References
- International Agency for Research on Cancer. GLOBOCAN 2012: Estimated cancer incidence, mortality and prevalence worldwide in 2012 [Internet]. Lyon: International Agency for Research on Cancer; 2012 [cited 2017 August 01] Available from http://globocan.iarc.fr/Pages/fact_sheets_cancer/.
- National Cancer Information Center. Cancer Statistics in Korea. 2014 [Internet]. Goyang: National Cancer Information Center; 2014 [cited 2017 August 01] Korea Available from: http://www.cancer.go.kr/mbs/cancer/subview.jsp
- Brandao GD, Brega EF, Spatz A. The role of molecular pathology in non-small-cell lung carcinoma-now and in the future. Curr Oncol. 2012;19(1):24-32.
- Kingstone RE, Baldwin, AS, Sharp PA. Regulation of heat shock protein 70 gene expression by c-myc. Nature. 1984;312(5991):280-282. https://doi.org/10.1038/312280a0
- Konno A, Sato N, Yagihashi A, Torigoe T, Cho JM, Torimoto K, et al. Heat or stress inducible transformation associated cell surface antigen on the H-ras oncogene transfected rat fibroblasts. Cancer Res. 1989;49(23):6578-6582.
- Shrivastava PK, Maki RG. Stress induced proteins in immune response to cancer. Curr Top Microbiol Immunol. 1991;167:109-123.
- Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell. 1998;92(3):351-366. https://doi.org/10.1016/S0092-8674(00)80928-9
- Garcia-Carbonero R, Carnero A, Paz-Ares L. Inhibition of HSP90 molecular chaperones: moving into the clinic. Lancet Oncol. 2013;14(9):358-369. https://doi.org/10.1016/S1470-2045(13)70169-4
- McClellan AJ, Xia Y, Deutschbauer AM, Davis RW, Gerstein M, Frydman J. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell. 2007; 131(1):121-135. https://doi.org/10.1016/j.cell.2007.07.036
- Dobo C, Stavale JN, Lima Fde O, Ribeiro DA, Arias V, Gomes TS, et al. HSP27 is Commonly Expressed in Cervical Intraepithelial Lesions of Brazilian Women. Asian Pac J Cancer Prev. 2013; 14(9):5007-5010. https://doi.org/10.7314/APJCP.2013.14.9.5007
- Wu GQ, Liu NN, Xue XL, Cai LT, Zhang C, Qu QR, et al. Multiplex Real-time PCR for RRM1, XRCC1, TUBB3 and TS mRNA for prediction of response of non-small cell lung cancer to chemoradiotherapy. Asian Pac J Cancer Prev. 2014;15(10): 4153-4158. https://doi.org/10.7314/APJCP.2014.15.10.4153
- Hanahan D, Weinberg RA. The hallmarks of cancer. Cell. 2000;100(1):57-70. https://doi.org/10.1016/S0092-8674(00)81683-9
- Mahalingam D, Swords R, Carew JS, Nawrocki ST, Bhalla K, Giles FJ. Targeting HSP90 for cancer therapy. Br J Cancer. 2009;100(10):1523-1529. https://doi.org/10.1038/sj.bjc.6605066
- Sharp S. Workman P. Inhibitors of the HSP90 molecular chaperone: current status. Adv Cancer Res. 2006;95:323-348.
- Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell. 2011;144(5):646-674. https://doi.org/10.1016/j.cell.2011.02.013
- Beck R, Dejeans N, Glorieux C, Pedrosa RC, Vasquez D, Valderrama JA, Calderon PB, Verrax J. Molecular chaperone Hsp90 as a target for oxidant-based anticancer therapies. Curr Med Chem. 2011;18(18):2816-2825. https://doi.org/10.2174/092986711796011256
- Moser C, Lang SA, Stoeltzing O. Heat-shock protein 90(Hsp90) as a molecular target for therapy of gastrointestinal cancer. Anticancer Res. 2009;29(6):2031-2042.
- Whitesell L, Lindquist SL. Hsp90 and chaperoning of cancer. Nat Rev Cancer. 2005;5(10):761-772. https://doi.org/10.1038/nrc1716
- Jia JM, Liu F, Xu XL, Guo XK, Jiang F, Cherfaoui B, et al. Synthesis and evaluation of a novel class Hsp90 inhibitors containing 1-phenylpiperazine scaffold. Bioorg Med Chem Lett. 2014;24(6):1557-1561. https://doi.org/10.1016/j.bmcl.2014.01.070
-
Jiang H, Duan B, He C, Geng S, Shen X, Zhu H, et al. Cytoplasmic
$HSP90{\alpha}$ expression is associated with perineural invasion in pancreatic cancer. Int J Clin Exp Pathol. 2014; 7(6):3305-3311. - Tian WL, He F, Fu X, Lin JT, Tang P, Huang YM, et al. High expression of heat shock protein 90 alpha and its significance in human acute leukemia cells. Gene. 2014;542(2):122-128. https://doi.org/10.1016/j.gene.2014.03.046
- Romaniuk A, Lyndin M. Immune microenvironment as a factor of breast cancer progression. Diagnostic Pathology. 2015;10:79. https://doi.org/10.1186/s13000-015-0316-y
-
Zuo DS, Dai J, Bo AH, Fan J, Xiao XX. Significance of expression of heat shock
$protein90{\alpha}$ in human gastric cancer. World J Gastroenterol. 2003;9(11):2616-2618. https://doi.org/10.3748/wjg.v9.i11.2616 -
Jahns F, Wilhelm A, Greulich KO, Mothes H, Radeva M, Wolfert A, et al. Impact of butyrate on PKM2 and
$HSP90{\beta}$ expression in human colon tissues of different transformation stages: a comparison of gene and protein data. Genes Nutr. 2012;7(2):235-246. https://doi.org/10.1007/s12263-011-0254-6 - Mayer P, Harjung A, Breinig M, Fischer L, Ehemann V, Malz M, et al. Expression and therapeutic relevance of heat-shock protein 90 in pancreatic endocrine tumors. Endocr Relat Cancer. 2012;19(3):217-232. https://doi.org/10.1530/ERC-11-0227
- Lee JH, Kang KW, Kim JE, Hwang SW, Park JH, Kim SH, et al. Differential expression of heat shock protein 90 isoforms in small cell lung cancer. Int J Clin Exp Pathol. 2015;8(8):9487-9493.
- Biaoxue R, Xiling J, Shuanying Y, Wei Z, Xiguang C, Jinsui W, et al. Upregulation of Hsp90-beta and annexin A1 correlates with poor survival and lymphatic metastasis in lung cancer patients. J Exp Clin Cancer Res. 2012;31(1):70. https://doi.org/10.1186/1756-9966-31-70
- Chhabra S, Jain S, Wallace C, Hong F. Liu B. High expression of endoplasmic reticulum chaperone grp94 is a novel molecular hallmark of malignant plasma cells in multiple myeloma. J Hematol Oncol. 2015;8:77. https://doi.org/10.1186/s13045-015-0177-6
- Shen J, Yao L, Lin YG, DeMayo FJ, Lydon JP, Dubeau L, et al. Glucose-regulated protein 94 deficiency induces squamous cell metaplasia and suppresses PTEN-null driven endometrial epithelial tumor development. Oncotarget. 2016;7(12):14885-14897.
- Wang Q, He Z, Zhang J, Wang Y, Wang T, Tong S, et al. Overexpression of endoplasmic reticulum molecular chaperone GRP94 and GRP78 in human lung cancer tissues and its significance. Cancer Detect Prev. 2005;29(6):544-551. https://doi.org/10.1016/j.cdp.2005.09.010