메뉴 건너뛰기




Volumn 9, Issue 7, 2014, Pages

Carbamoylating activity associated with the activation of the antitumor agent laromustine inhibits angiogenesis by inducing ASK1-dependent endothelial cell death

Author keywords

[No Author keywords available]

Indexed keywords

1,2 BIS(METHYLSULFONYL) 1 (2 CHLOROETHYL) HYDRAZINE; 1,2 BIS(METHYLSULFONYL) 1 [(METHYLAMINO)CARBONYL]HYDRAZINE; APOPTOSIS SIGNAL REGULATING KINASE 1; CARMUSTINE; CYSTEINE; DRUG ANALOG; LAROMUSTINE; METHYL ISOCYANATE; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN 14 3 3; STRESS ACTIVATED PROTEIN KINASE; THIOREDOXIN; THIOREDOXIN 1; THIOREDOXIN REDUCTASE 1; UNCLASSIFIED DRUG; 1,2-BIS(METHYLSULFONYL)-1-(2-CHLOROETHYL)HYDRAZINE; ANTINEOPLASTIC AGENT; CARBAMIC ACID DERIVATIVE; HYDRAZINE DERIVATIVE; ISOCYANIC ACID DERIVATIVE; STRESS ACTIVATED PROTEIN KINASE 1; SULFONAMIDE; TXN PROTEIN, HUMAN; TXNRD1 PROTEIN, HUMAN;

EID: 84904893458     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0103224     Document Type: Article
Times cited : (11)

References (54)
  • 1
    • 30444446785 scopus 로고    scopus 로고
    • The antineoplastic efficacy of the prodrug cloretazine is produced by the synergistic interaction of carbamoylating and alkylating products of its activation
    • Baumann RP, Seow HA, Shyam K, Penketh PG, Sartorelli AC (2005) The antineoplastic efficacy of the prodrug Cloretazine is produced by the synergistic interaction of carbamoylating and alkylating products of its activation. Oncology Research 15(6): 313-25. (Pubitemid 43074226)
    • (2005) Oncology Research , vol.15 , Issue.6 , pp. 313-325
    • Baumann, R.P.1    Seow, H.A.2    Shyam, K.3    Penketh, P.G.4    Sartorelli, A.C.5
  • 3
    • 1642281458 scopus 로고    scopus 로고
    • 6- alkylguanine-DNA alkyltransferase (AGT) by electrophilic species generated by decomposition
    • DOI 10.1007/s00280-003-0740-7
    • Penketh PG, Shyam K, Baumann RP, Remack JS, Brent TP, et al. (2004) 1,2-Bis(methylsulfonyl)-1-(2-chloroethyl)-2-[(methylamino)carbonyl]hydrazi ne (VNP40101M): I. Direct inhibition of O6-alkylguanine-DNA alkyltransferase (AGT) by electrophilic species generated by decomposition. Cancer Chemother Pharmacol 53: 279-287. (Pubitemid 38392352)
    • (2004) Cancer Chemotherapy and Pharmacology , vol.53 , Issue.4 , pp. 279-287
    • Penketh, P.G.1    Shyam, K.2    Baumann, R.P.3    Remack, J.S.4    Brent, T.P.5    Sartorelli, A.C.6
  • 4
    • 84901017014 scopus 로고    scopus 로고
    • Influence of Phosphate and Phosphoesters on the Decomposition Pathway of 1,2-Bis(methylsulfonyl)-1-2-chloroethyhydrazine (90CE), the Active Anticancer Moiety Generated by Laromustine, KS119, and KS119W
    • Penketh PG, Shyam K, Zhu R, Baumann RP, Ishiguro K, et al. (2014) Influence of Phosphate and Phosphoesters on the Decomposition Pathway of 1,2-Bis(methylsulfonyl)-1-(2-chloroethyhydrazine (90CE), the Active Anticancer Moiety Generated by Laromustine, KS119, and KS119W. Chem Res Toxicol.
    • (2014) Chem Res Toxicol
    • Penketh, P.G.1    Shyam, K.2    Zhu, R.3    Baumann, R.P.4    Ishiguro, K.5
  • 6
    • 0018885999 scopus 로고
    • Mechanism of action of the nitrosoureas - IV. Reactions of bis-chloroethyl nitrosourea and chloroethyl cyclohexyl nitrosourea with deoxyribonucleic acid
    • DOI 10.1016/0006-2952(80)90079-9
    • Gombar CT, Tong WP, Ludlum DB (1980) Mechanism of action of the nitrosoureas-IV. Reactions of bis-chloroethyl nitrosourea and chloroethyl cyclohexyl nitrosourea with deoxyribonucleic acid. Biochem Pharmacol 29: 2639-2643. (Pubitemid 10060022)
    • (1980) Biochemical Pharmacology , vol.29 , Issue.19 , pp. 2639-2643
    • Gombar, C.T.1    Tong, W.P.2    Ludlum, D.V.3
  • 7
    • 0025045171 scopus 로고
    • Mechanism of action of (2-haloethyl)nitrosoureas on DNA: Discrimination between alternative pathways of DNA base modification by 1,3-bis(2-fluoroethyl)- 1-nitrosourea by using specific deuterium labeling and identification of reaction products by HPLC/tandem mass spectrometry
    • Naghipur A, Ikonomou MG, Kebarle P, Lown JW (1990) Mechanism of action of (2-haloethyl)nitrosoureas on DNA - discrimination between alternative pathways of DNA-base modification by 1,3-bis(2-fluoroethyl)-1-nitrosourea by using specific deuterium labeling and identification of reaction-products by HPLC tandem mass-spectrometry. J Am Chem Soc 112: 3178-3187. (Pubitemid 20321604)
    • (1990) Journal of the American Chemical Society , vol.112 , Issue.8 , pp. 3178-3187
    • Naghipur, A.1    Ikonomou, M.G.2    Kebarle, P.3    Lown, J.W.4
  • 8
    • 0032894654 scopus 로고    scopus 로고
    • Results and long term follow-up for 1581 patients with metastatic breast carcinoma treated with standard dose doxorubicin-containing chemotherapy: A reference
    • DOI 10.1002/(SICI)1097-0142(19990101)85:1<104::AID
    • Rahman ZU, Frye DK, Smith TL, Asmar L, Theriault RL, et al. (1999) Results and long term follow-up for 1581 patients with metastatic breast carcinoma treated with standard dose doxorubicin-containing chemotherapy: a reference. Cancer 85: 104-111. (Pubitemid 29031363)
    • (1999) Cancer , vol.85 , Issue.1 , pp. 104-111
    • Rahman, Z.U.1    Frye, D.K.2    Smith, T.L.3    Asmar, L.4    Theriault, R.L.5    Buzdar, A.U.6    Hortobagyi, G.N.7
  • 9
    • 18044386187 scopus 로고    scopus 로고
    • Differential inhibition of cellular glutathione reductase activity by isocyanates generated from the antitumor prodrugs Cloretazine and BCNU
    • DOI 10.1016/j.bcp.2005.02.016
    • Rice KP, Penketh PG, Shyam K, Sartorelli AC (2005) Differential inhibition of cellular glutathione reductase activity by isocyanates generated from the antitumor prodrugs Cloretazine and BCNU. Biochem Pharmacol 69: 1463-1472. (Pubitemid 40602446)
    • (2005) Biochemical Pharmacology , vol.69 , Issue.10 , pp. 1463-1472
    • Rice, K.P.1    Penketh, P.G.2    Shyam, K.3    Sartorelli, A.C.4
  • 10
    • 0035029131 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • DOI 10.1146/annurev.pharmtox.41.1.261
    • Powis G, Montfort WR (2001) Properties and biological activities of thioredoxins. Annu Rev Pharmacol Toxicol 41: 261-295. (Pubitemid 32385890)
    • (2001) Annual Review of Pharmacology and Toxicology , vol.41 , pp. 261-295
    • Powis, G.1    Montfort, W.R.2
  • 11
    • 84874051169 scopus 로고    scopus 로고
    • Thioredoxin and Thioredoxin Target Proteins: From Molecular Mechanisms to Functional Significance
    • Lee S, Kim SM, Lee RT (2013) Thioredoxin and Thioredoxin Target Proteins: From Molecular Mechanisms to Functional Significance. Antioxid Redox Signal 18: 1165-1207.
    • (2013) Antioxid Redox Signal , vol.18 , pp. 1165-1207
    • Lee, S.1    Kim, S.M.2    Lee, R.T.3
  • 12
    • 84867711090 scopus 로고    scopus 로고
    • Thioredoxin system in cell death progression
    • Lu J, Holmgren A (2012) Thioredoxin system in cell death progression. Antioxid Redox Signal 17: 1738-1747.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 1738-1747
    • Lu, J.1    Holmgren, A.2
  • 14
    • 0037188936 scopus 로고    scopus 로고
    • Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner
    • DOI 10.1161/01.RES.0000022160.64355.62
    • Liu Y, Min W (2002) Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner. Cir Res 90: 1259-1266. (Pubitemid 34787407)
    • (2002) Circulation Research , vol.90 , Issue.12 , pp. 1259-1266
    • Liu, Y.1    Min, W.2
  • 15
    • 0041743148 scopus 로고    scopus 로고
    • AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3
    • DOI 10.1172/JCI200317790
    • Zhang R, He X, Liu W, Lu M, Hsieh JT, et al. (2003) AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3. J Clin Invest 111: 1933-1943. (Pubitemid 38057738)
    • (2003) Journal of Clinical Investigation , vol.111 , Issue.12 , pp. 1933-1943
    • Zhang, R.1    He, X.2    Liu, W.3    Lu, M.4    Hsieh, J.-T.5    Min, W.6
  • 16
    • 2942696470 scopus 로고    scopus 로고
    • Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner
    • DOI 10.1161/01.RES.0000130525.37646.a7
    • Zhang R, Al-Lamki R, Bai L, Streb JW, Miano JM, et al. (2004) Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner. Circ Res 94: 1483-1491. (Pubitemid 38780321)
    • (2004) Circulation Research , vol.94 , Issue.11 , pp. 1483-1491
    • Zhang, R.1    Al-Lamki, R.2    Bai, L.3    Streb, J.W.4    Miano, J.M.5    Bradley, J.6    Min, W.7
  • 18
    • 77950547739 scopus 로고    scopus 로고
    • The roles of ASK family proteins in stress responses and diseases
    • Hattori K, Naguro I, Runchel C, Ichijo H (2009) The roles of ASK family proteins in stress responses and diseases. Cell Commun Signal 7: 9.
    • (2009) Cell Commun Signal , vol.7 , pp. 9
    • Hattori, K.1    Naguro, I.2    Runchel, C.3    Ichijo, H.4
  • 21
    • 0034714355 scopus 로고    scopus 로고
    • Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria-dependent caspase activation
    • Hatai T, Matsuzawa A, Inoshita S, Mochida Y, Kuroda T, et al. (2000) Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria-dependent caspase activation. J Biol Chem 275: 26576-26581.
    • (2000) J Biol Chem , vol.275 , pp. 26576-26581
    • Hatai, T.1    Matsuzawa, A.2    Inoshita, S.3    Mochida, Y.4    Kuroda, T.5
  • 22
    • 0035965345 scopus 로고    scopus 로고
    • A kinase-independent function of Ask1 in caspase-independent cell death
    • Charette SJ, Lambert H, Landry J (2001) A kinase-independent function of Ask1 in caspase-independent cell death. J Biol Chem 276: 36071-36074.
    • (2001) J Biol Chem , vol.276 , pp. 36071-36074
    • Charette, S.J.1    Lambert, H.2    Landry, J.3
  • 23
    • 0034001070 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin
    • DOI 10.1128/MCB.20.6.2198-2208.2000
    • Liu H, Nishitoh H, Ichijo H, Kyriakis JM (2000) Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin. Mol Cell Biol 20: 2198-2208. (Pubitemid 30123835)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.6 , pp. 2198-2208
    • Liu, H.1    Nishitoh, H.2    Ichijo, H.3    Kyriakis, J.M.4
  • 24
    • 22244445193 scopus 로고    scopus 로고
    • Dissociation of Akt1 from its negative regulator JIP1 is mediated through the ASK1-MEK-JNK signal transduction pathway during metabolic oxidative stress: A negative feedback loop
    • DOI 10.1083/jcb.200502070
    • Song JJ, Lee YJ (2005) Dissociation of Akt1 from its negative regulator JIP1 is mediated through the ASK1-MEK-JNK signal transduction pathway during metabolic oxidative stress: a negative feedback loop. J Cell Biol 170: 61-72. (Pubitemid 40994096)
    • (2005) Journal of Cell Biology , vol.170 , Issue.1 , pp. 61-72
    • Song, J.J.1    Lee, Y.J.2
  • 26
    • 0035064951 scopus 로고    scopus 로고
    • Laminar flow inhibits TNF-induced ASK1 activation by preventing dissociation of ASK1 from its inhibitor 14-3-3
    • Liu Y, Yin G, Surapisitchat J, Berk BC, Min W (2001) Laminar flow inhibits TNF-induced ASK1 activation by preventing dissociation of ASK1 from its inhibitor 14-3-3. J Clin Invest 107: 917-923. (Pubitemid 32274045)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.7 , pp. 917-923
    • Liu, Y.1    Yin, G.2    Surapisitchat, J.3    Berk, B.C.4    Min, W.5
  • 27
    • 34447531013 scopus 로고    scopus 로고
    • RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation
    • DOI 10.1074/jbc.M701148200
    • Zhang H, Zhang H, Lin Y, Li J, Pober JS, et al. (2007) RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation. J Biol Chem 282: 14788-14796. (Pubitemid 47093366)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.20 , pp. 14788-14796
    • Zhang, R.1    Zhang, H.2    Lin, Y.3    Li, J.4    Pober, J.S.5    Min, W.6
  • 28
    • 42049105550 scopus 로고    scopus 로고
    • AIP1 recruits phosphatase PP2A to ASK1 in tumor necrosis factor-induced ASK1-JNK activation
    • DOI 10.1161/CIRCRESAHA.107.168153
    • Min W, Lin Y, Tang S, Yu L, Zhang H, et al. (2008) AIP1 recruits phosphatase PP2A to ASK1 in tumor necrosis factor-induced ASK1-JNK activation. Circ Res 102: 840-848. (Pubitemid 351521590)
    • (2008) Circulation Research , vol.102 , Issue.7 , pp. 840-848
    • Min, W.1    Lin, Y.2    Tang, S.3    Yu, L.4    Zhang, H.5    Wan, T.6    Luhn, T.7    Fu, H.8    Chen, H.9
  • 30
    • 0035133227 scopus 로고    scopus 로고
    • Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1
    • DOI 10.1128/MCB.21.3.893-901.2001
    • Kim AH, Khursigara G, Sun X, Franke TF, Chao MV (2001) Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1. Mol Cell Biol 21: 893-901. (Pubitemid 32104737)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.3 , pp. 893-901
    • Kim, A.H.1    Khursigara, G.2    Sun, X.3    Franke, T.F.4    Chao, M.V.5
  • 31
    • 20544446881 scopus 로고    scopus 로고
    • Hsp90-Akt phosphorylates ASK1 and inhibits ASK1-mediated apoptosis
    • DOI 10.1038/sj.onc.1208548
    • Zhang R, Luo D, Miao R, Bai L, Ge Q, et al. (2005) Hsp90-Akt phosphorylates ASK1 and inhibits ASK1-mediated apoptosis. Oncogene 24: 3954-3963. (Pubitemid 40896407)
    • (2005) Oncogene , vol.24 , Issue.24 , pp. 3954-3963
    • Zhang, R.1    Luo, D.2    Miao, R.3    Bai, L.4    Ge, Q.5    Sessa, W.C.6    Min, W.7
  • 32
    • 0033583321 scopus 로고    scopus 로고
    • Microtubule dysfunction induced by paclitaxel initiates apoptosis through both c-Jun N-terminal kinase (JNK)-dependent and -independent pathways in ovarian cancer cells
    • Wang TH, Popp DM, Wang HS, Saitoh M, Mural JG, et al. (1999) Microtubule dysfunction induced by paclitaxel initiates apoptosis through both c-Jun N-terminal kinase (JNK)-dependent and -independent pathways in ovarian cancer cells. J Biol Chem 274: 8208-8216.
    • (1999) J Biol Chem , vol.274 , pp. 8208-8216
    • Wang, T.H.1    Popp, D.M.2    Wang, H.S.3    Saitoh, M.4    Mural, J.G.5
  • 33
    • 0029971486 scopus 로고    scopus 로고
    • Comparison of several antiangiogenic regimens alone and with cytotoxic therapies in the Lewis lung carcinoma
    • DOI 10.1007/s002800050466
    • Teicher BA, Holden SA, Ara G, Korbut T, Menon K (1996) Comparison of several antiangiogenic regimens alone and with cytotoxic therapies in the Lewis lung carcinoma. Cancer Chemother Pharmacol 38: 169-177. (Pubitemid 26132405)
    • (1996) Cancer Chemotherapy and Pharmacology , vol.38 , Issue.2 , pp. 169-177
    • Teicher, B.A.1    Holden, S.A.2    Ara, G.3    Korbut, T.4    Menon, K.5
  • 34
    • 0029061416 scopus 로고
    • 1,3-Bis(2-chloroethyl)-1-nitrosourea as thiolcarbamoylating agent in biological systems
    • Becker K, Schirmer RH (1995) 1,3-Bis(2-chloroethyl)-1-nitrosourea as thiolcarbamoylating agent in biological systems. Methods Enzymol 251: 173-188.
    • (1995) Methods Enzymol , vol.251 , pp. 173-188
    • Becker, K.1    Schirmer, R.H.2
  • 35
    • 84867332189 scopus 로고    scopus 로고
    • Thioredoxin reductase is inhibited by the carbamoylating activity of the anticancer sulfonylhydrazine drug laromustine
    • Rice KP, Klinkerch EJ, Gerber SA, Schleicher TR, Kraus TJ, et al. (2012) Thioredoxin reductase is inhibited by the carbamoylating activity of the anticancer sulfonylhydrazine drug laromustine. Mol Cell Biochem 370: 199-207.
    • (2012) Mol Cell Biochem , vol.370 , pp. 199-207
    • Rice, K.P.1    Klinkerch, E.J.2    Gerber, S.A.3    Schleicher, T.R.4    Kraus, T.J.5
  • 36
    • 0034652113 scopus 로고    scopus 로고
    • Thioredoxin reductase
    • DOI 10.1042/0264-6021:3460001
    • Mustacich D, Powis G (2000) Thioredoxin reductase. Biochem J 346 Pt 1: 1-8. (Pubitemid 30113812)
    • (2000) Biochemical Journal , vol.346 , Issue.1 , pp. 1-8
    • Mustacich, D.1    Powis, G.2
  • 37
    • 0025062053 scopus 로고
    • The mechanism of action of the nitrosourea anti-tumor drugs on thioredoxin reductase, glutathione reductase and ribonucleotide reductase
    • DOI 10.1016/0167-4889(90)90199-N
    • Schallreuter KU, Gleason FK, Wood JM (1990) The mechanism of action of the nitrosourea anti-tumor drugs on thioredoxin reductase, glutathione reductase and ribonucleotide reductase. Biochim Biophys Acta 1054: 14-20. (Pubitemid 20247791)
    • (1990) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1054 , Issue.1 , pp. 14-20
    • Schallreuter, K.U.1    Gleason, F.K.2    Wood, J.M.3
  • 39
    • 84884823502 scopus 로고    scopus 로고
    • CYLD deubiquitinates RIP1 in the TNFalpha-induced necrosome to facilitate kinase activation and programmed necrosis
    • Moquin DM, McQuade T, Chan FK (2013) CYLD deubiquitinates RIP1 in the TNFalpha-induced necrosome to facilitate kinase activation and programmed necrosis. PLoS One 8: e76841.
    • (2013) PLoS One , vol.8
    • Moquin, D.M.1    McQuade, T.2    Chan, F.K.3
  • 40
    • 79956328903 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical applications of angiogenesis
    • Carmeliet P, Jain RK (2011) Molecular mechanisms and clinical applications of angiogenesis. Nature 473: 298-307.
    • (2011) Nature , vol.473 , pp. 298-307
    • Carmeliet, P.1    Jain, R.K.2
  • 41
    • 0016439876 scopus 로고
    • Inhibition of rat liver DNA polymerase by nitrosoureas and isocyanates
    • Baril BB, Baril EF, Laszlo J, Wheeler GP (1975) Inhibition of rat liver DNA polymerase by nitrosoureas and isocyanates. Cancer Res 35: 1-5.
    • (1975) Cancer Res , vol.35 , pp. 1-5
    • Baril, B.B.1    Baril, E.F.2    Laszlo, J.3    Wheeler, G.P.4
  • 42
    • 0015962431 scopus 로고
    • Inhibition of DNA repair by the 1,3-bis(2-chloroethyl)-1-nitrosourea breakdown product, 2-chloroethyl isocyanate
    • Kann HE Jr, Kohn KW, Lyles JM (1974) Inhibition of DNA repair by the 1,3-bis(2-chloroethyl)-1-nitrosourea breakdown product, 2-chloroethyl isocyanate. Cancer Res 34: 398-402.
    • (1974) Cancer Res , vol.34 , pp. 398-402
    • Kann Jr., H.E.1    Kohn, K.W.2    Lyles, J.M.3
  • 43
    • 0017865443 scopus 로고
    • Inactivation of glutathione reductase by 2-chloroethyl nitrosourea-derived isocyanates
    • Babson JR, Reed DJ (1978) Inactivation of glutathione reductase by 2- chloroethyl nitrosourea-derived isocyanates. Biochem Biophys Res Commun 83: 754-762. (Pubitemid 8394482)
    • (1978) Biochemical and Biophysical Research Communications , vol.83 , Issue.2 , pp. 754-762
    • Babson, J.R.1    Reed, D.J.2
  • 44
    • 0019945031 scopus 로고
    • The role of isocyanates in the toxicity of antitumour haloalkylnitrosoureas
    • DOI 10.1016/0006-2952(82)90135-6
    • Gibson NW, Hickman JA (1982) The role of isocyanates in the toxicity of antitumour haloalkylnitrosoureas. Biochem Pharmacol 31: 2795-2800. (Pubitemid 12052513)
    • (1982) Biochemical Pharmacology , vol.31 , Issue.17 , pp. 2795-2800
    • Gibson, N.W.1    Hickman, J.A.2
  • 45
    • 0018103960 scopus 로고
    • Evaluation of the role of isocyanates in the action of therapeutic nitrosoureas
    • DOI 10.1016/0006-2952(78)90120-X
    • Hilton J, Maldarelli F, Sargent S (1978) Evaluation of the role of isocyanates in the action of therapeutic nitrosoureas. Biochem Pharmacol 27: 1359-1363. (Pubitemid 8401723)
    • (1978) Biochemical Pharmacology , vol.27 , Issue.9 , pp. 1359-1363
    • Hilton, J.1    Maldarelli, F.2    Sargent, S.3
  • 46
    • 0022588793 scopus 로고
    • Relationship of structure to anticancer activity and toxicity of the nitrosoureas in animal systems
    • Johnston TP, Montgomery JA (1986) Relationship of structure to anticancer activity and toxicity of the nitrosoureas in animal systems. Cancer Treat Rep 70: 13-30. (Pubitemid 16140366)
    • (1986) Cancer Treatment Reports , vol.70 , Issue.1 , pp. 13-30
    • Johnston, T.P.1    Montgomery, J.A.2
  • 47
    • 0033775650 scopus 로고    scopus 로고
    • Thioredoxin reductase as a pathophysiological factor and drug target
    • Becker K, Gromer S, Schirmer RH, Muller S (2000) Thioredoxin reductase as a pathophysiological factor and drug target. Eur J Biochem 267: 6118-6125.
    • (2000) Eur J Biochem , vol.267 , pp. 6118-6125
    • Becker, K.1    Gromer, S.2    Schirmer, R.H.3    Muller, S.4
  • 48
    • 66149102423 scopus 로고    scopus 로고
    • Mechanisms of Endothelial Dysfunction, Injury, and Death
    • Pober JS, Min W, Bradley JR (2009) Mechanisms of Endothelial Dysfunction, Injury, and Death. Annu Rev Pathol 4: 71-95.
    • (2009) Annu Rev Pathol , vol.4 , pp. 71-95
    • Pober, J.S.1    Min, W.2    Bradley, J.R.3
  • 50
    • 43249095919 scopus 로고    scopus 로고
    • Tumor angiogenesis
    • Kerbel RS (2008) Tumor angiogenesis. N Engl J Med 358: 2039-2049.
    • (2008) N Engl J Med , vol.358 , pp. 2039-2049
    • Kerbel, R.S.1
  • 53
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254: 9627-9632.
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 54
    • 57449115615 scopus 로고    scopus 로고
    • AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice
    • Zhang H, He Y, Dai S, Xu Z, Luo Y, et al. (2008) AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice. J Clin Invest 118: 3904-3916.
    • (2008) J Clin Invest , vol.118 , pp. 3904-3916
    • Zhang, H.1    He, Y.2    Dai, S.3    Xu, Z.4    Luo, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.