메뉴 건너뛰기




Volumn 35, Issue 10, 2014, Pages 501-509

Drugging the HDAC6-HSP90 interplay in malignant cells

Author keywords

Acetylation cancer; HDAC6; HDAC6 inhibitor; HSP90 leukemia

Indexed keywords

BCR ABL PROTEIN; BETA CATENIN; CASEIN KINASE I; CASEIN KINASE II; CD133 ANTIGEN; CHEMOKINE RECEPTOR CXCR4; ENTINOSTAT; G PROTEIN COUPLED RECEPTOR KINASE 2; GLYCOGEN SYNTHASE KINASE 3BETA; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HISTONE DEACETYLASE 6; HISTONE DEACETYLASE INHIBITOR; PANOBINOSTAT; RICOLINOSTAT; TRANSCRIPTION FACTOR FOXP3; VALPROIC ACID; ANTINEOPLASTIC AGENT; HISTONE DEACETYLASE;

EID: 84907886869     PISSN: 01656147     EISSN: 18733735     Source Type: Journal    
DOI: 10.1016/j.tips.2014.08.001     Document Type: Review
Times cited : (114)

References (67)
  • 1
    • 84921425001 scopus 로고    scopus 로고
    • Erasers of histone acetylation: The histone deacetylase enzymes
    • E. Seto, and M. Yoshida Erasers of histone acetylation: the histone deacetylase enzymes Cold Spring Harb. Perspect. Biol. 6 2014 a018713
    • (2014) Cold Spring Harb. Perspect. Biol. , vol.6 , pp. 018713
    • Seto, E.1    Yoshida, M.2
  • 2
    • 80053601510 scopus 로고    scopus 로고
    • Histone/protein deacetylases control Foxp3 expression and the heat shock response of T-regulatory cells
    • U.H. Beier Histone/protein deacetylases control Foxp3 expression and the heat shock response of T-regulatory cells Curr. Opin. Immunol. 23 2011 670
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 670
    • Beier, U.H.1
  • 3
    • 77950640292 scopus 로고    scopus 로고
    • Inhibitors of HDACs - Effective drugs against cancer?
    • S. Müller, and O.H. Krämer Inhibitors of HDACs - effective drugs against cancer? Curr. Cancer Drug Targets 10 2010 210
    • (2010) Curr. Cancer Drug Targets , vol.10 , pp. 210
    • Müller, S.1    Krämer, O.H.2
  • 4
    • 84896707316 scopus 로고    scopus 로고
    • Exploiting epigenetic vulnerabilities for cancer therapeutics
    • B. Mair Exploiting epigenetic vulnerabilities for cancer therapeutics Trends Pharmacol. Sci. 35 2014 136
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 136
    • Mair, B.1
  • 5
    • 70449675089 scopus 로고    scopus 로고
    • HDAC2: A critical factor in health and disease
    • O.H. Krämer HDAC2: a critical factor in health and disease Trends Pharmacol. Sci. 30 2009 647
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 647
    • Krämer, O.H.1
  • 6
    • 84873173538 scopus 로고    scopus 로고
    • Histone deacetylase 6 plays a role as a distinct regulator of diverse cellular processes
    • Y. Li Histone deacetylase 6 plays a role as a distinct regulator of diverse cellular processes FEBS J. 280 2013 775
    • (2013) FEBS J. , vol.280 , pp. 775
    • Li, Y.1
  • 7
    • 84864961112 scopus 로고    scopus 로고
    • Development and therapeutic impact of HDAC6-selective inhibitors
    • S. Dallavalle Development and therapeutic impact of HDAC6-selective inhibitors Biochem. Pharmacol. 84 2012 756
    • (2012) Biochem. Pharmacol. , vol.84 , pp. 756
    • Dallavalle, S.1
  • 8
    • 84865266255 scopus 로고    scopus 로고
    • Modulation of histone deacetylase 6 (HDAC6) nuclear import and tubulin deacetylase activity through acetylation
    • Y. Liu Modulation of histone deacetylase 6 (HDAC6) nuclear import and tubulin deacetylase activity through acetylation J. Biol. Chem. 287 2012 29168
    • (2012) J. Biol. Chem. , vol.287 , pp. 29168
    • Liu, Y.1
  • 9
    • 79951864878 scopus 로고    scopus 로고
    • Inhibition of histone deacetylases 1 and 6 enhances cytarabine-induced apoptosis in pediatric acute myeloid leukemia cells
    • X. Xu Inhibition of histone deacetylases 1 and 6 enhances cytarabine-induced apoptosis in pediatric acute myeloid leukemia cells PLoS ONE 6 2011 0017138
    • (2011) PLoS ONE , vol.6 , pp. 0017138
    • Xu, X.1
  • 11
    • 84888841680 scopus 로고    scopus 로고
    • LC3B-II deacetylation by histone deacetylase 6 is involved in serum-starvation-induced autophagic degradation
    • K.P. Liu LC3B-II deacetylation by histone deacetylase 6 is involved in serum-starvation-induced autophagic degradation Biochem. Biophys. Res. Commun. 441 2013 970
    • (2013) Biochem. Biophys. Res. Commun. , vol.441 , pp. 970
    • Liu, K.P.1
  • 12
    • 70349300539 scopus 로고    scopus 로고
    • Heat shock protein 90 - A potential target in the treatment of human acute myelogenous leukemia
    • H. Reikvam Heat shock protein 90 - a potential target in the treatment of human acute myelogenous leukemia Curr. Cancer Drug Targets 9 2009 761
    • (2009) Curr. Cancer Drug Targets , vol.9 , pp. 761
    • Reikvam, H.1
  • 13
    • 84881222631 scopus 로고    scopus 로고
    • Inhibition of HDAC6 deacetylase activity increases its binding with microtubules and suppresses microtubule dynamic instability in MCF-7 cells
    • J. Asthana Inhibition of HDAC6 deacetylase activity increases its binding with microtubules and suppresses microtubule dynamic instability in MCF-7 cells J. Biol. Chem. 288 2013 22516
    • (2013) J. Biol. Chem. , vol.288 , pp. 22516
    • Asthana, J.1
  • 14
    • 77955355838 scopus 로고    scopus 로고
    • Rational design and simple chemistry yield a superior neuroprotective HDAC6 inhibitor, tubastatin A
    • K.V. Butler Rational design and simple chemistry yield a superior neuroprotective HDAC6 inhibitor, tubastatin A J. Am. Chem. Soc. 132 2010 10842
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10842
    • Butler, K.V.1
  • 15
    • 84860819704 scopus 로고    scopus 로고
    • Rac2-MRC-cIII-generated ROS cause genomic instability in chronic myeloid leukemia stem cells and primitive progenitors
    • M. Nieborowska-Skorska Rac2-MRC-cIII-generated ROS cause genomic instability in chronic myeloid leukemia stem cells and primitive progenitors Blood 119 2012 4253
    • (2012) Blood , vol.119 , pp. 4253
    • Nieborowska-Skorska, M.1
  • 16
    • 84861060061 scopus 로고    scopus 로고
    • Cell transformation by FLT3 ITD in acute myeloid leukemia involves oxidative inactivation of the tumor suppressor protein-tyrosine phosphatase DEP-1/PTPRJ
    • R. Godfrey Cell transformation by FLT3 ITD in acute myeloid leukemia involves oxidative inactivation of the tumor suppressor protein-tyrosine phosphatase DEP-1/PTPRJ Blood 119 2012 4499
    • (2012) Blood , vol.119 , pp. 4499
    • Godfrey, R.1
  • 17
    • 84902599844 scopus 로고    scopus 로고
    • STAT5 acetylation: Mechanisms and consequences for immunological control and leukemogenesis
    • C. Kosan STAT5 acetylation: Mechanisms and consequences for immunological control and leukemogenesis JAKSTAT 2 2013 e26102
    • (2013) JAKSTAT , vol.2 , pp. 26102
    • Kosan, C.1
  • 18
    • 80053244315 scopus 로고    scopus 로고
    • A novel small molecule deubiquitinase inhibitor blocks Jak2 signaling through Jak2 ubiquitination
    • V. Kapuria A novel small molecule deubiquitinase inhibitor blocks Jak2 signaling through Jak2 ubiquitination Cell. Signal. 23 2011 2076
    • (2011) Cell. Signal. , vol.23 , pp. 2076
    • Kapuria, V.1
  • 19
    • 73949136283 scopus 로고    scopus 로고
    • Cotreatment with panobinostat and JAK2 inhibitor TG101209 attenuates JAK2V617F levels and signaling and exerts synergistic cytotoxic effects against human myeloproliferative neoplastic cells
    • Y. Wang Cotreatment with panobinostat and JAK2 inhibitor TG101209 attenuates JAK2V617F levels and signaling and exerts synergistic cytotoxic effects against human myeloproliferative neoplastic cells Blood 114 2009 5024
    • (2009) Blood , vol.114 , pp. 5024
    • Wang, Y.1
  • 20
    • 84876149637 scopus 로고    scopus 로고
    • SIAH proteins: Critical roles in leukemogenesis
    • O.H. Krämer SIAH proteins: critical roles in leukemogenesis Leukemia 27 2012 792
    • (2012) Leukemia , vol.27 , pp. 792
    • Krämer, O.H.1
  • 21
    • 27144475816 scopus 로고    scopus 로고
    • Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors
    • C.A. Bradbury Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors Leukemia 19 2005 1751
    • (2005) Leukemia , vol.19 , pp. 1751
    • Bradbury, C.A.1
  • 22
    • 84870750886 scopus 로고    scopus 로고
    • HDAC isoenzyme expression is deregulated in chronic lymphocytic leukemia B-cells and has a complex prognostic significance
    • M. Van Damme HDAC isoenzyme expression is deregulated in chronic lymphocytic leukemia B-cells and has a complex prognostic significance Epigenetics 7 2012 1403
    • (2012) Epigenetics , vol.7 , pp. 1403
    • Van Damme, M.1
  • 23
    • 50049108874 scopus 로고    scopus 로고
    • Prognostic significance of the therapeutic targets histone deacetylase 1, 2, 6 and acetylated histone H4 in cutaneous T-cell lymphoma
    • L. Marquard Prognostic significance of the therapeutic targets histone deacetylase 1, 2, 6 and acetylated histone H4 in cutaneous T-cell lymphoma Histopathology 53 2008 267
    • (2008) Histopathology , vol.53 , pp. 267
    • Marquard, L.1
  • 24
    • 84877701677 scopus 로고    scopus 로고
    • 3-Hydroxypyridin-2-thione as novel zinc binding group for selective histone deacetylase inhibition
    • V. Patil 3-Hydroxypyridin-2-thione as novel zinc binding group for selective histone deacetylase inhibition J. Med. Chem. 56 2013 3492
    • (2013) J. Med. Chem. , vol.56 , pp. 3492
    • Patil, V.1
  • 25
    • 84874638204 scopus 로고    scopus 로고
    • Potent and selective inhibition of histone deacetylase 6 (HDAC6) does not require a surface-binding motif
    • F.F. Wagner Potent and selective inhibition of histone deacetylase 6 (HDAC6) does not require a surface-binding motif J. Med. Chem. 56 2013 1772
    • (2013) J. Med. Chem. , vol.56 , pp. 1772
    • Wagner, F.F.1
  • 26
    • 84857509386 scopus 로고    scopus 로고
    • A novel class of small molecule inhibitors of HDAC6
    • E.S. Inks A novel class of small molecule inhibitors of HDAC6 ACS Chem. Biol. 7 2012 331
    • (2012) ACS Chem. Biol. , vol.7 , pp. 331
    • Inks, E.S.1
  • 27
    • 84870024675 scopus 로고    scopus 로고
    • Selective histone deacetylase 6 inhibitors bearing substituted urea linkers inhibit melanoma cell growth
    • J.A. Bergman Selective histone deacetylase 6 inhibitors bearing substituted urea linkers inhibit melanoma cell growth J. Med. Chem. 55 2012 9891
    • (2012) J. Med. Chem. , vol.55 , pp. 9891
    • Bergman, J.A.1
  • 28
    • 84873731735 scopus 로고    scopus 로고
    • A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth
    • M. Kaliszczak A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth Br. J. Cancer 108 2013 342
    • (2013) Br. J. Cancer , vol.108 , pp. 342
    • Kaliszczak, M.1
  • 29
    • 84884631782 scopus 로고    scopus 로고
    • Development of a histone deacetylase 6 inhibitor and its biological effects
    • J.H. Lee Development of a histone deacetylase 6 inhibitor and its biological effects Proc. Natl. Acad. Sci. U.S.A. 110 2013 15704
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 15704
    • Lee, J.H.1
  • 30
    • 84862548703 scopus 로고    scopus 로고
    • HDAC6 as a target for antileukemic drugs in acute myeloid leukemia
    • B. Hackanson HDAC6 as a target for antileukemic drugs in acute myeloid leukemia Leuk. Res. 36 2012 1055
    • (2012) Leuk. Res. , vol.36 , pp. 1055
    • Hackanson, B.1
  • 31
    • 84858640254 scopus 로고    scopus 로고
    • Preclinical activity, pharmacodynamic, and pharmacokinetic properties of a selective HDAC6 inhibitor, ACY-1215, in combination with bortezomib in multiple myeloma
    • L. Santo Preclinical activity, pharmacodynamic, and pharmacokinetic properties of a selective HDAC6 inhibitor, ACY-1215, in combination with bortezomib in multiple myeloma Blood 119 2012 2579
    • (2012) Blood , vol.119 , pp. 2579
    • Santo, L.1
  • 32
    • 84877064105 scopus 로고    scopus 로고
    • Tert-Butylcarbamate-containing histone deacetylase inhibitors: Apoptosis induction, cytodifferentiation, and antiproliferative activities in cancer cells
    • S. Valente tert-Butylcarbamate-containing histone deacetylase inhibitors: apoptosis induction, cytodifferentiation, and antiproliferative activities in cancer cells ChemMedChem 8 2013 800
    • (2013) ChemMedChem , vol.8 , pp. 800
    • Valente, S.1
  • 33
    • 84875170877 scopus 로고    scopus 로고
    • Tubulin polymerization promoting protein 1 (Tppp1) phosphorylation by Rho-associated coiled-coil kinase (rock) and cyclin-dependent kinase 1 (Cdk1) inhibits microtubule dynamics to increase cell proliferation
    • A.V. Schofield Tubulin polymerization promoting protein 1 (Tppp1) phosphorylation by Rho-associated coiled-coil kinase (rock) and cyclin-dependent kinase 1 (Cdk1) inhibits microtubule dynamics to increase cell proliferation J. Biol. Chem. 288 2013 7907
    • (2013) J. Biol. Chem. , vol.288 , pp. 7907
    • Schofield, A.V.1
  • 34
    • 84857044092 scopus 로고    scopus 로고
    • Post-translational modifications of Hsp90 and their contributions to chaperone regulation
    • M. Mollapour, and L. Neckers Post-translational modifications of Hsp90 and their contributions to chaperone regulation Biochim. Biophys. Acta 3 2012 648
    • (2012) Biochim. Biophys. Acta , vol.3 , pp. 648
    • Mollapour, M.1    Neckers, L.2
  • 35
    • 84867860444 scopus 로고    scopus 로고
    • A prescription for 'stress' - The role of Hsp90 in genome stability and cellular adaptation
    • K.B. Kaplan, and R. Li A prescription for 'stress' - the role of Hsp90 in genome stability and cellular adaptation Trends Cell Biol. 22 2012 576
    • (2012) Trends Cell Biol. , vol.22 , pp. 576
    • Kaplan, K.B.1    Li, R.2
  • 36
    • 84887831548 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase (ERK) phosphorylates histone deacetylase 6 (HDAC6) at serine 1035 to stimulate cell migration
    • K.A. Williams Extracellular signal-regulated kinase (ERK) phosphorylates histone deacetylase 6 (HDAC6) at serine 1035 to stimulate cell migration J. Biol. Chem. 288 2013 33156
    • (2013) J. Biol. Chem. , vol.288 , pp. 33156
    • Williams, K.A.1
  • 37
    • 52649133274 scopus 로고    scopus 로고
    • HDAC6 inhibition enhances 17-AAG-mediated abrogation of hsp90 chaperone function in human leukemia cells
    • R. Rao HDAC6 inhibition enhances 17-AAG-mediated abrogation of hsp90 chaperone function in human leukemia cells Blood 112 2008 1886
    • (2008) Blood , vol.112 , pp. 1886
    • Rao, R.1
  • 38
    • 78650049412 scopus 로고    scopus 로고
    • Pan-histone deacetylase inhibitor panobinostat depletes CXCR4 levels and signaling and exerts synergistic antimyeloid activity in combination with CXCR4 antagonists
    • A. Mandawat Pan-histone deacetylase inhibitor panobinostat depletes CXCR4 levels and signaling and exerts synergistic antimyeloid activity in combination with CXCR4 antagonists Blood 116 2010 5306
    • (2010) Blood , vol.116 , pp. 5306
    • Mandawat, A.1
  • 39
    • 77955463320 scopus 로고    scopus 로고
    • Chemical genetic strategy identifies histone deacetylase 1 (HDAC1) and HDAC2 as therapeutic targets in sickle cell disease
    • J.E. Bradner Chemical genetic strategy identifies histone deacetylase 1 (HDAC1) and HDAC2 as therapeutic targets in sickle cell disease Proc. Natl. Acad. Sci. U.S.A. 107 2010 12617
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 12617
    • Bradner, J.E.1
  • 40
    • 82455175292 scopus 로고    scopus 로고
    • PKC alpha regulates Sendai virus-mediated interferon induction through HDAC6 and beta-catenin
    • J. Zhu PKC alpha regulates Sendai virus-mediated interferon induction through HDAC6 and beta-catenin EMBO J. 30 2011 4838
    • (2011) EMBO J. , vol.30 , pp. 4838
    • Zhu, J.1
  • 41
    • 84868099762 scopus 로고    scopus 로고
    • Regulation of CD133 by HDAC6 promotes beta-catenin signaling to suppress cancer cell differentiation
    • A.B. Mak Regulation of CD133 by HDAC6 promotes beta-catenin signaling to suppress cancer cell differentiation Cell Rep. 2 2012 951
    • (2012) Cell Rep. , vol.2 , pp. 951
    • Mak, A.B.1
  • 42
    • 84875353320 scopus 로고    scopus 로고
    • Expression of CD133 in acute leukemia
    • F.M. Tolba Expression of CD133 in acute leukemia Med. Oncol. 30 2013 013
    • (2013) Med. Oncol. , vol.30 , pp. 013
    • Tolba, F.M.1
  • 43
    • 77956525855 scopus 로고    scopus 로고
    • HDAC6 regulates mitochondrial transport in hippocampal neurons
    • S. Chen HDAC6 regulates mitochondrial transport in hippocampal neurons PLoS ONE 5 2010 0010848
    • (2010) PLoS ONE , vol.5 , pp. 0010848
    • Chen, S.1
  • 44
    • 69049106387 scopus 로고    scopus 로고
    • Anti-proliferative activity of heat shock protein (Hsp) 90 inhibitors via beta-catenin/TCF7L2 pathway in adult T cell leukemia cells
    • R. Kurashina Anti-proliferative activity of heat shock protein (Hsp) 90 inhibitors via beta-catenin/TCF7L2 pathway in adult T cell leukemia cells Cancer Lett. 284 2009 62
    • (2009) Cancer Lett. , vol.284 , pp. 62
    • Kurashina, R.1
  • 45
    • 84880046989 scopus 로고    scopus 로고
    • Tubulin polymerization promoting protein 1 (TPPP1) increases beta-catenin expression through inhibition of HDAC6 activity in U2OS osteosarcoma cells
    • A.V. Schofield Tubulin polymerization promoting protein 1 (TPPP1) increases beta-catenin expression through inhibition of HDAC6 activity in U2OS osteosarcoma cells Biochem. Biophys. Res. Commun. 436 2013 571
    • (2013) Biochem. Biophys. Res. Commun. , vol.436 , pp. 571
    • Schofield, A.V.1
  • 46
    • 79955526987 scopus 로고    scopus 로고
    • Protein kinase CK2 regulates the formation and clearance of aggresomes in response to stress
    • M. Watabe, and T. Nakaki Protein kinase CK2 regulates the formation and clearance of aggresomes in response to stress J. Cell Sci. 124 2011 1519
    • (2011) J. Cell Sci. , vol.124 , pp. 1519
    • Watabe, M.1    Nakaki, T.2
  • 47
    • 84879412911 scopus 로고    scopus 로고
    • C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances
    • P. Muller C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances Oncogene 32 2013 3101
    • (2013) Oncogene , vol.32 , pp. 3101
    • Muller, P.1
  • 48
    • 84872399759 scopus 로고    scopus 로고
    • Novel players in multiple myeloma pathogenesis: Role of protein kinases CK2 and GSK3
    • F. Piazza Novel players in multiple myeloma pathogenesis: role of protein kinases CK2 and GSK3 Leuk. Res. 37 2013 221
    • (2013) Leuk. Res. , vol.37 , pp. 221
    • Piazza, F.1
  • 49
    • 64949116576 scopus 로고    scopus 로고
    • Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity
    • Y. Han Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity Biochem. Biophys. Res. Commun. 383 2009 88
    • (2009) Biochem. Biophys. Res. Commun. , vol.383 , pp. 88
    • Han, Y.1
  • 50
    • 43049173740 scopus 로고    scopus 로고
    • MS-275, a novel histone deacetylase inhibitor with selectivity against HDAC1, induces degradation of FLT3 via inhibition of chaperone function of heat shock protein 90 in AML cells
    • C. Nishioka MS-275, a novel histone deacetylase inhibitor with selectivity against HDAC1, induces degradation of FLT3 via inhibition of chaperone function of heat shock protein 90 in AML cells Leuk. Res. 32 2008 1382
    • (2008) Leuk. Res. , vol.32 , pp. 1382
    • Nishioka, C.1
  • 51
    • 77953648655 scopus 로고    scopus 로고
    • AR-42, a novel HDAC inhibitor, exhibits biologic activity against malignant mast cell lines via down-regulation of constitutively activated Kit
    • T-Y. Lin AR-42, a novel HDAC inhibitor, exhibits biologic activity against malignant mast cell lines via down-regulation of constitutively activated Kit Blood 115 2010 4217
    • (2010) Blood , vol.115 , pp. 4217
    • Lin, T.-Y.1
  • 52
    • 49649108912 scopus 로고    scopus 로고
    • Role of acetylation and extracellular location of heat shock protein 90α in tumor cell invasion
    • Y. Yang Role of acetylation and extracellular location of heat shock protein 90α in tumor cell invasion Cancer Res. 68 2008 4833
    • (2008) Cancer Res. , vol.68 , pp. 4833
    • Yang, Y.1
  • 53
    • 84890487090 scopus 로고    scopus 로고
    • Molecular and biologic analysis of histone deacetylase inhibitors with diverse specificities
    • A. Newbold Molecular and biologic analysis of histone deacetylase inhibitors with diverse specificities Mol. Cancer Ther. 12 2013 2709
    • (2013) Mol. Cancer Ther. , vol.12 , pp. 2709
    • Newbold, A.1
  • 54
    • 34047097863 scopus 로고    scopus 로고
    • FK228 inhibits Hsp90 chaperone function in K562 cells via hyperacetylation of Hsp70
    • Y. Wang FK228 inhibits Hsp90 chaperone function in K562 cells via hyperacetylation of Hsp70 Biochem. Biophys. Res. Commun. 356 2007 998
    • (2007) Biochem. Biophys. Res. Commun. , vol.356 , pp. 998
    • Wang, Y.1
  • 55
    • 53449090857 scopus 로고    scopus 로고
    • Molecular and biologic characterization and drug sensitivity of pan-histone deacetylase inhibitor-resistant acute myeloid leukemia cells
    • W. Fiskus Molecular and biologic characterization and drug sensitivity of pan-histone deacetylase inhibitor-resistant acute myeloid leukemia cells Blood 112 2008 2896
    • (2008) Blood , vol.112 , pp. 2896
    • Fiskus, W.1
  • 56
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • C. Choudhary Lysine acetylation targets protein complexes and co-regulates major cellular functions Science 325 2009 834
    • (2009) Science , vol.325 , pp. 834
    • Choudhary, C.1
  • 57
    • 33846014703 scopus 로고    scopus 로고
    • An acetylation site in the middle domain of Hsp90 regulates chaperone function
    • B.T. Scroggins An acetylation site in the middle domain of Hsp90 regulates chaperone function Mol. Cell 25 2007 151
    • (2007) Mol. Cell , vol.25 , pp. 151
    • Scroggins, B.T.1
  • 58
    • 84857036295 scopus 로고    scopus 로고
    • A novel GRK2/HDAC6 interaction modulates cell spreading and motility
    • V. Lafarga A novel GRK2/HDAC6 interaction modulates cell spreading and motility EMBO J. 31 2012 856
    • (2012) EMBO J. , vol.31 , pp. 856
    • Lafarga, V.1
  • 59
    • 80052963807 scopus 로고    scopus 로고
    • The HTLV-1 Tax protein inhibits formation of stress granules by interacting with histone deacetylase 6
    • S. Legros The HTLV-1 Tax protein inhibits formation of stress granules by interacting with histone deacetylase 6 Oncogene 30 2011 4050
    • (2011) Oncogene , vol.30 , pp. 4050
    • Legros, S.1
  • 60
    • 84888037891 scopus 로고    scopus 로고
    • HSP90 protects the human T-cell leukemia virus type 1 (HTLV-1) tax oncoprotein from proteasomal degradation to support NF-kappaB activation and HTLV-1 replication
    • L. Gao, and E.W. Harhaj HSP90 protects the human T-cell leukemia virus type 1 (HTLV-1) tax oncoprotein from proteasomal degradation to support NF-kappaB activation and HTLV-1 replication J. Virol. 87 2013 13640
    • (2013) J. Virol. , vol.87 , pp. 13640
    • Gao, L.1    Harhaj, E.W.2
  • 61
    • 84883423841 scopus 로고    scopus 로고
    • The HDAC inhibitor LBH589 induces ERK-dependent prometaphase arrest in prostate cancer via HDAC6 inactivation and down-regulation
    • M.J. Chuang The HDAC inhibitor LBH589 induces ERK-dependent prometaphase arrest in prostate cancer via HDAC6 inactivation and down-regulation PLoS ONE 8 2013 e73401
    • (2013) PLoS ONE , vol.8 , pp. 73401
    • Chuang, M.J.1
  • 62
    • 84886739871 scopus 로고    scopus 로고
    • A novel Hsp90 inhibitor AT13387 induces senescence in EBV-positive nasopharyngeal carcinoma cells and suppresses tumor formation
    • K.C. Chan A novel Hsp90 inhibitor AT13387 induces senescence in EBV-positive nasopharyngeal carcinoma cells and suppresses tumor formation Mol. Cancer 12 2013 1476
    • (2013) Mol. Cancer , vol.12 , pp. 1476
    • Chan, K.C.1
  • 63
    • 84896702711 scopus 로고    scopus 로고
    • 4,5,6,7-Tetrahydro-isoxazolo-[4,5-c]-pyridines as a new class of cytotoxic Hsp90 inhibitors
    • R. Baruchello 4,5,6,7-Tetrahydro-isoxazolo-[4,5-c]-pyridines as a new class of cytotoxic Hsp90 inhibitors Eur. J. Med. Chem. 76 2014 53
    • (2014) Eur. J. Med. Chem. , vol.76 , pp. 53
    • Baruchello, R.1
  • 64
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • D. Hanahan, and R.A. Weinberg Hallmarks of cancer: the next generation Cell 144 2011 646
    • (2011) Cell , vol.144 , pp. 646
    • Hanahan, D.1    Weinberg, R.A.2
  • 65
    • 38949141196 scopus 로고    scopus 로고
    • Phenylalanine-containing hydroxamic acids as selective inhibitors of class IIb histone deacetylases (HDACs)
    • S. Schaefer Phenylalanine-containing hydroxamic acids as selective inhibitors of class IIb histone deacetylases (HDACs) Bioorg. Med. Chem. 16 2008 2011
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 2011
    • Schaefer, S.1
  • 66
    • 84856390338 scopus 로고    scopus 로고
    • Second-generation histone deacetylase 6 inhibitors enhance the immunosuppressive effects of Foxp3+ T-regulatory cells
    • J.H. Kalin Second-generation histone deacetylase 6 inhibitors enhance the immunosuppressive effects of Foxp3+ T-regulatory cells J. Med. Chem. 55 2012 639
    • (2012) J. Med. Chem. , vol.55 , pp. 639
    • Kalin, J.H.1
  • 67
    • 84876123648 scopus 로고    scopus 로고
    • Potent and selective HDAC6 inhibitory activity of N-(4-hydroxycarbamoylbenzyl)-1,2,4,9-tetrahydro-3-thia-9-azafluorenes as novel sulfur analogues of tubastatin A
    • V.R. De Potent and selective HDAC6 inhibitory activity of N-(4-hydroxycarbamoylbenzyl)-1,2,4,9-tetrahydro-3-thia-9-azafluorenes as novel sulfur analogues of tubastatin A Chem. Commun. (Camb) 49 2013 3775
    • (2013) Chem. Commun. (Camb) , vol.49 , pp. 3775
    • De, V.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.