메뉴 건너뛰기




Volumn 275, Issue 15, 2008, Pages 3884-3899

Rhodanese-thioredoxin system and allyl sulfur compounds: Implications in apoptosis induction

Author keywords

Garlic; Mobile lipids; Sodium 2 propenyl thiosulfate (2 PTS); Sulfane sulfur; Sulfurtransferase

Indexed keywords

CYSTEINE; CYTOTOXIC AGENT; LIPID; N PROPYL THIOSULFATE; SODIUM 2 PROPENYL THIOSULFATE; THIOREDOXIN; THIOSULFATE SULFURTRANSFERASE;

EID: 47249151065     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06535.x     Document Type: Article
Times cited : (39)

References (71)
  • 1
    • 0022550131 scopus 로고
    • Persulfide sulfur is a growth factor for cells defective in sulfur metabolism
    • Toohey JI (1986) Persulfide sulfur is a growth factor for cells defective in sulfur metabolism. Biochem Cell Biol 64, 758 765.
    • (1986) Biochem Cell Biol , vol.64 , pp. 758-765
    • Toohey, J.I.1
  • 2
    • 0029970362 scopus 로고    scopus 로고
    • Diallyl disulfide induces apoptosis of human colon tumor cells
    • Sundaram SG Milner JA (1996) Diallyl disulfide induces apoptosis of human colon tumor cells. Carcinogenesis 17, 669 673.
    • (1996) Carcinogenesis , vol.17 , pp. 669-673
    • Sundaram, S.G.1    Milner, J.A.2
  • 3
    • 0031445546 scopus 로고    scopus 로고
    • Allyl sulfides from garlic suppress the in vitro proliferation of human A549 lung tumor cells
    • Sakamoto K, Lawson LD Milner JA (1997) Allyl sulfides from garlic suppress the in vitro proliferation of human A549 lung tumor cells. Nutr Cancer 29, 152 156.
    • (1997) Nutr Cancer , vol.29 , pp. 152-156
    • Sakamoto, K.1    Lawson, L.D.2    Milner, J.A.3
  • 4
    • 0035119745 scopus 로고    scopus 로고
    • Possible mechanism by which allyl sulfides suppress neoplastic cell proliferation
    • Knowles LM Milner JA (2001) Possible mechanism by which allyl sulfides suppress neoplastic cell proliferation. J Nutr 131, 1061S 1066S.
    • (2001) J Nutr , vol.131
    • Knowles, L.M.1    Milner, J.A.2
  • 5
    • 0141842655 scopus 로고    scopus 로고
    • Reactive oxygen species-dependent c-Jun NH2-terminal kinase/c-Jun signaling cascade mediates neuroblastoma cell death induced by diallyl disulfide
    • Filomeni G, Aquilano K, Rotilio G Ciriolo MR (2003) Reactive oxygen species-dependent c-Jun NH2-terminal kinase/c-Jun signaling cascade mediates neuroblastoma cell death induced by diallyl disulfide. Cancer Res 63, 5940 5949.
    • (2003) Cancer Res , vol.63 , pp. 5940-5949
    • Filomeni, G.1    Aquilano, K.2    Rotilio, G.3    Ciriolo, M.R.4
  • 6
    • 28044435379 scopus 로고    scopus 로고
    • Diallyl trisulfide-induced G(2)-M phase cell cycle arrest in human prostate cancer cells is caused by reactive oxygen species-dependent destruction and hyperphosphorylation of Cdc 25 C
    • Xiao D, Herman-Antosiewicz A, Antosiewicz J, Xiao H, Brisson M, Lazo JS Singh SV (2005) Diallyl trisulfide-induced G(2)-M phase cell cycle arrest in human prostate cancer cells is caused by reactive oxygen species-dependent destruction and hyperphosphorylation of Cdc 25 C. Oncogene 24, 6256 6268.
    • (2005) Oncogene , vol.24 , pp. 6256-6268
    • Xiao, D.1    Herman-Antosiewicz, A.2    Antosiewicz, J.3    Xiao, H.4    Brisson, M.5    Lazo, J.S.6    Singh, S.V.7
  • 7
    • 18844372222 scopus 로고    scopus 로고
    • Growth inhibitory effect of alk(en)yl thiosulfates derived from onion and garlic in human immortalized and tumor cell lines
    • Chang HS, Yamato O, Yamasaki M, Ko M Maede Y (2005) Growth inhibitory effect of alk(en)yl thiosulfates derived from onion and garlic in human immortalized and tumor cell lines. Cancer Lett 223, 47 55.
    • (2005) Cancer Lett , vol.223 , pp. 47-55
    • Chang, H.S.1    Yamato, O.2    Yamasaki, M.3    Ko, M.4    Maede, Y.5
  • 8
    • 0018847874 scopus 로고
    • A secreted glycoprotein induced by estrogen in human breast cancer cell lines
    • Westley B Rochefort H (1980) A secreted glycoprotein induced by estrogen in human breast cancer cell lines. Cell 20, 353 362.
    • (1980) Cell , vol.20 , pp. 353-362
    • Westley, B.1    Rochefort, H.2
  • 9
    • 0032508464 scopus 로고    scopus 로고
    • A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain
    • Hofmann K, Bucher P Kajava AV (1998) A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. J Mol Biol 282, 195 208.
    • (1998) J Mol Biol , vol.282 , pp. 195-208
    • Hofmann, K.1    Bucher, P.2    Kajava, A.V.3
  • 10
    • 0036668633 scopus 로고    scopus 로고
    • The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations
    • Bordo D Bork P (2002) The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations. EMBO Rep 3, 741 746.
    • (2002) EMBO Rep , vol.3 , pp. 741-746
    • Bordo, D.1    Bork, P.2
  • 11
    • 0034708503 scopus 로고    scopus 로고
    • Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate
    • Palenchar PM, Buck CJ, Cheng H, Larson TJ Mueller EG (2000) Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate. J Biol Chem 275, 8283 8286.
    • (2000) J Biol Chem , vol.275 , pp. 8283-8286
    • Palenchar, P.M.1    Buck, C.J.2    Cheng, H.3    Larson, T.J.4    Mueller, E.G.5
  • 12
    • 0035859880 scopus 로고    scopus 로고
    • Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: Possible role of a protein perselenide in a selenium delivery system
    • Ogasawara Y, Lacourciere G Stadtman TC (2001) Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: possible role of a protein perselenide in a selenium delivery system. Proc Natl Acad Sci USA 98, 9494 9498.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9494-9498
    • Ogasawara, Y.1    Lacourciere, G.2    Stadtman, T.C.3
  • 13
    • 0345826117 scopus 로고    scopus 로고
    • Functional diversity of the rhodanese homology domain: The Escherichia coli ybbB gene encodes a selenophosphate-dependent tRNA 2-selenouridine synthase
    • Wolfe MD, Ahmed F, Lacourciere GM, Lauhon CT, Stadtman TC Larson TJ (2004) Functional diversity of the rhodanese homology domain: the Escherichia coli ybbB gene encodes a selenophosphate-dependent tRNA 2-selenouridine synthase. J Biol Chem 279, 1801 1809.
    • (2004) J Biol Chem , vol.279 , pp. 1801-1809
    • Wolfe, M.D.1    Ahmed, F.2    Lacourciere, G.M.3    Lauhon, C.T.4    Stadtman, T.C.5    Larson, T.J.6
  • 14
    • 0017649249 scopus 로고
    • Insertion of sulfide into ferredoxins catalyzed by rhodanese
    • Bonomi F, Pagani S Cerletti P (1977) Insertion of sulfide into ferredoxins catalyzed by rhodanese. FEBS Lett 84, 149 152.
    • (1977) FEBS Lett , vol.84 , pp. 149-152
    • Bonomi, F.1    Pagani, S.2    Cerletti, P.3
  • 15
    • 34047108645 scopus 로고    scopus 로고
    • Effects of the deficiency of the rhodanese-like protein RhdA in Azotobacter vinelandii
    • Cereda A, Carpen A, Picariello G, Iriti M, Faoro F, Ferranti P Pagani S (2007) Effects of the deficiency of the rhodanese-like protein RhdA in Azotobacter vinelandii. FEBS Lett 581, 1625 1630.
    • (2007) FEBS Lett , vol.581 , pp. 1625-1630
    • Cereda, A.1    Carpen, A.2    Picariello, G.3    Iriti, M.4    Faoro, F.5    Ferranti, P.6    Pagani, S.7
  • 17
    • 27144442871 scopus 로고    scopus 로고
    • Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis
    • Nagahara N Katayama A (2005) Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis. J Biol Chem 280, 34569 34576.
    • (2005) J Biol Chem , vol.280 , pp. 34569-34576
    • Nagahara, N.1    Katayama, A.2
  • 18
    • 33847335589 scopus 로고    scopus 로고
    • Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation
    • Nagahara N, Yoshii T, Abe Y Matsumura T (2007) Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation. J Biol Chem 282, 1561 1569.
    • (2007) J Biol Chem , vol.282 , pp. 1561-1569
    • Nagahara, N.1    Yoshii, T.2    Abe, Y.3    Matsumura, T.4
  • 22
    • 0041808717 scopus 로고    scopus 로고
    • Decreased expression of genes involved in sulfur amino acid metabolism in frataxin-deficient cells
    • Tan G, Napoli E, Taroni F Cortopassi G (2003) Decreased expression of genes involved in sulfur amino acid metabolism in frataxin-deficient cells. Hum Mol Genet 12, 1699 1711.
    • (2003) Hum Mol Genet , vol.12 , pp. 1699-1711
    • Tan, G.1    Napoli, E.2    Taroni, F.3    Cortopassi, G.4
  • 23
    • 0031976715 scopus 로고    scopus 로고
    • Ajoene, a compound of garlic, induces apoptosis in human promyeloleukemic cells, accompanied by generation of reactive oxygen species and activation of nuclear factor kappaB
    • Dirsch VM, Gerbes AL Vollmar AM (1998) Ajoene, a compound of garlic, induces apoptosis in human promyeloleukemic cells, accompanied by generation of reactive oxygen species and activation of nuclear factor kappaB. Mol Pharmacol 53, 402 407.
    • (1998) Mol Pharmacol , vol.53 , pp. 402-407
    • Dirsch, V.M.1    Gerbes, A.L.2    Vollmar, A.M.3
  • 28
    • 0346789744 scopus 로고    scopus 로고
    • Isolation and identification of sodium 2-propenyl thiosulfate from boiled garlic (Allium sativum) that oxidizes canine erythrocytes
    • Yamato O, Sugiyama Y, Matsuura H, Lee KW, Goto K, Hossain MA, Maede Y Yoshihara T (2003) Isolation and identification of sodium 2-propenyl thiosulfate from boiled garlic (Allium sativum) that oxidizes canine erythrocytes. Biosci Biotechnol Biochem 67, 1594 1596.
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 1594-1596
    • Yamato, O.1    Sugiyama, Y.2    Matsuura, H.3    Lee, K.W.4    Goto, K.5    Hossain, M.A.6    Maede, Y.7    Yoshihara, T.8
  • 29
    • 17844369134 scopus 로고    scopus 로고
    • Modulatory influence of sodium 2-propenyl thiosulfate from garlic on cyclooxygenase activity in canine platelets: Possible mechanism for the anti-aggregatory effect
    • Chang HS, Yamato O, Yamasaki M Maede Y (2005) Modulatory influence of sodium 2-propenyl thiosulfate from garlic on cyclooxygenase activity in canine platelets: possible mechanism for the anti-aggregatory effect. Prostaglandins Leukot Essent Fatty Acids 72, 351 355.
    • (2005) Prostaglandins Leukot Essent Fatty Acids , vol.72 , pp. 351-355
    • Chang, H.S.1    Yamato, O.2    Yamasaki, M.3    Maede, Y.4
  • 31
    • 0029867422 scopus 로고    scopus 로고
    • Cloning, sequence analysis and overexpression of the rhodanese gene of Azotobacter vinelandii
    • Colnaghi R, Pagani S, Kennedy C Drummond M (1996) Cloning, sequence analysis and overexpression of the rhodanese gene of Azotobacter vinelandii. Eur J Biochem 236, 240 248.
    • (1996) Eur J Biochem , vol.236 , pp. 240-248
    • Colnaghi, R.1    Pagani, S.2    Kennedy, C.3    Drummond, M.4
  • 32
    • 0026084143 scopus 로고
    • Identification of sulfurtransferase enzymes in Azotobacter vinelandii
    • Pagani S, Franchi E, Colnaghi R Kennedy C (1991) Identification of sulfurtransferase enzymes in Azotobacter vinelandii. FEBS Lett 278, 151 154.
    • (1991) FEBS Lett , vol.278 , pp. 151-154
    • Pagani, S.1    Franchi, E.2    Colnaghi, R.3    Kennedy, C.4
  • 34
    • 0034640125 scopus 로고    scopus 로고
    • The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families
    • Bordo D, Deriu D, Colnaghi R, Carpen A, Pagani S Bolognesi M (2000) The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families. J Mol Biol 298, 691 704.
    • (2000) J Mol Biol , vol.298 , pp. 691-704
    • Bordo, D.1    Deriu, D.2    Colnaghi, R.3    Carpen, A.4    Pagani, S.5    Bolognesi, M.6
  • 35
    • 0142088879 scopus 로고    scopus 로고
    • Azotobacter vinelandii rhodanese: Selenium loading and ion interaction studies
    • Melino S, Cicero DO, Orsale M, Forlani F, Pagani S Paci M (2003) Azotobacter vinelandii rhodanese: selenium loading and ion interaction studies. Eur J Biochem 270, 4208 4215.
    • (2003) Eur J Biochem , vol.270 , pp. 4208-4215
    • Melino, S.1    Cicero, D.O.2    Orsale, M.3    Forlani, F.4    Pagani, S.5    Paci, M.6
  • 36
    • 33845426649 scopus 로고    scopus 로고
    • Backbone NMR assignment of the 29.6 kDa rhodanese protein from Azotobacter vinelandii
    • Gallo M, Melino S, Melis R, Paci M Cicero DO (2006) Backbone NMR assignment of the 29.6 kDa rhodanese protein from Azotobacter vinelandii. J Biomol NMR 36 (Suppl. 1 73.
    • (2006) J Biomol NMR , vol.36 , Issue.1 , pp. 73
    • Gallo, M.1    Melino, S.2    Melis, R.3    Paci, M.4    Cicero, D.O.5
  • 38
    • 0021958059 scopus 로고
    • Evidence for dynamically determined conformational states in rhodanese catalysis
    • Chow SF, Horowitz PM, Westley J Jarabak R (1985) Evidence for dynamically determined conformational states in rhodanese catalysis. J Biol Chem 260, 2763 2770.
    • (1985) J Biol Chem , vol.260 , pp. 2763-2770
    • Chow, S.F.1    Horowitz, P.M.2    Westley, J.3    Jarabak, R.4
  • 39
    • 0023052447 scopus 로고
    • Active site modifications quench intrinsic fluorescence of rhodanese by different mechanisms
    • Cannella C, Berni R, Rosato N Finazzi-Agro A (1986) Active site modifications quench intrinsic fluorescence of rhodanese by different mechanisms. Biochemistry 25, 7319 7323.
    • (1986) Biochemistry , vol.25 , pp. 7319-7323
    • Cannella, C.1    Berni, R.2    Rosato, N.3    Finazzi-Agro, A.4
  • 40
    • 28844486737 scopus 로고    scopus 로고
    • The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form
    • Forlani F, Cereda A, Freuer A, Nimtz M, Leimkuhler S Pagani S (2005) The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form. FEBS Lett 579, 6786 6790.
    • (2005) FEBS Lett , vol.579 , pp. 6786-6790
    • Forlani, F.1    Cereda, A.2    Freuer, A.3    Nimtz, M.4    Leimkuhler, S.5    Pagani, S.6
  • 41
    • 0021099750 scopus 로고
    • The use of intrinsic protein fluorescence to quantitate enzyme-bound persulfide and to measure equilibria between intermediates in rhodanese catalysis
    • Horowitz P Criscimagna NL (1983) The use of intrinsic protein fluorescence to quantitate enzyme-bound persulfide and to measure equilibria between intermediates in rhodanese catalysis. J Biol Chem 258, 7894 7896.
    • (1983) J Biol Chem , vol.258 , pp. 7894-7896
    • Horowitz, P.1    Criscimagna, N.L.2
  • 42
    • 9144268978 scopus 로고    scopus 로고
    • The N-terminal rhodanese domain from Azotobacter vinelandii has a stable and folded structure independently of the C-terminal domain
    • Melino S, Cicero DO, Forlani F, Pagani S Paci M (2004) The N-terminal rhodanese domain from Azotobacter vinelandii has a stable and folded structure independently of the C-terminal domain. FEBS Lett 577, 403 408.
    • (2004) FEBS Lett , vol.577 , pp. 403-408
    • Melino, S.1    Cicero, D.O.2    Forlani, F.3    Pagani, S.4    Paci, M.5
  • 43
    • 0024297011 scopus 로고
    • Sulfhydryl-directed triggering of conformational changes in the enzyme rhodanese
    • Horowitz PM Criscimagna NL (1988) Sulfhydryl-directed triggering of conformational changes in the enzyme rhodanese. J Biol Chem 263, 10278 10283.
    • (1988) J Biol Chem , vol.263 , pp. 10278-10283
    • Horowitz, P.M.1    Criscimagna, N.L.2
  • 44
    • 0024603419 scopus 로고
    • Oxidative inactivation of rhodanese by hydrogen peroxide produces states that show differential reactivation
    • Horowitz PM Bowman S (1989) Oxidative inactivation of rhodanese by hydrogen peroxide produces states that show differential reactivation. J Biol Chem 264, 3311 3316.
    • (1989) J Biol Chem , vol.264 , pp. 3311-3316
    • Horowitz, P.M.1    Bowman, S.2
  • 45
    • 0023664584 scopus 로고
    • Conformational changes accompany the oxidative inactivation of rhodanese by a variety of reagents
    • Horowitz PM Bowman S (1987) Conformational changes accompany the oxidative inactivation of rhodanese by a variety of reagents. J Biol Chem 262, 8728 8733.
    • (1987) J Biol Chem , vol.262 , pp. 8728-8733
    • Horowitz, P.M.1    Bowman, S.2
  • 46
    • 0031731452 scopus 로고    scopus 로고
    • Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese
    • Nandi DL Westley J (1998) Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese. Int J Biochem Cell Biol 30, 973 977.
    • (1998) Int J Biochem Cell Biol , vol.30 , pp. 973-977
    • Nandi, D.L.1    Westley, J.2
  • 48
    • 33846931878 scopus 로고    scopus 로고
    • Cancer chemoprevention with garlic and its constituents
    • Shukla Y Kalra N (2007) Cancer chemoprevention with garlic and its constituents. Cancer Lett 247, 167 181.
    • (2007) Cancer Lett , vol.247 , pp. 167-181
    • Shukla, Y.1    Kalra, N.2
  • 49
    • 33644843543 scopus 로고    scopus 로고
    • Preclinical perspectives on garlic and cancer
    • Milner JA (2006) Preclinical perspectives on garlic and cancer. J Nutr 136, 827S 831S.
    • (2006) J Nutr , vol.136
    • Milner, J.A.1
  • 50
    • 33744910333 scopus 로고    scopus 로고
    • C-Jun NH(2)-terminal kinase signaling axis regulates diallyl trisulfide-induced generation of reactive oxygen species and cell cycle arrest in human prostate cancer cells
    • Antosiewicz J, Herman-Antosiewicz A, Marynowski SW Singh SV (2006) c-Jun NH(2)-terminal kinase signaling axis regulates diallyl trisulfide-induced generation of reactive oxygen species and cell cycle arrest in human prostate cancer cells. Cancer Res 66, 5379 5386.
    • (2006) Cancer Res , vol.66 , pp. 5379-5386
    • Antosiewicz, J.1    Herman-Antosiewicz, A.2    Marynowski, S.W.3    Singh, S.V.4
  • 51
    • 29244484434 scopus 로고    scopus 로고
    • Diallyl trisulfide suppresses the proliferation and induces apoptosis of human colon cancer cells through oxidative modification of beta-tubulin
    • Hosono T, Fukao T, Ogihara J, Ito Y, Shiba H, Seki T Ariga T (2005) Diallyl trisulfide suppresses the proliferation and induces apoptosis of human colon cancer cells through oxidative modification of beta-tubulin. J Biol Chem 280, 41487 41493.
    • (2005) J Biol Chem , vol.280 , pp. 41487-41493
    • Hosono, T.1    Fukao, T.2    Ogihara, J.3    Ito, Y.4    Shiba, H.5    Seki, T.6    Ariga, T.7
  • 52
    • 0027473476 scopus 로고
    • Transamination and transsulphuration of L-cysteine in Ehrlich ascites tumor cells and mouse liver. the nonenzymatic reaction of L-cysteine with pyruvate
    • Wlodek L, Wrobel M Czubak J (1993) Transamination and transsulphuration of L-cysteine in Ehrlich ascites tumor cells and mouse liver. The nonenzymatic reaction of L-cysteine with pyruvate. Int J Biochem 25, 107 112.
    • (1993) Int J Biochem , vol.25 , pp. 107-112
    • Wlodek, L.1    Wrobel, M.2    Czubak, J.3
  • 53
    • 0034864255 scopus 로고    scopus 로고
    • Effects of diallyl disulfide and other donors of sulfane sulfur on the proliferation of human hepatoma cell line (HepG2)
    • Iciek MB, Rokita HB Wlodek LB (2001) Effects of diallyl disulfide and other donors of sulfane sulfur on the proliferation of human hepatoma cell line (HepG2). Neoplasma 48, 307 312.
    • (2001) Neoplasma , vol.48 , pp. 307-312
    • Iciek, M.B.1    Rokita, H.B.2    Wlodek, L.B.3
  • 54
    • 0030028330 scopus 로고    scopus 로고
    • Detection of apoptotic cell death by proton nuclear magnetic resonance spectroscopy
    • Blankenberg FG, Storrs RW, Naumovski L, Goralski T Spielman D (1996) Detection of apoptotic cell death by proton nuclear magnetic resonance spectroscopy. Blood 87, 1951 1956.
    • (1996) Blood , vol.87 , pp. 1951-1956
    • Blankenberg, F.G.1    Storrs, R.W.2    Naumovski, L.3    Goralski, T.4    Spielman, D.5
  • 56
    • 27844485127 scopus 로고    scopus 로고
    • Metabolic alterations in K562 cells exposed to taxol and tyrphostin AG957: 1H NMR and biochemical studies
    • Knijn A, Brisdelli F, Ferretti A, Iorio E, Marcheggiani D Bozzi A (2005) Metabolic alterations in K562 cells exposed to taxol and tyrphostin AG957: 1H NMR and biochemical studies. Cell Biol Int 29, 890 897.
    • (2005) Cell Biol Int , vol.29 , pp. 890-897
    • Knijn, A.1    Brisdelli, F.2    Ferretti, A.3    Iorio, E.4    Marcheggiani, D.5    Bozzi, A.6
  • 57
    • 0036494206 scopus 로고    scopus 로고
    • Nuclear magnetic resonance-visible lipids induced by cationic lipophilic chemotherapeutic agents are accompanied by increased lipid droplet formation and damaged mitochondria
    • Delikatny EJ, Cooper WA, Brammah S, Sathasivam N Rideout DC (2002) Nuclear magnetic resonance-visible lipids induced by cationic lipophilic chemotherapeutic agents are accompanied by increased lipid droplet formation and damaged mitochondria. Cancer Res 62, 1394 1400.
    • (2002) Cancer Res , vol.62 , pp. 1394-1400
    • Delikatny, E.J.1    Cooper, W.A.2    Brammah, S.3    Sathasivam, N.4    Rideout, D.C.5
  • 59
    • 34249944782 scopus 로고    scopus 로고
    • Alteration of mitochondrial function and cell sensitization to death
    • Gogvadze V Zhivotovsky B (2007) Alteration of mitochondrial function and cell sensitization to death. J Bioenerg Biomembr 39, 23 30.
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 23-30
    • Gogvadze, V.1    Zhivotovsky, B.2
  • 61
    • 77049229661 scopus 로고
    • Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
    • De Duve C, Pressman BC, Gianetto R, Wattiaux R Appelmans F (1955) Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem J 60, 604 617.
    • (1955) Biochem J , vol.60 , pp. 604-617
    • De Duve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 62
    • 0033796101 scopus 로고    scopus 로고
    • The role of the redox protein thioredoxin in cell growth and cancer
    • Powis G, Mustacich D Coon A (2000) The role of the redox protein thioredoxin in cell growth and cancer. Free Radic Biol Med 29, 312 322.
    • (2000) Free Radic Biol Med , vol.29 , pp. 312-322
    • Powis, G.1    Mustacich, D.2    Coon, A.3
  • 63
    • 0347600941 scopus 로고    scopus 로고
    • Regulation of the mammalian selenoprotein thioredoxin reductase 1 in relation to cellular phenotype, growth, and signaling events
    • Rundlof AK Arner ES (2004) Regulation of the mammalian selenoprotein thioredoxin reductase 1 in relation to cellular phenotype, growth, and signaling events. Antioxid Redox Signal 6, 41 52.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 41-52
    • Rundlof, A.K.1    Arner, E.S.2
  • 64
    • 0346690291 scopus 로고    scopus 로고
    • Thioredoxin as a key molecule in redox signaling
    • Nakamura H (2004) Thioredoxin as a key molecule in redox signaling. Antioxid Redox Signal 6, 15 17.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 15-17
    • Nakamura, H.1
  • 66
    • 39949083765 scopus 로고    scopus 로고
    • Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis
    • Cox AG, Pullar JM, Hughes G, Ledgerwood EC Hampton MB (2008) Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis. Free Radic Biol Med 44, 1001 1009.
    • (2008) Free Radic Biol Med , vol.44 , pp. 1001-1009
    • Cox, A.G.1    Pullar, J.M.2    Hughes, G.3    Ledgerwood, E.C.4    Hampton, M.B.5
  • 68
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti I, Migliorati G, Pagliacci MC, Grignani F Riccardi C (1991) A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J Immunol Methods 139, 271 279.
    • (1991) J Immunol Methods , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 69
    • 0019131878 scopus 로고
    • High-performance liquid chromatography analysis of nanomole levels of glutathione, glutathione disulfide, and related thiols and disulfides
    • Reed DJ, Babson JR, Beatty PW, Brodie AE, Ellis WW Potter DW (1980) High-performance liquid chromatography analysis of nanomole levels of glutathione, glutathione disulfide, and related thiols and disulfides. Anal Biochem 106, 55 62.
    • (1980) Anal Biochem , vol.106 , pp. 55-62
    • Reed, D.J.1    Babson, J.R.2    Beatty, P.W.3    Brodie, A.E.4    Ellis, W.W.5    Potter, D.W.6
  • 70
    • 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
    • Ruefli AA, Ausserlechner MJ, Bernhard D, Sutton VR, Tainton KM, Kofler R, Smyth MJ Johnstone RW (2001) 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 98, 10833 10838.
    • (2001) Proc Natl Acad Sci USA , 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
  • 71
    • 0000202110 scopus 로고
    • Crystalline rhodanese. II. the enzyme catalyzed reaction
    • 1145.
    • Sörbo BH (1953) Crystalline rhodanese. II. The enzyme catalyzed reaction. Acta Chem Scand 7, 1137 1145.
    • (1953) Acta Chem Scand , vol.7 , pp. 1137
    • Sörbo, B.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.