메뉴 건너뛰기




Volumn 3 S, Issue 1, 2011, Pages 341-351

Hsp60: Molecular anatomy and role in colorectal cancer diagnosis and treatment

Author keywords

Chaperoning system; Chaperonology; Chaperonopathies; Chaperonotherapy; Clinical oncology; Colorectal cancer; Hsp60; Review

Indexed keywords

ANTINEOPLASTIC AGENT; CASPASE 3; CASPASE 6; CHAPERONIN 60; CISPLATIN; EARLY PREGNANCY FACTOR; PROTEIN P53; STAUROSPORINE; SURVIVIN; TUMOR MARKER; CHAPERONIN;

EID: 79955969777     PISSN: 19450516     EISSN: 19450524     Source Type: Journal    
DOI: 10.2741/s155     Document Type: Review
Times cited : (26)

References (87)
  • 1
    • 77953228373 scopus 로고    scopus 로고
    • Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems
    • A.J.L Macario, F. Cappello, G. Zummo, E. Conway de Macario: Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems. Ann NY Acad Sci 1197, 85-93 (2010)
    • (2010) Ann NY Acad Sci , vol.1197 , pp. 85-93
    • Macario, A.J.L.1    Cappello, F.2    Zummo, G.3    Conway De Macario, E.4
  • 2
    • 2442718034 scopus 로고    scopus 로고
    • Evolution of assisted protein folding: The distribution of the main chaperoning systems within the phylogenetic domain Archaea
    • d1000-1499
    • A.J.L. Macario, M. Malz, E. Conway de Macario. Evolution of assisted protein folding: the distribution of the main chaperoning systems within the phylogenetic domain archaea. Front Biosci 9, 1318-32 (2004) (Pubitemid 39060845)
    • (2004) Frontiers in Bioscience , vol.9 , pp. 1318-1332
    • Macario, A.J.L.1    Malz, M.2    Conway De Macario, E.3
  • 3
    • 74049129476 scopus 로고    scopus 로고
    • Integrating the cell stress response: A new view of molecular chaperones as immunological and physiological homeostatic regulators
    • B. Henderson. Integrating the cell stress response: a new view of molecular chaperones as immunological and physiological homeostatic regulators. Cell Biochem Funct 28, 1 -14 (2010)
    • (2010) Cell Biochem Funct , vol.28 , Issue.1-14
    • Henderson, B.1
  • 7
    • 33751170698 scopus 로고    scopus 로고
    • Mitochondrial chaperones in cancer: From molecular biology to clinical diagnostics
    • A.M. Czarnecka, C. Campanella, G. Zummo, F. Cappello. Mitochondrial chaperones in cancer: from molecular biology to clinical diagnostics. Cancer Biol Ther 5, 714-20 (2006) (Pubitemid 44775122)
    • (2006) Cancer Biology and Therapy , vol.5 , Issue.7 , pp. 714-720
    • Czarnecka, A.M.1    Campanella, C.2    Zummo, G.3    Cappello, F.4
  • 10
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: Diagnostic, prognostic, predictive, and treatment implications
    • DOI 10.1379/CSC-99r.1, csac. 2005.CSC-99r
    • D.R. Ciocca, S.K. Calderwood. Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 10, 86-103 (2005) (Pubitemid 40942470)
    • (2005) Cell Stress and Chaperones , vol.10 , Issue.2 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 11
    • 56149106877 scopus 로고    scopus 로고
    • Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy
    • F. Cappello, E. Conway de Macario, L. Marasà, G. Zummo, A.J.L. Macario. Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy. Cancer Biol Ther 7, 801-9 (2008)
    • (2008) Cancer Biol Ther , vol.7 , pp. 801-809
    • Cappello, F.1    Conway De Macario, E.2    Marasà, L.3    Zummo, G.4    Macario, A.J.L.5
  • 13
    • 34447526219 scopus 로고    scopus 로고
    • Chaperonopathies and chaperonotherapy
    • DOI 10.1016/j.febslet.2007.04.030, PII S0014579307004206, Cellular Stress
    • A.J.L. Macario, E. Conway de Macario. Chaperonopathies and chaperonotherapy. FEBS Lett 581, 3681-8 (2007b) (Pubitemid 47081002)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3681-3688
    • Macario, A.J.L.1    Conway De Macario, E.2
  • 15
    • 0038645376 scopus 로고    scopus 로고
    • Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix
    • DOI 10.1016/S0304-3835(03)00212-X
    • F. Cappello, M. Bellafiore, S. David, R. Anzalone, G. Zummo. Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large b owel and uterine exocervix. Cancer Lett 196, 35-41 (2003c) (Pubitemid 36830908)
    • (2003) Cancer Letters , vol.196 , Issue.1 , pp. 35-41
    • Cappello, F.1    Bellafiore, M.2    David, S.3    Anzalone, R.4    Zummo, G.5
  • 17
    • 30444447791 scopus 로고    scopus 로고
    • Differential expression of Janus kinase 3 (JAK3), matrix metalloproteinase 13 (MMP13), heat shock protein 60 (HSP60), and mouse double minute 2 (MDM2) in human colorectal cancer progression using human cancer cDNA microarrays
    • DOI 10.1016/j.prp.2005.06.005, PII S0344033805001561
    • D. Mori, Y. Nakafusa, K. Miyazaki, O. Tokunaga. Differential expression of Janus kinase 3 ( JAK3), matrix metalloproteinase 13 (MMP13), heat shock protein 60 (HSP60), and mouse double minute 2 (MDM2) in human colorectal cancer progression using human cancer cDNA microarrays. Pathol Res Pract 201, 777-89 (2005) (Pubitemid 43071565)
    • (2005) Pathology Research and Practice , vol.201 , Issue.12 , pp. 777-789
    • Mori, D.1    Nakafusa, Y.2    Miyazaki, K.3    Tokunaga, O.4
  • 18
    • 38149095001 scopus 로고    scopus 로고
    • Proteomics-based identification of HSP60 as a tumor-associated antigen in colorectal cancer
    • Y. He, Y. Wu, Z. Mou, W. Li, L. Zou, T. Fu, A. Zhang, D. Xiang, H. Xiao, X. Wang. Proteomics-based identification of HSP60 as a tumor-associated antigen in colorectal cancer. Proteomics 1, 336-342 (2007)
    • (2007) Proteomics , vol.1 , pp. 336-342
    • He, Y.1    Wu, Y.2    Mou, Z.3    Li, W.4    Zou, L.5    Fu, T.6    Zhang, A.7    Xiang, D.8    Xiao, H.9    Wang, X.10
  • 19
    • 36048978462 scopus 로고    scopus 로고
    • Selecting differentially expressed genes using minimum probability of classification error
    • DOI 10.1016/j.jbi.2007.07.006, PII S1532046407000792, Intelligent Data Analysis in Biomedicine
    • P. Mahata, K. Mahata. Selecting differentially expressed genes using minimum probability of classification error. J Biomed Inform 40, 775-86 (2007) (Pubitemid 350088626)
    • (2007) Journal of Biomedical Informatics , vol.40 , Issue.6 , pp. 775-786
    • Mahata, P.1    Mahata, K.2
  • 21
    • 0028960169 scopus 로고
    • Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells
    • R.S Gupta. Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells. Mol Microbiol 15, 1-11 (1995)
    • (1995) Mol Microbiol , vol.15 , pp. 1-11
    • Gupta, R.S.1
  • 22
    • 74749086659 scopus 로고    scopus 로고
    • La Rocca. Human Hsp10 and Early Pregnancy Factor (EPF) and their relationship and involvement in cancer and immunity: Current knowledge and perspectives
    • S. Corrao, C. Campanella, R. Anzalone, F. Farina, G. Zummo, E. Conway de Macario, A.J.L. Macario, Cappello, G. La Rocca. Human Hsp10 and Early Pregnancy Factor (EPF) and their relationship and involvement in cancer and immunity: current knowledge and perspectives. Life Sci 86, 145-52 (2010)
    • (2010) Life Sci , vol.86 , pp. 145-152
    • Corrao, S.1    Campanella, C.2    Anzalone, R.3    Farina, F.4    Zummo, G.5    Conway De Macario, E.6    Macario, A.J.L.7    Cappello, G.8
  • 23
    • 0031959254 scopus 로고    scopus 로고
    • The ins and outs of a molecular chaperone machine
    • DOI 10.1016/S0968-0004(98)01193-1
    • A. Richardson, S.J. Landry, C. Georgopoulos. The ins and outs of a molecular chaperone machine. Trends Biochem Sci 23, 138-43 (1998) (Pubitemid 28189525)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.4 , pp. 138-143
    • Richardson, A.1    Landry, S.J.2    Georgopoulos, C.3
  • 24
    • 0035895947 scopus 로고    scopus 로고
    • The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: Humans versus Escherichia coli
    • A. Richardson, F. Schwager, S.J. Landry, C. Georgopoulos. The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli. J Biol Chem 276, 4981-7 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 4981-4987
    • Richardson, A.1    Schwager, F.2    Landry, S.J.3    Georgopoulos, C.4
  • 25
    • 0037010181 scopus 로고    scopus 로고
    • Type I chaperonins: Not all are created equal
    • DOI 10.1016/S0014-5793(02)03178-2, PII S0014579302031782
    • G. Levy-Rimler, R.E. Bell, N. Ben-Tal, A. Azem. Type I chaperonins: not all are created equal. FEBS Lett 529, 1-5 (2002) (Pubitemid 35283902)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 1-5
    • Levy-Rimler, G.1    Bell, R.E.2    Ben-Tal, N.3    Azem, A.4
  • 26
    • 0032113635 scopus 로고    scopus 로고
    • A single ring is sufficient for productive chaperonin-mediated folding in vivo
    • K.L. Nielsen, N.J. Cowan. A single ring is sufficient for productive chaperonin-mediated folding in vivo. Mol Cell 2, 93-99 (1998) (Pubitemid 128378970)
    • (1998) Molecular Cell , vol.2 , Issue.1 , pp. 93-99
    • Nielsen, K.L.1    Cowan, N.J.2
  • 27
    • 0032884582 scopus 로고    scopus 로고
    • A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo
    • K.L. Nielsen, N. McLennan, M. Masters, N.J. Cowan. A single-ring mitochondrial chaperonin (Hsp60-Hsp10) ca n substitute for GroEL-GroES in vivo. J Bacteriol 181, 5871-5875 (1999) (Pubitemid 29437165)
    • (1999) Journal of Bacteriology , vol.181 , Issue.18 , pp. 5871-5875
    • Nielsen, K.L.1    McLennan, N.2    Masters, M.3    Cowan, N.J.4
  • 28
    • 0032531727 scopus 로고    scopus 로고
    • Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10
    • DOI 10.1093/emboj/17.20.5868
    • Y. Dubaquie, R. Looser, U. Funfschilling, P. Jeno, S. Rospert. Identification of in vivo substrates of the yeast mi tochondrial chaperonins reveals overlapping but nonidentical requirement for hsp60 and hsp10. EMBO J 17, 5868-5876 (1998) (Pubitemid 28474781)
    • (1998) EMBO Journal , vol.17 , Issue.20 , pp. 5868-5876
    • Dubaquie, Y.1    Looser, R.2    Funfschilling, U.3    Jeno, P.4    Rospert, S.5
  • 29
    • 0037208893 scopus 로고    scopus 로고
    • Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter
    • DOI 10.1007/s00439-002-0837-9
    • J.J. Hansen, P. Bross, M. Westergaard, M.N. Nielsen, H. Eiberg, A. D. Brglum, J. Mogensen, K. Kristiansen, L. Bolund, N. Gregersen. Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter. Hum Genet 112, 71-7 (2003) (Pubitemid 36869118)
    • (2003) Human Genetics , vol.112 , Issue.1 , pp. 71-77
    • Hansen, J.J.1    Bross, P.2    Westergaard, M.3    Nielsen, M.N.4    Eiberg, H.5    Borglum, A.D.6    Mogensen, J.7    Kristiansen, K.8    Bolund, L.9    Gregersen, N.10
  • 31
    • 0037121087 scopus 로고    scopus 로고
    • Phylogenetic relationships of organellar Hsp90 homologs reveal fundamental differences to organellar Hsp70 and Hsp60 evolution
    • DOI 10.1016/S0378-1119(02)01021-1, PII S0378111902010211
    • V.V. Emelyanov. Phylogenetic relationships of organellar Hsp90 homologs reveal fundamental differences to organellar Hsp70 and Hsp60 evolution. Gene 299, 125-33 (2002) (Pubitemid 35379834)
    • (2002) Gene , vol.299 , Issue.1-2 , pp. 125-133
    • Emelyanov, V.V.1
  • 32
    • 0030023858 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells
    • DOI 10.1006/excr.1996.0003
    • B.J. Soltys, R.S. Gupta. Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells. Exp Cell Res 222, 16-27 (1996) (Pubitemid 26043708)
    • (1996) Experimental Cell Research , vol.222 , Issue.1 , pp. 16-27
    • Soltys, B.J.1    Gupta, R.S.2
  • 33
    • 0031147756 scopus 로고    scopus 로고
    • Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells
    • DOI 10.1006/cbir.1997.0144
    • B.J. Soltys, R.S. Gupta. Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells. Cell Biol Int 21, 315-20 (1997) (Pubitemid 27355093)
    • (1997) Cell Biology International , vol.21 , Issue.5 , pp. 315-320
    • Soltys, B.J.1    Gupta, R.S.2
  • 34
    • 35748929414 scopus 로고    scopus 로고
    • Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: Evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3
    • DOI 10.1074/jbc.M702777200
    • D. Chandra, G. Choy, D.G. Tang. Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its proapoptotic or pro-survival functions involve differential interactions with caspase-3. J Biol Chem 282, 31289-301 (2007) (Pubitemid 350044883)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.43 , pp. 31289-31301
    • Chandra, D.1    Choy, G.2    Tang, D.G.3
  • 36
    • 0026523132 scopus 로고
    • Immunocytochemical localization of heat-shock protein 60- related protein in beta-cell secretory granules and ist altered distribution in non-obese diabetic mice
    • K. Brudzynski, V. Martinez, R.S. Gupta. Immunocytochemical localization of heat-shock protein 60- related protein in beta-cell secretory granules and ist altered distribution in non-obese diabetic mice. Diabetologia 35, 316-24 (1992)
    • (1992) Diabetologia , vol.35 , pp. 316-324
    • Brudzynski, K.1    Martinez, V.2    Gupta, R.S.3
  • 37
    • 0033976869 scopus 로고    scopus 로고
    • Localization of mitochondrial 60-kD heat shock chaperonin protein (Hsp60) in pituitary growth hormone secretory granules and pancreatic zymogen granules
    • J.D. Cechett o, B.J. Soltys, R.S. Gupta. Localization of mitochondrial 60-kD heat shock chaperonin protein (Hsp60) in pituitary growth hormone secretory granules and pancreatic zymogen granules. J Histochem Cytochem 48, 45-56 (2000) (Pubitemid 30053565)
    • (2000) Journal of Histochemistry and Cytochemistry , vol.48 , Issue.1 , pp. 45-56
    • Cechetto, J.D.1    Soltys, B.J.2    Gupta, R.S.3
  • 40
    • 33947510303 scopus 로고    scopus 로고
    • Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide
    • DOI 10.1074/jbc.M608666200
    • A. Osterloh, U. Kalinke, S. Weiss, B. Fleischer, M. Breloer. Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide. J Biol Chem 282, 4669-80 (2007) (Pubitemid 47100986)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.7 , pp. 4669-4680
    • Osterloh, A.1    Kalinke, U.2    Weiss, S.3    Fleischer, B.4    Breloer, M.5
  • 44
    • 43049159563 scopus 로고    scopus 로고
    • Decreased ex pression of the mitochondrial matrix proteases Lon and ClpP in cells from a patient with hereditary spastic paraplegia (SPG13)
    • J. Hansen, T.J. Corydon, J. Palmfeldt, A. Dürr, B. Fontaine, M.N. Nielsen, J.H. Christensen, N. Gregersen, P. Bross. Decreased ex pression of the mitochondrial matrix proteases Lon and ClpP in cells from a patient with hereditary spastic paraplegia (SPG13). Neuroscience 153, 474-82 (2008)
    • (2008) Neuroscience , vol.153 , pp. 474-482
    • Hansen, J.1    Corydon, T.J.2    Palmfeldt, J.3    Dürr, A.4    Fontaine, B.5    Nielsen, M.N.6    Christensen, J.H.7    Gregersen, N.8    Bross, P.9
  • 53
    • 0033977056 scopus 로고    scopus 로고
    • The stress kit: A new method based on competitive reverse transcriptase-polymerase chain reaction to quantify the expression of human αB-crystallin, Hsp27, and Hsp60
    • J.J. Bajramović, S.B. Geutskens, M. Bsibsi, M. Boot, R. Hassankhan, K.C. Verhulst and J.M. van Noort. The stress kit: a new method based on competiti ve reverse transcriptase-polymerase chain reaction to quantify the expression of human alphaB-crystallin, Hsp27, and Hsp60. Cell Stress Chaperones 5, 30-35 (2000) (Pubitemid 30099053)
    • (2000) Cell Stress and Chaperones , vol.5 , Issue.1 , pp. 30-35
    • Bajramovic, J.J.1    Geutskens, S.B.2    Bsibsi, M.3    Boot, M.4    Hassankhan, R.5    Verhulst, K.C.6    Van Noort, J.M.7
  • 54
    • 0029011834 scopus 로고
    • Analysis of heatshock protein expression in myeloid leukaemia cells by flow cytometry
    • I.D. Chant, P.E. Rose, A.G. Morris. Analysis of heatshock protein expression in myeloid leukaemia cells by flow cytometry. Br J Haematol 90, 163-168 (1995)
    • (1995) Br J Haematol , vol.90 , pp. 163-168
    • Chant, I.D.1    Rose, P.E.2    Morris, A.G.3
  • 55
    • 22144458740 scopus 로고    scopus 로고
    • Expression of heat-shock proteins is associated with major adverse prognostic factors in acute myeloid leukemia
    • DOI 10.1016/j.leukres.2005.02.010, PII S014521260500086X
    • X. Thomas, L. Campos, C. Mounier, J. Cornillon, P. Flandrin, Q.H. Le, S. Piselli and D. Guyotat. Expression of heat-shock proteins is associated with major adverse prognostic factors in acute myeloid leukemia. Leuk Res 29, 1049-1058 (2005) (Pubitemid 40982599)
    • (2005) Leukemia Research , vol.29 , Issue.9 , pp. 1049-1058
    • Thomas, X.1    Campos, L.2    Mounier, C.3    Cornillon, J.4    Flandrin, P.5    Le, Q.-H.6    Piselli, S.7    Guyotat, D.8
  • 56
    • 0032403161 scopus 로고    scopus 로고
    • Abundance of heat shock proteins (hsp89, hsp60, and hsp27) in malignant cells of Hodgkin's disease
    • P.L. Hsu, S.M. Hsu. Abundance of heat shock proteins (hsp89, hsp60, and hsp27) in malignant cells of Hodgkin's disease. Cancer Res 58, 5507-5513 (1998)
    • (1998) Cancer Res , vol.58 , pp. 5507-5513
    • Hsu, P.L.1    Hsu, S.M.2
  • 57
    • 0033135727 scopus 로고    scopus 로고
    • Oral lichen planus: An immunohistochemical study of heat shock proteins (HSPS) and cytokeratins (CKS) and a unifying hypothesis of pathogenesis
    • P. Chaiyarit, A.H. Kafrawy, D.A. Miles, S.L. Zunt, M.L. Van Dis and R.L. Gregory. Oral lichen planus: an immunohistochemical study of heat shock proteins (HSPs) and cytokeratins (CKs) and a unifying hypothesis of pathogenesis. J Oral Pathol Med 28, 210-215 (1999) (Pubitemid 29188408)
    • (1999) Journal of Oral Pathology and Medicine , vol.28 , Issue.5 , pp. 210-215
    • Chaiyarit, P.1    Kafrawy, A.H.2    Miles, D.A.3    Zunt, S.L.4    Van Dis, M.L.5    Gregory, R.L.6
  • 58
    • 0033007931 scopus 로고    scopus 로고
    • Antibodies to human gastric epithelial cells and heat shock protein 60 in Helicobacter pylori positive mucosa associated lymphoid tissue lymphoma
    • Y. Kawahara, K. Yokota, M. Mizuno, N. Yunoki, T. Uesu, H. Okada, K. Kobayashi, Y. Hirai, K. Oguma and T. Tsuji. Antibodies to human gastric epithelial cells and heat shock protein 60 in Helicobacter pylori positive mucosa associated lymphoid tissue lymphoma. Gut 45, 20-23 (1999) (Pubitemid 29301840)
    • (1999) Gut , vol.45 , Issue.1 , pp. 20-23
    • Kawahara, Y.1    Yokota, K.2    Mizuno, M.3    Yunoki, N.4    Uesu, T.5    Okada, H.6    Kobayashi, K.7    Hirai, Y.8    Oguma, K.9    Tsuji, T.10
  • 59
    • 0031809926 scopus 로고    scopus 로고
    • Detection of Helicobacter pylori associated antigen and heat shock protein 60 on follicular dendritic cells in the germinal centres of low grade B cell lymphoma of gastric mucosa associated lymphoid tissue (MALT)
    • K. Kobayashi, K. Yokota, T. Yoshino, Y. Kawahara, A. Dey, Y. Hirai, K. Oguma and T. Akagi. Dete ction of Helicobacter pylori associated antigen and heat shock protein 60 on follicular dendritic cells in the germinal centres of low grade B cell lymphoma of gastric mucosa associated lymphoid tissue (MALT). J Clin Pathol 51, 396-398 (1998) (Pubitemid 28289129)
    • (1998) Journal of Clinical Pathology , vol.51 , Issue.5 , pp. 396-398
    • Kobayashi, K.1    Yokota, K.2    Yoshino, T.3    Kawahara, Y.4    Dey, A.5    Hirai, Y.6    Oguma, K.7    Akagi, T.8
  • 61
    • 23744443565 scopus 로고    scopus 로고
    • Current progress in proteomic study of hepatitis C virus-related human hepatocellular carcinoma
    • DOI 10.1586/14789450.2.4.589
    • Y. Kuramitsu, K. Nakamura. Current progress in proteomic study of hepatitis C virus-related human hepatocellular carcinoma. Expert Rev Proteomics 2, 589-601 (2005) (Pubitemid 41139841)
    • (2005) Expert Review of Proteomics , vol.2 , Issue.4 , pp. 589-601
    • Kuramitsu, Y.1    Nakamura, K.2
  • 62
    • 26444476479 scopus 로고    scopus 로고
    • Immunopositivity of heat shock protein 60 as a biomarker of bronchial carcinogenesis
    • DOI 10.1016/S1470-2045(05)70393-4, PII S1470204505703934
    • F. Cappello, A. Di Stefano, S.E. D'Anna, C.F. Donner, G. Z ummo. Immunopositivity of heat shock protein 60 as a biomarker of bronchial carcinogenesis. Lancet Oncol 6, 816 (2005b) (Pubitemid 41430724)
    • (2005) Lancet Oncology , vol.6 , Issue.10 , pp. 816
    • Cappello, F.1    Di Stefano, A.2    D'Anna, S.E.3    Donner, C.F.4    Zummo, G.5
  • 63
    • 33748342168 scopus 로고    scopus 로고
    • Proteomic comparison of prostate cancer cell lines LNCaP-FGC and LNCaP-r reveals heatshock protein 60 as a marker for prostate malignancy
    • DOI 10.1002/pros.20453
    • B. Johansson, M.R. Pourian, Y.C. Chuan, I. Byman, A. Bergh, S.T. Pang, G. Norstedt, T. Bergman and A. Pousette. Proteomic comparison of prostate cancer cell lines LNCaP-FGC and LNCaP-r reveals heat shock protein 60 as a marker for prostate malignancy. Prostate 66, 1235-1244 (2006) (Pubitemid 44384299)
    • (2006) Prostate , vol.66 , Issue.12 , pp. 1235-1244
    • Johansson, B.1    Pourian, M.R.2    Chuan, Y.-C.3    Byman, I.4    Bergh, A.5    Pang, S.-T.6    Norstedt, G.7    Bergman, T.8    Pousette, A.9
  • 66
    • 26444556837 scopus 로고    scopus 로고
    • Immunohistochemical evaluation of heat shock proteins in normal and preinvasive lesions of the cervix
    • DOI 10.1016/j.canlet.2005.06.045, PII S0304383505006245
    • P.E. Castle, R. Ashfaq, F. Ansari, C.Y. Muller. Immunohistochemical evaluation of heat shock protei ns in normal and preinvasive lesions of the cervix. Cancer Lett 229, 245-252 (2005) (Pubitemid 41429363)
    • (2005) Cancer Letters , vol.229 , Issue.2 , pp. 245-252
    • Castle, P.E.1    Ashfaq, R.2    Ansari, F.3    Muller, C.Y.4
  • 68
  • 69
    • 0344631749 scopus 로고    scopus 로고
    • Immunohistochemical detection of HSP60-expression in human ovarian cancer. Correlation with survival in a series of 247 patients
    • J. Schneider, E. Jiménez, K. Marenbach, H. Romero, D. Marx, H. Meden. Immunohistochemical detectio n of HSP60-expression in human ovarian cancer. Correlation with survival in a series of 247 patients. Anticancer Res 19, 2141-2146 (1999) (Pubitemid 29392784)
    • (1999) Anticancer Research , vol.19 , Issue.3 , pp. 2141-2146
    • Schneider, J.1    Jimenez, E.2    Marenbach, K.3    Romero, H.4    Marx, D.5    Meden, H.6
  • 71
    • 0038823634 scopus 로고    scopus 로고
    • Immunohistochemical study of heat shock proteins 27, 60 and 70 in the normal human adrenal and in adrenal tumors with suppressed ACTH production
    • DOI 10.1002/jemt.10341
    • D. Pignatelli, J. Ferreira, P. Soares, M.J. Costa, M.C. Magalhães. Immunohistochemical study of heat shock proteins 27, 60 and 70 in the normal human adrenal and in adrenal tumors with suppress ed ACTH production. Microsc Res Tech 61, 315-323 (2003) (Pubitemid 36618458)
    • (2003) Microscopy Research and Technique , vol.61 , Issue.3 , pp. 315-323
    • Pignatelli, D.1    Ferreira, J.2    Soares, P.3    Costa, M.J.4    Magalhaes, M.C.5
  • 72
    • 0031692853 scopus 로고    scopus 로고
    • Heat shock protein 72 expression in osteosarcomas correlates with good response to neoadjuvant chemotherapy
    • DOI 10.1016/S0046-8177(98)90412-9
    • K. Trieb, T. Lechleitner, S. Lang, R. Windhager, R. Kotz, S. Dirnhofer. Heat shock protein 72 expression in osteosarcomas corre lates with good response to neoadjuvant chemotherapy. Hum Pathol 29, 1050-1055 (1998) (Pubitemid 28467522)
    • (1998) Human Pathology , vol.29 , Issue.10 , pp. 1050-1055
    • Trieb, K.1    Lechleitner, T.2    Lang, S.3    Windhager, R.4    Kotz, R.5    Dirnhofer, S.6
  • 76
    • 0037900829 scopus 로고    scopus 로고
    • Immunohistochemical evaluation of PCNA, p53, HSP60, HSP10 and MUC-2 presence and expression in prostate carcinogenesis
    • F. Cappello, F. Rappa, S. David, R. Anzalone, G. Zummo. Immunohistochemical evaluation of PCNA, p53, HSP60, HSP10 and MUC-2 presence and expression in prostate carcinogenesis. Anticancer Re s 23, 1325-31 (2003b) (Pubitemid 36754095)
    • (2003) Anticancer Research , vol.23 , Issue.2 , pp. 1325-1331
    • Cappello, F.1    Rappa, F.2    David, S.3    Anzalone, R.4    Zummo, G.5
  • 77
    • 48749085401 scopus 로고    scopus 로고
    • Immunohistochemical analysis of possible chemoresistance markers identified by micro-arrays on serous ovarian carcinomas
    • B. Têtu, I. Popa, I. Bairati, S. L'Esperance, M. Bachvarova, M. Plante, F. Harel, D. Bachvarov. Immunohistochemical analysis of possible chemoresistance markers identified by micro-arrays on serous ovarian carcinomas. Modern Pathology 21, 1002-1010 (2008).
    • (2008) Modern Pathology , vol.21 , pp. 1002-1010
    • Têtu, B.1    Popa, I.2    Bairati, I.3    L'Esperance, S.4    Bachvarova, M.5    Plante, M.6    Harel, F.7    Bachvarov, D.8
  • 78
    • 33646717732 scopus 로고    scopus 로고
    • HSP-10 in ovarian cancer: Expression and suppression of T-cell signaling
    • DOI 10.1016/j.ygyno.2005.11.014, PII S0090825805010036
    • S. Akyol, C. Gercel-Taylor, L.C. Reynolds and D.D. Taylor. HSP10 in ovarian cancer: ex pression and suppression of T-cell signalling. Gynecologic Oncology 101(3), 481-486 (2006) (Pubitemid 43744564)
    • (2006) Gynecologic Oncology , vol.101 , Issue.3 , pp. 481-486
    • Akyol, S.1    Gercel-Taylor, C.2    Reynolds, L.C.3    Taylor, D.D.4
  • 79
    • 33845633819 scopus 로고    scopus 로고
    • Biomarker discovery: A proteomic approach for brain cancer profiling
    • DOI 10.1111/j.1349-7006.2007.00374.x
    • A.A. Khalil. Biomarker discovery: a proteomic approach for brain cancer profiling. Cancer Sci 98, 201-213 (2007) (Pubitemid 44941872)
    • (2007) Cancer Science , vol.98 , Issue.2 , pp. 201-213
    • Khalil, A.A.1    James, P.2
  • 80
    • 33750981850 scopus 로고    scopus 로고
    • HSP60 and HSP10 down-regulation predicts bronchial epithelial carcinogenesis in smokers with chronic obstructive pulmonary disease
    • DOI 10.1002/cncr.22265
    • F. Cappello, A. Di Stefano, S. David, F. Rappa, R. Anzalone, G. La Rocca, S.E. D'Anna, F. Magno, C.F. Donner, B. Balbi, G. Zummo. Hsp60 and Hsp10 downregulat ion predicts bronchial epithelial carcinogenesis in smokers with chronic obstructive pulmonary disease. Cancer 107, 2417-24 (2006a) (Pubitemid 44748525)
    • (2006) Cancer , vol.107 , Issue.10 , pp. 2417-2424
    • Cappello, F.1    Di Stefano, A.2    David, S.3    Rappa, F.4    Anzalone, R.5    La Rocca, G.6    D'Anna, S.E.7    Magno, F.8    Donner, C.F.9    Balbi, B.10    Zummo, G.11
  • 82
    • 0041386300 scopus 로고    scopus 로고
    • Heat shock proteins HSP27, HSP60, HSP70, and HSP90: Expression in bladder carcinoma
    • DOI 10.1002/cncr.11594
    • T. Lebret, R.W. Watson, V. M olinié, A. O'Neill, C. Gabriel, J.M. Fitzpatrick, H. Botto. Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma. Cancer 98, 970-7 (2003) (Pubitemid 37022097)
    • (2003) Cancer , vol.98 , Issue.5 , pp. 970-977
    • Lebret, T.1    Watson, R.W.G.2    Molinie, V.3    O'Neill, A.4    Gabriel, C.5    Fitzpatrick, J.M.6    Botto, H.7
  • 83
    • 34250209950 scopus 로고    scopus 로고
    • Expression of heat shock proteins Hsp10, Hsp27, Hsp60, Hsp70 and Hsp90 in urothelial carcinoma of urinary bladder
    • F. Cappello , S. David, N. Ardizzone, F. Rappa, L. Marasà, F. Bucchieri, G. Zummo: Expression of heat shock proteins Hsp10, Hsp27, Hsp60, Hsp70 and Hsp90 in urothelial carcinoma of urinary bladder. J Cancer Mol 2, 73-77 (2006b)
    • (2006) J Cancer Mol , vol.2 , pp. 73-77
    • Cappello, F.1    David, S.2    Ardizzone, N.3    Rappa, F.4    Marasà, L.5    Bucchieri, F.6    Zummo, G.7
  • 84
    • 0030943366 scopus 로고    scopus 로고
    • Carcinosarcoma of the urinary bladder: Expression of epithelial markers and different expression of heat shock proteins between epithelial and sarcomatous elements
    • T. Kamishima, T. Fukuda, H. Usuda, H. Takato, H. Iwamoto, H. Kaneko. Carcinosarcoma of the urinary bladder: expression of epithelial markers and different expression of heat shock protein s between epithelial and sarcomatous elements. Pathol Int 47, 166-173 (1997) (Pubitemid 27123806)
    • (1997) Pathology International , vol.47 , Issue.2-3 , pp. 166-173
    • Kamishima, T.1    Fukuda, T.2    Usuda, H.3    Takato, H.4    Iwamoto, H.5    Kaneko, H.6
  • 85
    • 0033561295 scopus 로고    scopus 로고
    • Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells
    • A. Samali, J. Cai, B. Zhivotovsky, D.P. Jones, S. Orrenius. Presence of pre-apoptotic complex of procaspase- 3 , Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBO J 18, 2040-2048 (1999) (Pubitemid 29179161)
    • (1999) EMBO Journal , vol.18 , Issue.8 , pp. 2040-2048
    • Samali, A.1    Cai, J.2    Zhivotovsky, B.3    Jones, D.P.4    Orrenius, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.