.2    Mccarthy, B.J.3
  • 16
    • 0021123117 scopus 로고
    • Two distinct systems in human B lymphocytes: Identification of cell surface and intracellular antigens using monoclonal antibodies
    • ISHII, I., TAJAMI, T., YUASA, H., TAKEI, T., and KIKUCHI, K. 1984. Two distinct systems in human B lymphocytes: identification of cell surface and intracellular antigens using monoclonal antibodies. Clin. Exp. Immunol., 58: 183-192.
    • (1984) Clin. Exp. Immunol. , vol.58 , pp. 183-192
    • Ishii, I.1    Tajami, T.2    Yuasa, H.3    Takei, T.4    Kikuchi, K.5
  • 17
    • 0027196670 scopus 로고
    • Human Peripheral γδ T cells recognize hsp60 molecules on Daudi Burkitt's lymphoma cells
    • KAUR, I., VOSS, S.D., GUPTA, R.S., SCHELL, K., FISCH, P., and SONDEL, P.M. 1993. Human Peripheral γδ T cells recognize hsp60 molecules on Daudi Burkitt's lymphoma cells. J. Immunol., 150: 2046-2055.
    • (1993) J. Immunol. , vol.150 , pp. 2046-2055
    • Kaur, I.1    Voss, S.D.2    Gupta, R.S.3    Schell, K.4    Fisch, P.5    Sondel, P.M.6
  • 18
    • 0026134144 scopus 로고
    • Sequence of two hsc70 cDNAs from Lycopersicon esculentum
    • LIN, T.Y., DUCK, N.B., WINTER, J., and FOLK, W.R. 1991. Sequence of two hsc70 cDNAs from Lycopersicon esculentum. Plant Mol. Biol., 16: 475-478.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 475-478
    • Lin, T.Y.1    Duck, N.B.2    Winter, J.3    Folk, W.R.4
  • 19
    • 0028923597 scopus 로고
    • Molecular chaperones and the biosynthesis of antigen receptors
    • MELNICK, J. and ARGON, Y. 1995. Molecular chaperones and the biosynthesis of antigen receptors. Immunol. Today., 16: 243-250.
    • (1995) Immunol. Today. , vol.16 , pp. 243-250
    • Melnick, J.1    Argon, Y.2
  • 21
    • 0023052239 scopus 로고
    • An hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • MUNRO, S. and PELHAM, R.B. 1986. An hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell, 46: 291-300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, R.B.2
  • 22
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • SRIVASTAVA, P., K., UDONO, H., BLACHERE, N., E., and LI, Z. 1994. Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics, 39: 93-98.
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4
  • 23
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • SUTO, R. and SRIVASTAVA, P.K. 1995. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science, 269: 1585-1588.
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivastava, P.K.2
  • 25
    • 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., TSUBOI, N., SATO, N., and KIKUCHI, K. 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: 5516-5524.
    • (1993) J. Immunol. , vol.151 , pp. 5516-5524
    • Tamura, Y.1    Tsuboi, N.2    Sato, N.3    Kikuchi, K.4
  • 26
    • 0027997530 scopus 로고
    • Monoclonal antibody specifically reacting against 73-kilodalton heat shock protein: Possible expression on mammalian cell surface
    • TSUBOI, N., ISHIKAWA, M., TAMURA, Y., TAKAYAMA, S., TOBIOKA, H., MATSUURA, A., HIRAYOSHI, K., NAGATA, K., SATO, N., and KIKUCHI, K. 1994. Monoclonal antibody specifically reacting against 73-kilodalton heat shock protein: possible expression on mammalian cell surface. Hybridoma, 13: 373-381.
    • (1994) Hybridoma , vol.13 , pp. 373-381
    • Tsuboi, N.1    Ishikawa, M.2    Tamura, Y.3    Takayama, S.4    Tobioka, H.5    Matsuura, A.6    Hirayoshi, K.7    Nagata, K.8    Sato, N.9    Kikuchi, K.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.