메뉴 건너뛰기




Volumn 787, Issue , 2011, Pages 289-302

Investigating Receptors for Extracellular Heat Shock Proteins

Author keywords

Extracellular; Heat; Immunity; Protein; Receptor; Scavenger; Shock

Indexed keywords

CELL SURFACE RECEPTOR; HEAT SHOCK PROTEIN 70; LECTIN; SCAVENGER RECEPTOR;

EID: 80054761699     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61779-295-3_22     Document Type: Chapter
Times cited : (48)

References (59)
  • 1
    • 34447550254 scopus 로고    scopus 로고
    • Extracellular heat shock proteins in cell signaling
    • Calderwood SK, Mambula SS, Gray PJ, Jr., Theriault JR. Extracellular heat shock proteins in cell signaling. FEBS Lett 2007;581(19): 3689–94.
    • (2007) FEBS Lett , vol.581 , Issue.19 , pp. 3689-3694
    • Calderwood, S.K.1    Mambula, S.S.2    Gray, P.J.3    Theriault, J.R.4
  • 2
    • 0037176975 scopus 로고    scopus 로고
    • Heat shock proteins, inflammation, and cardiovascular disease
    • Pockley AG. Heat shock proteins, inflammation, and cardiovascular disease. Circulation 2002; 105(8):1012–7.
    • (2002) Circulation , vol.105 , Issue.8 , pp. 1012-1017
    • Pockley, A.G.1
  • 3
    • 0031770945 scopus 로고    scopus 로고
    • Detection of heat shock protein 70 (Hsp70) and anti-Hsp70 antibodies in the serum of normal individuals
    • Pockley AG, Shepherd J, Corton JM. Detection of heat shock protein 70 (Hsp70) and anti-Hsp70 antibodies in the serum of normal individuals. Immunol Invest 1998;27(6):367–77.
    • (1998) Immunol Invest , vol.27 , Issue.6 , pp. 367-377
    • Pockley, A.G.1    Shepherd, J.2    Corton, J.M.3
  • 4
    • 33750567138 scopus 로고    scopus 로고
    • Heat induced release of Hsp70 from prostate carcinoma cells involves both active secretion and passive release from necrotic cells
    • Mambula SS, Calderwood SK. Heat induced release of Hsp70 from prostate carcinoma cells involves both active secretion and passive release from necrotic cells. Int J Hyperthermia 2006; 22(7):575–85.
    • (2006) Int J Hyperthermia , vol.22 , Issue.7 , pp. 575-585
    • Mambula, S.S.1    Calderwood, S.K.2
  • 5
    • 33750570923 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes
    • Mambula SS, Calderwood SK. Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes. J Immunol 2006;177(11):7849–57.
    • (2006) J Immunol , vol.177 , Issue.11 , pp. 7849-7857
    • Mambula, S.S.1    Calderwood, S.K.2
  • 6
    • 0037066427 scopus 로고    scopus 로고
    • The danger model: A renewed sense of self
    • Matzinger P. The danger model: a renewed sense of self. Science 2002;296(5566):301–5.
    • (2002) Science , vol.296 , Issue.5566 , pp. 301-305
    • Matzinger, P.1
  • 7
    • 0035903158 scopus 로고    scopus 로고
    • Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells
    • Vabulas RM, Ahmad-Nejad P, da Costa C, et al. Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells. J Biol Chem 2001;276(33): 31332–9.
    • (2001) J Biol Chem , vol.276 , Issue.33 , pp. 31332-31339
    • Vabulas, R.M.1    Ahmad-Nejad, P.2    da Costa, C.3
  • 10
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea A, Kraeft SK, Kurt-Jones EA, et al. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 2000;6(4):435–42.
    • (2000) Nat Med , vol.6 , Issue.4 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3
  • 11
    • 77950349873 scopus 로고    scopus 로고
    • Caught with their PAMPs down? The extracellular signalling actions of molecular chaperones are not due to microbial contaminants
    • Henderson B, Calderwood SK, Coates AR, et al. Caught with their PAMPs down? The extracellular signalling actions of molecular chaperones are not due to microbial contaminants. Cell Stress Chaperones 2009.
    • (2009) Cell Stress Chaperones
    • Henderson, B.1    Calderwood, S.K.2    Coates, A.R.3
  • 12
    • 0034608387 scopus 로고    scopus 로고
    • Cross-presentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptor-mediated endocytosis
    • Singh-Jasuja H, Toes RE, Spee P, et al. Cross-presentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptor-mediated endocytosis. J Exp Med 2000;191(11):1965–74.
    • (2000) J Exp Med , vol.191 , Issue.11 , pp. 1965-1974
    • Singh-Jasuja, H.1    Toes, R.E.2    Spee, P.3
  • 13
    • 0036214288 scopus 로고    scopus 로고
    • Interaction of heat shock proteins with peptides and antigen presenting cells: Chaperoning of the innate and adaptive immune responses
    • Srivastava P. Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Annu Rev Immunol 2002;20: 395–425.
    • (2002) Annu Rev Immunol , vol.20 , pp. 395-425
    • Srivastava, P.1
  • 14
    • 0142124336 scopus 로고    scopus 로고
    • The ins and outs of cross-presentation
    • Rock KL. The ins and outs of cross-presentation. Nat Immunol 2003;4(10):941–3.
    • (2003) Nat Immunol , vol.4 , Issue.10 , pp. 941-943
    • Rock, K.L.1
  • 15
    • 0036865303 scopus 로고    scopus 로고
    • Activation of natural killer cells by heat shock protein 70
    • Multhoff G. Activation of natural killer cells by heat shock protein 70. Int J Hyperthermia 2002;18(6):576–85.
    • (2002) Int J Hyperthermia , vol.18 , Issue.6 , pp. 576-585
    • Multhoff, G.1
  • 16
    • 0030224714 scopus 로고    scopus 로고
    • Cell surface expression of heat shock proteins and the immune response
    • Multhoff G, Hightower LE. Cell surface expression of heat shock proteins and the immune response. Cell Stress Chaperones 1996;1(3):167–76.
    • (1996) Cell Stress Chaperones , vol.1 , Issue.3 , pp. 167-176
    • Multhoff, G.1    Hightower, L.E.2
  • 17
    • 17144417382 scopus 로고    scopus 로고
    • Heat-shock proteins induce T-cell regulation of chronic inflammation
    • van Eden W, van der Zee R, Prakken B. Heat-shock proteins induce T-cell regulation of chronic inflammation. Nat Rev Immunol 2005;5(4): 318–30.
    • (2005) Nat Rev Immunol , vol.5 , Issue.4 , pp. 318-330
    • van Eden, W.1    van der Zee, R.2    Prakken, B.3
  • 18
    • 10944228434 scopus 로고    scopus 로고
    • SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin
    • Berwin B, Delneste Y, Lovingood RV, Post SR, Pizzo SV. SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin. J Biol Chem 2004;279(49):51250–7.
    • (2004) J Biol Chem , vol.279 , Issue.49 , pp. 51250-51257
    • Berwin, B.1    Delneste, Y.2    Lovingood, R.V.3    Post, S.R.4    Pizzo, S.V.5
  • 19
    • 0345305789 scopus 로고    scopus 로고
    • Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells
    • Berwin B, Hart JP, Rice S, et al. Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells. Embo J 2003;22(22):6127–36.
    • (2003) Embo J , vol.22 , Issue.22 , pp. 6127-6136
    • Berwin, B.1    Hart, J.P.2    Rice, S.3
  • 20
    • 0034252620 scopus 로고    scopus 로고
    • CD91: A receptor for heat shock protein gp96
    • Binder RJ, Han DK, Srivastava PK. CD91: a receptor for heat shock protein gp96. Nat Immunol 2000;1(2):151–5.
    • (2000) Nat Immunol , vol.1 , Issue.2 , pp. 151-155
    • Binder, R.J.1    Han, D.K.2    Srivastava, P.K.3
  • 21
    • 18644364531 scopus 로고    scopus 로고
    • Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation
    • Delneste Y, Magistrelli G, Gauchat J, et al. Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation. Immunity 2002;17(3):353–62.
    • (2002) Immunity , vol.17 , Issue.3 , pp. 353-362
    • Delneste, Y.1    Magistrelli, G.2    Gauchat, J.3
  • 22
    • 34547882750 scopus 로고    scopus 로고
    • Hsp110 and Grp170, members of the Hsp70 superfamily, bind to scavenger receptor-A and scavenger receptor expressed by endothelial cells-I
    • Facciponte JG, Wang XY, Subjeck JR. Hsp110 and Grp170, members of the Hsp70 superfamily, bind to scavenger receptor-A and scavenger receptor expressed by endothelial cells-I. Eur J Immunol 2007;37(8):2268–79.
    • (2007) Eur J Immunol , vol.37 , Issue.8 , pp. 2268-2279
    • Facciponte, J.G.1    Wang, X.Y.2    Subjeck, J.R.3
  • 23
    • 0037298742 scopus 로고    scopus 로고
    • Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94
    • Gross C, Hansch D, Gastpar R, Multhoff G. Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94. Biol Chem 2003;384(2):267–79.
    • (2003) Biol Chem , vol.384 , Issue.2 , pp. 267-279
    • Gross, C.1    Hansch, D.2    Gastpar, R.3    Multhoff, G.4
  • 24
    • 35649018633 scopus 로고    scopus 로고
    • EWI-2/ CD316 Is an Inducible Receptor of HSPA8 on Human Dendritic Cells
    • Kettner S, Kalthoff F, Graf P, et al. EWI-2/ CD316 Is an Inducible Receptor of HSPA8 on Human Dendritic Cells. Mol Cell Biol 2007;27(21):7718–26.
    • (2007) Mol Cell Biol , vol.27 , Issue.21 , pp. 7718-7726
    • Kettner, S.1    Kalthoff, F.2    Graf, P.3
  • 25
    • 0034500353 scopus 로고    scopus 로고
    • Characterization of a receptor for heat shock protein 70 on macrophages and monocytes
    • Sondermann H, Becker T, Mayhew M, Wieland F, Hartl FU. Characterization of a receptor for heat shock protein 70 on macrophages and monocytes. Biol Chem 2000;381(12): 1165–74.
    • (2000) Biol Chem , vol.381 , Issue.12 , pp. 1165-1174
    • Sondermann, H.1    Becker, T.2    Mayhew, M.3    Wieland, F.4    Hartl, F.U.5
  • 26
    • 33748869459 scopus 로고    scopus 로고
    • Interaction between the CCR5 chemokine receptors and microbial HSP70
    • Whittall T, Wang Y, Younson J, et al. Interaction between the CCR5 chemokine receptors and microbial HSP70. Eur J Immunol 2006; 36(9):2304–14.
    • (2006) Eur J Immunol , vol.36 , Issue.9 , pp. 2304-2314
    • Whittall, T.1    Wang, Y.2    Younson, J.3
  • 27
    • 70349235599 scopus 로고    scopus 로고
    • T Cell Activation by Heat Shock Protein 70 Vaccine Requires TLR Signaling and Scavenger Receptor Expressed by Endothelial Cells-1
    • Gong J, Zhu B, Murshid A, et al. T Cell Activation by Heat Shock Protein 70 Vaccine Requires TLR Signaling and Scavenger Receptor Expressed by Endothelial Cells-1. J Immunol 2009.
    • (2009) J Immunol
    • Gong, J.1    Zhu, B.2    Murshid, A.3
  • 28
    • 15544373100 scopus 로고    scopus 로고
    • Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/ epithelial cells
    • Theriault JR, Mambula SS, Sawamura T, Stevenson MA, Calderwood SK. Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/ epithelial cells. FEBS Lett 2005;579(9): 1951–60.
    • (2005) FEBS Lett , vol.579 , Issue.9 , pp. 1951-1960
    • Theriault, J.R.1    Mambula, S.S.2    Sawamura, T.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 29
    • 0037131427 scopus 로고    scopus 로고
    • Toll-like receptor (TLR) signaling in response to Aspergillus fumigatus
    • Mambula SS, Sau K, Henneke P, Golenbock DT, Levitz SM. Toll-like receptor (TLR) signaling in response to Aspergillus fumigatus. J Biol Chem 2002;277(42):39320–6.
    • (2002) J Biol Chem , vol.277 , Issue.42 , pp. 39320-39326
    • Mambula, S.S.1    Sau, K.2    Henneke, P.3    Golenbock, D.T.4    Levitz, S.M.5
  • 30
    • 0342547302 scopus 로고    scopus 로고
    • Purification of immunogenic heat shock protein 70-peptide complexes by ADP-affinity chromatography
    • Peng P, Menoret A, Srivastava PK. Purification of immunogenic heat shock protein 70-peptide complexes by ADP-affinity chromatography. J Immunol Methods 1997;204(1):13–21.
    • (1997) J Immunol Methods , vol.204 , Issue.1 , pp. 13-21
    • Peng, P.1    Menoret, A.2    Srivastava, P.K.3
  • 31
    • 29144488035 scopus 로고    scopus 로고
    • Lectin-like, oxidized low-density lipoprotein receptor-1 (LOX-1): A critical player in the development of atherosclerosis and related disorders
    • Mehta JL, Chen J, Hermonat PL, Romeo F, Novelli G. Lectin-like, oxidized low-density lipoprotein receptor-1 (LOX-1): a critical player in the development of atherosclerosis and related disorders. Cardiovasc Res 2006;69(1): 36–45.
    • (2006) Cardiovasc Res , vol.69 , Issue.1 , pp. 36-45
    • Mehta, J.L.1    Chen, J.2    Hermonat, P.L.3    Romeo, F.4    Novelli, G.5
  • 32
    • 0035993485 scopus 로고    scopus 로고
    • LOX-1, the receptor for oxidized low-density lipoprotein identified from endothelial cells: Implications in endothelial dysfunction and atherosclerosis
    • Chen M, Masaki T, Sawamura T. LOX-1, the receptor for oxidized low-density lipoprotein identified from endothelial cells: implications in endothelial dysfunction and atherosclerosis. Pharmacol Ther 2002;95(1):89–100.
    • (2002) Pharmacol Ther , vol.95 , Issue.1 , pp. 89-100
    • Chen, M.1    Masaki, T.2    Sawamura, T.3
  • 33
    • 29144452851 scopus 로고    scopus 로고
    • The C-type lectin-like domain superfamily
    • Zelensky AN, Gready JE. The C-type lectin-like domain superfamily. Febs J 2005;272(24): 6179–217.
    • (2005) Febs J , vol.272 , Issue.24 , pp. 6179-6217
    • Zelensky, A.N.1    Gready, J.E.2
  • 34
    • 0032860314 scopus 로고    scopus 로고
    • C-type lectin-like domains
    • Drickamer K. C-type lectin-like domains. Curr Opin Struct Biol 1999;9(5):585–90.
    • (1999) Curr Opin Struct Biol , vol.9 , Issue.5 , pp. 585-590
    • Drickamer, K.1
  • 35
    • 33745198927 scopus 로고    scopus 로고
    • Endothelial scavenger receptors
    • Adachi H, Tsujimoto M. Endothelial scavenger receptors. Prog Lipid Res 2006;45(5): 379–404.
    • (2006) Prog Lipid Res , vol.45 , Issue.5 , pp. 379-404
    • Adachi, H.1    Tsujimoto, M.2
  • 36
    • 0242718871 scopus 로고    scopus 로고
    • Scavenger receptors and atherosclerosis
    • Rigotti A. Scavenger receptors and atherosclerosis. Biol Res 2000;33(2):97–103.
    • (2000) Biol Res , vol.33 , Issue.2 , pp. 97-103
    • Rigotti, A.1
  • 38
    • 0030730023 scopus 로고    scopus 로고
    • The other side of scavenger receptors: Pattern recognition for host defense
    • Krieger M. The other side of scavenger receptors: pattern recognition for host defense. Curr Opin Lipidol 1997;8(5):275–80.
    • (1997) Curr Opin Lipidol , vol.8 , Issue.5 , pp. 275-280
    • Krieger, M.1
  • 39
    • 33845446813 scopus 로고    scopus 로고
    • Role of scavenger receptors in the binding and internalization of heat shock protein 70
    • Theriault JR, Adachi H, Calderwood SK. Role of scavenger receptors in the binding and internalization of heat shock protein 70. J Immunol 2006;177(12):8604–11.
    • (2006) J Immunol , vol.177 , Issue.12 , pp. 8604-8611
    • Theriault, J.R.1    Adachi, H.2    Calderwood, S.K.3
  • 40
    • 0037025397 scopus 로고    scopus 로고
    • Characterization of the human gene encoding the scavenger receptor expressed by endothelial cell and its regulation by a novel transcription factor, endothelial zinc finger protein-2
    • Adachi H, Tsujimoto M. Characterization of the human gene encoding the scavenger receptor expressed by endothelial cell and its regulation by a novel transcription factor, endothelial zinc finger protein-2. J Biol Chem 2002; 277(27):24014–21.
    • (2002) J Biol Chem , vol.277 , Issue.27 , pp. 24014-24021
    • Adachi, H.1    Tsujimoto, M.2
  • 41
    • 18244403201 scopus 로고    scopus 로고
    • Stabilin-1 and −2 constitute a novel family of fasciclin-like hyaluronan receptor homologues
    • Politz O, Gratchev A, McCourt PA, et al. Stabilin-1 and −2 constitute a novel family of fasciclin-like hyaluronan receptor homologues. Biochem J 2002;362(Pt 1):155–64.
    • (2002) Biochem J , vol.362 , Issue.1 , pp. 155-164
    • Politz, O.1    Gratchev, A.2    McCourt, P.A.3
  • 42
    • 34250378597 scopus 로고    scopus 로고
    • Scavenger receptor-A negatively regulates antitumor immunity
    • Wang XY, Facciponte J, Chen X, Subjeck JR, Repasky EA. Scavenger receptor-A negatively regulates antitumor immunity. Cancer Res 2007;67(10):4996–5002.
    • (2007) Cancer Res , vol.67 , Issue.10 , pp. 4996-5002
    • Wang, X.Y.1    Facciponte, J.2    Chen, X.3    Subjeck, J.R.4    Repasky, E.A.5
  • 43
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • Herz J, Strickland DK. LRP: a multifunctional scavenger and signaling receptor. J Clin Invest 2001;108(6):779–84.
    • (2001) J Clin Invest , vol.108 , Issue.6 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 44
    • 23044469458 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor-beta (PDGFR-beta) activation promotes its association with the low density lipoprotein receptor-related protein (LRP)
    • Newton CS, Loukinova E, Mikhailenko I, et al. Platelet-derived growth factor receptor-beta (PDGFR-beta) activation promotes its association with the low density lipoprotein receptor-related protein (LRP). Evidence for co-receptor function. J Biol Chem 2005; 280(30):27872–8.
    • (2005) Evidence for Co-Receptor Function. J Biol Chem , vol.280 , Issue.30 , pp. 27872-27878
    • Newton, C.S.1    Loukinova, E.2    Mikhailenko, I.3
  • 45
    • 0035057838 scopus 로고    scopus 로고
    • Dissection of receptor folding and ligand-binding property with functional minireceptors of LDL receptor-related protein
    • Obermoeller-McCormick LM, Li Y, Osaka H, FitzGerald DJ, Schwartz AL, Bu G. Dissection of receptor folding and ligand-binding property with functional minireceptors of LDL receptor-related protein. J Cell Sci 2001;114 (Pt 5):899–908.
    • (2001) J Cell Sci , vol.114 , Issue.5 , pp. 899-908
    • Obermoeller-McCormick, L.M.1    Li, Y.2    Osaka, H.3    Fitzgerald, D.J.4    Schwartz, A.L.5    Bu, G.6
  • 46
    • 27744555038 scopus 로고    scopus 로고
    • Differential CD91 dependence for calreticulin and Pseudomonas exo-toxin-A endocytosis
    • Walters JJ, Berwin B. Differential CD91 dependence for calreticulin and Pseudomonas exo-toxin-A endocytosis. Traffic 2005;6(12): 1173–82.
    • (2005) Traffic , vol.6 , Issue.12 , pp. 1173-1182
    • Walters, J.J.1    Berwin, B.2
  • 47
    • 34548654412 scopus 로고    scopus 로고
    • Efficient cross-presentation by heat shock protein 90-peptide complex-loaded dendritic cells via an endosomal pathway
    • Kurotaki T, Tamura Y, Ueda G, et al. Efficient cross-presentation by heat shock protein 90-peptide complex-loaded dendritic cells via an endosomal pathway. J Immunol 2007; 179(3):1803–13.
    • (2007) J Immunol , vol.179 , Issue.3 , pp. 1803-1813
    • Kurotaki, T.1    Tamura, Y.2    Ueda, G.3
  • 48
    • 20544433550 scopus 로고    scopus 로고
    • Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8+ T cells
    • Binder RJ, Srivastava PK. Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8+ T cells. Nat Immunol 2005;6(6): 593–9.
    • (2005) Nat Immunol , vol.6 , Issue.6 , pp. 593-599
    • Binder, R.J.1    Srivastava, P.K.2
  • 49
    • 0037144808 scopus 로고    scopus 로고
    • CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes
    • Becker T, Hartl FU, Wieland F. CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. J Cell Biol 2002;158(7):1277–85.
    • (2002) J Cell Biol , vol.158 , Issue.7 , pp. 1277-1285
    • Becker, T.1    Hartl, F.U.2    Wieland, F.3
  • 50
    • 21144456842 scopus 로고    scopus 로고
    • Complexity and complementarity of outer membrane protein A recognition by cellular and humoral innate immunity receptors
    • Jeannin P, Bottazzi B, Sironi M, et al. Complexity and complementarity of outer membrane protein A recognition by cellular and humoral innate immunity receptors. Immunity 2005;22(5):551–60.
    • (2005) Immunity , vol.22 , Issue.5 , pp. 551-560
    • Jeannin, P.1    Bottazzi, B.2    Sironi, M.3
  • 51
    • 70350218802 scopus 로고    scopus 로고
    • Antitumor Immunity Can Be Uncoupled from Autoimmunity following Heat Shock Protein 70-Mediated Inflammatory Killing of Normal Pancreas
    • Kottke T, Pulido J, Thompson J, et al. Antitumor Immunity Can Be Uncoupled from Autoimmunity following Heat Shock Protein 70-Mediated Inflammatory Killing of Normal Pancreas. Cancer Res 2009.
    • (2009) Cancer Res
    • Kottke, T.1    Pulido, J.2    Thompson, J.3
  • 53
    • 20444380998 scopus 로고    scopus 로고
    • Crystal structure of human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to OxLDL
    • Ohki I, Ishigaki T, Oyama T, et al. Crystal structure of human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to OxLDL. Structure 2005;13(6):905–17.
    • (2005) Structure , vol.13 , Issue.6 , pp. 905-917
    • Ohki, I.1    Ishigaki, T.2    Oyama, T.3
  • 54
    • 34848905092 scopus 로고    scopus 로고
    • Macrophage scavenger receptors and host-de-rived ligands
    • Pluddemann A, Neyen C, Gordon S. Macrophage scavenger receptors and host-de-rived ligands. Methods 2007;43(3):207–17.
    • (2007) Methods , vol.43 , Issue.3 , pp. 207-217
    • Pluddemann, A.1    Neyen, C.2    Gordon, S.3
  • 55
    • 0024284211 scopus 로고
    • Structure and function of epidermal growth factor-like regions in proteins
    • Appella E, Weber IT, Blasi F. Structure and function of epidermal growth factor-like regions in proteins. FEBS Lett 1988; 231(1):1–4.
    • (1988) FEBS Lett , vol.231 , Issue.1 , pp. 1-4
    • Appella, E.1    Weber, I.T.2    Blasi, F.3
  • 56
    • 4544370574 scopus 로고    scopus 로고
    • Type F scavenger receptor SREC-I interacts with advil-lin, a member of the gelsolin/villin family, and induces neurite-like outgrowth
    • Shibata M, Ishii J, Koizumi H, et al. Type F scavenger receptor SREC-I interacts with advil-lin, a member of the gelsolin/villin family, and induces neurite-like outgrowth. J Biol Chem 2004;279(38):40084–90.
    • (2004) J Biol Chem , vol.279 , Issue.38 , pp. 40084-40090
    • Shibata, M.1    Ishii, J.2    Koizumi, H.3
  • 57
    • 50249133197 scopus 로고    scopus 로고
    • Epidermal growth factor-like domain repeat of stabilin-2 recognizes phosphatidylserine during cell corpse clearance
    • Park SY, Kim SY, Jung MY, Bae DJ, Kim IS. Epidermal growth factor-like domain repeat of stabilin-2 recognizes phosphatidylserine during cell corpse clearance. Mol Cell Biol 2008;28(17):5288–98.
    • (2008) Mol Cell Biol , vol.28 , Issue.17 , pp. 5288-5298
    • Park, S.Y.1    Kim, S.Y.2    Jung, M.Y.3    Bae, D.J.4    Kim, I.S.5
  • 58
    • 33750359212 scopus 로고    scopus 로고
    • Enhanced immunogenicity of heat shock protein 70 peptide complexes from dendritic cell-tumor fusion cells
    • Enomoto Y, Bharti A, Khaleque AA, et al. Enhanced immunogenicity of heat shock protein 70 peptide complexes from dendritic cell-tumor fusion cells. J Immunol 2006;177(9): 5946–55.
    • (2006) J Immunol , vol.177 , Issue.9 , pp. 5946-5955
    • Enomoto, Y.1    Bharti, A.2    Khaleque, A.A.3
  • 59
    • 0036311017 scopus 로고    scopus 로고
    • Crystal structure of a non-canonical low-affinity peptide complexed with MHC class I: A new approach for vaccine design
    • Apostolopoulos V, Yu M, Corper AL, et al. Crystal structure of a non-canonical low-affinity peptide complexed with MHC class I: a new approach for vaccine design. J Mol Biol 2002;318(5):1293–305.
    • (2002) J Mol Biol , vol.318 , Issue.5 , pp. 1293-1305
    • Apostolopoulos, V.1    Yu, M.2    Corper, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.