메뉴 건너뛰기




Volumn 26, Issue 9, 2009, Pages 1181-1195

Differences in the sialylation patterns of membrane stress proteins in chemical carcinogen-induced tumors developed in BALB/c and IL-1α deficient mice

Author keywords

2 6 Neu5Ac; Heat shock proteins; IL 1 ; Immunogenicity; Sialylated N glycans

Indexed keywords

3 METHYLCHOLANTHRENE; ALPHA 2 6 N ACETYLNEURAMINIC ACID; CARCINOGEN; EPITOPE; GLUCOSE REGULATED PROTEIN; GLUCOSE REGULATED PROTEIN 75; GLYCAN DERIVATIVE; GLYCOPROTEIN GP 96; HEAT SHOCK PROTEIN 65; INTERLEUKIN 1ALPHA; N ACETYLNEURAMINIC ACID; UNCLASSIFIED DRUG; BETA D GALACTOSIDE ALPHA 2 6 SIALYLTRANSFERASE; BETA-D-GALACTOSIDE ALPHA 2-6-SIALYLTRANSFERASE; HEAT SHOCK PROTEIN; MEMBRANE PROTEIN; MESSENGER RNA; POLYSACCHARIDE; SIALYLTRANSFERASE;

EID: 77649259759     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-009-9238-9     Document Type: Article
Times cited : (12)

References (44)
  • 1
    • 20844437106 scopus 로고    scopus 로고
    • Glycans in cancer and inflammation - Potential for therapeutics and diagnostics
    • DOI 10.1038/nrd1751
    • Dube, D.H., Bertozzi, C.R.: Glycans in cancer and inflammationpotential for therapeutics and diagnostics. Nat. Rev. Drug Discov. 4, 477 (2005). doi:10.1038/nrd1751 (Pubitemid 40861990)
    • (2005) Nature Reviews Drug Discovery , vol.4 , Issue.6 , pp. 477-488
    • Dube, D.H.1    Bertozzi, C.R.2
  • 2
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • DOI 10.1038/nrc1649
    • Fuster, M.M., Esko, J.D.: The sweet and sour of cancer: glycans as novel therapeutic targets. Nat. Rev. Cancer. 5, 526 (2005). doi:10.1038/nrc1649 (Pubitemid 40942829)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.7 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 3
    • 0742306881 scopus 로고    scopus 로고
    • Expression of β-galactoside α2,6 sialyltransferase and of α2,6-sialylated glycoconjugates in normal human liver, hepatocarcinoma, and cirrhosis
    • DOI 10.1093/glycob/cwh002
    • Dall'olio, F., Chiricolo, M., Altimari, A., Fiorentino, M., Grigioni, W.F.: Expression of β-galactoside sialyltransferase and of α2, 6- sialyltransferase glycoconjugates in normal human liver, hepatocarcinoma and cirrhosis. Glycobiol. 14, 39-49 (2004). doi:10.1093/glycob/cwh002 (Pubitemid 38159407)
    • (2004) Glycobiology , vol.14 , Issue.1 , pp. 39-49
    • Dall'Olio, F.1    Chiricolo, M.2    D'Errico, A.3    Gruppioni, E.4    Altimari, A.5    Fiorentino, M.6    Grigioni, W.F.7
  • 4
    • 0035526267 scopus 로고    scopus 로고
    • Sialyltransferases in cancer
    • DOI 10.1023/A:1022288022969
    • Dall'olio, F., Chiricolo, M.: Sialyltransferases in cancer. Glycoconj. 18, 841 (2001). doi:10.1023/A:1022288022969 (Pubitemid 36315048)
    • (2001) Glycoconjugate Journal , vol.18 , Issue.11-12 , pp. 841-850
    • Dall'Olio, F.1    Chiricolo, M.2
  • 5
    • 31444433687 scopus 로고    scopus 로고
    • Altered glycosylation in cancer: Sialic acids and sialyltransferases
    • Wang, P.H.: Altered glycosylation in cancer: sialic acids and sialyltransferases. J. Cancer Mol. 1, 73 (2005)
    • (2005) J. Cancer Mol. , vol.1 , pp. 73
    • Wang, P.H.1
  • 6
    • 0042131904 scopus 로고    scopus 로고
    • Polysialic acid directs tumor cell growth by controlling heterophilic neural cell adhesion molecule interactions
    • DOI 10.1128/MCB.23.16.5908-5918.2003
    • Seidenfaden, R., Krauter, A., Schretzinger, F., Gerardy-Schahn, R., Hildebrandt, H.: Polysialic acid directs tumor cell growth by controlling heterophilic neural cell adhesion molecule interactions. Mol. Cell. Biol. 23, 5908 (2003). doi:10.1128/MCB.23.16.5908-5918.2003 (Pubitemid 36951351)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.16 , pp. 5908-5918
    • Seidenfaden, R.1    Krauter, A.2    Schertzinger, F.3    Gerardy-Schahn, R.4    Hildebrandt, H.5
  • 7
    • 34248193253 scopus 로고    scopus 로고
    • Immune surveillance of tumors
    • DOI 10.1172/JCI31405
    • Swann, J.B., Smyth, M.J.: Immune surveillance of tumors. J. Clin. Invest. 117, 137 (2007). doi:10.1172/JCI31405 (Pubitemid 46718398)
    • (2007) Journal of Clinical Investigation , vol.117 , Issue.5 , pp. 1137-1146
    • Swann, J.B.1    Smyth, M.J.2
  • 8
    • 33750321707 scopus 로고    scopus 로고
    • Interferons, immunity and cancer immunoediting
    • DOI 10.1038/nri1961, PII NRI1961
    • Dunn, G.P., Koabel, C.M., Schreiber, R.D.: Interferons, immunity and cancer immunoediting. Nat. Immunol. 6, 836 (2006). doi:10.1038/nri1961 (Pubitemid 44631652)
    • (2006) Nature Reviews Immunology , vol.6 , Issue.11 , pp. 836-848
    • Dunn, G.P.1    Koebel, C.M.2    Schreiber, R.D.3
  • 9
    • 33845546703 scopus 로고    scopus 로고
    • The involvement of IL-1 in tumorigenesis, tumor invasiveness, metastasis and tumor-host interactions
    • DOI 10.1007/s10555-006-9004-4, Special Issue on Pro-inflammatory Cytokines in Cancer
    • Apte, R.N., Dotan, S., Elkabets, M., White, R.M., Reich, E., Carmi, Y., Son, X., Dvozkin, T., Kerlin, Y., Voronov, E.: The involvement of IL-1 in tumorigenesis, tumor invasiveness, metastasis and host-interaction. Cancer Metastasis. Rev. 25, 387 (2006). doi:10.1007/s10555-006-9004-4 (Pubitemid 44922357)
    • (2006) Cancer and Metastasis Reviews , vol.25 , Issue.3 , pp. 387-408
    • Apte, R.N.1    Dotan, S.2    Elkabets, M.3    White, M.R.4    Reich, E.5    Carmi, Y.6    Song, X.7    Dvozkin, T.8    Krelin, Y.9    Voronov, E.10
  • 10
    • 33847060965 scopus 로고    scopus 로고
    • Interleukin-1β-driven inflammation promotes the development and invasiveness of chemical carcinogen-induced tumors
    • DOI 10.1158/0008-5472.CAN-06-2956
    • Krelin, Y., Voronov, E., Dotan, S., Elkabets, M., Reich, E., Fogel, M., Huszar, M., Iwakura, Y., Segal, S., Dinarello, C.A., Apte, R. N.: IL-1 beta-driven inflammation promotes the development and invasiveness of chemical carcinogen-induced tumors. Cancer Res. 67, 1062 (2007). doi:10.1158/0008-5472. CAN-06-2956 (Pubitemid 46270762)
    • (2007) Cancer Research , vol.67 , Issue.3 , pp. 1062-1071
    • Krelin, Y.1    Voronov, E.2    Dotan, S.3    Elkabets, M.4    Reich, E.5    Fogel, M.6    Huszar, M.7    Iwakura, Y.8    Segal, S.9    Dinarello, C.A.10    Apte, R.N.11
  • 12
    • 0031023592 scopus 로고    scopus 로고
    • Reduction of metastatic properties of BL6 melanoma cells expressing terminal fucose(alpha) 1-2-galactose after alpha1, 2- fucosyltransferase cDNA transfection
    • Gorelik, E., Xu, F., Henion, T., Anaraki, F., Galili, U.: Reduction of metastatic properties of BL6 melanoma cells expressing terminal fucose(alpha) 1-2-galactose after alpha1, 2- fucosyltransferase cDNA transfection. Cancer Res. 57, 332 (1997)
    • (1997) Cancer Res. , vol.57 , pp. 332
    • Gorelik, E.1    Xu, F.2    Henion, T.3    Anaraki, F.4    Galili, U.5
  • 14
    • 0031571138 scopus 로고    scopus 로고
    • Sequencing of N-linked oligosaccharides directly from protein gels: In- gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography
    • DOI 10.1006/abio.1997.2199
    • Küster, B., Wheeler, S.F., Hunter, P.A., Dwek, R.A., Harvey, D.J.: Sequencing of N-glycan oligosaccharides directly from protein gels: In gel deglycosylation and analyzing in HPLC and MALDITOF MS. Anal. Biochem. 250, 82 (1997). doi:10.1006/abio.1997.2199 (Pubitemid 27310317)
    • (1997) Analytical Biochemistry , vol.250 , Issue.1 , pp. 82-101
    • Kuster, B.1    Wheeler, S.F.2    Hunter, A.P.3    Dwek, R.A.4    Harvey, D.J.5
  • 16
    • 0029854379 scopus 로고    scopus 로고
    • Systematic nomenclature for sialyltransferases.
    • doi:10.1093/glycob/6.7.647
    • Tsuji, S., Datta, A.K., Paulson, J.C.: Systematic nomenclature for sialyltransferases. Glycobiol. 6, V (1996). doi:10.1093/glycob/6.7.647
    • (1996) Glycobiol. , vol.6
    • Tsuji, S.1    Datta, A.K.2    Paulson, J.C.3
  • 17
    • 0033597198 scopus 로고    scopus 로고
    • Molecular cloning of a novel α2,3-sialyltransferase (ST3Gal VI) that sialylates type II lactosamine structures on glycoproteins and glycolipids
    • DOI 10.1074/jbc.274.17.11479
    • Okajima, T., Fukumoto, S., Miyazaki, H., Ishida, H., Kiso, M., Furukawa, K., Urano, T., Furukawa, K.: Molecular cloning of a novel alpha2,3- sialyltransferase (ST3Gal VI) that sialylates type II lactosamine structures on glycoproteins and glycolipids. J. Biol. Chem. 274, 11479 (1999). doi:10.1074/jbc.274.17.11479 (Pubitemid 29197800)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.17 , pp. 11479-11486
    • Okajima, T.1    Fukumoto, S.2    Miyazaki, H.3    Ishida, H.4    Kiso, M.5    Furukawa, K.6    Urano, T.7    Furukawa, K.8
  • 18
    • 35548970287 scopus 로고    scopus 로고
    • Heat shock proteins in cancer
    • DOI 10.1196/annals.1391.030, Stress Responses
    • Sherman, M., Multhoff, G.: Heat shock proteins in cancer. Ann. N. Y. Acad. Sci. 1113, 192 (2007). doi:10.1196/annals.1391.030 (Pubitemid 350015025)
    • (2007) Annals of the New York Academy of Sciences , vol.1113 , pp. 192-201
    • Sherman, M.1    Multhoff, G.2
  • 21
    • 33748987908 scopus 로고    scopus 로고
    • Cancer despite immunosurveillance: Immunoselection and immunosubversion
    • DOI 10.1038/nri1936, PII NRI1936
    • Zitvogel, L., Tesniere, A., Kroemer, G.: Cancer despite immunosurveillance: immunoselection and immunosubversion. Nat. Immunol. Rev. 6, 715 (2006). doi:10.1038/nri1936 (Pubitemid 44453458)
    • (2006) Nature Reviews Immunology , vol.6 , Issue.10 , pp. 715-727
    • Zitvogel, L.1    Tesniere, A.2    Kroemer, G.3
  • 22
    • 39049137589 scopus 로고    scopus 로고
    • Alpha 2-6-Linked sialic acids on N-glycans modulate carcinoma differentiation in vivo
    • doi:10.1158/0008-5472.CAN-07-1340
    • Hedlund, M., Ng, E., Varki, A., Varki, N.M.: Alpha 2-6-Linked sialic acids on N-glycans modulate carcinoma differentiation in vivo. Cancer Res. 68, 388 (2008). doi:10.1158/0008-5472.CAN-07-1340
    • (2008) Cancer Res. , vol.68 , pp. 388
    • Hedlund, M.1    Ng, E.2    Varki, A.3    Varki, N.M.4
  • 23
    • 34547929295 scopus 로고    scopus 로고
    • Diversity in cell surface sialic acid presentations: Implications for biology and disease
    • DOI 10.1038/labinvest.3700656, PII 3700656
    • Varki, N.M., Varki, A.: Diversity in cell surface sialic acid presentations: implications for biology and disease. Lab. Invest. 87, 851 (2007). doi:10.1038/labinvest.3700656 (Pubitemid 47267816)
    • (2007) Laboratory Investigation , vol.87 , Issue.9 , pp. 851-857
    • Varki, N.M.1    Varki, A.2
  • 25
    • 0037744803 scopus 로고    scopus 로고
    • Ganglioside GD3 expression on target cells can modulate NK cell cytotoxicity via siglec-7-dependent and -independent mechanisms
    • DOI 10.1002/eji.200323693
    • Nicoll, G., Avril, T., Lock, K., Furukawa, K., Bovin, N., Crocker, P.R.: Ganglioside GD3 expression on target cells can modulate NK cell cytotoxicity via siglec-7-dependent and -independent mechanisms. Eur. J. Immunol. 33, 1642 (2003). doi:10.1002/eji.200323693 (Pubitemid 36790425)
    • (2003) European Journal of Immunology , vol.33 , Issue.6 , pp. 1642-1648
    • Nicoll, G.1    Avril, T.2    Lock, K.3    Furukawa, K.4    Bovin, N.5    Crocker, P.R.6
  • 26
    • 0026604647 scopus 로고
    • Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to endoplasmic reticulum
    • doi:10.1016/0092-8674(92)90476-S
    • Lewis, M.J., Pelham, H.R.: Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to endoplasmic reticulum. Cell. 68, 353 (1992). doi:10.1016/0092-8674(92)90476-S
    • (1992) Cell. , vol.68 , pp. 353
    • Lewis, M.J.1    Pelham, H.R.2
  • 27
    • 0029838338 scopus 로고    scopus 로고
    • Tumor-specific cell surface expression of the -KDEL containing, endoplasmic reticular heat shock protein gp96
    • DOI 10.1002/(SICI)1097-0215(19960822)69:4<340::AID-IJC18>3.0.CO;2-9
    • Altmeyer, A., Maki, G.R., Feldweg, A.M., Heike, M., Protoprov, V.P., Masur, S.K., Srivastava, P.K.: Tumor-specific cell surface expression of the -KDEL containing, endoplasmatic reticular heat shock protein gp96. Int. J. Cancer. 69, 340 (1996). doi:10.1002/(SICI)1097-0215(19960822)69:4<340::AID- IJC18>3.0.CO;2-9 (Pubitemid 26298302)
    • (1996) International Journal of Cancer , vol.69 , Issue.4 , pp. 340-349
    • Altmeyer, A.1    Maki, R.G.2    Feldweg, A.M.3    Heike, M.4    Protopopov, V.P.5    Masur, S.K.6    Srivastava, P.K.7
  • 28
    • 34848859541 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70): Membrane location, export and immunological relevance
    • DOI 10.1016/j.ymeth.2007.06.006, PII S1046202307001314, Heat Shock Proteins In Extracellular Signaling
    • Multhoff, G.: Heat shock protein 70 (HSP70): membrane location, export and immunological relevance. Methods. 43, 229 (2007). doi:10.1016/j.ymeth.2007. 06.006 (Pubitemid 47499077)
    • (2007) Methods , vol.43 , Issue.3 , pp. 229-237
    • Multhoff, G.1
  • 29
    • 0345035504 scopus 로고    scopus 로고
    • Cell surface expression of the endoplasmatic reticular heat shock protein gp96 is phylogenetically conserved
    • Robert, J., Menoret, M., Cohen, N.: Cell surface expression of the endoplasmatic reticular heat shock protein gp96 is phylogenetically conserved. J. Immunol. 163, 4133 (1999)
    • (1999) J. Immunol. , vol.163 , pp. 4133
    • Robert, J.1    Menoret, M.2    Cohen, N.3
  • 30
    • 44849084963 scopus 로고    scopus 로고
    • Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages
    • Vega, V.L., Rodríguez-Silva, M., Frey, T., Gehrmann, M., Diaz, J. C., Steinem, C., Multhoff, G., Arispe, N., De Maio, A.: Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages. J. Immunol. 180, 4299 (2008)
    • (2008) J. Immunol. , vol.180 , pp. 4299
    • Vega, V.L.1    Rodríguez-Silva, M.2    Frey, T.3    Gehrmann, M.4    Diaz, J.C.5    Steinem, C.6    Multhoff, G.7    Arispe, N.8    De Maio, A.9
  • 31
    • 34248571826 scopus 로고    scopus 로고
    • GRP78 induction in cancer: Therapeutic and prognostic implications
    • DOI 10.1158/0008-5472.CAN-07-0325
    • Lee, A.S.: GRP78 induction in cancer: therapeutic and prognostic implications. Cancer Res. 67, 3496 (2007). doi:10.1158/0008-5472.CAN-07-0325 (Pubitemid 46762126)
    • (2007) Cancer Research , vol.67 , Issue.8 , pp. 3496-3499
    • Lee, A.S.1
  • 32
    • 0036214288 scopus 로고    scopus 로고
    • Interaction of heat shock proteins with peptides and antigen presenting cells: Chaperoning of the innate and adaptive immune responses
    • DOI 10.1146/annurev.immunol.20.100301.064801
    • Srivastava, P.K.: Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immunity. Annu. Rev. Immunol. 20, 395 (2002). doi:10.1146/annurev.immunol.20.100301.064801 (Pubitemid 34293430)
    • (2002) Annual Review of Immunology , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 33
    • 33750364777 scopus 로고    scopus 로고
    • Heat shock proteins induce T cell regulation of chronic inflammation
    • Broere, F.H., Weiten, L., Zee, R.V.D., Berlo, S.: Heat shock proteins induce T cell regulation of chronic inflammation. Ann. Rheum. Dis. 65, 65 (2007)
    • (2007) Ann. Rheum. Dis. , vol.65 , pp. 65
    • Broere, F.H.1    Weiten, L.2    Zee, R.V.D.3    Berlo, S.4
  • 34
    • 2442517310 scopus 로고    scopus 로고
    • Glycoprotein 96 can chaperone both MHC class I- and class II-restricted epitopes for in vivo presentation, but selectively primes CD8 + T cell effector function
    • Doody, A.D.H., Kovalchin, T.J., Mihalyo, M.A., Hagymasi, A.T., Drake, C.G., Adler, A.J.: Glycoprotein 96 can chaperone both MHC class I- and class II-restricted epitopes for in vivo presentation, but selectively primes CD8 + T cell effector function. J. Immunol. 172, 6087 (2004)
    • (2004) J. Immunol. , vol.172 , pp. 6087
    • Doody, A.D.H.1    Kovalchin, T.J.2    Mihalyo, M.A.3    Hagymasi, A.T.4    Drake, C.G.5    Adler, A.J.6
  • 35
    • 0035205080 scopus 로고    scopus 로고
    • A 14-mer Hsp70 peptide stimulates natural killer (NK) cell activity
    • DOI 10.1379/1466-1268(2001)006<0337:AMHPSN>2.0.CO;2
    • Multhoff, G., Pfister, K., Gehrmann, M., Hantschel, M., Gross, C., Hafner, M., Hiddemann, W.: A 14-mer Hsp70 peptide stimulates natural killer (NK) cell activity. Cell Stress Chaperones. 6, 337 (2001). doi:10.1379/1466- 1268(2001)006<0337:AMHPSN>2.0.CO;2 (Pubitemid 33123486)
    • (2001) Cell Stress and Chaperones , vol.6 , Issue.4 , pp. 337-344
    • Multhoff, G.1    Pfister, K.2    Gehrmann, M.3    Hantschel, M.4    Gross, C.5    Hafner, M.6    Hiddemann, W.7
  • 36
    • 0041408691 scopus 로고    scopus 로고
    • Cell surface expression of heat shock protein gp96 enhances cross-presentation of cellular antigens and the generation of tumor-specific T cell memory
    • Dai, J., Liu, B., Caudill, M.M., Zheng, H., Qiao, Y., Podack, E.R., Li, Z.: Cell surface expression of heat shock protein gp96 enhances cross-presentation of cellular antigens and the generation of tumor-specific T cell memory. Cancer Immun. 3, 1 (2003)
    • (2003) Cancer Immun. , vol.3 , pp. 1
    • Dai, J.1    Liu, B.2    Caudill, M.M.3    Zheng, H.4    Qiao, Y.5    Podack, E.R.6    Li, Z.7
  • 38
    • 33845938807 scopus 로고    scopus 로고
    • Novel splice variants of ING4 and their possible roles in the regulation of cell growth and motility
    • DOI 10.1074/jbc.M606296200
    • Unoki, M., Shen, J.C., Zheng, Z.M., Harris, C.C.: Novel splice variants of ING4 and their possible roles in the regulation of cell growth and motility. J. Biol. Chem. 281, 34677 (2006). doi:10.1074/jbc.M606296200 (Pubitemid 46036673)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 34677-34686
    • Unoki, M.1    Shen, J.C.2    Zheng, Z.-M.3    Harris, C.C.4
  • 39
    • 40449115740 scopus 로고    scopus 로고
    • Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum
    • doi:10.1261/rna.721108
    • Pyhtila, B., Zheng, T., Lager, P.J., Keene, J.D., Reedy, M.C., Nicchitta, C.V.: Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum. RNA. 14, 445 (2008). doi:10.1261/rna.721108
    • (2008) RNA , vol.14 , pp. 445
    • Pyhtila, B.1    Zheng, T.2    Lager, P.J.3    Keene, J.D.4    Reedy, M.C.5    Nicchitta, C.V.6
  • 40
    • 34247565506 scopus 로고    scopus 로고
    • Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins
    • DOI 10.1038/nature05816, PII NATURE05816
    • Varki, A.: Glycan-based interactions involving vertebrate sialicacid- recognizing proteins. Nature. 443, 1023 (2007). doi:10.1038/nature05816 (Pubitemid 46676064)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1023-1029
    • Varki, A.1
  • 41
    • 22244467721 scopus 로고    scopus 로고
    • Differences in glycosylation patterns of heat shock protein, gp96: Implications for prostate cancer prevention
    • doi:10.1158/0008-5472. CAN-04-4639
    • Suriano, R., Ghosh, S.K., Ashok, B.T., Mittelman, A., Chen, Y., Banerjee, A., Tiwari, R.K.: Differences in glycosylation patterns of heat shock protein, gp96: implications for prostate cancer prevention. Cancer Res. 65, 6466 (2005). doi:10.1158/0008-5472. CAN-04-4639
    • (2005) Cancer Res. , vol.65 , pp. 6466
    • Suriano, R.1    Ghosh, S.K.2    Ashok, B.T.3    Mittelman, A.4    Chen, Y.5    Banerjee, A.6    Tiwari, R.K.7
  • 42
    • 2442687675 scopus 로고    scopus 로고
    • 70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine
    • DOI 10.1016/j.bbrc.2004.04.144, PII S0006291X04009167
    • Guinez, C., Lemoine, J., Michalski, J.C., Lefebvre, T.: 70-Kdaheat shock protein presents an adjustable lectinic activity towards O-linked N-acethylglucosamine. Biochem. Biophys. Res. Commun. 319, 21 (2004). doi:10.1016/j.bbrc.2004.04.144 (Pubitemid 38670155)
    • (2004) Biochemical and Biophysical Research Communications , vol.319 , Issue.1 , pp. 21-26
    • Guinez, C.1    Lemoine, J.2    Michalski, J.-C.3    Lefebvre, T.4
  • 43
    • 33847260278 scopus 로고    scopus 로고
    • Heat Shock Protein gp96 Is a Master Chaperone for Toll-like Receptors and Is Important in the Innate Function of Macrophages
    • DOI 10.1016/j.immuni.2006.12.005, PII S1074761307001161
    • Yang, Y., Liu, B., Dai, J., Srivastava, P.K., Zammit, D.J., Lefrancois, L., Li, Z.: Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages. Immunity. 26, 1 (2007). doi:10.1016/j.immuni.2006.12.005 (Pubitemid 46329432)
    • (2007) Immunity , vol.26 , Issue.2 , pp. 215-226
    • Yang, Y.1    Liu, B.2    Dai, J.3    Srivastava, P.K.4    Zammit, D.J.5    Lefrancois, L.6    Li, Z.7
  • 44
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • doi:10.1021/cr940283b
    • Dwek, R.A.: Glycobiology: toward understanding the function of sugars. Chem. Rev. 96, 683 (1996). doi:10.1021/cr940283b
    • (1996) Chem. Rev. , vol.96 , pp. 683
    • Dwek, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.