메뉴 건너뛰기




Volumn 31, Issue 1, 2011, Pages 10-19

Hydroxamic acids (therapeutics and mechanism): Chemistry, acyl nitroso, nitroxyl, reactive oxygen species, and cell signaling

Author keywords

Anticancer; Cell signaling; Hydroxamic acid; Reactive oxygen species

Indexed keywords

ANTINEOPLASTIC AGENT; BORTEZOMIB; HYDROXAMIC ACID DERIVATIVE; HYDROXYLAMINE; IMATINIB; NITRIC OXIDE; NITROSOBENZENE; REACTIVE OXYGEN METABOLITE; RITUXIMAB; SUBEROYL ANILIDE HYDROXAMIC ACID; UNCLASSIFIED DRUG; VORINOSTAT;

EID: 78649289537     PISSN: 10799893     EISSN: 15324281     Source Type: Journal    
DOI: 10.3109/10799893.2010.497152     Document Type: Review
Times cited : (21)

References (113)
  • 1
    • 72049117055 scopus 로고    scopus 로고
    • Dermal toxicity and environmental contamination: Electron transfer reactive oxygen species oxidative stress cell signaling and protection by antioxidants
    • Kovacic P, Somanathan R. Dermal toxicity and environmental contamination: electron transfer, reactive oxygen species, oxidative stress, cell signaling, and protection by antioxidants. Rev Environ Contam Toxicol 2010, 203, 119-138.
    • (2010) Rev. Environ. Contam. Toxicol. , vol.203 , pp. 119-138
    • Kovacic, P.1    Somanathan, R.2
  • 2
    • 34249056853 scopus 로고    scopus 로고
    • Development of new transition metal catalysts for the oxidation of a hydroxamic acid with in situ diels-Alder trapping of the acyl nitroso derivative
    • Howard JA, Ilyashenko G, Sparkes HA, Whiting A. Development of new transition metal catalysts for the oxidation of a hydroxamic acid with in situ Diels-Alder trapping of the acyl nitroso derivative. Dalton Trans 2007, 21, 2108-2111.
    • (2007) Dalton. Trans. , vol.21 , pp. 2108-2111
    • Howard, J.A.1    Ilyashenko, G.2    Sparkes, H.A.3    Whiting, A.4
  • 3
    • 0037433245 scopus 로고    scopus 로고
    • Direct observation of an acyl nitroso species in solution by time-resolved IR spectrocopy
    • Cohen AD, Zeng BB, King SB, Toscano JP. Direct observation of an acyl nitroso species in solution by time-resolved IR spectrocopy. J Am Chem Soc 2003, 125, 1444-1445.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1444-1445
    • Cohen, A.D.1    Zeng, B.B.2    King, S.B.3    Toscano, J.P.4
  • 4
    • 23844494816 scopus 로고    scopus 로고
    • N-hydroxyurea and acyl nitroso compounds as nitroxyl HNO and nitric oxide NO donors
    • King SB. N-hydroxyurea and acyl nitroso compounds as nitroxyl (HNO) and nitric oxide (NO) donors. Curr Top Med Chem 2005, 5, 665-673.
    • (2005) Curr. Top. Med. Chem. , vol.5 , pp. 665-673
    • King, S.B.1
  • 8
    • 21044451423 scopus 로고    scopus 로고
    • The chemistry and biology of nitroxyl HNO: A chemically unique species with novel and important biological activity
    • Fukuto JM, Dutton AS, Houk KN. The chemistry and biology of nitroxyl (HNO): a chemically unique species with novel and important biological activity. Chembiochem 2005, 6, 612-619.
    • (2005) Chembiochem. , vol.6 , pp. 612-619
    • Fukuto, J.M.1    Dutton, A.S.2    Houk, K.N.3
  • 9
    • 18944394614 scopus 로고    scopus 로고
    • The physiological chemistry and biological activity of nitroxyl HNO: The neglected misunderstood and enigmatic nitrogen oxide
    • Fukuto JM, Bartberger MD, Dutton AS, Paolocci N, Wink DA, Houk KN. The physiological chemistry and biological activity of nitroxyl (HNO): the neglected, misunderstood, and enigmatic nitrogen oxide. Chem Res Toxicol 2005, 18, 790-801.
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 790-801
    • Fukuto, J.M.1    Bartberger, M.D.2    Dutton, A.S.3    Paolocci, N.4    Wink, D.A.5    Houk, K.N.6
  • 12
    • 11844279035 scopus 로고    scopus 로고
    • The chemistry of nitroxyl HNO and implications in biology
    • Miranda KM. The chemistry of nitroxyl (HNO) and implications in biology. Coord Chem Rev 2005, 249, 433-455.
    • (2005) Coord Chem. Rev. , vol.249 , pp. 433-455
    • Miranda, K.M.1
  • 13
    • 67649836821 scopus 로고    scopus 로고
    • The inhibitors of histone deacetylase suberoylanilide hydroxamate and trichostatin a release nitric oxide upon oxidation
    • Samuni Y, Flores-Santana W, Krishna MC, Mitchell JB, Wink DA. The inhibitors of histone deacetylase suberoylanilide hydroxamate and trichostatin A release nitric oxide upon oxidation. Free Radic Biol Med 2009, 47, 419-423.
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 419-423
    • Samuni, Y.1    Flores-Santana, W.2    Krishna, M.C.3    Mitchell, J.B.4    Wink, D.A.5
  • 14
    • 0028394216 scopus 로고
    • Spin trapping of methyl radicals by the acyl nitroso compound Ph-C=O NO formed in the photochemical reaction between benzohydroxamic acid dimethyl sulfoxide and hydrogen peroxide an EPR study
    • Lagercrantz C, Larsson T. Spin trapping of methyl radicals by the acyl nitroso compound Ph-C(= O)NO formed in the photochemical reaction between benzohydroxamic acid, dimethyl sulfoxide and hydrogen peroxide. An EPR study. Free Radic Res 1994, 20, 181-187.
    • (1994) Free Radic. Res. , vol.20 , pp. 181-187
    • Lagercrantz, C.1    Larsson, T.2
  • 15
    • 0033403514 scopus 로고    scopus 로고
    • Nitrobenzene carcinogenicity in animals and human hazard evaluation
    • Holder JW. Nitrobenzene carcinogenicity in animals and human hazard evaluation. Toxicol Ind Health 1999, 15, 445-457.
    • (1999) Toxicol. Ind. Health , vol.15 , pp. 445-457
    • Holder, J.W.1
  • 16
    • 0018127048 scopus 로고
    • Oxidative degradation of haemoglobin by nitrosobenzene in the erythrocyte
    • Hirota K, Itano HA, Vedvick TS. Oxidative degradation of haemoglobin by nitrosobenzene in the erythrocyte. Biochem J 1978, 174, 693-697.
    • (1978) Biochem. J. , vol.174 , pp. 693-697
    • Hirota, K.1    Itano, H.A.2    Vedvick, T.S.3
  • 17
    • 0345552418 scopus 로고    scopus 로고
    • Reduction potentials of conjugated aliphatic ketones oximes and imines: Correlation with structure and bioactivity
    • Niufar NN, Haycock FL, Wesemann JL, MacStay JA, Heasley VL, Kovacic P. Reduction potentials of conjugated aliphatic ketones, oximes, and imines: correlation with structure and bioactivity. Rev Mex Chem Soc 2002, 46, 307-312.
    • (2002) Rev. Mex. Chem. Soc. , vol.46 , pp. 307-312
    • Niufar, N.N.1    Haycock, F.L.2    Wesemann, J.L.3    MacStay, J.A.4    Heasley, V.L.5    Kovacic, P.6
  • 19
    • 0004164226 scopus 로고
    • New York: Interscience
    • Russell GA. In 'Radical Ions'. New York: Interscience 1968, 87-150.
    • (1968) Radical Ions , pp. 87-150
    • Russell, G.A.1
  • 20
    • 72049092371 scopus 로고    scopus 로고
    • Electron transfer as a potential cause of diacetyl toxicity in popcorn lung disease
    • Kovacic P, Cooksy AL. Electron transfer as a potential cause of diacetyl toxicity in popcorn lung disease. Rev Environ Contam Toxicol 2010, 204, 133-148.
    • (2010) Rev. Environ. Contam. Toxicol. , vol.204 , pp. 133-148
    • Kovacic, P.1    Cooksy, A.L.2
  • 21
    • 66749136361 scopus 로고    scopus 로고
    • Pulmonary toxicity and environmental contamination: Radicals electron transfer and protection by antioxidants
    • Kovacic P, Somanathan R. Pulmonary toxicity and environmental contamination: radicals, electron transfer, and protection by antioxidants. Rev Environ Contam Toxicol 2009, 201, 41-69.
    • (2009) Rev. Environ. Contam. Toxicol. , vol.201 , pp. 41-69
    • Kovacic, P.1    Somanathan, R.2
  • 22
    • 33646097467 scopus 로고    scopus 로고
    • Novel electrochemical approach to enhanced toxicity of 4-oxo-2-nonenal vs 4-hydroxy-2-nonenal role of imine: Oxidative stress and therapeutic modalities
    • Kovacic P. Novel electrochemical approach to enhanced toxicity of 4-oxo-2-nonenal vs. 4-hydroxy-2-nonenal (role of imine): oxidative stress and therapeutic modalities. Med Hypotheses 2006, 67, 151-156.
    • (2006) Med. Hypotheses , vol.67 , pp. 151-156
    • Kovacic, P.1
  • 23
    • 34548729611 scopus 로고    scopus 로고
    • Unifying mechanism for bacterial cell signalers 4 5-dihydroxy-2 3-pentanedione lactones and oligopeptides: Electron transfer and reactive oxygen species practical medical features
    • Kovacic P. Unifying mechanism for bacterial cell signalers (4,5-dihydroxy- 2,3-pentanedione, lactones and oligopeptides): electron transfer and reactive oxygen species. Practical medical features. Med Hypotheses 2007, 69, 1105-1110.
    • (2007) Med. Hypotheses , vol.69 , pp. 1105-1110
    • Kovacic, P.1
  • 24
    • 48749090017 scopus 로고    scopus 로고
    • The role of oxidative stress in apoptosis induced by the histone deacetylase inhibitor suberoylanilide hydroxamic acid in human colon adenocarcinoma HT-29 cells
    • Portanova P, Russo T, Pellerito O, Calvaruso G, Giuliano M, Vento R, Tesoriere G. The role of oxidative stress in apoptosis induced by the histone deacetylase inhibitor suberoylanilide hydroxamic acid in human colon adenocarcinoma HT-29 cells. Int J Oncol 2008, 33, 325-331.
    • (2008) Int. J. Oncol. , vol.33 , pp. 325-331
    • Portanova, P.1    Russo, T.2    Pellerito, O.3    Calvaruso, G.4    Giuliano, M.5    Vento, R.6    Tesoriere, G.7
  • 25
    • 0035845541 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid SAHA induces a cell-death pathway characterized by cleavage of bid and production of reactive oxygen species
    • USA
    • Ruefli AA, Ausserlechner MJ, Bernhard D, Sutton VR, Tainton KM, Kofler R, Smyth MJ, Johnstone RW. The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species. Proc Natl Acad Sci USA 2001, 98, 10833-10838.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3    Sutton, V.R.4    Tainton, K.M.5    Kofler, R.6    Smyth, M.J.7    Johnstone, R.W.8
  • 26
    • 2542523228 scopus 로고    scopus 로고
    • Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors
    • Pei XY, Dai Y, Grant S. Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors. Clin Cancer Res 2004, 10, 3839-3852.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 3839-3852
    • Pei, X.Y.1    Dai, Y.2    Grant, S.3
  • 27
    • 17344366112 scopus 로고    scopus 로고
    • BMD188 a novel hydroxamic acid compound, demonstrates potent antiprostate cancer effects in vitro and in vivo by inducing apoptosis: Requirements for mitochondria reactive oxygen species and proteases
    • Tang DG, Li L, Zhu Z, Joshi B, Johnson CR, Marnett LJ, Honn KV, Crissman JD, Krajewski S, Reed JC, Timar J, Porter AT. BMD188, A novel hydroxamic acid compound, demonstrates potent antiprostate cancer effects in vitro and in vivo by inducing apoptosis: requirements for mitochondria, reactive oxygen species, and proteases. Pathol Oncol Res 1998, 4, 179-190.
    • (1998) Pathol. Oncol. Res. , vol.4 , pp. 179-190
    • Tang, D.G.1    Li, L.2    Zhu, Z.3    Joshi, B.4    Johnson, C.R.5    Marnett, L.J.6    Honn, K.V.7    Crissman, J.D.8    Krajewski, S.9    Reed, J.C.10    Timar, J.11    Porter, A.T.12
  • 28
    • 0345255903 scopus 로고    scopus 로고
    • Neurotransmission and neurotoxicity by nitric oxide catecholamines and glutamate: Unifying themes of reactive oxygen species and electron transfer
    • Jacintho JD, Kovacic P. Neurotransmission and neurotoxicity by nitric oxide, catecholamines, and glutamate: unifying themes of reactive oxygen species and electron transfer. Curr Med Chem 2003, 10, 2693-2703.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 2693-2703
    • Jacintho, J.D.1    Kovacic, P.2
  • 31
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • USA
    • Shao Y, Gao Z, Marks PA, Jiang X. Apoptotic and autophagic cell death induced by histone deacetylase inhibitors. Proc Natl Acad Sci USA 2004, 101, 18030-18035.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3    Jiang, X.4
  • 32
    • 36248982150 scopus 로고    scopus 로고
    • Autophagy induced by suberoylanilide hydroxamic acid in hela S3 cells involves inhibition of protein kinase B and up-regulation of beclin 1
    • Cao Q, Yu C, Xue R, Hsueh W, Pan P, Chen Z, Wang S, McNutt M, Gu J. Autophagy induced by suberoylanilide hydroxamic acid in Hela S3 cells involves inhibition of protein kinase B and up-regulation of Beclin 1. Int J Biochem Cell Biol 2008, 40, 272-283.
    • (2008) Int. J. Biochem. Cell. Biol. , vol.40 , pp. 272-283
    • Cao, Q.1    Yu, C.2    Xue, R.3    Hsueh, W.4    Pan, P.5    Chen, Z.6    Wang, S.7    McNutt, M.8    Gu, J.9
  • 33
    • 13944280578 scopus 로고    scopus 로고
    • Effects of suberoylanilide hydroxamic acid and trichostatin a on induction of cytochrome P450 enzymes and benzo a pyrene DNA adduct formation in human cells
    • Hooven LA, Mahadevan B, Keshava C, Johns C, Pereira C, Desai D, Amin S, Weston A, Baird WM. Effects of suberoylanilide hydroxamic acid and trichostatin A on induction of cytochrome P450 enzymes and benzo[a]pyrene DNA adduct formation in human cells. Bioorg Med Chem Lett 2005, 15, 1283-1287.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 1283-1287
    • Hooven, L.A.1    Mahadevan, B.2    Keshava, C.3    Johns, C.4    Pereira, C.5    Desai, D.6    Amin, S.7    Weston, A.8    Baird, W.M.9
  • 34
    • 0035724488 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce caspase-dependent apoptosis and downregulation of daxx in acute promyelocytic leukaemia with t 15 17
    • Amin HM, Saeed S, Alkan S. Histone deacetylase inhibitors induce caspase-dependent apoptosis and downregulation of daxx in acute promyelocytic leukaemia with t(15;17). Br J Haematol 2001, 115, 287-297.
    • (2001) Br. J. Haematol. , vol.115 , pp. 287-297
    • Amin, H.M.1    Saeed, S.2    Alkan, S.3
  • 35
    • 31644442355 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors require caspase activity to induce apoptosis in lung and prostate carcinoma cells
    • Sonnemann J, Hartwig M, Plath A, Saravana Kumar K, Müller C, Beck JF. Histone deacetylase inhibitors require caspase activity to induce apoptosis in lung and prostate carcinoma cells. Cancer Lett 2006, 232, 148-160.
    • (2006) Cancer Lett. , vol.232 , pp. 148-160
    • Sonnemann, J.1    Hartwig, M.2    Plath, A.3    Saravana Kumar, K.4    Müller, C.5    Beck, J.F.6
  • 37
    • 70149105660 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid SAHA induces growth arrest and apoptosis in pituitary adenoma cells
    • Sangeetha SR, Singh N, Vender JR, Dhandapani KM. Suberoylanilide hydroxamic acid (SAHA) induces growth arrest and apoptosis in pituitary adenoma cells. Endocrine 2009, 35, 389-396.
    • (2009) Endocrine , vol.35 , pp. 389-396
    • Sangeetha, S.R.1    Singh, N.2    Vender, J.R.3    Dhandapani, K.M.4
  • 38
    • 67649354926 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid zolinza/vorinostat sensitizes TRAIL-resistant breast cancer cells orthotopically implanted in BALB/c nude mice
    • Shankar S, Davis R, Singh KP, Kurzrock R, Ross DD, Srivastava RK. Suberoylanilide hydroxamic acid (Zolinza/vorinostat) sensitizes TRAIL-resistant breast cancer cells orthotopically implanted in BALB/c nude mice. Mol Cancer Ther 2009, 8, 1596-1605.
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 1596-1605
    • Shankar, S.1    Davis, R.2    Singh, K.P.3    Kurzrock, R.4    Ross, D.D.5    Srivastava, R.K.6
  • 39
    • 68749089762 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberoylanilide hydroxamic acid sensitises human hepatocellular carcinoma cells to trail-induced apoptosis by trail-disc activation
    • Carlisi D, Lauricella M, D'Anneo A, Emanuele S, Angileri L, Di Fazio P, Santulli A, Vento R, Tesoriere G. The histone deacetylase inhibitor suberoylanilide hydroxamic acid sensitises human hepatocellular carcinoma cells to TRAIL-induced apoptosis by TRAIL-DISC activation. Eur J Cancer 2009, 45, 2425-2438.
    • (2009) Eur. J. Cancer , vol.45 , pp. 2425-2438
    • Carlisi, D.1    Lauricella, M.2    D'Anneo, A.3    Emanuele, S.4    Angileri, L.5    Di Fazio, P.6    Santulli, A.7    Vento, R.8    Tesoriere, G.9
  • 40
    • 33744539154 scopus 로고    scopus 로고
    • Apoptosis signal-regulating kinase 1 is a direct target of E2F1 and contributes to histone deacetylase inhibitor-induced apoptosis through positive feedback regulation of E2F1 apoptotic activity
    • Tan J, Zhuang L, Jiang X, Yang KK, Karuturi KM, Yu Q. Apoptosis signal-regulating kinase 1 is a direct target of E2F1 and contributes to histone deacetylase inhibitor-induced apoptosis through positive feedback regulation of E2F1 apoptotic activity. J Biol Chem 2006, 281, 10508-10515.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10508-10515
    • Tan, J.1    Zhuang, L.2    Jiang, X.3    Yang, K.K.4    Karuturi, K.M.5    Yu, Q.6
  • 41
    • 34247115447 scopus 로고    scopus 로고
    • C-Myc overexpression sensitizes bimmediated bax activation for apoptosis induced by histone deacetylase inhibitor suberoylanilide hydroxamic acid SAHA through regulating Bcl-2/Bcl-xL expression
    • Jiang X, Tsang YH, Yu Q. c-Myc overexpression sensitizes Bimmediated Bax activation for apoptosis induced by histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) through regulating Bcl-2/Bcl-xL expression. Int J Biochem Cell Biol 2007, 39, 1016-1025.
    • (2007) Int. J. Biochem. Cell. Biol. , vol.39 , pp. 1016-1025
    • Jiang, X.1    Tsang, Y.H.2    Yu, Q.3
  • 42
    • 34347206854 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors sensitize prostate cancer cells to agents that produce DNA double-strand breaks by targeting Ku70 acetylation
    • Chen CS, Wang YC, Yang HC, Huang PH, Kulp SK, Yang CC, Lu YS, Matsuyama S, Chen CY, Chen CS. Histone deacetylase inhibitors sensitize prostate cancer cells to agents that produce DNA double-strand breaks by targeting Ku70 acetylation. Cancer Res 2007, 67, 5318-5327.
    • (2007) Cancer Res. , vol.67 , pp. 5318-5327
    • Chen, C.S.1    Wang, Y.C.2    Yang, H.C.3    Huang, P.H.4    Kulp, S.K.5    Yang, C.C.6    Lu, Y.S.7    Matsuyama, S.8    Chen, C.Y.9    Chen, C.S.10
  • 43
    • 33644486735 scopus 로고    scopus 로고
    • Interactive effects of histone deacetylase inhibitors and trail on apoptosis in human leukemia cells: Involvement of both death receptor and mitochondrial pathways
    • Shankar S, Singh TR, Fandy TE, Luetrakul T, Ross DD, Srivastava RK. Interactive effects of histone deacetylase inhibitors and TRAIL on apoptosis in human leukemia cells: involvement of both death receptor and mitochondrial pathways. Int J Mol Med 2005, 16, 1125-1138.
    • (2005) Int. J. Mol. Med. , vol.16 , pp. 1125-1138
    • Shankar, S.1    Singh, T.R.2    Fandy, T.E.3    Luetrakul, T.4    Ross, D.D.5    Srivastava, R.K.6
  • 44
    • 0035057791 scopus 로고    scopus 로고
    • Mechanisms of suberoylanilide hydroxamic acid inhibition of mammary cell growth
    • Said TK, Moraes RC, Sinha R, Medina D. Mechanisms of suberoylanilide hydroxamic acid inhibition of mammary cell growth. Breast Cancer Res 2001, 3, 122-133.
    • (2001) Breast Cancer Res. , vol.3 , pp. 122-133
    • Said, T.K.1    Moraes, R.C.2    Sinha, R.3    Medina, D.4
  • 45
    • 33644814867 scopus 로고    scopus 로고
    • Selective induction of apoptosis by histone deacetylase inhibitor saha in cutaneous T-cell lymphoma cells: Relevance to mechanism of therapeutic action
    • Zhang C, Richon V, Ni X, Talpur R, Duvic M. Selective induction of apoptosis by histone deacetylase inhibitor SAHA in cutaneous T-cell lymphoma cells: relevance to mechanism of therapeutic action. J Invest Dermatol 2005, 125, 1045-1052.
    • (2005) J. Invest. Dermatol. , vol.125 , pp. 1045-1052
    • Zhang, C.1    Richon, V.2    Ni, X.3    Talpur, R.4    Duvic, M.5
  • 46
    • 0038485588 scopus 로고    scopus 로고
    • Role of caspases bid and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin- A TSA and suberoylanilide hydroxamic acid saha
    • Henderson C, Mizzau M, Paroni G, Maestro R, Schneider C, Brancolini C. Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin- A (TSA) and suberoylanilide hydroxamic acid (SAHA). J Biol Chem 2003, 278, 12579-12589.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12579-12589
    • Henderson, C.1    Mizzau, M.2    Paroni, G.3    Maestro, R.4    Schneider, C.5    Brancolini, C.6
  • 48
    • 33847729212 scopus 로고    scopus 로고
    • Oxford University Press, New York
    • Hancock GT. 'Cell Signaling.' Oxford University Press, New York, 2000.
    • (2000) Cell Signaling
    • Hancock, G.T.1
  • 49
    • 84943256851 scopus 로고    scopus 로고
    • Oxidative stress and free radical signal transduction
    • Academic Press New York
    • Demple B. Oxidative stress and free radical signal transduction. In 'Handbook of Cell Signaling.' Academic Press, New York, 2004, 191-195.
    • (2004) Handbook of Cell Signaling , pp. 191-195
    • Demple, B.1
  • 50
    • 33847727031 scopus 로고    scopus 로고
    • Cell signaling mechanism and reproductive toxicity: Redox chains radicals electrons relays conduit electrochemistry and other medical implications
    • Kovacic P, Pozos RS. Cell signaling (mechanism and reproductive toxicity): redox chains, radicals, electrons, relays, conduit, electrochemistry, and other medical implications. Birth Defects Res C Embryo Today 2006, 78, 333-344.
    • (2006) Birth Defects Res. C Embryo Today , vol.78 , pp. 333-344
    • Kovacic, P.1    Pozos, R.S.2
  • 51
    • 34249992893 scopus 로고    scopus 로고
    • Protein electron transfer mechanism and reproductive toxicity: Iminium hydrogen bonding homoconjugation amino acid side chains redox and charged and cell signaling
    • Kovacic P. Protein electron transfer (mechanism and reproductive toxicity): iminium, hydrogen bonding, homoconjugation, amino acid side chains (redox and charged), and cell signaling. Birth Defects Res C Embryo Today 2007, 81, 51-64.
    • (2007) Birth Defects Res. C Embryo Today , vol.81 , pp. 51-64
    • Kovacic, P.1
  • 52
    • 0025052304 scopus 로고
    • Membrane electrostatics
    • Cerc G. Membrane electrostatics. Biochem Biophys Acta 1990, 1031, 311-382.
    • (1990) Biochem. Biophys. Acta. , vol.1031 , pp. 311-382
    • Cerc, G.1
  • 53
    • 77951023689 scopus 로고    scopus 로고
    • Simplifying the complexity of cell signaling in medicine and the life sciences: Radicals and electrochemistry
    • Kovacic P. Simplifying the complexity of cell signaling in medicine and the life sciences: Radicals and electrochemistry. Med Hypotheses 2010, 74, 769-771.
    • (2010) Med. Hypotheses , vol.74 , pp. 769-771
    • Kovacic, P.1
  • 54
    • 34548815034 scopus 로고    scopus 로고
    • Bioelectronome integrated approach to receptor chemistry radicals electrochemistry cell signaling and physiological effects based on electron transfer
    • Kovacic P, Pozos RS. Bioelectronome. Integrated approach to receptor chemistry, radicals, electrochemistry, cell signaling, and physiological effects based on electron transfer. J Recept Signal Transduct Res 2007, 27, 261-294.
    • (2007) J. Recept Signal Transduct. Res. , vol.27 , pp. 261-294
    • Kovacic, P.1    Pozos, R.S.2
  • 56
    • 37549039459 scopus 로고    scopus 로고
    • Unifying electrostatic mechanism for phosphates and sulfates in cell signaling
    • Kovacic P, Draskovich CD, Pozos RS. Unifying electrostatic mechanism for phosphates and sulfates in cell signaling. J Recept Signal Transduct Res 2007, 27, 433-443.
    • (2007) J. Recept. Signal Transduct. Res. , vol.27 , pp. 433-443
    • Kovacic, P.1    Draskovich, C.D.2    Pozos, R.S.3
  • 57
    • 45849084257 scopus 로고    scopus 로고
    • Unifying electrostatic mechanism for metal cations in receptors and cell signaling
    • Kovacic P. Unifying electrostatic mechanism for metal cations in receptors and cell signaling. J Recept Signal Transduct Res 2008, 28, 153-161.
    • (2008) J. Recept. Signal Transduct. Res. , vol.28 , pp. 153-161
    • Kovacic, P.1
  • 58
    • 3042785975 scopus 로고    scopus 로고
    • A review of depsipeptide and other histone deacetylase inhibitors in clinical trials
    • Piekarz R, Bates S. A review of depsipeptide and other histone deacetylase inhibitors in clinical trials. Curr Pharm Des 2004, 10, 2289-2298.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 2289-2298
    • Piekarz, R.1    Bates, S.2
  • 60
    • 67651155861 scopus 로고    scopus 로고
    • Antioxidant activity of nsaid hydroxamic acids
    • Koncic MZ, Rajic Z, Petric N, Zorc B. Antioxidant activity of NSAID hydroxamic acids. Acta Pharm 2009, 59, 235-242.
    • (2009) Acta. Pharm. , vol.59 , pp. 235-242
    • Koncic, M.Z.1    Rajic, Z.2    Petric, N.3    Zorc, B.4
  • 61
    • 73849101542 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid saha at subtoxic concentrations increases the adhesivity of human leukemic cells to fibronectin
    • Kuzelová K, Pluskalová M, Brodská B, Otevrelová P, Elknerová K, Grebenová D, Hrkal Z. Suberoylanilide hydroxamic acid (SAHA) at subtoxic concentrations increases the adhesivity of human leukemic cells to fibronectin. J Cell Biochem 2010, 109, 184-195.
    • (2010) J. Cell. Biochem. , vol.109 , pp. 184-195
    • Kuzelová, K.1    Pluskalová, M.2    Brodská, B.3    Otevrelová, P.4    Elknerová, K.5    Grebenová, D.6    Hrkal, Z.7
  • 62
    • 67650090545 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Potential in cancer therapy
    • Marks PA, Xu WS. Histone deacetylase inhibitors: Potential in cancer therapy. J Cell Biochem 2009, 107, 600-608.
    • (2009) J. Cell. Biochem. , vol.107 , pp. 600-608
    • Marks, P.A.1    Xu, W.S.2
  • 66
    • 49649085534 scopus 로고    scopus 로고
    • Evaluation of the in vitro and in vivo antitumor activity of histone deacetylase inhibitors for the therapy of retinoblastoma
    • Dalgard CL, Van Quill KR, O'Brien JM. Evaluation of the in vitro and in vivo antitumor activity of histone deacetylase inhibitors for the therapy of retinoblastoma. Clin Cancer Res 2008, 14, 3113-3123.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 3113-3123
    • Dalgard, C.L.1    Van Quill, K.R.2    O'Brien, J.M.3
  • 67
    • 64549164161 scopus 로고    scopus 로고
    • Suberoyl bis-hydroxamic acid induces p53-dependent apoptosis of MCF-7 breast cancer cells
    • Zhuang ZG, Fei F, Chen Y, Jin W. Suberoyl bis-hydroxamic acid induces p53-dependent apoptosis of MCF-7 breast cancer cells. Acta Pharmacol Sin 2008, 29, 1459-1466.
    • (2008) Acta. Pharmacol. Sin. , vol.29 , pp. 1459-1466
    • Zhuang, Z.G.1    Fei, F.2    Chen, Y.3    Jin, W.4
  • 68
    • 68949105725 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase suppresses EGF signaling pathways by destabilizing EGFR mRNA in ER-negative human breast cancer cells
    • Zhou Q, Shaw PG, Davidson NE. Inhibition of histone deacetylase suppresses EGF signaling pathways by destabilizing EGFR mRNA in ER-negative human breast cancer cells. Breast Cancer Res Treat 2009, 117, 443-451.
    • (2009) Breast Cancer Res. Treat. , vol.117 , pp. 443-451
    • Zhou, Q.1    Shaw, P.G.2    Davidson, N.E.3
  • 69
    • 0037015071 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor saha arrests cancer cell growth up-regulates thioredoxin-binding protein-2 and down-regulates thioredoxin
    • USA
    • Butler LM, Zhou X, Xu WS, Scher HI, Rifkind RA, Marks PA, Richon VM. The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin. Proc Natl Acad Sci USA 2002, 99, 11700-11705.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 11700-11705
    • Butler, L.M.1    Zhou, X.2    Xu, W.S.3    Scher, H.I.4    Rifkind, R.A.5    Marks, P.A.6    Richon, V.M.7
  • 70
  • 73
    • 4344716951 scopus 로고    scopus 로고
    • Modulation of pro-and anti-apoptotic factors in human melanoma cells exposed to histone deacetylase inhibitors
    • Facchetti F, Previdi S, Ballarini M, Minucci S, Perego P, La Porta CA. Modulation of pro- and anti-apoptotic factors in human melanoma cells exposed to histone deacetylase inhibitors. Apoptosis 2004, 9, 573-582.
    • (2004) Apoptosis , vol.9 , pp. 573-582
    • Facchetti, F.1    Previdi, S.2    Ballarini, M.3    Minucci, S.4    Perego, P.5    La Porta, C.A.6
  • 74
    • 33749331568 scopus 로고    scopus 로고
    • Antitumor activity of suberoylanilide hydroxamic acid against thyroid cancer cell lines in vitro and in vivo
    • Luong QT, O'Kelly J, Braunstein GD, Hershman JM, Koeffler HP. Antitumor activity of suberoylanilide hydroxamic acid against thyroid cancer cell lines in vitro and in vivo. Clin Cancer Res 2006, 12, 5570-5577.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 5570-5577
    • Luong, Q.T.1    O'Kelly, J.2    Braunstein, G.D.3    Hershman, J.M.4    Koeffler, H.P.5
  • 76
    • 33748581975 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid is effective in preclinical studies of medulloblastoma
    • Spiller SE, Ravanpay AC, Hahn AW, Olson JM. Suberoylanilide hydroxamic acid is effective in preclinical studies of medulloblastoma. J Neurooncol 2006, 79, 259-270.
    • (2006) J. Neurooncol. , vol.79 , pp. 259-270
    • Spiller, S.E.1    Ravanpay, A.C.2    Hahn, A.W.3    Olson, J.M.4
  • 77
    • 78650794267 scopus 로고    scopus 로고
    • Synergistic effects of proteasome inhibitor and histone deacetylase inhibitor on apoptosis and aggresome formation in T lymphoma cells
    • Jiang XX, Zhang QL, Chen XY, Wu WL, Shen ZX, Zhao WL. [Synergistic effects of proteasome inhibitor and histone deacetylase inhibitor on apoptosis and aggresome formation in T lymphoma cells]. Zhongguo Shi Yan Xue Ye Xue Za Zhi 2009, 17, 1215-1219.
    • (2009) Zhongguo. Shi. Yan. Xue. Ye. Xue. Za. Zhi. , vol.17 , pp. 1215-1219
    • Jiang, X.X.1    Zhang, Q.L.2    Chen, X.Y.3    Wu, W.L.4    Shen, Z.X.5    Zhao, W.L.6
  • 79
  • 80
    • 54349085057 scopus 로고    scopus 로고
    • Gene microarray analysis of human renal cell carcinoma: The effects of HDAC inhibition and retinoid treatment
    • Tavares TS, Nanus D, Yang XJ, Gudas LJ. Gene microarray analysis of human renal cell carcinoma: the effects of HDAC inhibition and retinoid treatment. Cancer Biol Ther 2008, 7, 1607-1618.
    • (2008) Cancer Biol. Ther. , vol.7 , pp. 1607-1618
    • Tavares, T.S.1    Nanus, D.2    Yang, X.J.3    Gudas, L.J.4
  • 81
    • 34347394714 scopus 로고    scopus 로고
    • Targeting autophagy augments the anticancer activity of the histone deacetylase inhibitor saha to overcome Bcr-Abl-mediated drug resistance
    • Carew JS, Nawrocki ST, Kahue CN, Zhang H, Yang C, Chung L, Houghton JA, Huang P, Giles FJ, Cleveland JL. Targeting autophagy augments the anticancer activity of the histone deacetylase inhibitor SAHA to overcome Bcr-Abl-mediated drug resistance. Blood 2007, 110, 313-322.
    • (2007) Blood , vol.110 , pp. 313-322
    • Carew, J.S.1    Nawrocki, S.T.2    Kahue, C.N.3    Zhang, H.4    Yang, C.5    Chung, L.6    Houghton, J.A.7    Huang, P.8    Giles, F.J.9    Cleveland, J.L.10
  • 83
    • 35348961982 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase enhances the anti-proliferative action of antiestrogens on breast cancer cells and blocks tamoxifen-induced proliferation of uterine cells
    • Hodges-Gallagher L, Valentine CD, Bader SE, Kushner PJ. Inhibition of histone deacetylase enhances the anti-proliferative action of antiestrogens on breast cancer cells and blocks tamoxifen-induced proliferation of uterine cells. Breast Cancer Res Treat 2007, 105, 297-309.
    • (2007) Breast Cancer Res. Treat. , vol.105 , pp. 297-309
    • Hodges-Gallagher, L.1    Valentine, C.D.2    Bader, S.E.3    Kushner, P.J.4
  • 84
    • 48449099915 scopus 로고    scopus 로고
    • Reprogramming epigenetic silencing: Artificial transcription factors synergize with chromatin remodeling drugs to reactivate the tumor suppressor mammary serine protease inhibitor
    • Beltran AS, Sun X, Lizardi PM, Blancafort P. Reprogramming epigenetic silencing: artificial transcription factors synergize with chromatin remodeling drugs to reactivate the tumor suppressor mammary serine protease inhibitor. Mol Cancer Ther 2008, 7, 1080-1090.
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 1080-1090
    • Beltran, A.S.1    Sun, X.2    Lizardi, P.M.3    Blancafort, P.4
  • 87
    • 6344229760 scopus 로고    scopus 로고
    • Proteasome inhibition sensitizes non-small cell lung cancer to histone deacetylase inhibitor-induced apoptosis through the generation of reactive oxygen species
    • Denlinger CE, Rundall BK, Jones DR. Proteasome inhibition sensitizes non-small cell lung cancer to histone deacetylase inhibitor- induced apoptosis through the generation of reactive oxygen species. J Thorac Cardiovasc Surg 2004, 128, 740-748.
    • (2004) J. Thorac. Cardiovasc. Surg. , vol.128 , pp. 740-748
    • Denlinger, C.E.1    Rundall, B.K.2    Jones, D.R.3
  • 88
    • 24344498688 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid combined with gemcitabine enhances apoptosis in nonsmall cell lung cancer
    • Rundall BK, Denlinger CE, Jones DR. Suberoylanilide hydroxamic acid combined with gemcitabine enhances apoptosis in nonsmall cell lung cancer. Surgery 2005, 138, 360-367.
    • (2005) Surgery , vol.138 , pp. 360-367
    • Rundall, B.K.1    Denlinger, C.E.2    Jones, D.R.3
  • 90
    • 34347226747 scopus 로고    scopus 로고
    • Combined treatment with Ad-htrail and dtic or saha is associated with increased mitochondrialmediated apoptosis in human melanoma cell lines
    • Lillehammer T, Engesaeter BO, Prasmickaite L, Maelandsmo GM, Fodstad O, Engebraaten O. Combined treatment with Ad-hTRAIL and DTIC or SAHA is associated with increased mitochondrialmediated apoptosis in human melanoma cell lines. J Gene Med 2007, 9, 440-451.
    • (2007) J. Gene. Med. , vol.9 , pp. 440-451
    • Lillehammer, T.1    Engesaeter, B.O.2    Prasmickaite, L.3    Maelandsmo, G.M.4    Fodstad, O.5    Engebraaten, O.6
  • 91
    • 33748360764 scopus 로고    scopus 로고
    • Vorinostat a histone deacetylase inhibitor enhances the response f human tumor cells to ionizing radiation through prolongation of gamma-H2AX foci
    • Munshi A, Tanaka T, Hobbs ML, Tucker SL, Richon VM, Meyn RE. Vorinostat, a histone deacetylase inhibitor, enhances the response f human tumor cells to ionizing radiation through prolongation of gamma-H2AX foci. Mol Cancer Ther 2006, 5, 1967-1974.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1967-1974
    • Munshi, A.1    Tanaka, T.2    Hobbs, M.L.3    Tucker, S.L.4    Richon, V.M.5    Meyn, R.E.6
  • 93
    • 70349481308 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid sensitizes human oral cancer cells to trailinduced apoptosis through increase DR5 expression
    • Yeh CC, Deng YT, Sha DY, Hsiao M, Kuo MY. Suberoylanilide hydroxamic acid sensitizes human oral cancer cells to TRAILinduced apoptosis through increase DR5 expression. Mol Cancer Ther 2009, 8, 2718-2725.
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 2718-2725
    • Yeh, C.C.1    Deng, Y.T.2    Sha, D.Y.3    Hsiao, M.4    Kuo, M.Y.5
  • 94
    • 33846839622 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid vorinostat represses androgen receptor expression and acts synergistically with an androgen receptor antagonist to inhibit prostate cancer cell proliferation
    • Marrocco DL, Tilley WD, Bianco-Miotto T, Evdokiou A, Scher HI, Rifkind RA, Marks PA, Richon VM, Butler LM. Suberoylanilide hydroxamic acid (vorinostat) represses androgen receptor expression and acts synergistically with an androgen receptor antagonist to inhibit prostate cancer cell proliferation. Mol Cancer Ther 2007, 6, 51-60.
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 51-60
    • Marrocco, D.L.1    Tilley, W.D.2    Bianco-Miotto, T.3    Evdokiou, A.4    Scher, H.I.5    Rifkind, R.A.6    Marks, P.A.7    Richon, V.M.8    Butler, L.M.9
  • 95
    • 36749055778 scopus 로고    scopus 로고
    • Synergistic activity of the histone deacetylase inhibitor suberoylanilide hydroxamic acid and the bisphosphonate zoledronic acid against prostate cancer cells in vitro
    • Sonnemann J, Bumbul B, Beck JF. Synergistic activity of the histone deacetylase inhibitor suberoylanilide hydroxamic acid and the bisphosphonate zoledronic acid against prostate cancer cells in vitro. Mol Cancer Ther 2007, 6, 2976-2984.
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 2976-2984
    • Sonnemann, J.1    Bumbul, B.2    Beck, J.F.3
  • 96
    • 33847130464 scopus 로고    scopus 로고
    • Comparative evaluation of the treatment efficacy of suberoylanilide hydroxamic acid saha and paclitaxel in ovarian cancer cell lines and primary ovarian cancer cells from patients
    • Sonnemann J, Gänge J, Pilz S, Stötzer C, Ohlinger R, Belau A, Lorenz G, Beck JF. Comparative evaluation of the treatment efficacy of suberoylanilide hydroxamic acid (SAHA) and paclitaxel in ovarian cancer cell lines and primary ovarian cancer cells from patients. BMC Cancer 2006, 6, 183.
    • (2006) BMC Cancer , vol.6 , pp. 183
    • Sonnemann, J.1    Gänge, J.2    Pilz, S.3    Stötzer, C.4    Ohlinger, R.5    Belau, A.6    Lorenz, G.7    Beck, J.F.8
  • 97
    • 23844505701 scopus 로고    scopus 로고
    • Fundamental, electron transfer mechanism by pyrylium-type ions for the anticancer drugs 5 6-dimethylxanthenone-4-acetic acid DMXAA and flavone-8-acetic acid FAA
    • Kovacic P. Fundamental, electron transfer mechanism by pyrylium-type ions for the anticancer drugs 5,6-dimethylxanthenone- 4-acetic acid (DMXAA) and flavone-8-acetic acid (FAA). Curr Med Chem Anticancer Agents 2005, 5, 501-506.
    • (2005) Curr. Med. Chem. Anticancer Agents , vol.5 , pp. 501-506
    • Kovacic, P.1
  • 98
    • 34447272264 scopus 로고    scopus 로고
    • Unifying mechanism for anticancer agents involving electron transfer and oxidative stress: Clinical implications
    • Kovacic P. Unifying mechanism for anticancer agents involving electron transfer and oxidative stress: clinical implications. Med Hypotheses 2007, 69, 510-516.
    • (2007) Med. Hypotheses , vol.69 , pp. 510-516
    • Kovacic, P.1
  • 99
    • 78650779163 scopus 로고    scopus 로고
    • Fixing function in cystic fibrosis
    • Drahl C. Fixing function in cystic fibrosis. Chem Eng News 2009, 87, 35.
    • (2009) Chem. Eng. News , vol.87 , pp. 35
    • Drahl, C.1
  • 104
    • 72049124418 scopus 로고    scopus 로고
    • Beneficial effects of antioxidants in relation to carcinogens toxins and various illnesses
    • Nova Science New York
    • Kovacic P, Somanathan R. Beneficial effects of antioxidants in relation to carcinogens, toxins and various illnesses. In 'Frontiers in Antioxidant Research.' Nova Science, New York, 2006, 1-38.
    • (2006) Frontiers in Antioxidant Research , pp. 1-38
    • Kovacic, P.1    Somanathan, R.2
  • 107
    • 33244458274 scopus 로고    scopus 로고
    • Potential role of histone deacetylase inhibitors in mesothelioma: Clinical experience with suberoylanilide hydroxamic acid
    • Krug LM, Curley T, Schwartz L, Richardson S, Marks P, Chiao J, Kelly WK. Potential role of histone deacetylase inhibitors in mesothelioma: clinical experience with suberoylanilide hydroxamic acid. Clin Lung Cancer 2006, 7, 257-261.
    • (2006) Clin. Lung. Cancer , vol.7 , pp. 257-261
    • Krug, L.M.1    Curley, T.2    Schwartz, L.3    Richardson, S.4    Marks, P.5    Chiao, J.6    Kelly, W.K.7
  • 110
    • 38149140216 scopus 로고    scopus 로고
    • Phase II trial of the histone deacetylase inhibitor vorinostat zolinza suberoylanilide hydroxamic acid saha in patients with recurrent and/ or metastatic head and neck cancer
    • Blumenschein GR Jr, Kies MS, Papadimitrakopoulou VA, Lu C, Kumar AJ, Ricker JL, Chiao JH, Chen C, Frankel SR. Phase II trial of the histone deacetylase inhibitor vorinostat (Zolinza, suberoylanilide hydroxamic acid, SAHA) in patients with recurrent and/ or metastatic head and neck cancer. Invest New Drugs 2008, 26, 81-87.
    • (2008) Invest. New Drugs , vol.26 , pp. 81-87
    • Blumenschein Jr., G.R.1    Kies, M.S.2    Papadimitrakopoulou, V.A.3    Lu, C.4    Kumar, A.J.5    Ricker, J.L.6    Chiao, J.H.7    Chen, C.8    Frankel, S.R.9
  • 111
    • 33845996135 scopus 로고    scopus 로고
    • Phase 2 trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) for refractory cutaneous T-cell lymphoma (CTCL)
    • DOI 10.1182/blood-2006-06-025999
    • Duvic M, Talpur R, Ni X, Zhang C, Hazarika P, Kelly C, Chiao JH, Reilly JF, Ricker JL, Richon VM, Frankel SR. Phase 2 trial of oral vorinostat (suberoylanilide hydroxamic acid, SAHA) for refractory cutaneous T-cell lymphoma (CTCL). Blood 2007, 109, 31-39. (Pubitemid 46053039)
    • (2007) Blood , vol.109 , Issue.1 , pp. 31-39
    • Duvic, M.1    Talpur, R.2    Ni, X.3    Zhang, C.4    Hazarika, P.5    Kelly, C.6    Chiao, J.H.7    Reilly, J.F.8    Ricker, J.L.9    Richon, V.M.10    Frankel, S.R.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.