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Volumn 17, Issue 12, 2016, Pages

p53 as a regulator of lipid metabolism in cancer

Author keywords

Cancer; Fatty acid oxidation; Lipid metabolism; Mevalonate pathway; p53

Indexed keywords

ACYL COENZYME A DEHYDROGENASE; AROMATASE; CAVEOLIN 1; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTAMINE; LIPIN 1; MALONYL COENZYME A DECARBOXYLASE; NUCLEAR PROTEIN; OXIDOREDUCTASE; PROTEIN P53; SIRTUIN 1; STEROL REGULATORY ELEMENT BINDING PROTEIN 1; UNCLASSIFIED DRUG; MUTANT PROTEIN; TUMOR PROTEIN;

EID: 85006091069     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms17122074     Document Type: Review
Times cited : (76)

References (79)
  • 1
    • 84903738928 scopus 로고    scopus 로고
    • Reprogrammed metabolism of cancer cells as a potential therapeutic target
    • Keijer, J.; van Dartel, D.A. Reprogrammed metabolism of cancer cells as a potential therapeutic target. Curr. Pharm. Des. 2014, 20, 2580–2594.
    • (2014) Curr. Pharm. Des. , vol.20 , pp. 2580-2594
    • Keijer, J.1    Van Dartel, D.A.2
  • 3
  • 4
    • 37449034854 scopus 로고    scopus 로고
    • Beyond aerobic glycolysis: Transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis
    • DeBerardinis, R.J.; Mancuso, A.; Daikhin, E.; Nissim, I.; Yudkoff, M.; Wehrli, S.; Thompson, C.B. Beyond aerobic glycolysis: Transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis. Proc. Natl. Acad. Sci. USA 2007, 104, 19345–19350.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19345-19350
    • Deberardinis, R.J.1    Mancuso, A.2    Daikhin, E.3    Nissim, I.4    Yudkoff, M.5    Wehrli, S.6    Thompson, C.B.7
  • 5
    • 84863837081 scopus 로고    scopus 로고
    • Lipid metabolism in cancer
    • Santos, C.R.; Schulze, A. Lipid metabolism in cancer. FEBS J. 2012, 279, 2610–2623.
    • (2012) FEBS J. , vol.279 , pp. 2610-2623
    • Santos, C.R.1
  • 10
    • 84903703282 scopus 로고    scopus 로고
    • Targeting SREBP-1-driven lipid metabolism to treat cancer
    • Guo, D.; Bell, E.H.; Mischel, P.; Chakravarti, A. Targeting SREBP-1-driven lipid metabolism to treat cancer. Curr. Pharm. Des. 2014, 20, 2619–2626.
    • (2014) Curr. Pharm. Des. , vol.20 , pp. 2619-2626
    • Guo, D.1    Bell, E.H.2    Mischel, P.3    Chakravarti, A.4
  • 11
    • 84862636275 scopus 로고    scopus 로고
    • Mutant p53: One name, many proteins
    • Freed-Pastor, W.A.; Prives, C. Mutant p53: One name, many proteins. Genes Dev. 2012, 26, 1268–1286.
    • (2012) Genes Dev , vol.26 , pp. 1268-1286
    • Freed-Pastor, W.A.1    Prives, C.2
  • 12
    • 80053039210 scopus 로고    scopus 로고
    • Mutations in the p53 tumor suppressor gene: Important milestones at the various steps of tumorigenesis
    • Rivlin, N.; Brosh, R.; Oren, M.; Rotter, V. Mutations in the p53 tumor suppressor gene: Important milestones at the various steps of tumorigenesis. Genes Cancer 2011, 2, 466–474.
    • (2011) Genes Cancer , vol.2 , pp. 466-474
    • Rivlin, N.1    Brosh, R.2    Oren, M.3    Rotter, V.4
  • 15
    • 84920189113 scopus 로고    scopus 로고
    • Tumor suppressor p53 and its mutants in cancer metabolism
    • Liu, J.; Zhang, C.; Hu, W.; Feng, Z. Tumor suppressor p53 and its mutants in cancer metabolism. Cancer Lett. 2015, 356, 197–203.
    • (2015) Cancer Lett , vol.356 , pp. 197-203
    • Liu, J.1    Zhang, C.2    Hu, W.3    Feng, Z.4
  • 16
    • 79952280229 scopus 로고    scopus 로고
    • P53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase
    • Jiang, P.; Du, W.; Wang, X.; Mancuso, A.; Gao, X.; Wu, M.; Yang, X. p53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase. Nat. Cell Biol. 2011, 13, 310–316.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 310-316
    • Jiang, P.1    Du, W.2    Wang, X.3    Mancuso, A.4    Gao, X.5    Wu, M.6    Yang, X.7
  • 21
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates sirt1 through a forkhead-dependent pathway
    • Nemoto, S.; Fergusson, M.M.; Finkel, T. Nutrient availability regulates sirt1 through a forkhead-dependent pathway. Science 2004, 306, 2105–2108.
    • (2004) Science , vol.306 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 22
    • 84875747902 scopus 로고    scopus 로고
    • A new role of p53 in regulating lipid metabolism
    • Wang, X.; Zhao, X.; Gao, X.; Mei, Y.; Wu, M. A new role of p53 in regulating lipid metabolism. J. Mol. Cell Biol. 2013, 5, 147–150.
    • (2013) J. Mol. Cell Biol. , vol.5 , pp. 147-150
    • Wang, X.1    Zhao, X.2    Gao, X.3    Mei, Y.4    Wu, M.5
  • 25
    • 84902131086 scopus 로고    scopus 로고
    • Ribosomal protein-Mdm2-p53 pathway coordinates nutrient stress with lipid metabolism by regulating mcd and promoting fatty acid oxidation
    • Liu, Y.; He, Y.; Jin, A.; Tikunov, A.P.; Zhou, L.; Tollini, L.A.; Leslie, P.; Kim, T.H.; Li, L.O.; Coleman, R.A. et al. Ribosomal protein-Mdm2-p53 pathway coordinates nutrient stress with lipid metabolism by regulating mcd and promoting fatty acid oxidation. Proc. Natl. Acad. Sci. USA 2014, 111, E2414–E2422.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E2414-E2422
    • Liu, Y.1    He, Y.2    Jin, A.3    Tikunov, A.P.4    Zhou, L.5    Tollini, L.A.6    Leslie, P.7    Kim, T.H.8    Li, L.O.9    Coleman, R.A.10
  • 26
    • 80051517670 scopus 로고    scopus 로고
    • P53-inducible DHRS3 is an endoplasmic reticulum protein associated with lipid droplet accumulation
    • Deisenroth, C.; Itahana, Y.; Tollini, L.; Jin, A.; Zhang, Y. p53-inducible DHRS3 is an endoplasmic reticulum protein associated with lipid droplet accumulation. J. Biol. Chem. 2011, 286, 28343–28356.
    • (2011) J. Biol. Chem. , vol.286 , pp. 28343-28356
    • Deisenroth, C.1    Itahana, Y.2    Tollini, L.3    Jin, A.4    Zhang, Y.5
  • 27
    • 77953601542 scopus 로고    scopus 로고
    • The retinal dehydrogenase/reductase retSDR1/DHRS3 gene is activated by p53 and p63 but not by mutants derived from tumors or EEC/ADULT malformation syndromes
    • Kirschner, R.D.; Rother, K.; Muller, G.A.; Engeland, K. The retinal dehydrogenase/reductase retSDR1/DHRS3 gene is activated by p53 and p63 but not by mutants derived from tumors or EEC/ADULT malformation syndromes. Cell Cycle 2010, 9, 2177–2188.
    • (2010) Cell Cycle , vol.9 , pp. 2177-2188
    • Kirschner, R.D.1    Rother, K.2    Muller, G.A.3    Engeland, K.4
  • 28
    • 0034728387 scopus 로고    scopus 로고
    • P53 regulates caveolin gene transcription, cell cholesterol, and growth by a novel mechanism
    • Bist, A.; Fielding, C.J.; Fielding, P.E. p53 regulates caveolin gene transcription, cell cholesterol, and growth by a novel mechanism. Biochemistry 2000, 39, 1966–1972.
    • (2000) Biochemistry , vol.39 , pp. 1966-1972
    • Bist, A.1    Fielding, C.J.2    Fielding, P.E.3
  • 29
    • 0028834278 scopus 로고
    • Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress
    • Pandolfi, P.P.; Sonati, F.; Rivi, R.; Mason, P.; Grosveld, F.; Luzzatto, L. Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J. 1995, 14, 5209–5215.
    • (1995) EMBO J , vol.14 , pp. 5209-5215
    • Pandolfi, P.P.1    Sonati, F.2    Rivi, R.3    Mason, P.4    Grosveld, F.5    Luzzatto, L.6
  • 30
    • 84859787172 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase, NADPH, and cell survival
    • Stanton, R.C. Glucose-6-phosphate dehydrogenase, NADPH, and cell survival. IUBMB Life 2012, 64, 362–369.
    • (2012) IUBMB Life , vol.64 , pp. 362-369
    • Stanton, R.C.1
  • 31
    • 84943815265 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase expression is correlated with poor clinical prognosis in esophageal squamous cell carcinoma
    • Wang, X.; Li, X.; Zhang, X.; Fan, R.; Gu, H.; Shi, Y.; Liu, H. Glucose-6-phosphate dehydrogenase expression is correlated with poor clinical prognosis in esophageal squamous cell carcinoma. Eur. J. Surg. Oncol. 2015, 41, 1293–1299.
    • (2015) Eur. J. Surg. Oncol. , vol.41 , pp. 1293-1299
    • Wang, X.1    Li, X.2    Zhang, X.3    Fan, R.4    Gu, H.5    Shi, Y.6    Liu, H.7
  • 32
    • 10044271037 scopus 로고    scopus 로고
    • SREBP transcription factors: Master regulators of lipid homeostasis
    • Eberle, D.; Hegarty, B.; Bossard, P.; Ferre, P.; Foufelle, F. SREBP transcription factors: Master regulators of lipid homeostasis. Biochimie 2004, 86, 839–848.
    • (2004) Biochimie , vol.86 , pp. 839-848
    • Eberle, D.1    Hegarty, B.2    Bossard, P.3    Ferre, P.4    Foufelle, F.5
  • 33
    • 0032568557 scopus 로고    scopus 로고
    • Regulation of sterol regulatory element binding proteins in livers of fasted and refed mice
    • Horton, J.D.; Bashmakov, Y.; Shimomura, I.; Shimano, H. Regulation of sterol regulatory element binding proteins in livers of fasted and refed mice. Proc. Natl. Acad. Sci. USA 1998, 95, 5987–5992.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5987-5992
    • Horton, J.D.1    Bashmakov, Y.2    Shimomura, I.3    Shimano, H.4
  • 34
    • 77649216053 scopus 로고    scopus 로고
    • EGFR signaling through an Akt-SREBP-1-dependent, rapamycin-resistant pathway sensitizes glioblastomas to antilipogenic therapy
    • Guo, D.; Prins, R.M.; Dang, J.; Kuga, D.; Iwanami, A.; Soto, H.; Lin, K.Y.; Huang, T.T.; Akhavan, D.; Hock, M.B. et al. EGFR signaling through an Akt-SREBP-1-dependent, rapamycin-resistant pathway sensitizes glioblastomas to antilipogenic therapy. Sci. Signal. 2009, 2.
    • (2009) Sci. Signal , vol.2
    • Guo, D.1    Prins, R.M.2    Dang, J.3    Kuga, D.4    Iwanami, A.5    Soto, H.6    Lin, K.Y.7    Huang, T.T.8    Akhavan, D.9    Hock, M.B.10
  • 35
    • 1542615071 scopus 로고    scopus 로고
    • Dysregulation of sterol response element-binding proteins and downstream effectors in prostate cancer during progression to androgen independence
    • Ettinger, S.L.; Sobel, R.; Whitmore, T.G.; Akbari, M.; Bradley, D.R.; Gleave, M.E.; Nelson, C.C. Dysregulation of sterol response element-binding proteins and downstream effectors in prostate cancer during progression to androgen independence. Cancer Res. 2004, 64, 2212–2221.
    • (2004) Cancer Res , vol.64 , pp. 2212-2221
    • Ettinger, S.L.1    Sobel, R.2    Whitmore, T.G.3    Akbari, M.4    Bradley, D.R.5    Gleave, M.E.6    Nelson, C.C.7
  • 36
    • 79953898189 scopus 로고    scopus 로고
    • Sirtuin 1 in lipid metabolism and obesity
    • Schug, T.T.; Li, X. Sirtuin 1 in lipid metabolism and obesity. Ann. Med. 2011, 43, 198–211.
    • (2011) Ann. Med. , vol.43 , pp. 198-211
    • Schug, T.T.1    Li, X.2
  • 37
    • 63449112017 scopus 로고    scopus 로고
    • Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation
    • Purushotham, A.; Schug, T.T.; Xu, Q.; Surapureddi, S.; Guo, X.; Li, X. Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation. Cell Metab. 2009, 9, 327–338.
    • (2009) Cell Metab , vol.9 , pp. 327-338
    • Purushotham, A.1    Schug, T.T.2    Xu, Q.3    Surapureddi, S.4    Guo, X.5    Li, X.6
  • 38
    • 34948883324 scopus 로고    scopus 로고
    • SIRT1 deacetylates and positively regulates the nuclear receptor LXR
    • Li, X.; Zhang, S.; Blander, G.; Tse, J.G.; Krieger, M.; Guarente, L. SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol. Cell 2007, 28, 91–106.
    • (2007) Mol. Cell , vol.28 , pp. 91-106
    • Li, X.1    Zhang, S.2    Blander, G.3    Tse, J.G.4    Krieger, M.5    Guarente, L.6
  • 43
    • 0035163850 scopus 로고    scopus 로고
    • Lipodystrophy in the FLD mouse results from mutation of a new gene encoding a nuclear protein, lipin
    • Peterfy, M.; Phan, J.; Xu, P.; Reue, K. Lipodystrophy in the FLD mouse results from mutation of a new gene encoding a nuclear protein, lipin. Nat. Genet. 2001, 27, 121–124.
    • (2001) Nat. Genet. , vol.27 , pp. 121-124
    • Peterfy, M.1    Phan, J.2    Xu, P.3    Reue, K.4
  • 46
    • 33846617807 scopus 로고    scopus 로고
    • Cancer-associated mutations in the Mdm2 zinc finger domain disrupt ribosomal protein interaction and attenuate Mdm2-induced p53 degradation
    • Lindstrom, M.S.; Jin, A.; Deisenroth, C.; White Wolf, G.; Zhang, Y. Cancer-associated mutations in the Mdm2 zinc finger domain disrupt ribosomal protein interaction and attenuate Mdm2-induced p53 degradation. Mol. Cell. Biol. 2007, 27, 1056–1068.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1056-1068
    • Lindstrom, M.S.1    Jin, A.2    Deisenroth, C.3    White Wolf, G.4    Zhang, Y.5
  • 47
    • 84865765909 scopus 로고    scopus 로고
    • DHRS3, a retinal reductase, is differentially regulated by retinoic acid and lipopolysaccharide-induced inflammation in THP-1 cells and rat liver
    • Zolfaghari, R.; Chen, Q.; Ross, A.C. DHRS3, a retinal reductase, is differentially regulated by retinoic acid and lipopolysaccharide-induced inflammation in THP-1 cells and rat liver. Am. J. Physiol. Gastrointest. Liver Physiol. 2012, 303, G578–G588.
    • (2012) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.303 , pp. G578-G588
    • Zolfaghari, R.1    Chen, Q.2    Ross, A.C.3
  • 48
    • 84957937629 scopus 로고    scopus 로고
    • Characteristics and functions of lipid droplets and associated proteins in enterocytes
    • Beilstein, F.; Carriere, V.; Leturque, A.; Demignot, S. Characteristics and functions of lipid droplets and associated proteins in enterocytes. Exp. Cell Res. 2016, 340, 172–179.
    • (2016) Exp. Cell Res. , vol.340 , pp. 172-179
    • Beilstein, F.1    Carriere, V.2    Leturque, A.3    Demignot, S.4
  • 49
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • Liu, P.; Rudick, M.; Anderson, R.G. Multiple functions of caveolin-1. J. Biol. Chem. 2002, 277, 41295–41298.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41295-41298
    • Liu, P.1    Rudick, M.2    Anderson, R.G.3
  • 51
    • 0033596725 scopus 로고    scopus 로고
    • Intracellular cholesterol transport in synchronized human skin fibroblasts
    • Fielding, C.J.; Bist, A.; Fielding, P.E. Intracellular cholesterol transport in synchronized human skin fibroblasts. Biochemistry 1999, 38, 2506–2513.
    • (1999) Biochemistry , vol.38 , pp. 2506-2513
    • Fielding, C.J.1    Bist, A.2    Fielding, P.E.3
  • 53
    • 84948140060 scopus 로고    scopus 로고
    • Caveolin-1 in breast cancer: Single molecule regulation of multiple key signaling pathways
    • Anwar, S.L.; Wahyono, A.; Aryandono, T.; Haryono, S.J. Caveolin-1 in breast cancer: Single molecule regulation of multiple key signaling pathways. Asian Pac. J. Cancer Prev. 2015, 16, 6803–6812.
    • (2015) Asian Pac. J. Cancer Prev. , vol.16 , pp. 6803-6812
    • Anwar, S.L.1    Wahyono, A.2    Aryandono, T.3    Haryono, S.J.4
  • 54
    • 84997355381 scopus 로고    scopus 로고
    • Caveolin-1 in the regulation of cell metabolism: A cancer perspective
    • Nwosu, Z.C.; Ebert, M.P.; Dooley, S.; Meyer, C. Caveolin-1 in the regulation of cell metabolism: A cancer perspective. Mol. Cancer 2016, 15, 71.
    • (2016) Mol. Cancer , vol.15 , pp. 71
    • Nwosu, Z.C.1    Ebert, M.P.2    Dooley, S.3    Meyer, C.4
  • 60
    • 84858782079 scopus 로고    scopus 로고
    • AMPK: A nutrient and energy sensor that maintains energy homeostasis
    • Hardie, D.G.; Ross, F.A.; Hawley, S.A. AMPK: A nutrient and energy sensor that maintains energy homeostasis. Nat. Rev. Mol. Cell Biol. 2012, 13, 251–262.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 62
    • 79953755370 scopus 로고    scopus 로고
    • AMPK phosphorylates and inhibits srebp activity to attenuate hepatic steatosis and atherosclerosis in diet-induced insulin-resistant mice
    • Li, Y.; Xu, S.; Mihaylova, M.M.; Zheng, B.; Hou, X.; Jiang, B.; Park, O.; Luo, Z.; Lefai, E.; Shyy, J.Y. et al. AMPK phosphorylates and inhibits srebp activity to attenuate hepatic steatosis and atherosclerosis in diet-induced insulin-resistant mice. Cell Metab. 2011, 13, 376–388.
    • (2011) Cell Metab , vol.13 , pp. 376-388
    • Li, Y.1    Xu, S.2    Mihaylova, M.M.3    Zheng, B.4    Hou, X.5    Jiang, B.6    Park, O.7    Luo, Z.8    Lefai, E.9    Shyy, J.Y.10
  • 64
    • 84958068650 scopus 로고    scopus 로고
    • Allele-specific silencing of mutant p53 attenuates dominant-negative and gain-of-function activities
    • Iyer, S.V.; Parrales, A.; Begani, P.; Narkar, A.; Adhikari, A.S.; Martinez, L.A.; Iwakuma, T. Allele-specific silencing of mutant p53 attenuates dominant-negative and gain-of-function activities. Oncotarget 2016, 7, 5401–5415.
    • (2016) Oncotarget , vol.7 , pp. 5401-5415
    • Iyer, S.V.1    Parrales, A.2    Begani, P.3    Narkar, A.4    Adhikari, A.S.5    Martinez, L.A.6    Iwakuma, T.7
  • 65
    • 84872811756 scopus 로고    scopus 로고
    • Silencing of mutant p53 by siRNA induces cell cycle arrest and apoptosis in human bladder cancer cells
    • Zhu, H.B.; Yang, K.; Xie, Y.Q.; Lin, Y.W.; Mao, Q.Q.; Xie, L.P. Silencing of mutant p53 by siRNA induces cell cycle arrest and apoptosis in human bladder cancer cells. World J. Surg. Oncol. 2013, 11, 22.
    • (2013) World J. Surg. Oncol. , vol.11 , pp. 22
    • Zhu, H.B.1    Yang, K.2    Xie, Y.Q.3    Lin, Y.W.4    Mao, Q.Q.5    Xie, L.P.6
  • 66
    • 30544452870 scopus 로고    scopus 로고
    • Mutant p53 gain of function: Reduction of tumor malignancy of human cancer cell lines through abrogation of mutant p53 expression
    • Bossi, G.; Lapi, E.; Strano, S.; Rinaldo, C.; Blandino, G.; Sacchi, A. Mutant p53 gain of function: Reduction of tumor malignancy of human cancer cell lines through abrogation of mutant p53 expression. Oncogene 2006, 25, 304–309.
    • (2006) Oncogene , vol.25 , pp. 304-309
    • Bossi, G.1    Lapi, E.2    Strano, S.3    Rinaldo, C.4    Blandino, G.5    Sacchi, A.6
  • 67
    • 70350654373 scopus 로고    scopus 로고
    • Mutant p53 mediates survival of breast cancer cells
    • Lim, L.Y.; Vidnovic, N.; Ellisen, L.W.; Leong, C.O. Mutant p53 mediates survival of breast cancer cells. Br. J. Cancer 2009, 101, 1606–1612.
    • (2009) Br. J. Cancer , vol.101 , pp. 1606-1612
    • Lim, L.Y.1    Vidnovic, N.2    Ellisen, L.W.3    Leong, C.O.4
  • 70
    • 84920688856 scopus 로고    scopus 로고
    • Statin use and risk for ovarian cancer: A Danish nationwide case-control study
    • Baandrup, L.; Dehlendorff, C.; Friis, S.; Olsen, J.H.; Kjaer, S.K. Statin use and risk for ovarian cancer: A Danish nationwide case-control study. Br. J. Cancer 2015, 112, 157–161.
    • (2015) Br. J. Cancer , vol.112 , pp. 157-161
    • Baandrup, L.1    Dehlendorff, C.2    Friis, S.3    Olsen, J.H.4    Kjaer, S.K.5
  • 71
    • 84988354894 scopus 로고    scopus 로고
    • Statins improve outcomes of nonsurgical curative treatments in hepatocellular carcinoma patients
    • Wu, L.L.; Hsieh, M.C.; Chow, J.M.; Liu, S.H.; Chang, C.L.; Wu, S.Y. Statins improve outcomes of nonsurgical curative treatments in hepatocellular carcinoma patients. Medicine 2016, 95, e4639.
    • (2016) Medicine , vol.95
    • Wu, L.L.1    Hsieh, M.C.2    Chow, J.M.3    Liu, S.H.4    Chang, C.L.5    Wu, S.Y.6
  • 73
    • 84991687189 scopus 로고    scopus 로고
    • Inhibition of fatty acid synthesis induces apoptosis of human pancreatic cancer cells
    • Nishi, K.; Suzuki, K.; Sawamoto, J.; Tokizawa, Y.; Iwase, Y.; Yumita, N.; Ikeda, T. Inhibition of fatty acid synthesis induces apoptosis of human pancreatic cancer cells. Anticancer Res. 2016, 36, 4655–4660.
    • (2016) Anticancer Res , vol.36 , pp. 4655-4660
    • Nishi, K.1    Suzuki, K.2    Sawamoto, J.3    Tokizawa, Y.4    Iwase, Y.5    Yumita, N.6    Ikeda, T.7
  • 77
    • 0035015891 scopus 로고    scopus 로고
    • Elevated androgens and prolactin in aromatase-deficient mice cause enlargement, but not malignancy, of the prostate gland
    • McPherson, S.J.; Wang, H.; Jones, M.E.; Pedersen, J.; Iismaa, T.P.; Wreford, N.; Simpson, E.R.; Risbridger, G.P. Elevated androgens and prolactin in aromatase-deficient mice cause enlargement, but not malignancy, of the prostate gland. Endocrinology 2001, 142, 2458–2467.
    • (2001) Endocrinology , vol.142 , pp. 2458-2467
    • McPherson, S.J.1    Wang, H.2    Jones, M.E.3    Pedersen, J.4    Iismaa, T.P.5    Wreford, N.6    Simpson, E.R.7    Risbridger, G.P.8
  • 78
    • 0033836079 scopus 로고    scopus 로고
    • Overexpression of aromatase leads to development of testicular Leydig cell tumors: An in vivo model for hormone-mediated testicularcancer
    • Fowler, K.A.; Gill, K.; Kirma, N.; Dillehay, D.L.; Tekmal, R.R. Overexpression of aromatase leads to development of testicular Leydig cell tumors: An in vivo model for hormone-mediated testicularcancer. Am. J. Pathol. 2000, 156, 347–353.
    • (2000) Am. J. Pathol. , vol.156 , pp. 347-353
    • Fowler, K.A.1    Gill, K.2    Kirma, N.3    Dillehay, D.L.4    Tekmal, R.R.5
  • 79
    • 80051700986 scopus 로고    scopus 로고
    • Comparison of increased aromatase versus ERα in the generation of mammary hyperplasia and cancer
    • Diaz-Cruz, E.S.; Sugimoto, Y.; Gallicano, G.I.; Brueggemeier, R.W.; Furth, P.A. Comparison of increased aromatase versus ERα in the generation of mammary hyperplasia and cancer. Cancer Res. 2011, 71, 5477–5487.
    • (2011) Cancer Res , vol.71 , pp. 5477-5487
    • Diaz-Cruz, E.S.1    Sugimoto, Y.2    Gallicano, G.I.3    Brueggemeier, R.W.4    Furth, P.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.