메뉴 건너뛰기




Volumn 3, Issue 6, 2009, Pages 636-653

Proteomic profiling of heat shock proteins: An emerging molecular approach with direct pathophysiological and clinical implications

Author keywords

Biomarkers; Cellular stress response; Diagnostics; Neurodegeneration; Oncoproteomics

Indexed keywords

AUTOANTIBODY; GELDANAMYCIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 70 AUTOANTIBODY; HEAT SHOCK PROTEIN 90; IMATINIB; UNCLASSIFIED DRUG;

EID: 70449589907     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200800195     Document Type: Review
Times cited : (14)

References (182)
  • 1
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in drosophila
    • Ritossa, F., A new puffing pattern induced by temperature shock and DNP in drosophila. Cell Mol. Life Sci. 1962, 18, 571-573.
    • (1962) Cell Mol. Life Sci , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 2
    • 0032416104 scopus 로고    scopus 로고
    • Molecular chaperones: Biology and prospects for pharmacological intervention
    • Smith, D. F., Whitesell, L., Katsanis, E., Molecular chaperones: biology and prospects for pharmacological intervention. Pharmacol. Res. 1998, 50, 493-513.
    • (1998) Pharmacol. Res , vol.50 , pp. 493-513
    • Smith, D.F.1    Whitesell, L.2    Katsanis, E.3
  • 3
    • 85012430068 scopus 로고    scopus 로고
    • Heat shock proteins in health and disease: Therapeutic targets or therapeutics agents?
    • Pockley, A. G., Heat shock proteins in health and disease: therapeutic targets or therapeutics agents? Expert Rev. Mol. Med. 2001, 3, 1-21.
    • (2001) Expert Rev. Mol. Med , vol.3 , pp. 1-21
    • Pockley, A.G.1
  • 4
    • 34248197864 scopus 로고    scopus 로고
    • Heat shock responses for understanding diseases of protein denaturation
    • Kim, H. J., Hwang, N. R., Lee, K. J., Heat shock responses for understanding diseases of protein denaturation. Mol. Cells 2007, 23, 123-131.
    • (2007) Mol. Cells , vol.23 , pp. 123-131
    • Kim, H.J.1    Hwang, N.R.2    Lee, K.J.3
  • 5
    • 27744517366 scopus 로고    scopus 로고
    • Heat shock proteins as emerging therapeutic targets
    • Soti, C., Nagy, E., Giricz, Z., Vigh, L. et al., Heat shock proteins as emerging therapeutic targets. Br. J. Pharmacol. 2005, 146, 769-780.
    • (2005) Br. J. Pharmacol , vol.146 , pp. 769-780
    • Soti, C.1    Nagy, E.2    Giricz, Z.3    Vigh, L.4
  • 6
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • Westerheide, S. D., Morimoto, R. I., Heat shock response modulators as therapeutic tools for diseases of protein conformation. J. Biol. Chem. 2005, 280, 33097-33100.
    • (2005) J. Biol. Chem , vol.280 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 7
    • 0028232354 scopus 로고
    • Analysis of cellular phosphoproteins by two-dimensional gel electrophoresis: Applications for cell signaling in normal and cancer cells
    • Guy, G. R., Philip, R., Tan, Y. H., Analysis of cellular phosphoproteins by two-dimensional gel electrophoresis: applications for cell signaling in normal and cancer cells. Electrophoresis 1994, 15, 417-440.
    • (1994) Electrophoresis , vol.15 , pp. 417-440
    • Guy, G.R.1    Philip, R.2    Tan, Y.H.3
  • 8
    • 44349192262 scopus 로고    scopus 로고
    • Orphan nuclear receptor estrogen-related receptor-beta suppresses in vitro and in vivo growth of prostate cancer cells via p21(WAF1/CIP1) induction and as a potential therapeutic target in prostate cancer
    • Yu, S., Wong, Y. C., Wang, X. H., Ling, M. T. et al., Orphan nuclear receptor estrogen-related receptor-beta suppresses in vitro and in vivo growth of prostate cancer cells via p21(WAF1/CIP1) induction and as a potential therapeutic target in prostate cancer. Oncogene 2008, 27, 3313-3328.
    • (2008) Oncogene , vol.27 , pp. 3313-3328
    • Yu, S.1    Wong, Y.C.2    Wang, X.H.3    Ling, M.T.4
  • 9
    • 40749124091 scopus 로고    scopus 로고
    • Felts, S. J., Karnitz, L. M., Toft, D. O., Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR). Cell Stress Chaperones 2007, 12, 353-363.
    • Felts, S. J., Karnitz, L. M., Toft, D. O., Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR). Cell Stress Chaperones 2007, 12, 353-363.
  • 10
    • 42549158533 scopus 로고    scopus 로고
    • HIF-1alpha and STAT3 client proteins interacting with the cancer chaperone Hsp90: Therapeutic considerations
    • Kim, H. L., Cassone, M., Otvos, L., Jr., Vogiatzi, P., HIF-1alpha and STAT3 client proteins interacting with the cancer chaperone Hsp90: therapeutic considerations. Cancer Biol. Ther. 2008, 7, 10-14.
    • (2008) Cancer Biol. Ther , vol.7 , pp. 10-14
    • Kim, H.L.1    Cassone, M.2    Otvos Jr., L.3    Vogiatzi, P.4
  • 11
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell, L., Lindquist, S. L., HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 2005, 5, 761-772.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 12
    • 0033970942 scopus 로고    scopus 로고
    • Characterization of native interaction of hsp110 with hsp25 and hsc70
    • Wang, X. Y., Chen, X., Oh, H. J., Repasky, E. et al., Characterization of native interaction of hsp110 with hsp25 and hsc70. FEBS Lett. 2000, 465, 98-102.
    • (2000) FEBS Lett , vol.465 , pp. 98-102
    • Wang, X.Y.1    Chen, X.2    Oh, H.J.3    Repasky, E.4
  • 13
    • 0025175208 scopus 로고
    • Reduced levels of hsp90 compromise steroid receptor action in vivo
    • Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G. et al., Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 1990, 348, 166-168.
    • (1990) Nature , vol.348 , pp. 166-168
    • Picard, D.1    Khursheed, B.2    Garabedian, M.J.3    Fortin, M.G.4
  • 14
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman, B. C., Yamamoto, K. R., Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 2002, 296, 2232-2235.
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 15
    • 0038466354 scopus 로고    scopus 로고
    • Tumor derived, chaperone-rich cell lysate activates dendritic cells and elicits potent antitumor immunity
    • Zeng, Y., Feng, H., Graner, M. W., Katsanis, E., Tumor derived, chaperone-rich cell lysate activates dendritic cells and elicits potent antitumor immunity. Blood 2003, 101, 4485-4491.
    • (2003) Blood , vol.101 , pp. 4485-4491
    • Zeng, Y.1    Feng, H.2    Graner, M.W.3    Katsanis, E.4
  • 16
    • 19944425916 scopus 로고    scopus 로고
    • Heat shock proteins and their use as anticancer vaccines
    • Parmiani, G., Testori, A., Maio, M., Castelli, C. et al., Heat shock proteins and their use as anticancer vaccines. Clin. Cancer Res. 2004, 10, 8142-8146.
    • (2004) Clin. Cancer Res , vol.10 , pp. 8142-8146
    • Parmiani, G.1    Testori, A.2    Maio, M.3    Castelli, C.4
  • 17
    • 33845913216 scopus 로고    scopus 로고
    • Intracellular and extracellular functions of heat shock proteins: Repercussions in cancer therapy
    • Schmitt, E., Gehrmann, M., Brunet, M., Multhoff, G., Garrido, C., Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy. J. Leukoc. Biol. 2007, 81, 15-27.
    • (2007) J. Leukoc. Biol , vol.81 , pp. 15-27
    • Schmitt, E.1    Gehrmann, M.2    Brunet, M.3    Multhoff, G.4    Garrido, C.5
  • 18
    • 38449100535 scopus 로고    scopus 로고
    • Extracellular heat shock proteins in cell signaling and immunity
    • Calderwood, S. K., Mambula, S. S., Gray, P. J., Jr., Extracellular heat shock proteins in cell signaling and immunity. Ann. NY Acad. Sci. 2007, 1113, 28-39.
    • (2007) Ann. NY Acad. Sci , vol.1113 , pp. 28-39
    • Calderwood, S.K.1    Mambula, S.S.2    Gray Jr., P.J.3
  • 19
    • 33947117494 scopus 로고    scopus 로고
    • Extracellular heat shock protein-90alpha: Linking hypoxia to skin cell motility and wound healing
    • Li, W., Li, Y., Guan, S., Fan, J. et al., Extracellular heat shock protein-90alpha: linking hypoxia to skin cell motility and wound healing. EMBO J. 2007, 26, 1221-1233.
    • (2007) EMBO J , vol.26 , pp. 1221-1233
    • Li, W.1    Li, Y.2    Guan, S.3    Fan, J.4
  • 21
    • 33947596924 scopus 로고    scopus 로고
    • Heat shock protein 70 and glycoprotein 96 are differentially expressed on the surface of malignant and nonmalignant breast cells
    • Melendez, K., Wallen, E. S., Edwards, B. S., Mobarak, C. D. et al., Heat shock protein 70 and glycoprotein 96 are differentially expressed on the surface of malignant and nonmalignant breast cells. Cell Stress Chaperones 2006, 11, 334-342.
    • (2006) Cell Stress Chaperones , vol.11 , pp. 334-342
    • Melendez, K.1    Wallen, E.S.2    Edwards, B.S.3    Mobarak, C.D.4
  • 22
    • 33645959208 scopus 로고    scopus 로고
    • Heat shock proteins in immunity
    • Multhoff, G., Heat shock proteins in immunity. Handb. Exp. Pharmacol. 2006, 172, 279-304.
    • (2006) Handb. Exp. Pharmacol , vol.172 , pp. 279-304
    • Multhoff, G.1
  • 23
    • 34250329955 scopus 로고    scopus 로고
    • Heat shock paradox and a new role of heat shock proteins and their receptors as anti-inflammation targets
    • Chen, Y., Voegeli, T. S., Liu, P. P., Noble, E. G., Currie, R. W., Heat shock paradox and a new role of heat shock proteins and their receptors as anti-inflammation targets. Inflamm. Allergy Drug Targets 2007, 6, 91-100.
    • (2007) Inflamm. Allergy Drug Targets , vol.6 , pp. 91-100
    • Chen, Y.1    Voegeli, T.S.2    Liu, P.P.3    Noble, E.G.4    Currie, R.W.5
  • 24
    • 42949165604 scopus 로고    scopus 로고
    • Chaperones as integrators of cellular networks: Changes of cellular integrity in stress and diseases
    • Palotai, R., Szalay, M. S., Csermely, P., Chaperones as integrators of cellular networks: changes of cellular integrity in stress and diseases. IUBMB Life 2008, 60, 10-18.
    • (2008) IUBMB Life , vol.60 , pp. 10-18
    • Palotai, R.1    Szalay, M.S.2    Csermely, P.3
  • 25
    • 31544446624 scopus 로고    scopus 로고
    • Plasma antibody titres to heat shock proteins-60, -65 and-70: Their relationship to coronary risk factors in dyslipidaemic patients and healthy individuals
    • Ghayour-Mobarhan, M., Lamb, D. J., Lovell, D. P., Livingstone, C. et al., Plasma antibody titres to heat shock proteins-60, -65 and-70: their relationship to coronary risk factors in dyslipidaemic patients and healthy individuals. Scand. J. Clin. Lab. Invest. 2005, 65, 601-614.
    • (2005) Scand. J. Clin. Lab. Invest , vol.65 , pp. 601-614
    • Ghayour-Mobarhan, M.1    Lamb, D.J.2    Lovell, D.P.3    Livingstone, C.4
  • 26
    • 38549116650 scopus 로고    scopus 로고
    • Stress proteins in CNS inflammation
    • van Noort, J. M., Stress proteins in CNS inflammation. J. Pathol. 2008, 214, 267-275.
    • (2008) J. Pathol , vol.214 , pp. 267-275
    • van Noort, J.M.1
  • 27
    • 34247248357 scopus 로고    scopus 로고
    • Origin of immunomodulation after soft tissue trauma: Potential involvement of extracellular heat-shock proteins
    • Flohé, S. B., Bangen, J. M., Flohé, S., Agrawal, H. et al., Origin of immunomodulation after soft tissue trauma: potential involvement of extracellular heat-shock proteins. Shock 2007, 27, 494-502.
    • (2007) Shock , vol.27 , pp. 494-502
    • Flohé, S.B.1    Bangen, J.M.2    Flohé, S.3    Agrawal, H.4
  • 28
    • 0842308738 scopus 로고    scopus 로고
    • Mycobacterial heat shock protein 70 induces interleukin-10 production: Immunomodulation of synovial cell cytokine profile and dendritic cell maturation
    • Detanico, T., Rodrigues, L., Sabritto, A. C., Keisermann, M. et al., Mycobacterial heat shock protein 70 induces interleukin-10 production: immunomodulation of synovial cell cytokine profile and dendritic cell maturation. Clin. Exp. Immunol. 2004, 135, 336-342.
    • (2004) Clin. Exp. Immunol , vol.135 , pp. 336-342
    • Detanico, T.1    Rodrigues, L.2    Sabritto, A.C.3    Keisermann, M.4
  • 29
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: Biology and pharmacology
    • Powers, M. V., Workman, P., Inhibitors of the heat shock response: biology and pharmacology. FEBS Lett. 2007, 581, 3758-3769.
    • (2007) FEBS Lett , vol.581 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 30
    • 32944454483 scopus 로고    scopus 로고
    • Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors
    • Zaarur, N., Gabai, V. L., Porco, J. A., Jr., Calderwood, S., Sherman, M. Y., Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors. Cancer Res. 2006, 66, 1783-1791.
    • (2006) Cancer Res , vol.66 , pp. 1783-1791
    • Zaarur, N.1    Gabai, V.L.2    Porco Jr., J.A.3    Calderwood, S.4    Sherman, M.Y.5
  • 31
    • 34447631322 scopus 로고    scopus 로고
    • The role of chaperone proteins in autoimmunity
    • Routsias, J. G., Tzioufas, A. G., The role of chaperone proteins in autoimmunity. Ann. NY Acad. Sci. 2006, 1088, 52-64.
    • (2006) Ann. NY Acad. Sci , vol.1088 , pp. 52-64
    • Routsias, J.G.1    Tzioufas, A.G.2
  • 32
    • 34447559600 scopus 로고    scopus 로고
    • a role for HSP inducing compounds as antiinflammatory immuno-modulators?
    • Cell stress induced HSP are targets of regulatory T cells
    • Wieten, L., Broere, F., van der Zee, R., Koerkamp, E. K. et al., Cell stress induced HSP are targets of regulatory T cells: a role for HSP inducing compounds as antiinflammatory immuno-modulators? FEBS Lett. 2007, 581, 3716-3722.
    • (2007) FEBS Lett , vol.581 , pp. 3716-3722
    • Wieten, L.1    Broere, F.2    van der Zee, R.3    Koerkamp, E.K.4
  • 33
    • 38149095001 scopus 로고    scopus 로고
    • Proteomics-based identification of HSP60 as a tumor-associated antigen in colorectal cancer
    • Yujun, H., Yuzhang, W., Zhirong, M., Wanlin, L. et al., Proteomics-based identification of HSP60 as a tumor-associated antigen in colorectal cancer. Proteomics Clin. Appl. 2007, 1, 336-342.
    • (2007) Proteomics Clin. Appl , vol.1 , pp. 336-342
    • Yujun, H.1    Yuzhang, W.2    Zhirong, M.3    Wanlin, L.4
  • 34
    • 43549094212 scopus 로고    scopus 로고
    • Déjàvu in proteomics. A hit parade of repeatedly identified differentially expressed proteins
    • Petrak, J., Ivanek, R., Toman, O., Cmejla, R. et al., Déjàvu in proteomics. A hit parade of repeatedly identified differentially expressed proteins. Proteomics 2008, 8, 1744-1749.
    • (2008) Proteomics , vol.8 , pp. 1744-1749
    • Petrak, J.1    Ivanek, R.2    Toman, O.3    Cmejla, R.4
  • 36
    • 38949187296 scopus 로고    scopus 로고
    • Proteomic characterization of differentially expressed proteins in breast cancer: Expression of hnRNP H1, RKIP and GRP78 is strongly associated with HER-2/ neu status
    • Zhang, D., Tai, L. K., Wong, L. L., Putti, T. C. et al., Proteomic characterization of differentially expressed proteins in breast cancer: expression of hnRNP H1, RKIP and GRP78 is strongly associated with HER-2/ neu status. Proteomics Clin. Appl. 2008, 2, 99-107.
    • (2008) Proteomics Clin. Appl , vol.2 , pp. 99-107
    • Zhang, D.1    Tai, L.K.2    Wong, L.L.3    Putti, T.C.4
  • 37
    • 15744402283 scopus 로고    scopus 로고
    • Cotreatment with suberanoylanilide hydroxamic acid and 17-allylamino 17-demethoxygeldanamycin synergistically induces apoptosis in Bcr-Abl1cells sensitive and resistant to STI571 (imatinib mesylate) in association with down-regulation of Bcr-Abl, abrogation of signal transducer and activator of transcription 5 activity, and Bax conformational change
    • Rahmani, M., Reese, E., Dai, Y., Bauer, C. et al., Cotreatment with suberanoylanilide hydroxamic acid and 17-allylamino 17-demethoxygeldanamycin synergistically induces apoptosis in Bcr-Abl1cells sensitive and resistant to STI571 (imatinib mesylate) in association with down-regulation of Bcr-Abl, abrogation of signal transducer and activator of transcription 5 activity, and Bax conformational change. Mol. Pharmacol. 2005, 67, 1166-1176.
    • (2005) Mol. Pharmacol , vol.67 , pp. 1166-1176
    • Rahmani, M.1    Reese, E.2    Dai, Y.3    Bauer, C.4
  • 38
    • 22244485706 scopus 로고    scopus 로고
    • Epidermal growth factor receptors harboring kinase domain mutations associate with the heat shock protein 90 chaperone and are destabilized following exposure to geldanamycins
    • Shimamura, T., Lowell, A. M., Engelman, J. A., Shapiro, G. I., Epidermal growth factor receptors harboring kinase domain mutations associate with the heat shock protein 90 chaperone and are destabilized following exposure to geldanamycins. Cancer Res. 2005, 65, 6401-6408.
    • (2005) Cancer Res , vol.65 , pp. 6401-6408
    • Shimamura, T.1    Lowell, A.M.2    Engelman, J.A.3    Shapiro, G.I.4
  • 40
    • 42149106909 scopus 로고    scopus 로고
    • Hsp27 regulates proinflammatory mediator release in keratinocytes by modulating NF-kappaB signaling
    • Sur, R., Lyte, P. A., Southall, M. D., Hsp27 regulates proinflammatory mediator release in keratinocytes by modulating NF-kappaB signaling. J. Invest. Dermatol. 2008, 128, 1116-1122.
    • (2008) J. Invest. Dermatol , vol.128 , pp. 1116-1122
    • Sur, R.1    Lyte, P.A.2    Southall, M.D.3
  • 41
    • 38449087767 scopus 로고    scopus 로고
    • Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase
    • Arthur, J. C., Lich, J. D., Aziz, R. K., Kotb, M., Ting, J. P., Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase. J. Immunol. 2007, 179, 6291-6296.
    • (2007) J. Immunol , vol.179 , pp. 6291-6296
    • Arthur, J.C.1    Lich, J.D.2    Aziz, R.K.3    Kotb, M.4    Ting, J.P.5
  • 42
    • 1842691021 scopus 로고    scopus 로고
    • PI3K/Akt is required for heat shock proteins to protect hypoxia-inducible factor 1alpha from pVHL-independent degradation
    • Zhou, J., Schmid, T., Frank, R., Brune, B., PI3K/Akt is required for heat shock proteins to protect hypoxia-inducible factor 1alpha from pVHL-independent degradation. J. Biol. Chem. 2004, 279, 13506-13513.
    • (2004) J. Biol. Chem , vol.279 , pp. 13506-13513
    • Zhou, J.1    Schmid, T.2    Frank, R.3    Brune, B.4
  • 43
    • 0141953996 scopus 로고    scopus 로고
    • Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin
    • Keezer, S. M., Ivie, S. E., Krutzsch, H. C., Tandle, A. et al., Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin. Cancer Res. 2003, 63, 6405-6412.
    • (2003) Cancer Res , vol.63 , pp. 6405-6412
    • Keezer, S.M.1    Ivie, S.E.2    Krutzsch, H.C.3    Tandle, A.4
  • 44
    • 0033899869 scopus 로고    scopus 로고
    • A novel association between the human heat shock transcription factor 1 (HSF1) and prostate adenocarcinoma
    • Hoang, A. T., Huang, J., Rudra-Ganguly, N., Zheng, J. et al., A novel association between the human heat shock transcription factor 1 (HSF1) and prostate adenocarcinoma. Am. J. Pathol. 2000, 156, 857-864.
    • (2000) Am. J. Pathol , vol.156 , pp. 857-864
    • Hoang, A.T.1    Huang, J.2    Rudra-Ganguly, N.3    Zheng, J.4
  • 45
    • 34447631322 scopus 로고    scopus 로고
    • The role of chaperone proteins in autoimmunity
    • Routsias, J. G., Tzioufas, A. G., The role of chaperone proteins in autoimmunity. Ann. NY Acad. Sci. 2006, 1088, 52-64.
    • (2006) Ann. NY Acad. Sci , vol.1088 , pp. 52-64
    • Routsias, J.G.1    Tzioufas, A.G.2
  • 46
    • 34447559600 scopus 로고    scopus 로고
    • a role for HSP inducing compounds as antiinflammatory immuno-modulators?
    • Cell stress induced HSP are targets of regulatory T cells
    • Wieten, L., Broere, F., van der Zee, R., Koerkamp, E. K. et al., Cell stress induced HSP are targets of regulatory T cells: a role for HSP inducing compounds as antiinflammatory immuno-modulators? FEBS Lett. 2007, 581, 3716-3722.
    • (2007) FEBS Lett , vol.581 , pp. 3716-3722
    • Wieten, L.1    Broere, F.2    van der Zee, R.3    Koerkamp, E.K.4
  • 48
    • 38949134137 scopus 로고    scopus 로고
    • The dual immunoregulatory roles of stress proteins
    • Pockley, A., Muthana, M., Calderwood, S. K., The dual immunoregulatory roles of stress proteins. TIBS 2008, 33, 71-79.
    • (2008) TIBS , vol.33 , pp. 71-79
    • Pockley, A.1    Muthana, M.2    Calderwood, S.K.3
  • 49
    • 36549055112 scopus 로고    scopus 로고
    • Proteomic analysis identified N-cadherin, clusterin, and HSP27 as mediators of SPARC (secreted protein, acidic and rich in cysteines) activity in melanoma cells
    • Sosa, M. S., Girotti, M. R., Salvatierra, E., Prada, F., Proteomic analysis identified N-cadherin, clusterin, and HSP27 as mediators of SPARC (secreted protein, acidic and rich in cysteines) activity in melanoma cells. Proteomics 2007, 7, 4123-4134.
    • (2007) Proteomics , vol.7 , pp. 4123-4134
    • Sosa, M.S.1    Girotti, M.R.2    Salvatierra, E.3    Prada, F.4
  • 50
    • 3543060077 scopus 로고    scopus 로고
    • Expression of heat shock protein 27 in human renal cell carcinoma
    • Sarto, C., Valsecchi, C., Magni, F., Tremolada, L. et al., Expression of heat shock protein 27 in human renal cell carcinoma. Proteomics 2004, 4, 2252-2260.
    • (2004) Proteomics , vol.4 , pp. 2252-2260
    • Sarto, C.1    Valsecchi, C.2    Magni, F.3    Tremolada, L.4
  • 51
    • 28444451204 scopus 로고    scopus 로고
    • Heat-shock protein 27: A potential biomarker for hepatocellular carcinoma identified by serum proteome analysis
    • Feng, J. T., Liu, Y. K., Song, H. Y., Dai, Z. et al., Heat-shock protein 27: a potential biomarker for hepatocellular carcinoma identified by serum proteome analysis. Proteomics 2005, 5, 4581-4588.
    • (2005) Proteomics , vol.5 , pp. 4581-4588
    • Feng, J.T.1    Liu, Y.K.2    Song, H.Y.3    Dai, Z.4
  • 52
    • 32944457371 scopus 로고    scopus 로고
    • Proteomic profiling of hepatocellular carcinoma in Chinese cohort reveals heat-shock proteins (Hsp27, Hsp70, GRP78) upregulation and their associated prognostic values
    • Luk, J. M., Lam, C. T., Siu, A. F., Lam, B. Y. et al., Proteomic profiling of hepatocellular carcinoma in Chinese cohort reveals heat-shock proteins (Hsp27, Hsp70, GRP78) upregulation and their associated prognostic values. Proteomics 2006, 6, 1049-1057.
    • (2006) Proteomics , vol.6 , pp. 1049-1057
    • Luk, J.M.1    Lam, C.T.2    Siu, A.F.3    Lam, B.Y.4
  • 53
    • 38449118227 scopus 로고    scopus 로고
    • Proteomics finding heat shock protein 27 as a biomarker for resistance of pancreatic cancer cells to gemcitabine
    • Mori-Iwamoto, S., Kuramitsu, Y., Ryozawa, S., Mikuria, K. et al., Proteomics finding heat shock protein 27 as a biomarker for resistance of pancreatic cancer cells to gemcitabine. Int. J. Oncol. 2007, 31, 1345-1350.
    • (2007) Int. J. Oncol , vol.31 , pp. 1345-1350
    • Mori-Iwamoto, S.1    Kuramitsu, Y.2    Ryozawa, S.3    Mikuria, K.4
  • 54
    • 36549031220 scopus 로고    scopus 로고
    • Dominant negative Rac1 attenuates paclitaxel-induced apoptosis in human melanoma cells through upregulation of heat shock protein 27: A functional proteomic analysis
    • Lee, S. C., Sim, N., Clement, M. V., Yadav, S. K., Pervaiz, S., Dominant negative Rac1 attenuates paclitaxel-induced apoptosis in human melanoma cells through upregulation of heat shock protein 27: a functional proteomic analysis. Proteomics 2007, 7, 4112-4122.
    • (2007) Proteomics , vol.7 , pp. 4112-4122
    • Lee, S.C.1    Sim, N.2    Clement, M.V.3    Yadav, S.K.4    Pervaiz, S.5
  • 55
    • 49849090629 scopus 로고    scopus 로고
    • Identification of 5-fluorouracil response proteins in colorectal carcinoma cell line SW480 by two-dimensional electrophoresis and MALDI-TOF mass spectrometry
    • Wong, C. S., Wong, V. W., Chan, C. M., Ma, B. B. et al., Identification of 5-fluorouracil response proteins in colorectal carcinoma cell line SW480 by two-dimensional electrophoresis and MALDI-TOF mass spectrometry. Oncol. Rep. 2008, 20, 89-98.
    • (2008) Oncol. Rep , vol.20 , pp. 89-98
    • Wong, C.S.1    Wong, V.W.2    Chan, C.M.3    Ma, B.B.4
  • 56
    • 39749116808 scopus 로고    scopus 로고
    • Proteomic analysis of liver cancer cells treated with suberonylanilide hydroxamic acid
    • Tong, A., Zhang, H., Li, Z., Gou, L. et al., Proteomic analysis of liver cancer cells treated with suberonylanilide hydroxamic acid. Cancer Chemother. Pharmacol. 2008, 61, 791-802.
    • (2008) Cancer Chemother. Pharmacol , vol.61 , pp. 791-802
    • Tong, A.1    Zhang, H.2    Li, Z.3    Gou, L.4
  • 57
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins
    • Ellen, A., Nollen, A., Morimoto, R. I., Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins. J. Cell Sci. 2002, 115, 2809-2816.
    • (2002) J. Cell Sci , vol.115 , pp. 2809-2816
    • Ellen, A.1    Nollen, A.2    Morimoto, R.I.3
  • 58
    • 5644266041 scopus 로고    scopus 로고
    • Diverse proteomic alterations in gastric adenocarcinoma
    • He, Q. Y., Cheung, Y. H., Leung, S. Y., Yuen, S. T. et al., Diverse proteomic alterations in gastric adenocarcinoma. Proteomics 2004, 4, 3276-3287.
    • (2004) Proteomics , vol.4 , pp. 3276-3287
    • He, Q.Y.1    Cheung, Y.H.2    Leung, S.Y.3    Yuen, S.T.4
  • 59
    • 24044514711 scopus 로고    scopus 로고
    • A two-dimensional electrophoresis preliminary approach to human hepatocarcinoma differentiation induced by PPAR-agonists
    • Bottoni, P., Giardina, B., Martorana, G. E., Zuppi, C. et al., A two-dimensional electrophoresis preliminary approach to human hepatocarcinoma differentiation induced by PPAR-agonists. J. Cell. Mol. Med. 2005, 9, 462-467.
    • (2005) J. Cell. Mol. Med , vol.9 , pp. 462-467
    • Bottoni, P.1    Giardina, B.2    Martorana, G.E.3    Zuppi, C.4
  • 60
    • 33845419068 scopus 로고    scopus 로고
    • Identification of squamous cell carcinoma associated proteins by proteomics and loss of beta tropomyosin expression in esophageal cancer
    • Jazii, F. R., Najafi, Z., Malekzadeh, R., Conrads, T. P. et al., Identification of squamous cell carcinoma associated proteins by proteomics and loss of beta tropomyosin expression in esophageal cancer. World J. Gastroenterol. 2006, 12, 7104-7112.
    • (2006) World J. Gastroenterol , vol.12 , pp. 7104-7112
    • Jazii, F.R.1    Najafi, Z.2    Malekzadeh, R.3    Conrads, T.P.4
  • 61
    • 11144349225 scopus 로고    scopus 로고
    • Mortalin is over-expressed by colorectal adenocarcinomas and correlates with poor survival
    • Dundas, S. R., Lawrie, L. C., Rooney, P. H., Murray, G. I., Mortalin is over-expressed by colorectal adenocarcinomas and correlates with poor survival. J. Pathol. 2005, 205, 74-81.
    • (2005) J. Pathol , vol.205 , pp. 74-81
    • Dundas, S.R.1    Lawrie, L.C.2    Rooney, P.H.3    Murray, G.I.4
  • 62
    • 0142213549 scopus 로고    scopus 로고
    • Proteomic identification of heat shock protein 70 as a candidate target for enhancing apoptosis induced by farnesyl transferase inhibitor
    • Hu, W., Wu, W., Verschraegen, C. F., Chen, L. et al., Proteomic identification of heat shock protein 70 as a candidate target for enhancing apoptosis induced by farnesyl transferase inhibitor. Proteomics 2003, 3, 1904-1911.
    • (2003) Proteomics , vol.3 , pp. 1904-1911
    • Hu, W.1    Wu, W.2    Verschraegen, C.F.3    Chen, L.4
  • 63
    • 34748902479 scopus 로고    scopus 로고
    • Apoptosis induced by staurosporine alters chaperone and endoplasmic reticulum proteins: Identification by quantitative proteomics
    • Short, D. M., Heron, I. D., Birse-Archbold, J. L., Kerr, L. E. et al., Apoptosis induced by staurosporine alters chaperone and endoplasmic reticulum proteins: Identification by quantitative proteomics. Proteomics 2007, 7, 3085-3096.
    • (2007) Proteomics , vol.7 , pp. 3085-3096
    • Short, D.M.1    Heron, I.D.2    Birse-Archbold, J.L.3    Kerr, L.E.4
  • 64
    • 0035863476 scopus 로고    scopus 로고
    • Correlation of clinical data with proteomics profiles in 24 patients with B-cell chronic lymphocytic leukemia
    • Voss, T., Ahorn, H., Haberl, P., Dohner, H. et al., Correlation of clinical data with proteomics profiles in 24 patients with B-cell chronic lymphocytic leukemia. Int. J. Cancer 2001, 91, 180-186.
    • (2001) Int. J. Cancer , vol.91 , pp. 180-186
    • Voss, T.1    Ahorn, H.2    Haberl, P.3    Dohner, H.4
  • 65
    • 0038326942 scopus 로고    scopus 로고
    • Identification of differentially expressed proteins in human glioblastoma cell lines and tumors
    • Zhang, R., Tremblay, T. L., McDermid, A., Thibault, P., Stanimirovic, D., Identification of differentially expressed proteins in human glioblastoma cell lines and tumors. Glia 2003, 42, 194-208.
    • (2003) Glia , vol.42 , pp. 194-208
    • Zhang, R.1    Tremblay, T.L.2    McDermid, A.3    Thibault, P.4    Stanimirovic, D.5
  • 66
    • 5644294264 scopus 로고    scopus 로고
    • A proteomic approach to cisplatin resistance in the cervix squamous cell carcinoma cell line A431
    • Castagna, A., Antonioli, P., Astner, H., Hamdan, M. et al., A proteomic approach to cisplatin resistance in the cervix squamous cell carcinoma cell line A431. Proteomics 2004, 4, 3246-3267.
    • (2004) Proteomics , vol.4 , pp. 3246-3267
    • Castagna, A.1    Antonioli, P.2    Astner, H.3    Hamdan, M.4
  • 67
    • 3543055316 scopus 로고    scopus 로고
    • Radioresistance-related proteins in rectal cancer
    • Allal, A. S., Kahne, T., Reverdin, A. K., Lippert, H. et al., Radioresistance-related proteins in rectal cancer. Proteomics 2004, 4, 2261-2269.
    • (2004) Proteomics , vol.4 , pp. 2261-2269
    • Allal, A.S.1    Kahne, T.2    Reverdin, A.K.3    Lippert, H.4
  • 68
    • 38949198706 scopus 로고    scopus 로고
    • The proteomic analysis of cisplatin resistance in breast cancer cells
    • Smith, L., Welham, K. J., Watson, M. B., Drew, P. J. et al., The proteomic analysis of cisplatin resistance in breast cancer cells. Oncol. Res. 2007, 16, 497-506.
    • (2007) Oncol. Res , vol.16 , pp. 497-506
    • Smith, L.1    Welham, K.J.2    Watson, M.B.3    Drew, P.J.4
  • 69
    • 48249094972 scopus 로고    scopus 로고
    • Proteomic analysis of an imatinib-resistant K562 cell line highlights opposing roles of heat shock cognate 70 and heat shock 70 proteins in resistance
    • Pocaly, M., Lagarde, V., Etienne, G., Dupouy, M. et al., Proteomic analysis of an imatinib-resistant K562 cell line highlights opposing roles of heat shock cognate 70 and heat shock 70 proteins in resistance. Proteomics 2008, 8, 2394-2406.
    • (2008) Proteomics , vol.8 , pp. 2394-2406
    • Pocaly, M.1    Lagarde, V.2    Etienne, G.3    Dupouy, M.4
  • 70
    • 41649107031 scopus 로고    scopus 로고
    • Proteomics-based identification of autoantibody against heat shock protein 70 as a diagnostic marker in esophageal squamous cell carcinoma
    • Fujita, Y., Nakanishi, T., Miyamoto, Y., Hiramatsu, M. et al., Proteomics-based identification of autoantibody against heat shock protein 70 as a diagnostic marker in esophageal squamous cell carcinoma. Cancer Lett. 2008, 263, 280-290.
    • (2008) Cancer Lett , vol.263 , pp. 280-290
    • Fujita, Y.1    Nakanishi, T.2    Miyamoto, Y.3    Hiramatsu, M.4
  • 71
    • 33745998837 scopus 로고    scopus 로고
    • Proteomic analysis of autoantibodies in patients with hepatocellular carcinoma
    • Takashima, M., Kuramitsu, Y., Yokoyama, Y., Iizuka, N. et al., Proteomic analysis of autoantibodies in patients with hepatocellular carcinoma. Proteomics 2006, 6, 3894-3900.
    • (2006) Proteomics , vol.6 , pp. 3894-3900
    • Takashima, M.1    Kuramitsu, Y.2    Yokoyama, Y.3    Iizuka, N.4
  • 72
    • 1642268986 scopus 로고    scopus 로고
    • Hsp90 isoforms: Functions, expression and clinical importance
    • Sreedhar, A. S., Kalmár, E., Csermely, P., Shen, Y. F., Hsp90 isoforms: functions, expression and clinical importance. FEBS Lett. 2004, 562, 11-15.
    • (2004) FEBS Lett , vol.562 , pp. 11-15
    • Sreedhar, A.S.1    Kalmár, E.2    Csermely, P.3    Shen, Y.F.4
  • 73
    • 54049146850 scopus 로고    scopus 로고
    • Hsp90n - an accidental product of a fortuitous chromosomal translocation rather than a regular Hsp90 family member of human proteome
    • Zurawska, A., Urbanski, J., Bieganowski, P., Hsp90n - an accidental product of a fortuitous chromosomal translocation rather than a regular Hsp90 family member of human proteome. Biochim. Biophys. Acta 2008, 1784, 1844-1846.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1844-1846
    • Zurawska, A.1    Urbanski, J.2    Bieganowski, P.3
  • 74
    • 52649133274 scopus 로고    scopus 로고
    • HDAC6 inhibition enhances 17-AAG-mediated abrogation of hsp90 chaperone function in human leukemia cells
    • Rao, R., Fiskus, W., Yang, Y., Lee, P. et al., HDAC6 inhibition enhances 17-AAG-mediated abrogation of hsp90 chaperone function in human leukemia cells. Blood 2008, 112, 1886-1893.
    • (2008) Blood , vol.112 , pp. 1886-1893
    • Rao, R.1    Fiskus, W.2    Yang, Y.3    Lee, P.4
  • 75
    • 49649108912 scopus 로고    scopus 로고
    • Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion
    • Yang, Y., Rao, R., Shen, J., Tang, Y. et al., Role of acetylation and extracellular location of heat shock protein 90alpha in tumor cell invasion. Cancer Res. 2008, 68, 4833-4842.
    • (2008) Cancer Res , vol.68 , pp. 4833-4842
    • Yang, Y.1    Rao, R.2    Shen, J.3    Tang, Y.4
  • 76
    • 16344381930 scopus 로고    scopus 로고
    • Proteomic profiling for cancer progression: Differential display analysis for the expression of intracellular proteins between regressive and progressive cancer cell lines
    • Hayashi, E., Kuramitsu, Y., Okada, F., Fujimoto, M. et al., Proteomic profiling for cancer progression: differential display analysis for the expression of intracellular proteins between regressive and progressive cancer cell lines. Proteomics 2005, 5, 1024-1032.
    • (2005) Proteomics , vol.5 , pp. 1024-1032
    • Hayashi, E.1    Kuramitsu, Y.2    Okada, F.3    Fujimoto, M.4
  • 77
    • 47949123468 scopus 로고    scopus 로고
    • Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: Dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding
    • Butler, G. S., Dean, R. A., Tam, E. M., Overall, C. M., Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding. Mol. Cell. Biol. 2008, 28, 4896-4914.
    • (2008) Mol. Cell. Biol , vol.28 , pp. 4896-4914
    • Butler, G.S.1    Dean, R.A.2    Tam, E.M.3    Overall, C.M.4
  • 78
    • 34547910622 scopus 로고    scopus 로고
    • Proteome-wide changes induced by the Hsp90 inhibitor, geldanamycin in anaplastic large cell lymphoma cells
    • Schumacher, J. A., Crockett, D. K., Elenitoba-Johnson, K. S., Lim, M. S., Proteome-wide changes induced by the Hsp90 inhibitor, geldanamycin in anaplastic large cell lymphoma cells. Proteomics 2007, 7, 2603-2616.
    • (2007) Proteomics , vol.7 , pp. 2603-2616
    • Schumacher, J.A.1    Crockett, D.K.2    Elenitoba-Johnson, K.S.3    Lim, M.S.4
  • 79
    • 34147150867 scopus 로고    scopus 로고
    • Gene and protein expression profiling of human ovarian cancer cells treated with the heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin
    • Maloney, A., Clarke, P. A., Naaby-Hansen, S., Stein, R. et al., Gene and protein expression profiling of human ovarian cancer cells treated with the heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin. Cancer Res. 2007, 67, 3239-3253.
    • (2007) Cancer Res , vol.67 , pp. 3239-3253
    • Maloney, A.1    Clarke, P.A.2    Naaby-Hansen, S.3    Stein, R.4
  • 80
    • 33644877241 scopus 로고    scopus 로고
    • Proteomic identification of heat shock protein 90 as a candidate target for p53 mutation reactivation by PRIMA-1 in breast cancer cells
    • Rehman, A., Chahal, M. S., Tang, X., Bruce, J. E. et al., Proteomic identification of heat shock protein 90 as a candidate target for p53 mutation reactivation by PRIMA-1 in breast cancer cells. Breast Cancer Res. 2005, 7, R765-R774.
    • (2005) Breast Cancer Res , vol.7
    • Rehman, A.1    Chahal, M.S.2    Tang, X.3    Bruce, J.E.4
  • 81
    • 20944433868 scopus 로고    scopus 로고
    • Proteomic analysis of mantle-cell lymphoma by protein microarray
    • Ghobrial, I. M., McCormick, D. J., Kaufmann, S. H., Leontovich, A. A. et al., Proteomic analysis of mantle-cell lymphoma by protein microarray. Blood 2005, 105, 3722-3730.
    • (2005) Blood , vol.105 , pp. 3722-3730
    • Ghobrial, I.M.1    McCormick, D.J.2    Kaufmann, S.H.3    Leontovich, A.A.4
  • 82
    • 34248571776 scopus 로고    scopus 로고
    • Proteomic analysis of waldenstrom macroglobulinemia
    • Hatjiharissi, E., Ngo, H., Leontovich, A. A., Leleu, X. et al., Proteomic analysis of waldenstrom macroglobulinemia. Cancer Res. 2007, 67, 3777-3784.
    • (2007) Cancer Res , vol.67 , pp. 3777-3784
    • Hatjiharissi, E.1    Ngo, H.2    Leontovich, A.A.3    Leleu, X.4
  • 83
    • 35748984929 scopus 로고    scopus 로고
    • Proteomic evaluation of pathways associated with dexamethasone-mediated apoptosis and resistance in multiple myeloma
    • Rees-Unwin, K. S., Craven, R. A., Davenport, E., Hanrahan, S. et al., Proteomic evaluation of pathways associated with dexamethasone-mediated apoptosis and resistance in multiple myeloma. Br. J. Haematol. 2007, 139, 559-567.
    • (2007) Br. J. Haematol , vol.139 , pp. 559-567
    • Rees-Unwin, K.S.1    Craven, R.A.2    Davenport, E.3    Hanrahan, S.4
  • 84
    • 36549016590 scopus 로고    scopus 로고
    • Proteome analysis of metastatic colorectal cancer cells recognized by the lectin Helix pomatia agglutinin (HPA)
    • Saint-Guirons, J., Zeqiraj, E., Schumacher, U., Greenwell, P., Dwek, M., Proteome analysis of metastatic colorectal cancer cells recognized by the lectin Helix pomatia agglutinin (HPA). Proteomics 2007, 7, 4082-4089.
    • (2007) Proteomics , vol.7 , pp. 4082-4089
    • Saint-Guirons, J.1    Zeqiraj, E.2    Schumacher, U.3    Greenwell, P.4    Dwek, M.5
  • 85
    • 35648963627 scopus 로고    scopus 로고
    • Proteome analysis of hepatocellular carcinoma by two-dimensional difference gel electrophoresis: Novel protein markers in hepatocellular carcinoma tissues
    • Sun, W., Xing, B., Sun, Y., Du, X. et al., Proteome analysis of hepatocellular carcinoma by two-dimensional difference gel electrophoresis: novel protein markers in hepatocellular carcinoma tissues. Mol. Cell. Proteomics 2007, 6, 1798-1808.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1798-1808
    • Sun, W.1    Xing, B.2    Sun, Y.3    Du, X.4
  • 86
    • 34547229135 scopus 로고    scopus 로고
    • A proteomic approach towards the Hsp90-dependent ubiquitinylated proteome
    • Falsone, S. F., Gesslbauer, B., Rek, A., Kungl, A. J., A proteomic approach towards the Hsp90-dependent ubiquitinylated proteome. Proteomics 2007, 7, 2375-2383.
    • (2007) Proteomics , vol.7 , pp. 2375-2383
    • Falsone, S.F.1    Gesslbauer, B.2    Rek, A.3    Kungl, A.J.4
  • 87
    • 28744447585 scopus 로고    scopus 로고
    • Wilson, P. W., CDC/AHA workshop on markers of inflammation and cardiovascular disease: application to clinical and public health practice: ability of inflammatory markers to predict disease in asymptomatic patients: a background paper. Circulation 2004, 110, e568-e571.
    • Wilson, P. W., CDC/AHA workshop on markers of inflammation and cardiovascular disease: application to clinical and public health practice: ability of inflammatory markers to predict disease in asymptomatic patients: a background paper. Circulation 2004, 110, e568-e571.
  • 88
    • 39749142228 scopus 로고    scopus 로고
    • The search for new cardiovascular biomarkers
    • Gerszten, R. E., Wang, T. J., The search for new cardiovascular biomarkers. Nature 2008, 451, 949-952.
    • (2008) Nature , vol.451 , pp. 949-952
    • Gerszten, R.E.1    Wang, T.J.2
  • 89
    • 33748362201 scopus 로고    scopus 로고
    • Heat-shock proteins and atherosclerosis
    • Wick, G., Heat-shock proteins and atherosclerosis. Circulation 2006, 114, 870-872.
    • (2006) Circulation , vol.114 , pp. 870-872
    • Wick, G.1
  • 90
    • 0042882763 scopus 로고    scopus 로고
    • Infections, heat shock proteins, and atherosclerosis
    • Xu, Q., Infections, heat shock proteins, and atherosclerosis. Curr. Opin. Cardiol. 2003, 18, 245-252.
    • (2003) Curr. Opin. Cardiol , vol.18 , pp. 245-252
    • Xu, Q.1
  • 91
    • 36148995895 scopus 로고    scopus 로고
    • T-cell reactivity against HSP60 relates to early but not advanced atherosclerosis
    • Knoflach, M., Kiechl, S., Mayrl, B., Kind, M. et al., T-cell reactivity against HSP60 relates to early but not advanced atherosclerosis. Atherosclerosis 2007, 195, 333-338.
    • (2007) Atherosclerosis , vol.195 , pp. 333-338
    • Knoflach, M.1    Kiechl, S.2    Mayrl, B.3    Kind, M.4
  • 92
    • 0033903935 scopus 로고    scopus 로고
    • Circulating heat shock protein 60 is associated with early cardiovascular disease
    • Pockley, A. G., Wu, R., Lemne, C., Kiessling, R. et al., Circulating heat shock protein 60 is associated with early cardiovascular disease. Hypertension 2000, 36, 303-307.
    • (2000) Hypertension , vol.36 , pp. 303-307
    • Pockley, A.G.1    Wu, R.2    Lemne, C.3    Kiessling, R.4
  • 93
    • 14244250847 scopus 로고    scopus 로고
    • Myocardial ischaemia and the inflammatory response: Release of heat shock protein 70 after myocardial infarction
    • Dybdahl, B., Slordahl, S. A., Waage, A., Kierulf, P. et al., Myocardial ischaemia and the inflammatory response: release of heat shock protein 70 after myocardial infarction. Heart 2005, 91, 299-304.
    • (2005) Heart , vol.91 , pp. 299-304
    • Dybdahl, B.1    Slordahl, S.A.2    Waage, A.3    Kierulf, P.4
  • 94
    • 0032053546 scopus 로고    scopus 로고
    • Differential expression of heat shock proteins in normal and failing human hearts
    • Knowlton, A. A., Kapadia, S., Torre-Amione, G., Durand, J. B. et al., Differential expression of heat shock proteins in normal and failing human hearts. J. Mol. Cell. Cardiol. 1998, 30, 811-818.
    • (1998) J. Mol. Cell. Cardiol , vol.30 , pp. 811-818
    • Knowlton, A.A.1    Kapadia, S.2    Torre-Amione, G.3    Durand, J.B.4
  • 95
    • 0035570685 scopus 로고    scopus 로고
    • Temporal expression of heat shock proteins 60 and 70 at lesion-prone sites during atherogenesis in ApoE-deficient mice
    • Kanwar, R. K., Kanwar, J. R., Wang, D., Ormrod, D. J., Krissansen, G. W., Temporal expression of heat shock proteins 60 and 70 at lesion-prone sites during atherogenesis in ApoE-deficient mice. Arterioscler Thromb. Vasc. Biol. 2001, 21, 1991-1997.
    • (2001) Arterioscler Thromb. Vasc. Biol , vol.21 , pp. 1991-1997
    • Kanwar, R.K.1    Kanwar, J.R.2    Wang, D.3    Ormrod, D.J.4    Krissansen, G.W.5
  • 96
    • 2342435070 scopus 로고    scopus 로고
    • Neoangiogenesis, T-lymphocyte infiltration, and heat shock protein-60 are biological hallmarks of an immunomediated inflammatory process in end-stage calcified aortic valve stenosis
    • Mazzone, A., Epistolato, M. C., De Caterina, R., Storti, S. et al., Neoangiogenesis, T-lymphocyte infiltration, and heat shock protein-60 are biological hallmarks of an immunomediated inflammatory process in end-stage calcified aortic valve stenosis. J. Am. Coll. Cardiol. 2004, 43, 1670-1676.
    • (2004) J. Am. Coll. Cardiol , vol.43 , pp. 1670-1676
    • Mazzone, A.1    Epistolato, M.C.2    De Caterina, R.3    Storti, S.4
  • 97
    • 0038338586 scopus 로고    scopus 로고
    • Antibody response to chlamydial heat shock protein 60 is strongly associated with acute coronary syndromes
    • Biasucci, L. M., Liuzzo, G., Ciervo, A., Petrucca, A. et al., Antibody response to chlamydial heat shock protein 60 is strongly associated with acute coronary syndromes. Circulation 2003, 107, 3015-3017.
    • (2003) Circulation , vol.107 , pp. 3015-3017
    • Biasucci, L.M.1    Liuzzo, G.2    Ciervo, A.3    Petrucca, A.4
  • 98
    • 4143081494 scopus 로고    scopus 로고
    • Program of cell survival underlying human and experimental hibernating myocardium
    • Depre, C., Kim, S. J., John, A. S., Huang, Y. et al., Program of cell survival underlying human and experimental hibernating myocardium. Circ. Res. 2004, 95, 433-440.
    • (2004) Circ. Res , vol.95 , pp. 433-440
    • Depre, C.1    Kim, S.J.2    John, A.S.3    Huang, Y.4
  • 99
    • 0033967128 scopus 로고    scopus 로고
    • Apoptosis in cardiac diseases: Stress- and mitogen-activated signaling pathways
    • Feuerstein, G. Z., Young, P. R., Apoptosis in cardiac diseases: stress- and mitogen-activated signaling pathways. Cardiovasc. Res. 2000, 45, 560-569.
    • (2000) Cardiovasc. Res , vol.45 , pp. 560-569
    • Feuerstein, G.Z.1    Young, P.R.2
  • 100
    • 34250811600 scopus 로고    scopus 로고
    • Hsp70 may protect cardiomyocytes from stress-induced injury by inhibiting Fas-mediated apoptosis
    • Zhao, Y., Wang, W., Qian, L., Hsp70 may protect cardiomyocytes from stress-induced injury by inhibiting Fas-mediated apoptosis. Cell Stress Chaperones 2007, 12, 83-95.
    • (2007) Cell Stress Chaperones , vol.12 , pp. 83-95
    • Zhao, Y.1    Wang, W.2    Qian, L.3
  • 101
    • 35348854947 scopus 로고    scopus 로고
    • Circulating heat shock proteins and inflammatory markers in patients with idiopathic left ventricular dysfunction: Their relationships with myocardial and microvascular impairment
    • Giannessi, D., Colotti, C., Maltinti, M., Del Ry, S. et al., Circulating heat shock proteins and inflammatory markers in patients with idiopathic left ventricular dysfunction: their relationships with myocardial and microvascular impairment. Cell Stress Chaperones 2007, 12, 265-274.
    • (2007) Cell Stress Chaperones , vol.12 , pp. 265-274
    • Giannessi, D.1    Colotti, C.2    Maltinti, M.3    Del Ry, S.4
  • 102
    • 0344734062 scopus 로고    scopus 로고
    • Identification and characterization of heat shock protein 27 protein species in human myocardial two-dimensional electrophoresis patterns
    • Scheler, C., Muller, E. C., Stahl, J., Muller-Werdan, U. et al., Identification and characterization of heat shock protein 27 protein species in human myocardial two-dimensional electrophoresis patterns. Electrophoresis 1997, 18, 2823-2831.
    • (1997) Electrophoresis , vol.18 , pp. 2823-2831
    • Scheler, C.1    Muller, E.C.2    Stahl, J.3    Muller-Werdan, U.4
  • 103
    • 0031854297 scopus 로고    scopus 로고
    • Protein changes observed in pacing-induced heart failure using two-dimensional electrophoresis
    • Heinke, M. Y., Wheeler, C. H., Chang, D., Einstein, R. et al., Protein changes observed in pacing-induced heart failure using two-dimensional electrophoresis. Electrophoresis 1998, 19, 2021-2030.
    • (1998) Electrophoresis , vol.19 , pp. 2021-2030
    • Heinke, M.Y.1    Wheeler, C.H.2    Chang, D.3    Einstein, R.4
  • 104
    • 0032953661 scopus 로고    scopus 로고
    • Bovine dilated cardiomyopathy: Proteomic analysis of an animal model of human dilated cardiomyopathy
    • Weekes, J., Wheeler, C. H., Yan, J. X., Weil, J. et al., Bovine dilated cardiomyopathy: proteomic analysis of an animal model of human dilated cardiomyopathy. Electrophoresis 1999, 20, 898-906.
    • (1999) Electrophoresis , vol.20 , pp. 898-906
    • Weekes, J.1    Wheeler, C.H.2    Yan, J.X.3    Weil, J.4
  • 106
    • 27844504681 scopus 로고    scopus 로고
    • Proteomic approach to identify changes in protein expression modified by 17beta-oestradiol in bovine vascular smooth muscle cells
    • Molero, L., García-Mendez, A., Alonso-Orgaz, S., Carrasco, C. et al., Proteomic approach to identify changes in protein expression modified by 17beta-oestradiol in bovine vascular smooth muscle cells. Clin. Sci. 2005, 109, 457-463.
    • (2005) Clin. Sci , vol.109 , pp. 457-463
    • Molero, L.1    García-Mendez, A.2    Alonso-Orgaz, S.3    Carrasco, C.4
  • 107
    • 0035570685 scopus 로고    scopus 로고
    • Temporal expression of heat shock proteins 60 and 70 at lesion-prone sites during atherogenesis in ApoE-deficient mice
    • Kanwar, R. K., Kanwar, J. R., Wang, D., Ormrod, D. J., Krissansen, G. W., Temporal expression of heat shock proteins 60 and 70 at lesion-prone sites during atherogenesis in ApoE-deficient mice. Arterioscler. Throm. Vasc. Biol. 1991, 21, 1991-1997.
    • (1991) Arterioscler. Throm. Vasc. Biol , vol.21 , pp. 1991-1997
    • Kanwar, R.K.1    Kanwar, J.R.2    Wang, D.3    Ormrod, D.J.4    Krissansen, G.W.5
  • 108
    • 0142120088 scopus 로고    scopus 로고
    • Chlamydia pneumoniae stimulates proliferation of vascular smooth muscle cells through induction of endogenous heat shock protein 60
    • Hirono, S., Dibrov, E., Hurtado, C., Kostenuk, A. et al., Chlamydia pneumoniae stimulates proliferation of vascular smooth muscle cells through induction of endogenous heat shock protein 60. Circ. Res. 2003, 93, 710-716.
    • (2003) Circ. Res , vol.93 , pp. 710-716
    • Hirono, S.1    Dibrov, E.2    Hurtado, C.3    Kostenuk, A.4
  • 109
    • 8444238954 scopus 로고    scopus 로고
    • immune cross-regulation with the 60-kd heat-shock protein
    • Inhibition of adjuvant-induced arthritis by DNA vaccination with the 70-kd or the 90-kd human heat-shock protein
    • Quintana, F. J., Carmi, P., Mor, F., Cohen, I. R., Inhibition of adjuvant-induced arthritis by DNA vaccination with the 70-kd or the 90-kd human heat-shock protein: immune cross-regulation with the 60-kd heat-shock protein. Arthritis Rheum. 2004, 50, 3712-3720.
    • (2004) Arthritis Rheum , vol.50 , pp. 3712-3720
    • Quintana, F.J.1    Carmi, P.2    Mor, F.3    Cohen, I.R.4
  • 110
    • 17044438302 scopus 로고    scopus 로고
    • Heat shock proteins and other components of cellular machinery for protein synthesis are up-regulated in vascular endothelial cell growth factor-activated human endothelial cells
    • Pawlowska, Z., Baranska, P., Jerczynska, H., Koziolkiewicz, W., Cierniewski, C. S., Heat shock proteins and other components of cellular machinery for protein synthesis are up-regulated in vascular endothelial cell growth factor-activated human endothelial cells. Proteomics 2005, 5, 1217-1227.
    • (2005) Proteomics , vol.5 , pp. 1217-1227
    • Pawlowska, Z.1    Baranska, P.2    Jerczynska, H.3    Koziolkiewicz, W.4    Cierniewski, C.S.5
  • 111
    • 20944446903 scopus 로고    scopus 로고
    • The proteome and secretome of human arterial smooth muscle cells
    • Dupont, A., Corseaux, D., Dekeyzer, O., Drobecq, H. et al., The proteome and secretome of human arterial smooth muscle cells. Proteomics 2005, 5, 585-596.
    • (2005) Proteomics , vol.5 , pp. 585-596
    • Dupont, A.1    Corseaux, D.2    Dekeyzer, O.3    Drobecq, H.4
  • 112
    • 10744232300 scopus 로고    scopus 로고
    • Interaction of antibodies against cytomegalovirus with heat-shock protein 60 in pathogenesis of atherosclerosis
    • Bason, C., Corrocher, R., Lunardi, C., Puccetti, P. et al., Interaction of antibodies against cytomegalovirus with heat-shock protein 60 in pathogenesis of atherosclerosis. Lancet 2003, 362, 1971-1977.
    • (2003) Lancet , vol.362 , pp. 1971-1977
    • Bason, C.1    Corrocher, R.2    Lunardi, C.3    Puccetti, P.4
  • 113
    • 0029854465 scopus 로고    scopus 로고
    • Identification of human myocardial proteins separated by two-dimensional electrophoresis using an effective sample preparation for mass spectrometry
    • Otto, A., Thiede, B., Müller, E. C., Scheler, C. et al., Identification of human myocardial proteins separated by two-dimensional electrophoresis using an effective sample preparation for mass spectrometry. Electrophoresis 1996, 17, 1643-1650.
    • (1996) Electrophoresis , vol.17 , pp. 1643-1650
    • Otto, A.1    Thiede, B.2    Müller, E.C.3    Scheler, C.4
  • 114
    • 0029997223 scopus 로고    scopus 로고
    • Identification of human myocardial proteins separated by two-dimensional electrophoresis with matrix-assisted laser desorption/ionization mass spectrometry
    • Thiede, B., Otto, A., Zimny-Arndt, U., Müller, E. C., Jungblut, P., Identification of human myocardial proteins separated by two-dimensional electrophoresis with matrix-assisted laser desorption/ionization mass spectrometry. Electrophoresis 1996, 17, 588-599.
    • (1996) Electrophoresis , vol.17 , pp. 588-599
    • Thiede, B.1    Otto, A.2    Zimny-Arndt, U.3    Müller, E.C.4    Jungblut, P.5
  • 115
    • 0031458894 scopus 로고    scopus 로고
    • HSC-2D PAGE and the two dimensional gel electrophoresis database of dog heart proteins
    • Dunn, M. J., Corbett, J. M., Wheeler, C. H., HSC-2D PAGE and the two dimensional gel electrophoresis database of dog heart proteins. Electrophoresis 1997, 18, 2795-2802.
    • (1997) Electrophoresis , vol.18 , pp. 2795-2802
    • Dunn, M.J.1    Corbett, J.M.2    Wheeler, C.H.3
  • 116
    • 0030905110 scopus 로고    scopus 로고
    • Construction of HSC-2D PAGE: A two-dimensional gel electrophoresis database of heart proteins
    • Evans, G., Wheeler, C. H., Corbett, J. M., Dunn, M. J., Construction of HSC-2D PAGE: a two-dimensional gel electrophoresis database of heart proteins. Electrophoresis 1997, 18, 471-479.
    • (1997) Electrophoresis , vol.18 , pp. 471-479
    • Evans, G.1    Wheeler, C.H.2    Corbett, J.M.3    Dunn, M.J.4
  • 117
    • 0028318350 scopus 로고
    • Protein composition of the human heart: The construction of a myocardial two-dimensional electrophoresis database
    • Jungblut, P., Otto, A., Zeindl-Eberhart, E., Plessner, K. P. et al., Protein composition of the human heart: the construction of a myocardial two-dimensional electrophoresis database. Electrophoresis 1994, 15, 685-707.
    • (1994) Electrophoresis , vol.15 , pp. 685-707
    • Jungblut, P.1    Otto, A.2    Zeindl-Eberhart, E.3    Plessner, K.P.4
  • 118
    • 39649123510 scopus 로고    scopus 로고
    • Clinical application of proteomics approaches in vascular diseases
    • Wang, X. L., Fu, A., Spiro, C., Lee, H. C., Clinical application of proteomics approaches in vascular diseases. Proteomics Clin. Appl. 2008, 2, 238-250.
    • (2008) Proteomics Clin. Appl , vol.2 , pp. 238-250
    • Wang, X.L.1    Fu, A.2    Spiro, C.3    Lee, H.C.4
  • 119
    • 39649090972 scopus 로고    scopus 로고
    • Modulation of cancer cell line differentiation. A neglected proteomic analysis with potential implications in pathophysiology, diagnosis, prognosis and therapy of cancer
    • Scatena, R., Bottoni, P., Giardina, B., Modulation of cancer cell line differentiation. A neglected proteomic analysis with potential implications in pathophysiology, diagnosis, prognosis and therapy of cancer. Proteomics Clin. Appl. 2008, 2, 229-237.
    • (2008) Proteomics Clin. Appl , vol.2 , pp. 229-237
    • Scatena, R.1    Bottoni, P.2    Giardina, B.3
  • 120
    • 23944449609 scopus 로고    scopus 로고
    • Cardiovascular-related proteins identified in human plasma by the HUPO Plasma Proteome Project Pilot Phase
    • Berhane, B. T., Zong, C., Liem, D. A., Huang, A. et al., Cardiovascular-related proteins identified in human plasma by the HUPO Plasma Proteome Project Pilot Phase. Proteomics 2005, 5, 3520-3530.
    • (2005) Proteomics , vol.5 , pp. 3520-3530
    • Berhane, B.T.1    Zong, C.2    Liem, D.A.3    Huang, A.4
  • 121
    • 20844438189 scopus 로고    scopus 로고
    • Identification by a differential proteomic approach of heat shock protein 27 as a potential marker of atherosclerosis
    • Martin-Ventura, J. L., Duran, M. C., Blanco-Colio, L. M., Meilhac, O. et al., Identification by a differential proteomic approach of heat shock protein 27 as a potential marker of atherosclerosis. Circulation 2004, 110, 2216-2219.
    • (2004) Circulation , vol.110 , pp. 2216-2219
    • Martin-Ventura, J.L.1    Duran, M.C.2    Blanco-Colio, L.M.3    Meilhac, O.4
  • 122
    • 33748372961 scopus 로고    scopus 로고
    • Expression of heat shock protein 27 in human atherosclerotic plaques and increased plasma level of heat shock protein 27 in patients with acute coronary syndrome
    • Park, H. K., Park, E. C., Bae, S. W., Park, M. Y. et al., Expression of heat shock protein 27 in human atherosclerotic plaques and increased plasma level of heat shock protein 27 in patients with acute coronary syndrome. Circulation 2006, 114, 886-893.
    • (2006) Circulation , vol.114 , pp. 886-893
    • Park, H.K.1    Park, E.C.2    Bae, S.W.3    Park, M.Y.4
  • 123
    • 22744445856 scopus 로고    scopus 로고
    • Heat shock protein 27 is associated with freedom from graft vasculopathy after human cardiac transplantation
    • De Souza, A. I., Wait, R., Mitchell, A. G., Banner, N. R. et al., Heat shock protein 27 is associated with freedom from graft vasculopathy after human cardiac transplantation. Circ. Res. 2005, 97, 192-198.
    • (2005) Circ. Res , vol.97 , pp. 192-198
    • De Souza, A.I.1    Wait, R.2    Mitchell, A.G.3    Banner, N.R.4
  • 124
    • 0034614624 scopus 로고    scopus 로고
    • Purification and identification of secreted oxidative stress-induced factors from vascular smooth muscle cells
    • Liao, D. F., Jin, Z. G., Baas, A. S., Daum, G. et al., Purification and identification of secreted oxidative stress-induced factors from vascular smooth muscle cells. J. Biol. Chem. 2000, 275, 189-196.
    • (2000) J. Biol. Chem , vol.275 , pp. 189-196
    • Liao, D.F.1    Jin, Z.G.2    Baas, A.S.3    Daum, G.4
  • 126
    • 0030069517 scopus 로고    scopus 로고
    • HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress
    • Huot, J., Houle, F., Spitz, D. R., Landry, J., HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Cancer Res. 1996, 56, 273-279.
    • (1996) Cancer Res , vol.56 , pp. 273-279
    • Huot, J.1    Houle, F.2    Spitz, D.R.3    Landry, J.4
  • 127
    • 38749121717 scopus 로고    scopus 로고
    • Plasma concentration of heat shock protein 27 and risk of cardiovascular disease: A prospective, nested case-control study
    • Kardys, I., Rifai, N., Meilhac, O., Michel, J. B. et al., Plasma concentration of heat shock protein 27 and risk of cardiovascular disease: a prospective, nested case-control study. Clin. Chem. 2008, 54, 139-146.
    • (2008) Clin. Chem , vol.54 , pp. 139-146
    • Kardys, I.1    Rifai, N.2    Meilhac, O.3    Michel, J.B.4
  • 128
    • 0032502928 scopus 로고    scopus 로고
    • An integrated approach to proteome analysis: Identification of proteins associated with cardiac hypertrophy
    • Arnott, D., O'Connell, K. L., King, K. L., Stults, J. T., An integrated approach to proteome analysis: identification of proteins associated with cardiac hypertrophy. Anal. Biochem. 1998, 258, 1-18.
    • (1998) Anal. Biochem , vol.258 , pp. 1-18
    • Arnott, D.1    O'Connell, K.L.2    King, K.L.3    Stults, J.T.4
  • 129
    • 22044445138 scopus 로고    scopus 로고
    • Proteomic changes in the pressure overloaded right ventricle after 6 weeks in young rats: Correlations with the degree of hypertrophy
    • Faber,M. J., Dalinghaus,M., Lankhuizen, I.M., Bezstarosti, K. et al., Proteomic changes in the pressure overloaded right ventricle after 6 weeks in young rats: correlations with the degree of hypertrophy. Proteomics 2005, 5, 2519-2530.
    • (2005) Proteomics , vol.5 , pp. 2519-2530
    • Faber, M.J.1    Dalinghaus, M.2    Lankhuizen, I.M.3    Bezstarosti, K.4
  • 130
    • 2642566768 scopus 로고    scopus 로고
    • F-actin capping (CapZ) and other contractile saphenous vein smooth muscle proteins are altered by hemodynamic stress: A proteonomic approach
    • McGregor, E., Kempster, L., Wait, R., Gosling, M. et al., F-actin capping (CapZ) and other contractile saphenous vein smooth muscle proteins are altered by hemodynamic stress: a proteonomic approach. Mol. Cell. Proteomics 2004, 3, 115-124.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 115-124
    • McGregor, E.1    Kempster, L.2    Wait, R.3    Gosling, M.4
  • 131
    • 36448983582 scopus 로고    scopus 로고
    • Proteomic alterations in heat shock protein 27 and identification of phosphoproteins in ascending aortic aneurysm associated with bicuspid and tricuspid aortic valve
    • Matt, P., Fu, Z., Carrel, T., Huso, D. L. et al., Proteomic alterations in heat shock protein 27 and identification of phosphoproteins in ascending aortic aneurysm associated with bicuspid and tricuspid aortic valve. J. Mol. Cell. Cardiol. 2007, 43, 792-801.
    • (2007) J. Mol. Cell. Cardiol , vol.43 , pp. 792-801
    • Matt, P.1    Fu, Z.2    Carrel, T.3    Huso, D.L.4
  • 132
    • 34548175708 scopus 로고    scopus 로고
    • Cochaperone FKBP38 promotes HERG trafficking
    • Walker, V. E., Atanasiu, R., Lam, H., Shrier, A., Cochaperone FKBP38 promotes HERG trafficking. J. Biol. Chem. 2007, 282, 23509-23516.
    • (2007) J. Biol. Chem , vol.282 , pp. 23509-23516
    • Walker, V.E.1    Atanasiu, R.2    Lam, H.3    Shrier, A.4
  • 133
    • 27144463441 scopus 로고    scopus 로고
    • Extracellular heat shock protein 70: A critical component for motoneuron survival
    • Robinson, M. B., Tidwell, J. L., Gould, T., Taylor, A. R. et al., Extracellular heat shock protein 70: a critical component for motoneuron survival. J. Neurosci. 2005, 25, 9735-9745.
    • (2005) J. Neurosci , vol.25 , pp. 9735-9745
    • Robinson, M.B.1    Tidwell, J.L.2    Gould, T.3    Taylor, A.R.4
  • 134
    • 24944495594 scopus 로고    scopus 로고
    • Induction of heat shock proteins in B-cell exosomes
    • Clayton, A., Turkes, A., Navabi, H., Mason, M. D., Tabi, Z., Induction of heat shock proteins in B-cell exosomes. J. Cell Sci. 2005, 118, 3631-3638.
    • (2005) J. Cell Sci , vol.118 , pp. 3631-3638
    • Clayton, A.1    Turkes, A.2    Navabi, H.3    Mason, M.D.4    Tabi, Z.5
  • 135
    • 33745164580 scopus 로고    scopus 로고
    • Heat shock proteins form part of a danger signal cascade in response to lipopolysaccharide and GroEL
    • Davies, E. L., Bacelar, M. M., Marshall, M. J., Johnson, E. et al., Heat shock proteins form part of a danger signal cascade in response to lipopolysaccharide and GroEL. Clin. Exp. Immunol. 2006, 145, 183-189.
    • (2006) Clin. Exp. Immunol , vol.145 , pp. 183-189
    • Davies, E.L.1    Bacelar, M.M.2    Marshall, M.J.3    Johnson, E.4
  • 136
    • 0024541931 scopus 로고
    • Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins
    • Hightower, L. E., Guidon, P. T., Jr., Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins. J. Cell. Physiol. 1989, 138, 257-266.
    • (1989) J. Cell. Physiol , vol.138 , pp. 257-266
    • Hightower, L.E.1    Guidon Jr., P.T.2
  • 137
    • 0034713677 scopus 로고    scopus 로고
    • Stress proteins and the immune response
    • Moseley, P., Stress proteins and the immune response. Immunopharmacology 2000, 48, 299-302.
    • (2000) Immunopharmacology , vol.48 , pp. 299-302
    • Moseley, P.1
  • 138
    • 34848885422 scopus 로고    scopus 로고
    • Molecular and cellular requirements for enhanced antigen cross-presentation to CD8 cytotoxic T lymphocytes
    • Oizumi, S., Strbo, N., Pahwa, S., Deyev, V., Podack, E. R., Molecular and cellular requirements for enhanced antigen cross-presentation to CD8 cytotoxic T lymphocytes. J. Immunol. 2007, 179, 2310-2317.
    • (2007) J. Immunol , vol.179 , pp. 2310-2317
    • Oizumi, S.1    Strbo, N.2    Pahwa, S.3    Deyev, V.4    Podack, E.R.5
  • 139
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • Ferrarini, M., Heltai, S., Zocchi, M. R., Rugarli, C., Unusual expression and localization of heat-shock proteins in human tumor cells. Int. J. Cancer 1992, 51, 613-619.
    • (1992) Int. J. Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 140
    • 0032033123 scopus 로고    scopus 로고
    • Cell surface expression of 70 kDa heat shock protein in human oral dysplasia and squamous cell carcinoma: Correlation with clinicopathological features
    • Kaur, J., Das, S. N., Srivastava, A., Ralhan, R., Cell surface expression of 70 kDa heat shock protein in human oral dysplasia and squamous cell carcinoma: correlation with clinicopathological features. Oral Oncol. 1998, 34, 93-98.
    • (1998) Oral Oncol , vol.34 , pp. 93-98
    • Kaur, J.1    Das, S.N.2    Srivastava, A.3    Ralhan, R.4
  • 141
    • 0031052152 scopus 로고    scopus 로고
    • Heat shock protein 72 (HSP72), a hyperthermia inducible immunogenic determinant on leukemic K562 and Ewing's sarcoma cells
    • Multhoff, G., Heat shock protein 72 (HSP72), a hyperthermia inducible immunogenic determinant on leukemic K562 and Ewing's sarcoma cells. Int. J. Hyperthermia 1997, 13, 39-48.
    • (1997) Int. J. Hyperthermia , vol.13 , pp. 39-48
    • Multhoff, G.1
  • 142
    • 0031755079 scopus 로고    scopus 로고
    • Heat shock protein (HSP72) surface expression enhances the lysis of a human renal cell carcinoma by IL-2 stimulated NK cells
    • Roigas, J., Wallen, E. S., Loening, S. A., Moseley, P. L., Heat shock protein (HSP72) surface expression enhances the lysis of a human renal cell carcinoma by IL-2 stimulated NK cells. Adv. Exp. Med. Biol. 1998, 451, 225-229.
    • (1998) Adv. Exp. Med. Biol , vol.451 , pp. 225-229
    • Roigas, J.1    Wallen, E.S.2    Loening, S.A.3    Moseley, P.L.4
  • 143
    • 0029417040 scopus 로고
    • Interleukin-1 beta induces the expression of hsp70, heme oxygenase and Mn-SOD in FACS-purified rat islet beta-cells, but not in alpha-cells
    • Strandell, E., Buschard, K., Saldeen, J., Welsh, N., Interleukin-1 beta induces the expression of hsp70, heme oxygenase and Mn-SOD in FACS-purified rat islet beta-cells, but not in alpha-cells. Immunol. Lett. 1995, 48, 145-148.
    • (1995) Immunol. Lett , vol.48 , pp. 145-148
    • Strandell, E.1    Buschard, K.2    Saldeen, J.3    Welsh, N.4
  • 144
    • 0026573448 scopus 로고
    • Two monoclonal antibodies generated against human hsp60 show reactivity with synovial membranes of patients with juvenile chronic arthritis
    • Boog, C. J., de Graeff-Meeder, E. R., Lucassen, M. A., van der Zee, R. et al., Two monoclonal antibodies generated against human hsp60 show reactivity with synovial membranes of patients with juvenile chronic arthritis. J. Exp. Med. 1992, 175, 1805-1810.
    • (1992) J. Exp. Med , vol.175 , pp. 1805-1810
    • Boog, C.J.1    de Graeff-Meeder, E.R.2    Lucassen, M.A.3    van der Zee, R.4
  • 145
    • 0026322837 scopus 로고
    • Vaccination against autoimmune mouse diabetes with a T-cell epitope of the human 65-kDa heat shock protein
    • Elias, D., Reshef, T., Birk, O. S., van der Zee, R., Walker, M. D., Cohen, I. R., Vaccination against autoimmune mouse diabetes with a T-cell epitope of the human 65-kDa heat shock protein. Proc. Natl. Acad. Sci. USA 1991, 88, 3088-3091.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3088-3091
    • Elias, D.1    Reshef, T.2    Birk, O.S.3    van der Zee, R.4    Walker, M.D.5    Cohen, I.R.6
  • 146
    • 0033106415 scopus 로고    scopus 로고
    • T cell proliferative responses of type 1 diabetes patients and healthy individuals to human hsp60 and its peptides
    • Abulafia-Lapid, R., Elias, D., Raz, I., Keren-Zur, Y. et al., T cell proliferative responses of type 1 diabetes patients and healthy individuals to human hsp60 and its peptides. J. Autoimmun. 1999, 12, 121-129.
    • (1999) J. Autoimmun , vol.12 , pp. 121-129
    • Abulafia-Lapid, R.1    Elias, D.2    Raz, I.3    Keren-Zur, Y.4
  • 147
    • 43349090939 scopus 로고    scopus 로고
    • Immunological efficacy of heat shock protein 60 peptide DiaPep277 therapy in clinical type I diabetes
    • Huurman, V. A., van der Meide, P. E., Duinkerken, G., Willemen, S. et al., Immunological efficacy of heat shock protein 60 peptide DiaPep277 therapy in clinical type I diabetes. Clin. Exp. Immunol. 2008, 152, 488-497.
    • (2008) Clin. Exp. Immunol , vol.152 , pp. 488-497
    • Huurman, V.A.1    van der Meide, P.E.2    Duinkerken, G.3    Willemen, S.4
  • 148
    • 50249094538 scopus 로고    scopus 로고
    • a quantitative proteomics approach
    • The identification of potential factors associated with the development of type 2 diabetes
    • Lu, H., Yang, Y., Allister, E. M., Wijesekara, N., Wheeler, M. B., The identification of potential factors associated with the development of type 2 diabetes: a quantitative proteomics approach. Mol. Cell. Proteomics 2008, 7, 1434-1451.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1434-1451
    • Lu, H.1    Yang, Y.2    Allister, E.M.3    Wijesekara, N.4    Wheeler, M.B.5
  • 149
    • 33847677975 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress contributes to beta cell apoptosis in type 2 diabetes
    • Laybutt, D. R., Preston, A. M., Akerfeldt, M. C., Kench, J. G. et al., Endoplasmic reticulum stress contributes to beta cell apoptosis in type 2 diabetes. Diabetologia 2007, 50, 752-763.
    • (2007) Diabetologia , vol.50 , pp. 752-763
    • Laybutt, D.R.1    Preston, A.M.2    Akerfeldt, M.C.3    Kench, J.G.4
  • 150
    • 43449114799 scopus 로고    scopus 로고
    • Back-regulation of six oxidative stress proteins with grape seed proanthocyanidin extracts in rat diabetic nephropathy
    • Li, B. Y., Cheng, M., Gao, H. Q., Ma, Y. B. et al., Back-regulation of six oxidative stress proteins with grape seed proanthocyanidin extracts in rat diabetic nephropathy. J. Cell. Biochem. 2008, 104, 668-679.
    • (2008) J. Cell. Biochem , vol.104 , pp. 668-679
    • Li, B.Y.1    Cheng, M.2    Gao, H.Q.3    Ma, Y.B.4
  • 151
    • 16844382825 scopus 로고    scopus 로고
    • Glucose-induced changes of multiple mouse islet proteins analysed by two-dimensional gel electrophoresis and mass spectrometry
    • Ahmed, M., Bergsten, P., Glucose-induced changes of multiple mouse islet proteins analysed by two-dimensional gel electrophoresis and mass spectrometry. Diabetologia 2005, 48, 477-485.
    • (2005) Diabetologia , vol.48 , pp. 477-485
    • Ahmed, M.1    Bergsten, P.2
  • 152
    • 38349025873 scopus 로고    scopus 로고
    • new insights into the pathways involved
    • Proteomics analysis of cytokine-induced dysfunction and death in insulin-producing INS-1E cells
    • D'Hertog, W., Overbergh, L., Lage, K., Ferreira, G. B. et al., Proteomics analysis of cytokine-induced dysfunction and death in insulin-producing INS-1E cells: new insights into the pathways involved. Mol. Cell. Proteomics 2007, 6, 2180-2199.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2180-2199
    • D'Hertog, W.1    Overbergh, L.2    Lage, K.3    Ferreira, G.B.4
  • 153
    • 34247170807 scopus 로고    scopus 로고
    • Interleukin-1-receptor antagonist in type 2 diabetes mellitus
    • Larsen, C. M., Faulenbach, M., Vaag, A., Volund, A. et al., Interleukin-1-receptor antagonist in type 2 diabetes mellitus. N. Engl. J. Med. 2007, 356, 1517-1526.
    • (2007) N. Engl. J. Med , vol.356 , pp. 1517-1526
    • Larsen, C.M.1    Faulenbach, M.2    Vaag, A.3    Volund, A.4
  • 155
    • 10444279155 scopus 로고    scopus 로고
    • Identification of a new autoantibody in patients with chronic hepatitis
    • Fukuda, Y., Yotsuyanagi, H., Ooka, S., Sekine, T. et al., Identification of a new autoantibody in patients with chronic hepatitis. Hum. Immunol. 2004, 65, 1530-1538.
    • (2004) Hum. Immunol , vol.65 , pp. 1530-1538
    • Fukuda, Y.1    Yotsuyanagi, H.2    Ooka, S.3    Sekine, T.4
  • 156
    • 0029057031 scopus 로고
    • Auto-antibody against 70 kD heat shock protein in patients with autoimmune liver diseases
    • Shingai, R., Maeda, T., Onishi, S., Yamamoto, Y., Auto-antibody against 70 kD heat shock protein in patients with autoimmune liver diseases. J. Hepatol. 1995, 23, 382-390.
    • (1995) J. Hepatol , vol.23 , pp. 382-390
    • Shingai, R.1    Maeda, T.2    Onishi, S.3    Yamamoto, Y.4
  • 157
    • 40949149443 scopus 로고    scopus 로고
    • Identification of plasma membrane autoantigens in autoimmune hepatitis type 1 using a proteomics tool
    • Tahiri, F., Le Naour, F., Huguet, S., Lai-Kuen, R. et al., Identification of plasma membrane autoantigens in autoimmune hepatitis type 1 using a proteomics tool. Hepatology 2008, 47, 937-948.
    • (2008) Hepatology , vol.47 , pp. 937-948
    • Tahiri, F.1    Le Naour, F.2    Huguet, S.3    Lai-Kuen, R.4
  • 158
    • 0033571116 scopus 로고    scopus 로고
    • Activation of T cells recognizing an epitope of heat-shock protein 70 can protect against rat adjuvant arthritis
    • Tanaka, S., Kimura, Y., Mitani, A., Yamamoto, G. et al., Activation of T cells recognizing an epitope of heat-shock protein 70 can protect against rat adjuvant arthritis. J. Immunol. 1999, 163, 5560-5565.
    • (1999) J. Immunol , vol.163 , pp. 5560-5565
    • Tanaka, S.1    Kimura, Y.2    Mitani, A.3    Yamamoto, G.4
  • 159
    • 0034163391 scopus 로고    scopus 로고
    • A conserved mycobacterial heat shock protein (hsp) 70 sequence prevents adjuvant arthritis upon nasal administration and induces IL-10-producing T cells that cross-react with the mammalian self-hsp70 homologue
    • Wendling, U., Paul, L., van der Zee, R., Prakken, B. et al., A conserved mycobacterial heat shock protein (hsp) 70 sequence prevents adjuvant arthritis upon nasal administration and induces IL-10-producing T cells that cross-react with the mammalian self-hsp70 homologue. J. Immunol. 2000, 164, 2711-2717.
    • (2000) J. Immunol , vol.164 , pp. 2711-2717
    • Wendling, U.1    Paul, L.2    van der Zee, R.3    Prakken, B.4
  • 160
    • 8444238954 scopus 로고    scopus 로고
    • immune cross-regulation with the 60-kd heat-shock protein
    • Inhibition of adjuvant-induced arthritis by DNA vaccination with the 70-kd or the 90-kd human heat-shock protein
    • Quintana, F. J., Carmi, P., Mor, F., Cohen, I. R., Inhibition of adjuvant-induced arthritis by DNA vaccination with the 70-kd or the 90-kd human heat-shock protein: immune cross-regulation with the 60-kd heat-shock protein. Arthritis Rheum. 2004, 50, 3712-3720.
    • (2004) Arthritis Rheum , vol.50 , pp. 3712-3720
    • Quintana, F.J.1    Carmi, P.2    Mor, F.3    Cohen, I.R.4
  • 161
    • 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, 318-330.
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 318-330
    • van Eden, W.1    van der Zee, R.2    Prakken, B.3
  • 162
    • 8744313771 scopus 로고    scopus 로고
    • Restoration of heat shock protein70 suppresses gastric mucosal inducible nitric oxide synthase expression induced by Helicobacter pylori
    • Yeo, M., Park, H. K., Kim, D. K., Cho, S. W. et al., Restoration of heat shock protein70 suppresses gastric mucosal inducible nitric oxide synthase expression induced by Helicobacter pylori. Proteomics 2004, 4, 3335-3342.
    • (2004) Proteomics , vol.4 , pp. 3335-3342
    • Yeo, M.1    Park, H.K.2    Kim, D.K.3    Cho, S.W.4
  • 164
    • 33646237341 scopus 로고    scopus 로고
    • Proteomics-driven progress in neurodegeneration research
    • Fountoulakis, M., Kossida, S., Proteomics-driven progress in neurodegeneration research. Electrophoresis 2006, 27, 1556-1573.
    • (2006) Electrophoresis , vol.27 , pp. 1556-1573
    • Fountoulakis, M.1    Kossida, S.2
  • 165
    • 0037299969 scopus 로고    scopus 로고
    • Stress proteins in neural cells: Functional roles in health and disease
    • Richter-Landsberg, C., Goldbaum, O., Stress proteins in neural cells: functional roles in health and disease. Cell. Mol. Life Sci. 2003, 60, 337-349.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 337-349
    • Richter-Landsberg, C.1    Goldbaum, O.2
  • 166
    • 13844321711 scopus 로고    scopus 로고
    • Great mood in proteomics: Beijing and the HUPO Human Brain Proteome Project
    • Hamacher, M., Meyer, H. E., Great mood in proteomics: Beijing and the HUPO Human Brain Proteome Project. Proteomics 2005, 5, 334-336.
    • (2005) Proteomics , vol.5 , pp. 334-336
    • Hamacher, M.1    Meyer, H.E.2
  • 167
    • 34248197864 scopus 로고    scopus 로고
    • Heat shock responses for understanding diseases of protein denaturation
    • Kim, H. J., Hwang, N. R., Lee, K. J., Heat shock responses for understanding diseases of protein denaturation. Mol. Cells 2007, 23, 123-131.
    • (2007) Mol. Cells , vol.23 , pp. 123-131
    • Kim, H.J.1    Hwang, N.R.2    Lee, K.J.3
  • 169
    • 38149110518 scopus 로고    scopus 로고
    • Suppression of in vivo beta-amyloid peptide toxicity by overexpression of the HSP-16.2 small chaperone protein
    • Fonte, V., Kipp, D. R., Yerg III. J., Merin, D. et al., Suppression of in vivo beta-amyloid peptide toxicity by overexpression of the HSP-16.2 small chaperone protein. J. Biol. Chem. 2008, 283, 784-791.
    • (2008) J. Biol. Chem , vol.283 , pp. 784-791
    • Fonte, V.1    Kipp, D.R.2    Yerg III, J.3    Merin, D.4
  • 170
    • 0036551332 scopus 로고    scopus 로고
    • Microglial activation and amyloid-beta clearance induced by exogenous heat-shock proteins
    • Kakimura, J., Kitamura, Y., Takata, K., Umeki, M. et al., Microglial activation and amyloid-beta clearance induced by exogenous heat-shock proteins. FASEB J. 2002, 16, 601-603.
    • (2002) FASEB J , vol.16 , pp. 601-603
    • Kakimura, J.1    Kitamura, Y.2    Takata, K.3    Umeki, M.4
  • 171
    • 34547127902 scopus 로고    scopus 로고
    • PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1
    • Pridgeon, J. W., Olzmann, J. A., Chin, L. S., Li, L., PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol. 2007, 5, e172.
    • (2007) PLoS Biol , vol.5
    • Pridgeon, J.W.1    Olzmann, J.A.2    Chin, L.S.3    Li, L.4
  • 172
    • 55249125950 scopus 로고    scopus 로고
    • Proteome response to the panneural expression of human wild-type alpha-synuclein: A Drosophila model of Parkinson's disease
    • Xun, Z., Kaufman, T. C., Clemmer, D. E., Proteome response to the panneural expression of human wild-type alpha-synuclein: a Drosophila model of Parkinson's disease. J. Proteome Res. 2008, 7, 3911-3921.
    • (2008) J. Proteome Res , vol.7 , pp. 3911-3921
    • Xun, Z.1    Kaufman, T.C.2    Clemmer, D.E.3
  • 173
    • 33646873952 scopus 로고    scopus 로고
    • Protective role of heat shock and heat shock protein 70 in lactacystin-induced cell death both in the rat substantia nigra and PC12 cells
    • Ahn, T. B., Jeon, B. S., Protective role of heat shock and heat shock protein 70 in lactacystin-induced cell death both in the rat substantia nigra and PC12 cells. Brain Res. 2006, 1087, 159-167.
    • (2006) Brain Res , vol.1087 , pp. 159-167
    • Ahn, T.B.1    Jeon, B.S.2
  • 174
    • 28844451001 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
    • Shen, H. Y., He, J. C., Wang, Y., Huang, Q. Y., Chen, J. F., Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice. J. Biol. Chem. 2005, 280, 39962-39969.
    • (2005) J. Biol. Chem , vol.280 , pp. 39962-39969
    • Shen, H.Y.1    He, J.C.2    Wang, Y.3    Huang, Q.Y.4    Chen, J.F.5
  • 175
    • 2442453433 scopus 로고    scopus 로고
    • Effects of divalent metal ions on the alphaB-crystallin chaperone-like activity: Spectroscopic evidence for a complex between copper(II) and protein
    • Ganadu, M. L., Aru, M., Mura, G. M., Coi, A. et al., Effects of divalent metal ions on the alphaB-crystallin chaperone-like activity: spectroscopic evidence for a complex between copper(II) and protein. J. Inorg. Biochem. 2004, 98, 1103-1109.
    • (2004) J. Inorg. Biochem , vol.98 , pp. 1103-1109
    • Ganadu, M.L.1    Aru, M.2    Mura, G.M.3    Coi, A.4
  • 176
    • 44449179474 scopus 로고    scopus 로고
    • Chaperone-dependent amyloid assembly protects cells from prion toxicity
    • Douglas, P. M., Treusch, S., Ren, H. Y., Halfmann, R. et al., Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proc. Natl. Acad. Sci. USA 2008, 105, 7206-7211.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7206-7211
    • Douglas, P.M.1    Treusch, S.2    Ren, H.Y.3    Halfmann, R.4
  • 177
    • 33845979139 scopus 로고    scopus 로고
    • Prion infection-impaired functional blocks identified by proteomics enlighten the targets and the curing pathways of an anti-prion drug
    • Chich, J. F., Schaeffer, B., Bouin, A. P., Mouthon, F. et al., Prion infection-impaired functional blocks identified by proteomics enlighten the targets and the curing pathways of an anti-prion drug. Biochim. Biophys. Acta 2007, 1774, 154-167.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 154-167
    • Chich, J.F.1    Schaeffer, B.2    Bouin, A.P.3    Mouthon, F.4
  • 178
    • 44649175712 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: Protein chaperone dysfunction revealed by proteomic studies of animal models
    • Jain, M. R., Ge, W. W., Elkabes, S., Li, H., Amyotrophic lateral sclerosis: protein chaperone dysfunction revealed by proteomic studies of animal models. Proteomics Clin. Appl. 2008, 2, 670-684.
    • (2008) Proteomics Clin. Appl , vol.2 , pp. 670-684
    • Jain, M.R.1    Ge, W.W.2    Elkabes, S.3    Li, H.4
  • 180
    • 34547893834 scopus 로고    scopus 로고
    • Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: Clues to a possible strategy for treating ALS
    • Yamashita, H., Kawamata, J., Okawa, K., Kanki, R. et al., Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS. J. Neurochem. 2007, 102, 1497-1505.
    • (2007) J. Neurochem , vol.102 , pp. 1497-1505
    • Yamashita, H.1    Kawamata, J.2    Okawa, K.3    Kanki, R.4
  • 181
    • 34249679116 scopus 로고    scopus 로고
    • p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis
    • Gal, J., Strom, A. L., Kilt, R., Zhang, F., Zhu, H., p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis. J. Biol. Chem. 2007, 282, 11068-11077.
    • (2007) J. Biol. Chem , vol.282 , pp. 11068-11077
    • Gal, J.1    Strom, A.L.2    Kilt, R.3    Zhang, F.4    Zhu, H.5
  • 182
    • 0035918258 scopus 로고    scopus 로고
    • Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis
    • Shinder, G. A., Lacourse, M. C., Minotti, S., Durham, H. D., Mutant Cu/ Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis. J. Biol. Chem. 2001, 276, 12791-12796.
    • (2001) J. Biol. Chem , vol.276 , pp. 12791-12796
    • Shinder, G.A.1    Lacourse, M.C.2    Minotti, S.3    Durham, H.D.4    Mutant, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.