메뉴 건너뛰기




Volumn 2011, Issue , 2011, Pages

Histone deacetylase inhibitors: The epigenetic therapeutics that repress hypoxia-inducible factors

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ALPHA TUBULIN; AR 42; CUDC101; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE 4; HISTONE DEACETYLASE 5; HISTONE DEACETYLASE 6; HISTONE DEACETYLASE 7; HISTONE DEACETYLASE 8; HISTONE DEACETYLASE INHIBITOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; MOCETINOSTAT; PANOBINOSTAT; PROTEIN C MYB; PROTEIN P300; ROMIDEPSIN; SIRTUIN; TRICHOSTATIN A; UNCLASSIFIED DRUG; VALPROIC ACID; VASCULOTROPIN; VORINOSTAT; BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; ENDOTHELIAL PAS DOMAIN CONTAINING PROTEIN 1; ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1; HYPOXIA INDUCIBLE FACTOR 1;

EID: 79251576774     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2011/197946     Document Type: Review
Times cited : (67)

References (170)
  • 2
    • 76349095132 scopus 로고    scopus 로고
    • Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics
    • Semenza G. L., Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics Oncogene 2010 29 5 625 634
    • (2010) Oncogene , vol.29 , Issue.5 , pp. 625-634
    • Semenza, G.L.1
  • 3
    • 62349084794 scopus 로고    scopus 로고
    • Prognostic significance of hypoxia-inducible factor 1 alpha(HIF-1alpha) expression in serous ovarian cancer: An immunohistochemical study
    • Daponte A., Ioannou M., Mylonis I., Simos G., Minas M., Messinis I. E., Koukoulis G., Prognostic significance of hypoxia-inducible factor 1 alpha(HIF-1alpha) expression in serous ovarian cancer: an immunohistochemical study BMC Cancer 2008 8, article no. 335
    • (2008) BMC Cancer , vol.8335
    • Daponte, A.1    Ioannou, M.2    Mylonis, I.3    Simos, G.4    Minas, M.5    Messinis, I.E.6    Koukoulis, G.7
  • 5
    • 33645376457 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 (HIF-1 ) correlated with tumor growth and apoptosis in ovarian cancer
    • Jiang H., Feng Y., Hypoxia-inducible factor 1 (HIF-1 ) correlated with tumor growth and apoptosis in ovarian cancer International Journal of Gynecological Cancer 2006 16 supplement 1 405 412
    • (2006) International Journal of Gynecological Cancer , vol.16 , Issue.SUPPL. 1 , pp. 405-412
    • Jiang, H.1    Feng, Y.2
  • 6
    • 2942590732 scopus 로고    scopus 로고
    • Exploiting tumour hypoxia in cancer treatment
    • Brown J. M., Wilson W. R., Exploiting tumour hypoxia in cancer treatment Nature Reviews Cancer 2004 4 6 437 447
    • (2004) Nature Reviews Cancer , vol.4 , Issue.6 , pp. 437-447
    • Brown, J.M.1    Wilson, W.R.2
  • 8
    • 4444311880 scopus 로고    scopus 로고
    • Hypoxia inducible factor-1 as a cancer drug target
    • Powis G., Kirkpatrick L., Hypoxia inducible factor-1 as a cancer drug target Molecular Cancer Therapeutics 2004 3 5 647 654
    • (2004) Molecular Cancer Therapeutics , vol.3 , Issue.5 , pp. 647-654
    • Powis, G.1    Kirkpatrick, L.2
  • 9
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza G. L., Targeting HIF-1 for cancer therapy Nature Reviews Cancer 2003 3 10 721 732
    • (2003) Nature Reviews Cancer , vol.3 , Issue.10 , pp. 721-732
    • Semenza, G.L.1
  • 10
    • 0347512126 scopus 로고    scopus 로고
    • Hypoxia inducible factor as a cancer drug target
    • Welsh S. J., Powis G., Hypoxia inducible factor as a cancer drug target Current Cancer Drug Targets 2003 3 6 391 405
    • (2003) Current Cancer Drug Targets , vol.3 , Issue.6 , pp. 391-405
    • Welsh, S.J.1    Powis, G.2
  • 13
    • 4444369682 scopus 로고    scopus 로고
    • Antitumor activity and pharmacodynamic properties of PX-478, an inhibitor of hypoxia-inducible factor-1 α
    • Welsh S., Williams R., Kirkpatrick L., Paine-Murrieta G., Powis G., Antitumor activity and pharmacodynamic properties of PX-478, an inhibitor of hypoxia-inducible factor-1 Molecular Cancer Therapeutics 2004 3 3 233 244
    • (2004) Molecular Cancer Therapeutics , vol.3 , Issue.3 , pp. 233-244
    • Welsh, S.1    Williams, R.2    Kirkpatrick, L.3    Paine-Murrieta, G.4    Powis, G.5
  • 15
    • 0041347519 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target?
    • Johnstone R. W., Licht J. D., Histone deacetylase inhibitors in cancer therapy: is transcription the primary target? Cancer Cell 2003 4 1 13 18
    • (2003) Cancer Cell , vol.4 , Issue.1 , pp. 13-18
    • Johnstone, R.W.1    Licht, J.D.2
  • 17
    • 33744963443 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF- α
    • Fath D. M., Kong X., Liang D., Lin Z., Chou A., Jiang Y., Fang J., Caro J., Sang N., Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF- Journal of Biological Chemistry 2006 281 19 13612 13619
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.19 , pp. 13612-13619
    • Fath, D.M.1    Kong, X.2    Liang, D.3    Lin, Z.4    Chou, A.5    Jiang, Y.6    Fang, J.7    Caro, J.8    Sang, N.9
  • 18
    • 33644780111 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1 α
    • Kong X., Lin Z., Liang D., Fath D., Sang N., Caro J., Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1 Molecular and Cellular Biology 2006 26 6 2019 2028
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.6 , pp. 2019-2028
    • Kong, X.1    Lin, Z.2    Liang, D.3    Fath, D.4    Sang, N.5    Caro, J.6
  • 19
    • 0034254857 scopus 로고    scopus 로고
    • NuRD and SIN3: Histone deacetylase complexes in development
    • Ahringer J., NuRD and SIN3: histone deacetylase complexes in development Trends in Genetics 2000 16 8 351 356
    • (2000) Trends in Genetics , vol.16 , Issue.8 , pp. 351-356
    • Ahringer, J.1
  • 20
    • 16244366803 scopus 로고    scopus 로고
    • Class II histone deacetylases: From sequence to function, regulation, and clinical implication
    • Yang X.-J., Grgoire S., Class II histone deacetylases: from sequence to function, regulation, and clinical implication Molecular and Cellular Biology 2005 25 8 2873 2884
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.8 , pp. 2873-2884
    • Yang, X.-J.1    Grgoire, S.2
  • 21
    • 0037382681 scopus 로고    scopus 로고
    • Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression
    • Yang X.-J., Seto E., Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression Current Opinion in Genetics and Development 2003 13 2 143 153
    • (2003) Current Opinion in Genetics and Development , vol.13 , Issue.2 , pp. 143-153
    • Yang, X.-J.1    Seto, E.2
  • 22
  • 23
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P., Pranpat M., Bradner J., Balasis M., Fiskus W., Guo F., Rocha K., Kumaraswamy S., Boyapalle S., Atadja P., Seto E., Bhalla K., Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors Journal of Biological Chemistry 2005 280 29 26729 26734
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadja, P.10    Seto, E.11    Bhalla, K.12
  • 24
    • 28644440158 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Discovery and development as anticancer agents
    • Marks P. A., Dokmanovic M., Histone deacetylase inhibitors: discovery and development as anticancer agents Expert Opinion on Investigational Drugs 2005 14 12 1497 1511
    • (2005) Expert Opinion on Investigational Drugs , vol.14 , Issue.12 , pp. 1497-1511
    • Marks, P.A.1    Dokmanovic, M.2
  • 26
    • 33748345191 scopus 로고    scopus 로고
    • Corepressors: Custom tailoring and alterations while you wait
    • Goodson M., Jonas B. A., Privalsky M. A., Corepressors: custom tailoring and alterations while you wait Nuclear Receptor Signal 2005 3, article no. e003
    • (2005) Nuclear Receptor Signal , vol.3003
    • Goodson, M.1    Jonas, B.A.2    Privalsky, M.A.3
  • 27
    • 33744792310 scopus 로고    scopus 로고
    • Sensors and signals: A coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response
    • Rosenfeld M. G., Lunyak V. V., Glass C. K., Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response Genes and Development 2006 20 11 1405 1428
    • (2006) Genes and Development , vol.20 , Issue.11 , pp. 1405-1428
    • Rosenfeld, M.G.1    Lunyak, V.V.2    Glass, C.K.3
  • 28
    • 4344685827 scopus 로고    scopus 로고
    • Expression profiling of sodium butyrate (NaB)-treated cells: Identification of regulation of genes related to cytokine signaling and cancer metastasis by NaB
    • Joseph J., Mudduluru G., Antony S., Vashistha S., Ajitkumar P., Somasundaram K., Expression profiling of sodium butyrate (NaB)-treated cells: identification of regulation of genes related to cytokine signaling and cancer metastasis by NaB Oncogene 2004 23 37 6304 6315
    • (2004) Oncogene , vol.23 , Issue.37 , pp. 6304-6315
    • Joseph, J.1    Mudduluru, G.2    Antony, S.3    Vashistha, S.4    Ajitkumar, P.5    Somasundaram, K.6
  • 29
    • 0037642133 scopus 로고    scopus 로고
    • Deacetylase activity is required for recruitment of the basal transcription machinery and transactivation by STAT5
    • Rascle A., Johnston J. A., Amati B., Deacetylase activity is required for recruitment of the basal transcription machinery and transactivation by STAT5 Molecular and Cellular Biology 2003 23 12 4162 4173
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.12 , pp. 4162-4173
    • Rascle, A.1    Johnston, J.A.2    Amati, B.3
  • 30
    • 52049102233 scopus 로고    scopus 로고
    • PTEN acetylation modulates its interaction with PDZ domain
    • Ikenoue T., Inoki K., Zhao B., Guan K.-L., PTEN acetylation modulates its interaction with PDZ domain Cancer Research 2008 68 17 6908 6912
    • (2008) Cancer Research , vol.68 , Issue.17 , pp. 6908-6912
    • Ikenoue, T.1    Inoki, K.2    Zhao, B.3    Guan, K.-L.4
  • 31
    • 35948935327 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation, and acetylationtriple threat in muscle wasting
    • Hasselgren P.-O., Ubiquitination, phosphorylation, and acetylationtriple threat in muscle wasting Journal of Cellular Physiology 2007 213 3 679 689
    • (2007) Journal of Cellular Physiology , vol.213 , Issue.3 , pp. 679-689
    • Hasselgren, P.-O.1
  • 32
    • 58149389397 scopus 로고    scopus 로고
    • HDAC4 regulates neuronal survival in normal and diseased retinas
    • Chen B., Cepko C. L., HDAC4 regulates neuronal survival in normal and diseased retinas Science 2009 323 5911 256 259
    • (2009) Science , vol.323 , Issue.5911 , pp. 256-259
    • Chen, B.1    Cepko, C.L.2
  • 36
    • 0033957792 scopus 로고    scopus 로고
    • Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway
    • Huang E. Y., Zhang J., Miska E. A., Guenther M. G., Kouzarides T., Lazar M. A., Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway Genes and Development 2000 14 1 45 54
    • (2000) Genes and Development , vol.14 , Issue.1 , pp. 45-54
    • Huang, E.Y.1    Zhang, J.2    Miska, E.A.3    Guenther, M.G.4    Kouzarides, T.5    Lazar, M.A.6
  • 44
    • 42349091446 scopus 로고    scopus 로고
    • Role of the aggresome pathway in cancer: Targeting histone deacetylase 6-dependent protein degradation
    • Rodriguez-Gonzalez A., Lin T., Ikeda A. K., Simms-Waldrip T., Fu C., Sakamoto K. M., Role of the aggresome pathway in cancer: targeting histone deacetylase 6-dependent protein degradation Cancer Research 2008 68 8 2557 2560
    • (2008) Cancer Research , vol.68 , Issue.8 , pp. 2557-2560
    • Rodriguez-Gonzalez, A.1    Lin, T.2    Ikeda, A.K.3    Simms-Waldrip, T.4    Fu, C.5    Sakamoto, K.M.6
  • 45
    • 37549026223 scopus 로고    scopus 로고
    • Localization of mouse mitochondrial SIRT proteins: Shift of SIRT3 to nucleus by co-expression with SIRT5
    • Nakamura Y., Ogura M., Tanaka D., Inagaki N., Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5 Biochemical and Biophysical Research Communications 2008 366 1 174 179
    • (2008) Biochemical and Biophysical Research Communications , vol.366 , Issue.1 , pp. 174-179
    • Nakamura, Y.1    Ogura, M.2    Tanaka, D.3    Inagaki, N.4
  • 46
    • 19344377042 scopus 로고    scopus 로고
    • Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation
    • Liou G.-G., Tanny J. C., Kruger R. G., Walz T., Moazed D., Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation Cell 2005 121 4 515 527
    • (2005) Cell , vol.121 , Issue.4 , pp. 515-527
    • Liou, G.-G.1    Tanny, J.C.2    Kruger, R.G.3    Walz, T.4    Moazed, D.5
  • 47
    • 34248151365 scopus 로고    scopus 로고
    • The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation
    • Inoue T., Hiratsuka M., Osaki M., Oshimura M., The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation Cell Cycle 2007 6 9 1011 1018
    • (2007) Cell Cycle , vol.6 , Issue.9 , pp. 1011-1018
    • Inoue, T.1    Hiratsuka, M.2    Osaki, M.3    Oshimura, M.4
  • 48
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD + -dependent tubulin deacetylase
    • North B. J., Marshall B. L., Borra M. T., Denu J. M., Verdin E., The human Sir2 ortholog, SIRT2, is an NAD + -dependent tubulin deacetylase Molecular Cell 2003 11 2 437 444
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 49
    • 34547875013 scopus 로고    scopus 로고
    • NAD + -dependent deacetylation of H4 lysine 16 by class III HDACs
    • Vaquero A., Sternglanz R., Reinberg D., NAD + -dependent deacetylation of H4 lysine 16 by class III HDACs Oncogene 2007 26 37 5505 5520
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5505-5520
    • Vaquero, A.1    Sternglanz, R.2    Reinberg, D.3
  • 51
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • Araki T., Sasaki Y., Milbrandt J., Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration Science 2004 305 5686 1010 1013
    • (2004) Science , vol.305 , Issue.5686 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 52
    • 33744942130 scopus 로고    scopus 로고
    • Tracking in the wldsthe hunting of the SIRT and the luring of the draper
    • Fainzilber M., Twiss J. L., Tracking in the wldsthe hunting of the SIRT and the luring of the draper Neuron 2006 50 6 819 821
    • (2006) Neuron , vol.50 , Issue.6 , pp. 819-821
    • Fainzilber, M.1    Twiss, J.L.2
  • 53
    • 57849096553 scopus 로고    scopus 로고
    • The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance
    • Villagra A., Cheng F., Wang H-W., The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance Nature Immunology 2008 10 92 100
    • (2008) Nature Immunology , vol.10 , pp. 92-100
    • Villagra, A.1    Cheng, F.2    Wang, H.-W.3
  • 54
    • 34547924046 scopus 로고    scopus 로고
    • HATs and HDACs: From structure, function and regulation to novel strategies for therapy and prevention
    • Yang X.-J., Seto E., HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention Oncogene 2007 26 37 5310 5318
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5310-5318
    • Yang, X.-J.1    Seto, E.2
  • 57
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • Gregoretti I. V., Lee Y.-M., Goodson H. V., Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis Journal of Molecular Biology 2004 338 1 17 31
    • (2004) Journal of Molecular Biology , vol.338 , Issue.1 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.-M.2    Goodson, H.V.3
  • 59
    • 0036479127 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel histone deacetylase HDAC10
    • Guardiola A. R., Yao T.-P., Molecular cloning and characterization of a novel histone deacetylase HDAC10 Journal of Biological Chemistry 2002 277 5 3350 3356
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3350-3356
    • Guardiola, A.R.1    Yao, T.-P.2
  • 61
    • 0037067696 scopus 로고    scopus 로고
    • Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
    • Gao L., Cueto M. A., Asselbergs F., Atadja P., Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family Journal of Biological Chemistry 2002 277 28 25748 25755
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25748-25755
    • Gao, L.1    Cueto, M.A.2    Asselbergs, F.3    Atadja, P.4
  • 63
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug
    • Marks P. A., Breslow R., Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug Nature Biotechnology 2007 25 1 84 90
    • (2007) Nature Biotechnology , vol.25 , Issue.1 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 64
    • 39749098365 scopus 로고    scopus 로고
    • Improved total synthesis of the potent HDAC inhibitor FK228 (FR-901228)
    • Greshock T. J., Johns D. M., Noguchi Y., Williams R. M., Improved total synthesis of the potent HDAC inhibitor FK228 (FR-901228) Organic Letters 2008 10 4 613 616
    • (2008) Organic Letters , vol.10 , Issue.4 , pp. 613-616
    • Greshock, T.J.1    Johns, D.M.2    Noguchi, Y.3    Williams, R.M.4
  • 65
    • 25144445798 scopus 로고    scopus 로고
    • Trichostatin a (TSA) sensitizes the human prostatic cancer cell line DU145 to death receptor ligands treatment
    • Taghiyev A. F., Guseva N. V., Sturm M. T., Rokhlin O. W., Cohen M. B., Trichostatin a (TSA) sensitizes the human prostatic cancer cell line DU145 to death receptor ligands treatment Cancer Biology and Therapy 2005 4 4 382 390
    • (2005) Cancer Biology and Therapy , vol.4 , Issue.4 , pp. 382-390
    • Taghiyev, A.F.1    Guseva, N.V.2    Sturm, M.T.3    Rokhlin, O.W.4    Cohen, M.B.5
  • 66
    • 0034901985 scopus 로고    scopus 로고
    • Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo
    • Vigushin D. M., Ali S., Pace P. E., Mirsaidi N., Ito K., Adcock I., Coombes R. C., Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo Clinical Cancer Research 2001 7 4 971 976
    • (2001) Clinical Cancer Research , vol.7 , Issue.4 , pp. 971-976
    • Vigushin, D.M.1    Ali, S.2    Pace, P.E.3    Mirsaidi, N.4    Ito, K.5    Adcock, I.6    Coombes, R.C.7
  • 69
    • 0033233243 scopus 로고    scopus 로고
    • Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1
    • Semenza G. L., Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1 Annual Review of Cell and Developmental Biology 1999 15 551 578
    • (1999) Annual Review of Cell and Developmental Biology , vol.15 , pp. 551-578
    • Semenza, G.L.1
  • 70
    • 0033991530 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor 1: Mechanisms and consequences
    • Semenza G. L., Expression of hypoxia-inducible factor 1: mechanisms and consequences Biochemical Pharmacology 2000 59 1 47 53
    • (2000) Biochemical Pharmacology , vol.59 , Issue.1 , pp. 47-53
    • Semenza, G.L.1
  • 71
    • 35848938945 scopus 로고    scopus 로고
    • The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1 and HIF-2 α
    • Hu C.-J., Sataur A., Wang L., Chen H., Simon M. C., The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1 and HIF-2 Molecular Biology of the Cell 2007 18 11 4528 4542
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.11 , pp. 4528-4542
    • Hu, C.-J.1    Sataur, A.2    Wang, L.3    Chen, H.4    Simon, M.C.5
  • 72
    • 0345491599 scopus 로고    scopus 로고
    • Differential roles of hypoxia-inducible factor 1 (HIF-1 ) and HIF-2 in hypoxic gene regulation
    • Hu C.-J., Wang L.-Y., Chodosh L. A., Keith B., Simon M. C., Differential roles of hypoxia-inducible factor 1 (HIF-1 ) and HIF-2 in hypoxic gene regulation Molecular and Cellular Biology 2003 23 24 9361 9374
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.24 , pp. 9361-9374
    • Hu, C.-J.1    Wang, L.-Y.2    Chodosh, L.A.3    Keith, B.4    Simon, M.C.5
  • 73
    • 33745685879 scopus 로고    scopus 로고
    • Role of hypoxia-inducible factor (HIF)-1 versus HIF-2 in the regulation of HIF target genes in response to hypoxia, insulin-like growth factor-I, or loss of von Hippel-Lindau function: Implications for targeting the HIF pathway
    • Carroll V. A., Ashcroft M., Role of hypoxia-inducible factor (HIF)-1 versus HIF-2 in the regulation of HIF target genes in response to hypoxia, insulin-like growth factor-I, or loss of von Hippel-Lindau function: implications for targeting the HIF pathway Cancer Research 2006 66 12 6264 6270
    • (2006) Cancer Research , vol.66 , Issue.12 , pp. 6264-6270
    • Carroll, V.A.1    Ashcroft, M.2
  • 74
    • 33846879810 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein and clear cell renal carcinoma
    • Kaelin W. G. Jr., The von Hippel-Lindau tumor suppressor protein and clear cell renal carcinoma Clinical Cancer Research 2007 13 2 680s 684s
    • (2007) Clinical Cancer Research , vol.13 , Issue.2
    • Kaelin Jr., W.G.1
  • 75
    • 34547124062 scopus 로고    scopus 로고
    • Hypoxia: A key regulator of angiogenesis in cancer
    • Liao D., Johnson R. S., Hypoxia: a key regulator of angiogenesis in cancer Cancer and Metastasis Reviews 2007 26 2 281 290
    • (2007) Cancer and Metastasis Reviews , vol.26 , Issue.2 , pp. 281-290
    • Liao, D.1    Johnson, R.S.2
  • 76
    • 13244284943 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 is associated with angiogenesis, and expression of bFGF, PDGF-BB, and EGFR in invasive breast cancer
    • Bos R., Van Diest P. J., De Jong J. S., Van Der Groep P., Van Der Valk P., Van Der Wall E., Hypoxia-inducible factor-1 is associated with angiogenesis, and expression of bFGF, PDGF-BB, and EGFR in invasive breast cancer Histopathology 2005 46 1 31 36
    • (2005) Histopathology , vol.46 , Issue.1 , pp. 31-36
    • Bos, R.1    Van Diest, P.J.2    De Jong, J.S.3    Van Der Groep, P.4    Van Der Valk, P.5    Van Der Wall, E.6
  • 77
    • 33645504221 scopus 로고    scopus 로고
    • Hypoxic induction of an HIF-1 -dependent bFGF autocrine loop drives angiogenesis in human endothelial cells
    • Calvani M., Rapisarda A., Uranchimeg B., Shoemaker R. H., Melillo G., Hypoxic induction of an HIF-1 -dependent bFGF autocrine loop drives angiogenesis in human endothelial cells Blood 2006 107 7 2705 2712
    • (2006) Blood , vol.107 , Issue.7 , pp. 2705-2712
    • Calvani, M.1    Rapisarda, A.2    Uranchimeg, B.3    Shoemaker, R.H.4    Melillo, G.5
  • 78
    • 27544477748 scopus 로고    scopus 로고
    • The von Hippel-Lindau protein, HIF hydroxylation, and oxygen sensing
    • Kaelin W. G. Jr., The von Hippel-Lindau protein, HIF hydroxylation, and oxygen sensing Biochemical and Biophysical Research Communications 2005 338 1 627 628
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 627-628
    • Kaelin Jr., W.G.1
  • 79
    • 0037337763 scopus 로고    scopus 로고
    • Oxygen-dependent regulation of hypoxia-inducible factors by prolyl and asparaginyl hydroxylation
    • Lando D., Gorman J. J., Whitelaw M. L., Peet D. J., Oxygen-dependent regulation of hypoxia-inducible factors by prolyl and asparaginyl hydroxylation European Journal of Biochemistry 2003 270 5 781 790
    • (2003) European Journal of Biochemistry , vol.270 , Issue.5 , pp. 781-790
    • Lando, D.1    Gorman, J.J.2    Whitelaw, M.L.3    Peet, D.J.4
  • 80
    • 8344237449 scopus 로고    scopus 로고
    • Hydroxylation of HIF-1: Oxygen sensing at the molecular level
    • Semenza G. L., Hydroxylation of HIF-1: oxygen sensing at the molecular level Physiology 2004 19 4 176 182
    • (2004) Physiology , vol.19 , Issue.4 , pp. 176-182
    • Semenza, G.L.1
  • 82
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 (HIF-1 ) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
    • Salceda S., Caro J., Hypoxia-inducible factor 1 (HIF-1 ) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes Journal of Biological Chemistry 1997 272 36 22642 22647
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.36 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 84
    • 0033986948 scopus 로고    scopus 로고
    • Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia, inducible factor 1 α
    • Carrero P., Okamoto K., Coumailleau P., O'Brien S. A., Tanaka H., Poellinger L., Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia, inducible factor 1 Molecular and Cellular Biology 2000 20 1 402 415
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.1 , pp. 402-415
    • Carrero, P.1    Okamoto, K.2    Coumailleau, P.3    O'Brien, S.A.4    Tanaka, H.5    Poellinger, L.6
  • 85
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch
    • Lando D., Peet D. J., Whelan D. A., Gorman J. J., Whitelaw M. L., Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch Science 2002 295 5556 858 861
    • (2002) Science , vol.295 , Issue.5556 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 86
    • 0036232662 scopus 로고    scopus 로고
    • Carboxyl-terminal transactivation activity of hypoxia-inducible factor 1 is governed by a von Hippel-Lindau protein-independent, hydroxylation-regulated association with p300/CBP
    • Sang N., Fang J., Srinivas V., Leshchinsky I., Caro J., Carboxyl-terminal transactivation activity of hypoxia-inducible factor 1 is governed by a von Hippel-Lindau protein-independent, hydroxylation-regulated association with p300/CBP Molecular and Cellular Biology 2002 22 9 2984 2992
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.9 , pp. 2984-2992
    • Sang, N.1    Fang, J.2    Srinivas, V.3    Leshchinsky, I.4    Caro, J.5
  • 89
    • 77958478353 scopus 로고    scopus 로고
    • Nitrogen anabolism underlies the importance of glutaminolysis in proliferating cells
    • Meng M., Chen S., Lao T., Liang D., Sang N., Nitrogen anabolism underlies the importance of glutaminolysis in proliferating cells Cell Cycle 2010 9 19 3921 3932
    • (2010) Cell Cycle , vol.9 , Issue.19 , pp. 3921-3932
    • Meng, M.1    Chen, S.2    Lao, T.3    Liang, D.4    Sang, N.5
  • 90
    • 2342661143 scopus 로고    scopus 로고
    • Intratumoral hypoxia, radiation resistance, and HIF-1
    • Semenza G. L., Intratumoral hypoxia, radiation resistance, and HIF-1 Cancer Cell 2004 5 5 405 406
    • (2004) Cancer Cell , vol.5 , Issue.5 , pp. 405-406
    • Semenza, G.L.1
  • 91
    • 33645786505 scopus 로고    scopus 로고
    • Development of novel therapeutic strategies that target HIF-1
    • Semenza G. L., Development of novel therapeutic strategies that target HIF-1 Expert Opinion on Therapeutic Targets 2006 10 2 267 280
    • (2006) Expert Opinion on Therapeutic Targets , vol.10 , Issue.2 , pp. 267-280
    • Semenza, G.L.1
  • 92
    • 0034654174 scopus 로고    scopus 로고
    • Modulation of hypoxia-inducible factor 1 expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: Implications for tumor angiogenesis and therapeutics
    • Zhong H., Chiles K., Feldser D., Laughner E., Hanrahan C., Georgescu M.-M., Simons J. W., Semenza G. L., Modulation of hypoxia-inducible factor 1 expression by the epidermal growth factor/phosphatidylinositol 3-kinase/PTEN/AKT/FRAP pathway in human prostate cancer cells: implications for tumor angiogenesis and therapeutics Cancer Research 2000 60 6 1541 1545
    • (2000) Cancer Research , vol.60 , Issue.6 , pp. 1541-1545
    • Zhong, H.1    Chiles, K.2    Feldser, D.3    Laughner, E.4    Hanrahan, C.5    Georgescu, M.-M.6    Simons, J.W.7    Semenza, G.L.8
  • 93
    • 34447506424 scopus 로고    scopus 로고
    • Detection and characterization of tumor hypoxia using pO 2 histography
    • Vaupel P., Hckel M., Mayer A., Detection and characterization of tumor hypoxia using pO 2 histography Antioxidants and Redox Signaling 2007 9 8 1221 1235
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.8 , pp. 1221-1235
    • Vaupel, P.1    Hckel, M.2    Mayer, A.3
  • 94
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1 is required for solid tumor formation and embryonic vascularization
    • Ryan H. E., Lo J., Johnson R. S., HIF-1 is required for solid tumor formation and embryonic vascularization EMBO Journal 1998 17 11 3005 3015
    • (1998) EMBO Journal , vol.17 , Issue.11 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 97
    • 34447103275 scopus 로고    scopus 로고
    • Targeting tumor stroma and exploiting mature tumor vasculature to improve anti-cancer drug delivery
    • Bouzin C., Feron O., Targeting tumor stroma and exploiting mature tumor vasculature to improve anti-cancer drug delivery Drug Resistance Updates 2007 10 3 109 120
    • (2007) Drug Resistance Updates , vol.10 , Issue.3 , pp. 109-120
    • Bouzin, C.1    Feron, O.2
  • 98
    • 30444442692 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor activity in endothelial cells disrupts embryonic cardiovascular development
    • Licht A. H., Mller-Holtkamp F., Flamme I., Breier G., Inhibition of hypoxia-inducible factor activity in endothelial cells disrupts embryonic cardiovascular development Blood 2006 107 2 584 590
    • (2006) Blood , vol.107 , Issue.2 , pp. 584-590
    • Licht, A.H.1    Mller-Holtkamp, F.2    Flamme, I.3    Breier, G.4
  • 107
    • 14344264703 scopus 로고    scopus 로고
    • Heat-shock protein 90 inhibitors as novel cancer chemotherapeuticsan update
    • Neckers L., Neckers K., Heat-shock protein 90 inhibitors as novel cancer chemotherapeuticsan update Expert Opinion on Emerging Drugs 2005 10 1 137 149
    • (2005) Expert Opinion on Emerging Drugs , vol.10 , Issue.1 , pp. 137-149
    • Neckers, L.1    Neckers, K.2
  • 108
    • 15544385359 scopus 로고    scopus 로고
    • Hsp90 inhibitor geldanamycin and its derivatives as novel cancer chemotherapeutic agents
    • Miyata Y., Hsp90 inhibitor geldanamycin and its derivatives as novel cancer chemotherapeutic agents Current Pharmaceutical Design 2005 11 9 1131 1138
    • (2005) Current Pharmaceutical Design , vol.11 , Issue.9 , pp. 1131-1138
    • Miyata, Y.1
  • 109
    • 33645731530 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system stress sensitizes ovarian cancer to proteasome inhibitor-induced apoptosis
    • Bazzaro M., Lee M. K., Zoso A., Stirling W. L. H., Santillan A., Shih I.-M., Roden R. B. S., Ubiquitin-proteasome system stress sensitizes ovarian cancer to proteasome inhibitor-induced apoptosis Cancer Research 2006 66 7 3754 3763
    • (2006) Cancer Research , vol.66 , Issue.7 , pp. 3754-3763
    • Bazzaro, M.1    Lee, M.K.2    Zoso, A.3    Stirling, W.L.H.4    Santillan, A.5    Shih, I.-M.6    Roden, R.B.S.7
  • 112
    • 0034902354 scopus 로고    scopus 로고
    • Novel proteasome inhibitor PS-341 inhibits activation of nuclear factor- B, cell survival, tumor growth, and angiogenesis in squamous cell carcinoma
    • Sunwoo J. B., Chen Z., Dong G., Yeh N., Bancroft C. C., Sausville E., Adams J., Elliott P., Van Waes C., Novel proteasome inhibitor PS-341 inhibits activation of nuclear factor- B, cell survival, tumor growth, and angiogenesis in squamous cell carcinoma Clinical Cancer Research 2001 7 5 1419 1428
    • (2001) Clinical Cancer Research , vol.7 , Issue.5 , pp. 1419-1428
    • Sunwoo, J.B.1    Chen, Z.2    Dong, G.3    Yeh, N.4    Bancroft, C.C.5    Sausville, E.6    Adams, J.7    Elliott, P.8    Van Waes, C.9
  • 113
    • 25444465116 scopus 로고    scopus 로고
    • Both microtubule-stabilizing and microtubule-destabilizing drugs inhibit hypoxia-inducible factor-1 accumulation and activity by disrupting microtubule function
    • Escuin D., Kline E. R., Giannakakou P., Both microtubule-stabilizing and microtubule-destabilizing drugs inhibit hypoxia-inducible factor-1 accumulation and activity by disrupting microtubule function Cancer Research 2005 65 19 9021 9028
    • (2005) Cancer Research , vol.65 , Issue.19 , pp. 9021-9028
    • Escuin, D.1    Kline, E.R.2    Giannakakou, P.3
  • 115
    • 33646829811 scopus 로고    scopus 로고
    • Noscapine inhibits hypoxia-mediated HIF-1alpha expression andangiogenesis in vitro: A novel function for an old drug
    • Newcomb E. W., Lukyanov Y., Schnee T., Ali M. A., Lan L., Zagzag D., Noscapine inhibits hypoxia-mediated HIF-1alpha expression andangiogenesis in vitro: a novel function for an old drug International Journal of Oncology 2006 28 5 1121 1130
    • (2006) International Journal of Oncology , vol.28 , Issue.5 , pp. 1121-1130
    • Newcomb, E.W.1    Lukyanov, Y.2    Schnee, T.3    Ali, M.A.4    Lan, L.5    Zagzag, D.6
  • 116
    • 33749006252 scopus 로고    scopus 로고
    • Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1 α
    • Qian D. Z., Kachhap S. K., Collis S. J., Verheul H. M.W., Carducci M. A., Atadja P., Pili R., Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1 Cancer Research 2006 66 17 8814 8821
    • (2006) Cancer Research , vol.66 , Issue.17 , pp. 8814-8821
    • Qian, D.Z.1    Kachhap, S.K.2    Collis, S.J.3    Verheul, H.M.W.4    Carducci, M.A.5    Atadja, P.6    Pili, R.7
  • 117
    • 4744368147 scopus 로고    scopus 로고
    • Histone deacetylase 7 associates with hypoxia-inducible factor 1 and increases transcriptional activity
    • Kato H., Tamamizu-Kato S., Shibasaki F., Histone deacetylase 7 associates with hypoxia-inducible factor 1 and increases transcriptional activity Journal of Biological Chemistry 2004 279 40 41966 41974
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 41966-41974
    • Kato, H.1    Tamamizu-Kato, S.2    Shibasaki, F.3
  • 119
    • 24344502368 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-dependent histone deacetylase activity determines stem cell fate in the placenta
    • Maltepe E., Krampitz G. W., Okazaki K. M., Red-Horse K., Mak W., Simon M. C., Fisher S. J., Hypoxia-inducible factor-dependent histone deacetylase activity determines stem cell fate in the placenta Development 2005 132 15 3393 3403
    • (2005) Development , vol.132 , Issue.15 , pp. 3393-3403
    • Maltepe, E.1    Krampitz, G.W.2    Okazaki, K.M.3    Red-Horse, K.4    Mak, W.5    Simon, M.C.6    Fisher, S.J.7
  • 121
    • 0042261694 scopus 로고    scopus 로고
    • Antitumor efficacy of FK228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors
    • Sasakawa Y., Naoe Y., Noto T., Inoue T., Sasakawa T., Matsuo M., Manda T., Mutoh S., Antitumor efficacy of FK228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors Biochemical Pharmacology 2003 66 6 897 906
    • (2003) Biochemical Pharmacology , vol.66 , Issue.6 , pp. 897-906
    • Sasakawa, Y.1    Naoe, Y.2    Noto, T.3    Inoue, T.4    Sasakawa, T.5    Matsuo, M.6    Manda, T.7    Mutoh, S.8
  • 123
    • 34248151365 scopus 로고    scopus 로고
    • The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation
    • Inoue T., Hiratsuka M., Osaki M., Oshimura M., The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation Cell Cycle 2007 6 9 1011 1018
    • (2007) Cell Cycle , vol.6 , Issue.9 , pp. 1011-1018
    • Inoue, T.1    Hiratsuka, M.2    Osaki, M.3    Oshimura, M.4
  • 126
  • 127
    • 34249946937 scopus 로고    scopus 로고
    • Inhibition of hypoxia-induced angiogenesis by sodium butyrate, a histone deacetylase inhibitor, through hypoxia-inducible factor-1alpha suppression
    • Kim S. H., Kim K. W., Jeong J. W., Inhibition of hypoxia-induced angiogenesis by sodium butyrate, a histone deacetylase inhibitor, through hypoxia-inducible factor-1alpha suppression Oncology Report 2007 17 4 793 797
    • (2007) Oncology Report , vol.17 , Issue.4 , pp. 793-797
    • Kim, S.H.1    Kim, K.W.2    Jeong, J.W.3
  • 130
    • 31144440795 scopus 로고    scopus 로고
    • Mammalian gene expression program resiliency: The roles of multiple coactivator mechanisms in hypoxia-responsive transcription
    • Kasper L. H., Brindle P. K., Mammalian gene expression program resiliency: the roles of multiple coactivator mechanisms in hypoxia-responsive transcription Cell Cycle 2006 5 2 142 146
    • (2006) Cell Cycle , vol.5 , Issue.2 , pp. 142-146
    • Kasper, L.H.1    Brindle, P.K.2
  • 131
    • 33947217916 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation
    • Stiehl D. P., Fath D. M., Liang D., Jiang Y., Sang N., Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation Cancer Research 2007 67 5 2256 2264
    • (2007) Cancer Research , vol.67 , Issue.5 , pp. 2256-2264
    • Stiehl, D.P.1    Fath, D.M.2    Liang, D.3    Jiang, Y.4    Sang, N.5
  • 135
    • 0033964512 scopus 로고    scopus 로고
    • P300 Collaborates with Sp1 and Sp3 in p21(waf1/cip1) promoter activation induced by histone deacetylase inhibitor
    • Xiao H., Hasegawa T., Isobe K.-I., p300 Collaborates with Sp1 and Sp3 in p21(waf1/cip1) promoter activation induced by histone deacetylase inhibitor Journal of Biological Chemistry 2000 275 2 1371 1376
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 1371-1376
    • Xiao, H.1    Hasegawa, T.2    Isobe, K.-I.3
  • 136
    • 77449159578 scopus 로고    scopus 로고
    • Complex regulation of the transactivation function of hypoxia-inducible factor-1 by direct interaction with two distinct domains of the creb-binding protein/p300
    • Ruas J. L., Berchner-Pfannschmidt U., Malik S., Gradin K., Fandrey J., Roeder R. G., Pereira T., Poellinger L., Complex regulation of the transactivation function of hypoxia-inducible factor-1 by direct interaction with two distinct domains of the creb-binding protein/p300 Journal of Biological Chemistry 2010 285 4 2601 2609
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.4 , pp. 2601-2609
    • Ruas, J.L.1    Berchner-Pfannschmidt, U.2    Malik, S.3    Gradin, K.4    Fandrey, J.5    Roeder, R.G.6    Pereira, T.7    Poellinger, L.8
  • 137
    • 33751249589 scopus 로고    scopus 로고
    • Effects of histone deacetylase inhibitors on HIF-1
    • Liang D., Kong X., Sang N., Effects of histone deacetylase inhibitors on HIF-1 Cell Cycle 2006 5 21 2430 2435
    • (2006) Cell Cycle , vol.5 , Issue.21 , pp. 2430-2435
    • Liang, D.1    Kong, X.2    Sang, N.3
  • 138
    • 38649092744 scopus 로고    scopus 로고
    • Regulation of protein turnover by acetyltransferases and deacetylases
    • Sadoul K., Boyault C., Pabion M., Khochbin S., Regulation of protein turnover by acetyltransferases and deacetylases Biochimie 2008 90 2 306 312
    • (2008) Biochimie , vol.90 , Issue.2 , pp. 306-312
    • Sadoul, K.1    Boyault, C.2    Pabion, M.3    Khochbin, S.4
  • 139
    • 17844385784 scopus 로고    scopus 로고
    • Regulatory cross-talk between lysine acetylation and ubiquitination: Role in the control of protein stability
    • Caron C., Boyault C., Khochbin S., Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability BioEssays 2005 27 4 408 415
    • (2005) BioEssays , vol.27 , Issue.4 , pp. 408-415
    • Caron, C.1    Boyault, C.2    Khochbin, S.3
  • 141
    • 24744460523 scopus 로고    scopus 로고
    • Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1 and is not induced by hypoxia or HIF
    • Bilton R., Mazure N., Trottier E., Hattab M., Dry M.-A., Richard D. E., Pouyssgur J., Brahimi-Horn M. C., Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1 and is not induced by hypoxia or HIF Journal of Biological Chemistry 2005 280 35 31132 31140
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.35 , pp. 31132-31140
    • Bilton, R.1    Mazure, N.2    Trottier, E.3    Hattab, M.4    Dry, M.-A.5    Richard, D.E.6    Pouyssgur, J.7    Brahimi-Horn, M.C.8
  • 142
    • 20544431636 scopus 로고    scopus 로고
    • Analysis of ARD1 function in hypoxia response using retroviral RNA interference
    • Fisher T. S., Des Etages S., Hayes L., Crimin K., Li B., Analysis of ARD1 function in hypoxia response using retroviral RNA interference Journal of Biological Chemistry 2005 280 18 17749 17757
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 17749-17757
    • Fisher, T.S.1    Des Etages, S.2    Hayes, L.3    Crimin, K.4    Li, B.5
  • 143
    • 33645236747 scopus 로고    scopus 로고
    • Purified recombinant hARD1 does not catalyse acetylation of Lys 532 of HIF-1 fragments in vitro
    • Murray-Rust T. A., Oldham N. J., Hewitson K. S., Schofield C. J., Purified recombinant hARD1 does not catalyse acetylation of Lys 532 of HIF-1 fragments in vitro FEBS Letters 2006 580 8 1911 1918
    • (2006) FEBS Letters , vol.580 , Issue.8 , pp. 1911-1918
    • Murray-Rust, T.A.1    Oldham, N.J.2    Hewitson, K.S.3    Schofield, C.J.4
  • 145
    • 33746491112 scopus 로고    scopus 로고
    • Characterization of the native and fibrillar conformation of the human nalpha-acetyltransferase ard1
    • Sanchez-Puig N., Fersht A. R., Characterization of the native and fibrillar conformation of the human nalpha-acetyltransferase ard1 Protein Science 2006 15 8 1968 1976
    • (2006) Protein Science , vol.15 , Issue.8 , pp. 1968-1976
    • Sanchez-Puig, N.1    Fersht, A.R.2
  • 150
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1
    • Dioum E. M., Chen R., Alexander M. S., Zhang Q., Hogg R. T., Gerard R. D., Garcia J. A., Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1 Science 2009 324 5932 1289 1293
    • (2009) Science , vol.324 , Issue.5932 , pp. 1289-1293
    • Dioum, E.M.1    Chen, R.2    Alexander, M.S.3    Zhang, Q.4    Hogg, R.T.5    Gerard, R.D.6    Garcia, J.A.7
  • 151
    • 77950473770 scopus 로고    scopus 로고
    • Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1 but not HIF-2 α
    • Luo W., Zhong J., Chang R., Hu H., Pandey A., Semenza G. L., Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1 but not HIF-2 Journal of Biological Chemistry 2010 285 6 3651 3663
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.6 , pp. 3651-3663
    • Luo, W.1    Zhong, J.2    Chang, R.3    Hu, H.4    Pandey, A.5    Semenza, G.L.6
  • 152
    • 0022412036 scopus 로고
    • Further characterization of the phenotype of ts20, a DNA(ts) mutant of BALB/3T3 cells
    • Zeng G.-C., Ozer H. L., Hand R., Further characterization of the phenotype of ts20, a DNA(ts) mutant of BALB/3T3 cells Experimental Cell Research 1985 160 1 184 196
    • (1985) Experimental Cell Research , vol.160 , Issue.1 , pp. 184-196
    • Zeng, G.-C.1    Ozer, H.L.2    Hand, R.3
  • 153
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 and Co.a holding for folding
    • Buchner J., Hsp90 and Co.a holding for folding Trends in Biochemical Sciences 1999 24 4 136 141
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.4 , pp. 136-141
    • Buchner, J.1
  • 155
    • 0042885973 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex as a novel target for cancer therapy
    • Goetz M. P., Toft D. O., Ames M. M., Erlichman C., The Hsp90 chaperone complex as a novel target for cancer therapy Annals of Oncology 2003 14 8 1169 1176
    • (2003) Annals of Oncology , vol.14 , Issue.8 , pp. 1169-1176
    • Goetz, M.P.1    Toft, D.O.2    Ames, M.M.3    Erlichman, C.4
  • 156
    • 73249149751 scopus 로고    scopus 로고
    • HDAC6 regulates androgen receptor hypersensitivity and nuclear localization via modulating Hsp90 acetylation in castration-resistant prostate cancer
    • Ai J., Wang Y., Dar J. A., Liu J., Liu L., Nelson J. B., Wang Z., HDAC6 regulates androgen receptor hypersensitivity and nuclear localization via modulating Hsp90 acetylation in castration-resistant prostate cancer Molecular Endocrinology 2009 23 12 1963 1972
    • (2009) Molecular Endocrinology , vol.23 , Issue.12 , pp. 1963-1972
    • Ai, J.1    Wang, Y.2    Dar, J.A.3    Liu, J.4    Liu, L.5    Nelson, J.B.6    Wang, Z.7
  • 157
    • 65549166880 scopus 로고    scopus 로고
    • HDAC6 modulates Hsp90 chaperone activity and regulates activation of aryl hydrocarbon receptor signaling
    • Kekatpure V. D., Dannenberg A. J., Subbaramaiah K., HDAC6 modulates Hsp90 chaperone activity and regulates activation of aryl hydrocarbon receptor signaling Journal of Biological Chemistry 2009 284 12 7436 7445
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.12 , pp. 7436-7445
    • Kekatpure, V.D.1    Dannenberg, A.J.2    Subbaramaiah, K.3
  • 158
    • 55749097776 scopus 로고    scopus 로고
    • Genistein down-regulates androgen receptor by modulating HDAC6-Hsp90 chaperone function
    • Basak S., Pookot D., Noonan E. J., Dahiya R., Genistein down-regulates androgen receptor by modulating HDAC6-Hsp90 chaperone function Molecular Cancer Therapeutics 2008 7 10 3195 3202
    • (2008) Molecular Cancer Therapeutics , vol.7 , Issue.10 , pp. 3195-3202
    • Basak, S.1    Pookot, D.2    Noonan, E.J.3    Dahiya, R.4
  • 161
    • 0021993649 scopus 로고
    • Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine
    • L'Hernault S. W., Rosenbaum J. L., Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine Biochemistry 1985 24 2 473 478
    • (1985) Biochemistry , vol.24 , Issue.2 , pp. 473-478
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 162
    • 0022452231 scopus 로고
    • The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules
    • Maruta H., Greer K., Rosenbaum J. L., The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules Journal of Cell Biology 1986 103 2 571 579
    • (1986) Journal of Cell Biology , vol.103 , Issue.2 , pp. 571-579
    • Maruta, H.1    Greer, K.2    Rosenbaum, J.L.3
  • 164
    • 34547684065 scopus 로고    scopus 로고
    • HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
    • Boyault C., Sadoul K., Pabion M., Khochbin S., HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination Oncogene 2007 26 37 5468 5476
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5468-5476
    • Boyault, C.1    Sadoul, K.2    Pabion, M.3    Khochbin, S.4
  • 166
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha
    • Lim J. H., Lee Y. M., Chun Y. S., Chen J., Kim J. E., Park J. W., Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha Molecular cell 2010 38 6 864 878
    • (2010) Molecular Cell , vol.38 , Issue.6 , pp. 864-878
    • Lim, J.H.1    Lee, Y.M.2    Chun, Y.S.3    Chen, J.4    Kim, J.E.5    Park, J.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.