메뉴 건너뛰기




Volumn 122, Issue , 2014, Pages 143-175

Pleiotropic functions of glutathione S-transferase P

Author keywords

Allelic variants; Cysteine; Glutathione; Glutathione S transferase; Kinase signaling; Nitric oxide; Nitrosylation; Peroxiredoxins; Protein protein interactions; Sulfur

Indexed keywords

GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE P; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; UNCLASSIFIED DRUG; GLUTATHIONE; GLUTATHIONE TRANSFERASE P1; GSTP1 PROTEIN, HUMAN; GSTP1 PROTEIN, MOUSE; LIGAND; PEROXIREDOXIN; REACTIVE OXYGEN METABOLITE;

EID: 84902978663     PISSN: 0065230X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-420117-0.00004-9     Document Type: Chapter
Times cited : (61)

References (124)
  • 2
    • 0033230607 scopus 로고    scopus 로고
    • Role of redox potential and reactive oxygen species in stress signaling
    • Adler V., Yin Z., Tew K.D., Ronai Z. Role of redox potential and reactive oxygen species in stress signaling. Oncogene 1999, 18:6104-6111.
    • (1999) Oncogene , vol.18 , pp. 6104-6111
    • Adler, V.1    Yin, Z.2    Tew, K.D.3    Ronai, Z.4
  • 3
    • 0030899372 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins
    • Ali-Osman F., Akande O., Antoun G., Mao J.X., Buolamwini J. Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins. The Journal of Biological Chemistry 1997, 272:10004-10012.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 10004-10012
    • Ali-Osman, F.1    Akande, O.2    Antoun, G.3    Mao, J.X.4    Buolamwini, J.5
  • 4
    • 0031408932 scopus 로고    scopus 로고
    • Prognostic significance of glutathione S-transferase pi expression and subcellular localization in human gliomas
    • Ali-Osman F., Brunner J.M., Kutluk T.M., Hess K. Prognostic significance of glutathione S-transferase pi expression and subcellular localization in human gliomas. Clinical Cancer Research 1997, 3:2253-2261.
    • (1997) Clinical Cancer Research , vol.3 , pp. 2253-2261
    • Ali-Osman, F.1    Brunner, J.M.2    Kutluk, T.M.3    Hess, K.4
  • 5
    • 33846233486 scopus 로고    scopus 로고
    • Expression of glutathione S-transferase pi and glutathione synthase correlates with survival in early stage non-small cell carcinomas of the lung
    • Allen T.C., Granville L.A., Cagle P.T., Haque A., Zander D.S., Barrios R. Expression of glutathione S-transferase pi and glutathione synthase correlates with survival in early stage non-small cell carcinomas of the lung. Human Pathology 2007, 38:220-227.
    • (2007) Human Pathology , vol.38 , pp. 220-227
    • Allen, T.C.1    Granville, L.A.2    Cagle, P.T.3    Haque, A.4    Zander, D.S.5    Barrios, R.6
  • 8
    • 34250003256 scopus 로고    scopus 로고
    • Conformational change in the active center region of GST P1-1, due to binding of a synthetic conjugate of DXR with GSH, enhanced JNK-mediated apoptosis
    • Asakura T., Sasagawa A., Takeuchi H., Shibata S., Marushima H., Mamori S., et al. Conformational change in the active center region of GST P1-1, due to binding of a synthetic conjugate of DXR with GSH, enhanced JNK-mediated apoptosis. Apoptosis 2007, 12:1269-1280.
    • (2007) Apoptosis , vol.12 , pp. 1269-1280
    • Asakura, T.1    Sasagawa, A.2    Takeuchi, H.3    Shibata, S.4    Marushima, H.5    Mamori, S.6
  • 9
    • 72749095187 scopus 로고    scopus 로고
    • Glutathione transferases are structural and functional outliers in the thioredoxin fold
    • Atkinson H.J., Babbitt P.C. Glutathione transferases are structural and functional outliers in the thioredoxin fold. Biochemistry 2009, 48:11108-11116.
    • (2009) Biochemistry , vol.48 , pp. 11108-11116
    • Atkinson, H.J.1    Babbitt, P.C.2
  • 14
    • 84867057699 scopus 로고    scopus 로고
    • Sulfiredoxin redox-sensitive interaction with S100A4 and non-muscle myosin IIA regulates cancer cell motility
    • Bowers R.R., Manevich Y., Townsend D.M., Tew K.D. Sulfiredoxin redox-sensitive interaction with S100A4 and non-muscle myosin IIA regulates cancer cell motility. Biochemistry 2012, 51:7740-7754.
    • (2012) Biochemistry , vol.51 , pp. 7740-7754
    • Bowers, R.R.1    Manevich, Y.2    Townsend, D.M.3    Tew, K.D.4
  • 15
    • 29144533949 scopus 로고    scopus 로고
    • Peptide-bond modified glutathione conjugate analogs modulate GSTpi function in GSH-conjugation, drug sensitivity and JNK signaling
    • Burg D., Riepsaame J., Pont C., Mulder G., van de Water B. Peptide-bond modified glutathione conjugate analogs modulate GSTpi function in GSH-conjugation, drug sensitivity and JNK signaling. Biochemical Pharmacology 2006, 71:268-277.
    • (2006) Biochemical Pharmacology , vol.71 , pp. 268-277
    • Burg, D.1    Riepsaame, J.2    Pont, C.3    Mulder, G.4    van de Water, B.5
  • 16
    • 17144395926 scopus 로고    scopus 로고
    • Single nucleotide polymorphism of pi-class glutathione s-transferase and susceptibility to endometrial carcinoma
    • Chan Q.K., Khoo U.S., Ngan H.Y., Yang C.Q., Xue W.C., Chan K.Y., et al. Single nucleotide polymorphism of pi-class glutathione s-transferase and susceptibility to endometrial carcinoma. Clinical Cancer Research 2005, 11:2981-2985.
    • (2005) Clinical Cancer Research , vol.11 , pp. 2981-2985
    • Chan, Q.K.1    Khoo, U.S.2    Ngan, H.Y.3    Yang, C.Q.4    Xue, W.C.5    Chan, K.Y.6
  • 18
    • 22044437820 scopus 로고    scopus 로고
    • The S-thiolating activity of membrane gamma-glutamyltransferase: Formation of cysteinyl-glycine mixed disulfides with cellular proteins and in the cell microenvironment
    • Corti A., Paolicchi A., Franzini M., Dominici S., Casini A.F., Pompella A. The S-thiolating activity of membrane gamma-glutamyltransferase: Formation of cysteinyl-glycine mixed disulfides with cellular proteins and in the cell microenvironment. Antioxidants & Redox Signaling 2005, 7:911-918.
    • (2005) Antioxidants & Redox Signaling , vol.7 , pp. 911-918
    • Corti, A.1    Paolicchi, A.2    Franzini, M.3    Dominici, S.4    Casini, A.F.5    Pompella, A.6
  • 20
    • 84872094899 scopus 로고    scopus 로고
    • Integrated redox sensor and effector functions for tetrahydrobiopterin- and glutathionylation-dependent endothelial nitric-oxide synthase uncoupling
    • Crabtree M.J., Brixey R., Batchelor H., Hale A.B., Channon K.M. Integrated redox sensor and effector functions for tetrahydrobiopterin- and glutathionylation-dependent endothelial nitric-oxide synthase uncoupling. The Journal of Biological Chemistry 2013, 288:561-569.
    • (2013) The Journal of Biological Chemistry , vol.288 , pp. 561-569
    • Crabtree, M.J.1    Brixey, R.2    Batchelor, H.3    Hale, A.B.4    Channon, K.M.5
  • 21
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis R.J. Signal transduction by the JNK group of MAP kinases. Cell 2000, 103:239-252.
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 22
    • 84866385940 scopus 로고    scopus 로고
    • New insights into the mechanism of JNK1 inhibition by glutathione transferase p1-1
    • De Luca A., Federici L., De Canio M., Stella L., Caccuri A.M. New insights into the mechanism of JNK1 inhibition by glutathione transferase p1-1. Biochemistry 2012, 51:7304-7312.
    • (2012) Biochemistry , vol.51 , pp. 7304-7312
    • De Luca, A.1    Federici, L.2    De Canio, M.3    Stella, L.4    Caccuri, A.M.5
  • 23
    • 26844441928 scopus 로고    scopus 로고
    • Activation of C-Jun N-terminal kinase is required for glutathione transferase A4 induction during oxidative stress, not during cell proliferation, in mouse hepatocytes
    • Desmots F., Loyer P., Rissel M., Guillouzo A., Morel F. Activation of C-Jun N-terminal kinase is required for glutathione transferase A4 induction during oxidative stress, not during cell proliferation, in mouse hepatocytes. FEBS Letters 2005, 579:5691-5696.
    • (2005) FEBS Letters , vol.579 , pp. 5691-5696
    • Desmots, F.1    Loyer, P.2    Rissel, M.3    Guillouzo, A.4    Morel, F.5
  • 24
    • 70350236453 scopus 로고    scopus 로고
    • Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases
    • Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F., Federici G., et al. Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases. Cancer Research 2009, 69:8025-8034.
    • (2009) Cancer Research , vol.69 , pp. 8025-8034
    • Federici, L.1    Lo Sterzo, C.2    Pezzola, S.3    Di Matteo, A.4    Scaloni, F.5    Federici, G.6
  • 25
    • 70350236453 scopus 로고    scopus 로고
    • Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases
    • Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F., Federici G., et al. Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases. Cancer Research 2009, 69:8025-8034.
    • (2009) Cancer Research , vol.69 , pp. 8025-8034
    • Federici, L.1    Lo Sterzo, C.2    Pezzola, S.3    Di Matteo, A.4    Scaloni, F.5    Federici, G.6
  • 30
    • 84875709337 scopus 로고    scopus 로고
    • The fairytale of the GSSG/GSH redox potential
    • Flohe L. The fairytale of the GSSG/GSH redox potential. Biochimica et Biophysica Acta 2012, 1830(5):3139-3142.
    • (2012) Biochimica et Biophysica Acta , vol.1830 , Issue.5 , pp. 3139-3142
    • Flohe, L.1
  • 32
    • 51349142890 scopus 로고    scopus 로고
    • Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: Implications for intracellular roles
    • Gallogly M.M., Starke D.W., Leonberg A.K., Ospina S.M., Mieyal J.J. Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: Implications for intracellular roles. Biochemistry 2008, 47:11144-11157.
    • (2008) Biochemistry , vol.47 , pp. 11144-11157
    • Gallogly, M.M.1    Starke, D.W.2    Leonberg, A.K.3    Ospina, S.M.4    Mieyal, J.J.5
  • 33
    • 27244462713 scopus 로고    scopus 로고
    • Development of a peptide antibody specific to human glutathione S-transferase alpha 4-4 (hGSTA4-4) reveals preferential localization in human liver mitochondria
    • Gardner J.L., Gallagher E.P. Development of a peptide antibody specific to human glutathione S-transferase alpha 4-4 (hGSTA4-4) reveals preferential localization in human liver mitochondria. Archives of Biochemistry and Biophysics 2001, 390:19-27.
    • (2001) Archives of Biochemistry and Biophysics , vol.390 , pp. 19-27
    • Gardner, J.L.1    Gallagher, E.P.2
  • 35
    • 1542365411 scopus 로고    scopus 로고
    • Increased myeloproliferation in glutathione S-transferase pi-deficient mice is associated with a deregulation of JNK and Janus kinase/STAT pathways
    • Gate L., Majumdar R.S., Lunk A., Tew K.D. Increased myeloproliferation in glutathione S-transferase pi-deficient mice is associated with a deregulation of JNK and Janus kinase/STAT pathways. The Journal of Biological Chemistry 2004, 279:8608-8616.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 8608-8616
    • Gate, L.1    Majumdar, R.S.2    Lunk, A.3    Tew, K.D.4
  • 36
    • 8644244731 scopus 로고    scopus 로고
    • Influence of glutathione S-transferase pi and p53 expression on tumor frequency and spectrum in mice
    • Gate L., Majumdar R.S., Lunk A., Tew K.D. Influence of glutathione S-transferase pi and p53 expression on tumor frequency and spectrum in mice. International Journal of Cancer 2005, 113:29-35.
    • (2005) International Journal of Cancer , vol.113 , pp. 29-35
    • Gate, L.1    Majumdar, R.S.2    Lunk, A.3    Tew, K.D.4
  • 37
    • 77953654496 scopus 로고    scopus 로고
    • Class Pi glutathione transferase unfolds via a dimeric and not monomeric intermediate: Functional implications for an unstable monomer
    • Gildenhuys S., Wallace L.A., Burke J.P., Balchin D., Sayed Y., Dirr H.W. Class Pi glutathione transferase unfolds via a dimeric and not monomeric intermediate: Functional implications for an unstable monomer. Biochemistry 2010, 49:5074-5081.
    • (2010) Biochemistry , vol.49 , pp. 5074-5081
    • Gildenhuys, S.1    Wallace, L.A.2    Burke, J.P.3    Balchin, D.4    Sayed, Y.5    Dirr, H.W.6
  • 38
    • 0035199575 scopus 로고    scopus 로고
    • Doxorubicin-induced DNA intercalation and scavenging by nuclear glutathione S-transferase pi
    • Goto S., Ihara Y., Urata Y., Izumi S., Abe K., Koji T., et al. Doxorubicin-induced DNA intercalation and scavenging by nuclear glutathione S-transferase pi. The FASEB Journal 2001, 15:2702-2714.
    • (2001) The FASEB Journal , vol.15 , pp. 2702-2714
    • Goto, S.1    Ihara, Y.2    Urata, Y.3    Izumi, S.4    Abe, K.5    Koji, T.6
  • 39
    • 0035199575 scopus 로고    scopus 로고
    • Doxorubicin-induced DNA intercalation and scavenging by nuclear glutathione S-transferase pi
    • Goto S., Ihara Y., Urata Y., Izumi S., Abe K., Koji T., et al. Doxorubicin-induced DNA intercalation and scavenging by nuclear glutathione S-transferase pi. The FASEB Journal 2001, 15:2702-2714.
    • (2001) The FASEB Journal , vol.15 , pp. 2702-2714
    • Goto, S.1    Ihara, Y.2    Urata, Y.3    Izumi, S.4    Abe, K.5    Koji, T.6
  • 40
    • 0032734575 scopus 로고    scopus 로고
    • Overexpression of glutathione S-transferase pi enhances the adduct formation of cisplatin with glutathione in human cancer cells
    • Goto S., Iida T., Cho S., Oka M., Kohno S., Kondo T. Overexpression of glutathione S-transferase pi enhances the adduct formation of cisplatin with glutathione in human cancer cells. Free Radical Research 1999, 31:549-558.
    • (1999) Free Radical Research , vol.31 , pp. 549-558
    • Goto, S.1    Iida, T.2    Cho, S.3    Oka, M.4    Kohno, S.5    Kondo, T.6
  • 41
    • 0024588467 scopus 로고
    • Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase
    • Graminski G.F., Kubo Y., Armstrong R.N. Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase. Biochemistry 1989, 28:3562-3568.
    • (1989) Biochemistry , vol.28 , pp. 3562-3568
    • Graminski, G.F.1    Kubo, Y.2    Armstrong, R.N.3
  • 42
    • 0024403592 scopus 로고
    • Formation of the 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate anion at the active site of glutathione S-transferase: Evidence for enzymic stabilization of sigma-complex intermediates in nucleophilic aromatic substitution reactions
    • Graminski G.F., Zhang P.H., Sesay M.A., Ammon H.L., Armstrong R.N. Formation of the 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate anion at the active site of glutathione S-transferase: Evidence for enzymic stabilization of sigma-complex intermediates in nucleophilic aromatic substitution reactions. Biochemistry 1989, 28:6252-6258.
    • (1989) Biochemistry , vol.28 , pp. 6252-6258
    • Graminski, G.F.1    Zhang, P.H.2    Sesay, M.A.3    Ammon, H.L.4    Armstrong, R.N.5
  • 45
    • 0031427094 scopus 로고    scopus 로고
    • Identification of genetic polymorphisms at the glutathione S-transferase Pi locus and association with susceptibility to bladder, testicular and prostate cancer
    • Harries L.W., Stubbins M.J., Forman D., Howard G.C., Wolf C.R. Identification of genetic polymorphisms at the glutathione S-transferase Pi locus and association with susceptibility to bladder, testicular and prostate cancer. Carcinogenesis 1997, 18:641-644.
    • (1997) Carcinogenesis , vol.18 , pp. 641-644
    • Harries, L.W.1    Stubbins, M.J.2    Forman, D.3    Howard, G.C.4    Wolf, C.R.5
  • 47
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J.D., Pulford D.J. The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Critical Reviews in Biochemistry and Molecular Biology 1995, 30:445-600.
    • (1995) Critical Reviews in Biochemistry and Molecular Biology , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 50
    • 36148958662 scopus 로고    scopus 로고
    • Differential effects of glutathione S-transferase pi (GSTP1) haplotypes on cell proliferation and apoptosis
    • Holley S.L., Fryer A.A., Haycock J.W., Grubb S.E., Strange R.C., Hoban P.R. Differential effects of glutathione S-transferase pi (GSTP1) haplotypes on cell proliferation and apoptosis. Carcinogenesis 2007, 28:2268-2273.
    • (2007) Carcinogenesis , vol.28 , pp. 2268-2273
    • Holley, S.L.1    Fryer, A.A.2    Haycock, J.W.3    Grubb, S.E.4    Strange, R.C.5    Hoban, P.R.6
  • 51
    • 0033563005 scopus 로고    scopus 로고
    • Differential protection against benzo[a]pyrene-7,8-dihydrodiol-9,10-epoxide-induced DNA damage in HepG2 cells stably transfected with allelic variants of pi class human glutathione S-transferase
    • Hu X., Herzog C., Zimniak P., Singh S.V. Differential protection against benzo[a]pyrene-7,8-dihydrodiol-9,10-epoxide-induced DNA damage in HepG2 cells stably transfected with allelic variants of pi class human glutathione S-transferase. Cancer Research 1999, 59:2358-2362.
    • (1999) Cancer Research , vol.59 , pp. 2358-2362
    • Hu, X.1    Herzog, C.2    Zimniak, P.3    Singh, S.V.4
  • 52
    • 0038457738 scopus 로고    scopus 로고
    • Prognostic significance of glutathione S-transferase-pi in invasive breast cancer
    • Huang J., Tan P.H., Thiyagarajan J., Bay B.H. Prognostic significance of glutathione S-transferase-pi in invasive breast cancer. Modern Pathology 2003, 16:558-565.
    • (2003) Modern Pathology , vol.16 , pp. 558-565
    • Huang, J.1    Tan, P.H.2    Thiyagarajan, J.3    Bay, B.H.4
  • 53
    • 84856067661 scopus 로고    scopus 로고
    • Cellular resistance to a nitric oxide releasing glutathione S-transferase P-activated prodrug, PABA/NO
    • Hutchens S., Manevich Y., He L., Tew K.D., Townsend D.M. Cellular resistance to a nitric oxide releasing glutathione S-transferase P-activated prodrug, PABA/NO. Investigational New Drugs 2011, 29:719-729.
    • (2011) Investigational New Drugs , vol.29 , pp. 719-729
    • Hutchens, S.1    Manevich, Y.2    He, L.3    Tew, K.D.4    Townsend, D.M.5
  • 54
    • 60749091126 scopus 로고    scopus 로고
    • Regulation of nitric oxide signalling by thrombospondin 1: Implications for anti-angiogenic therapies
    • Isenberg J.S., Martin-Manso G., Maxhimer J.B., Roberts D.D. Regulation of nitric oxide signalling by thrombospondin 1: Implications for anti-angiogenic therapies. Nature Reviews. Cancer 2009, 9:182-194.
    • (2009) Nature Reviews. Cancer , vol.9 , pp. 182-194
    • Isenberg, J.S.1    Martin-Manso, G.2    Maxhimer, J.B.3    Roberts, D.D.4
  • 55
    • 84861437627 scopus 로고    scopus 로고
    • Glutathione S-transferase Pi expression predicts response to adjuvant chemotherapy for stage C colon cancer: A matched historical control study
    • Jankova L., Robertson G., Chan C., Tan K.L., Kohonen-Corish M., Fung C.L., et al. Glutathione S-transferase Pi expression predicts response to adjuvant chemotherapy for stage C colon cancer: A matched historical control study. BMC Cancer 2012, 12:196.
    • (2012) BMC Cancer , vol.12 , pp. 196
    • Jankova, L.1    Robertson, G.2    Chan, C.3    Tan, K.L.4    Kohonen-Corish, M.5    Fung, C.L.6
  • 56
    • 84863463209 scopus 로고    scopus 로고
    • Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression
    • Jeong W., Bae S.H., Toledano M.B., Rhee S.G. Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression. Free Radical Biology & Medicine 2012, 53:447-456.
    • (2012) Free Radical Biology & Medicine , vol.53 , pp. 447-456
    • Jeong, W.1    Bae, S.H.2    Toledano, M.B.3    Rhee, S.G.4
  • 57
    • 77949434537 scopus 로고    scopus 로고
    • Phase 2 study of canfosfamide in combination with pegylated liposomal doxorubicin in platinum and paclitaxel refractory or resistant epithelial ovarian cancer
    • Kavanagh J.J., Levenback C.F., Ramirez P.T., Wolf J.L., Moore C.L., Jones M.R., et al. Phase 2 study of canfosfamide in combination with pegylated liposomal doxorubicin in platinum and paclitaxel refractory or resistant epithelial ovarian cancer. Journal of Hematology & Oncology 2010, 3:9.
    • (2010) Journal of Hematology & Oncology , vol.3 , pp. 9
    • Kavanagh, J.J.1    Levenback, C.F.2    Ramirez, P.T.3    Wolf, J.L.4    Moore, C.L.5    Jones, M.R.6
  • 58
    • 84872712440 scopus 로고    scopus 로고
    • GSTP1 negatively regulates Stat3 activation in epidermal growth factor signaling
    • Kou X., Chen N., Feng Z., Luo L., Yin Z. GSTP1 negatively regulates Stat3 activation in epidermal growth factor signaling. Oncology Letters 2013, 5:1053-1057.
    • (2013) Oncology Letters , vol.5 , pp. 1053-1057
    • Kou, X.1    Chen, N.2    Feng, Z.3    Luo, L.4    Yin, Z.5
  • 59
    • 77955713764 scopus 로고    scopus 로고
    • Glutathione transferases as mediators of signaling pathways involved in cell proliferation and cell death
    • Laborde E. Glutathione transferases as mediators of signaling pathways involved in cell proliferation and cell death. Cell Death and Differentiation 2010, 17:1373-1380.
    • (2010) Cell Death and Differentiation , vol.17 , pp. 1373-1380
    • Laborde, E.1
  • 60
    • 50049129246 scopus 로고    scopus 로고
    • Protein cysteine sulfinic acid reductase (sulfiredoxin) as a regulator of cell proliferation and drug response
    • Lei K., Townsend D.M., Tew K.D. Protein cysteine sulfinic acid reductase (sulfiredoxin) as a regulator of cell proliferation and drug response. Oncogene 2008, 27:4877-4887.
    • (2008) Oncogene , vol.27 , pp. 4877-4887
    • Lei, K.1    Townsend, D.M.2    Tew, K.D.3
  • 62
    • 0032562382 scopus 로고    scopus 로고
    • Structure of the human allelic glutathione S-transferase-pi gene variant, hGSTP1 C, cloned from a glioblastoma multiforme cell line
    • Lo H.W., Ali-Osman F. Structure of the human allelic glutathione S-transferase-pi gene variant, hGSTP1 C, cloned from a glioblastoma multiforme cell line. Chemico-Biological Interactions 1998, 111-112:91-102.
    • (1998) Chemico-Biological Interactions , pp. 91-102
    • Lo, H.W.1    Ali-Osman, F.2
  • 63
    • 80055112021 scopus 로고    scopus 로고
    • Oral ezatiostat HCl (Telintra(R), TLK199) and Idiopathic Chronic Neutropenia (ICN): A case report of complete response of a patient with G-CSF resistant ICN following treatment with ezatiostat, a glutathione S-transferase P1-1 (GSTP1-1) inhibitor
    • Lyons R.M., Wilks S.T., Young S., Brown G.L. Oral ezatiostat HCl (Telintra(R), TLK199) and Idiopathic Chronic Neutropenia (ICN): A case report of complete response of a patient with G-CSF resistant ICN following treatment with ezatiostat, a glutathione S-transferase P1-1 (GSTP1-1) inhibitor. Journal of Hematology & Oncology 2011, 4:43.
    • (2011) Journal of Hematology & Oncology , vol.4 , pp. 43
    • Lyons, R.M.1    Wilks, S.T.2    Young, S.3    Brown, G.L.4
  • 64
    • 21144440291 scopus 로고    scopus 로고
    • The chemistry and biology of inhibitors and pro-drugs targeted to glutathione S-transferases
    • Mahajan S., Atkins W.M. The chemistry and biology of inhibitors and pro-drugs targeted to glutathione S-transferases. Cellular and Molecular Life Sciences 2005, 62:1221-1233.
    • (2005) Cellular and Molecular Life Sciences , vol.62 , pp. 1221-1233
    • Mahajan, S.1    Atkins, W.M.2
  • 66
    • 18844400905 scopus 로고    scopus 로고
    • Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
    • Manevich Y., Fisher A.B. Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radical Biology & Medicine 2005, 38:1422-1432.
    • (2005) Free Radical Biology & Medicine , vol.38 , pp. 1422-1432
    • Manevich, Y.1    Fisher, A.B.2
  • 67
    • 18844400905 scopus 로고    scopus 로고
    • Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
    • Manevich Y., Fisher A.B. Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radical Biology & Medicine 2005, 38:1422-1432.
    • (2005) Free Radical Biology & Medicine , vol.38 , pp. 1422-1432
    • Manevich, Y.1    Fisher, A.B.2
  • 68
    • 84870312437 scopus 로고    scopus 로고
    • Allelic variants of glutathione S-transferase P1-1 differentially mediate the peroxidase function of peroxiredoxin VI and alter membrane lipid peroxidation
    • Manevich Y., Hutchens S., Tew K.D., Townsend D.M. Allelic variants of glutathione S-transferase P1-1 differentially mediate the peroxidase function of peroxiredoxin VI and alter membrane lipid peroxidation. Free Radical Biology & Medicine 2012, 54C:62-70.
    • (2012) Free Radical Biology & Medicine , vol.54 C , pp. 62-70
    • Manevich, Y.1    Hutchens, S.2    Tew, K.D.3    Townsend, D.M.4
  • 69
    • 84870312437 scopus 로고    scopus 로고
    • Allelic variants of glutathione S-transferase P1-1 differentially mediate the peroxidase function of peroxiredoxin VI and alter membrane lipid peroxidation
    • Manevich Y., Hutchens S., Tew K.D., Townsend D.M. Allelic variants of glutathione S-transferase P1-1 differentially mediate the peroxidase function of peroxiredoxin VI and alter membrane lipid peroxidation. Free Radical Biology & Medicine 2013, 54:62-70.
    • (2013) Free Radical Biology & Medicine , vol.54 , pp. 62-70
    • Manevich, Y.1    Hutchens, S.2    Tew, K.D.3    Townsend, D.M.4
  • 70
    • 78649778002 scopus 로고    scopus 로고
    • Diazeniumdiolate mediated nitrosative stress alters nitric oxide homeostasis through intracellular calcium and S-glutathionylation of nitric oxide synthetase
    • Manevich Y., Townsend D.M., Hutchens S., Tew K.D. Diazeniumdiolate mediated nitrosative stress alters nitric oxide homeostasis through intracellular calcium and S-glutathionylation of nitric oxide synthetase. PloS One 2010, 5:e14151.
    • (2010) PloS One , vol.5
    • Manevich, Y.1    Townsend, D.M.2    Hutchens, S.3    Tew, K.D.4
  • 71
    • 73649121243 scopus 로고    scopus 로고
    • Structural analysis of cysteine S-nitrosylation: A modified acid-based motif and the emerging role of trans-nitrosylation
    • Marino S.M., Gladyshev V.N. Structural analysis of cysteine S-nitrosylation: A modified acid-based motif and the emerging role of trans-nitrosylation. Journal of Molecular Biology 2010, 395:844-859.
    • (2010) Journal of Molecular Biology , vol.395 , pp. 844-859
    • Marino, S.M.1    Gladyshev, V.N.2
  • 72
    • 58849158293 scopus 로고    scopus 로고
    • Reactive nitrogen species: Molecular mechanisms and potential significance in health and disease
    • Martinez M.C., Andriantsitohaina R. Reactive nitrogen species: Molecular mechanisms and potential significance in health and disease. Antioxidants & Redox Signaling 2009, 11:669-702.
    • (2009) Antioxidants & Redox Signaling , vol.11 , pp. 669-702
    • Martinez, M.C.1    Andriantsitohaina, R.2
  • 73
    • 33645111448 scopus 로고    scopus 로고
    • Glutathione S-transferase polymorphisms: Cancer incidence and therapy
    • McIlwain C.C., Townsend D.M., Tew K.D. Glutathione S-transferase polymorphisms: Cancer incidence and therapy. Oncogene 2006, 25:1639-1648.
    • (2006) Oncogene , vol.25 , pp. 1639-1648
    • McIlwain, C.C.1    Townsend, D.M.2    Tew, K.D.3
  • 74
    • 0025895933 scopus 로고
    • Thioltransferase in human red blood cells: Purification and properties
    • Mieyal J.J., Starke D.W., Gravina S.A., Dothey C., Chung J.S. Thioltransferase in human red blood cells: Purification and properties. Biochemistry 1991, 30:6088-6097.
    • (1991) Biochemistry , vol.30 , pp. 6088-6097
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Dothey, C.4    Chung, J.S.5
  • 75
    • 0025887464 scopus 로고
    • Thioltransferase in human red blood cells: Kinetics and equilibrium
    • Mieyal J.J., Starke D.W., Gravina S.A., Hocevar B.A. Thioltransferase in human red blood cells: Kinetics and equilibrium. Biochemistry 1991, 30:8883-8891.
    • (1991) Biochemistry , vol.30 , pp. 8883-8891
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Hocevar, B.A.4
  • 76
    • 53149137878 scopus 로고    scopus 로고
    • Identification of a glutathione-S-transferase effector domain for inhibition of jun kinase, by molecular dynamics
    • Monaco R., Friedman F.K., Hyde M.J., Chen J.M., Manolatus S., Adler V., et al. Identification of a glutathione-S-transferase effector domain for inhibition of jun kinase, by molecular dynamics. Journal of Protein Chemistry 1999, 18:859-866.
    • (1999) Journal of Protein Chemistry , vol.18 , pp. 859-866
    • Monaco, R.1    Friedman, F.K.2    Hyde, M.J.3    Chen, J.M.4    Manolatus, S.5    Adler, V.6
  • 77
    • 0026347638 scopus 로고
    • Phase I study of thiotepa in combination with the glutathione transferase inhibitor ethacrynic acid
    • O'Dwyer P.J., LaCreta F., Nash S., Tinsley P.W., Schilder R., Clapper M.L., et al. Phase I study of thiotepa in combination with the glutathione transferase inhibitor ethacrynic acid. Cancer Research 1991, 51:6059-6065.
    • (1991) Cancer Research , vol.51 , pp. 6059-6065
    • O'Dwyer, P.J.1    LaCreta, F.2    Nash, S.3    Tinsley, P.W.4    Schilder, R.5    Clapper, M.L.6
  • 78
    • 0034213865 scopus 로고    scopus 로고
    • Catalytic efficiencies of allelic variants of human glutathione S-transferase Pi in the glutathione conjugation of alpha, beta-unsaturated aldehydes
    • Pal A., Hu X., Zimniak P., Singh S.V. Catalytic efficiencies of allelic variants of human glutathione S-transferase Pi in the glutathione conjugation of alpha, beta-unsaturated aldehydes. Cancer Letters 2000, 154:39-43.
    • (2000) Cancer Letters , vol.154 , pp. 39-43
    • Pal, A.1    Hu, X.2    Zimniak, P.3    Singh, S.V.4
  • 79
    • 69949115433 scopus 로고    scopus 로고
    • Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin
    • Park J.W., Mieyal J.J., Rhee S.G., Chock P.B. Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin. The Journal of Biological Chemistry 2009, 284:23364-23374.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 23364-23374
    • Park, J.W.1    Mieyal, J.J.2    Rhee, S.G.3    Chock, P.B.4
  • 80
    • 28744458907 scopus 로고    scopus 로고
    • Taurine chloramine is more selective than hypochlorous acid at targeting critical cysteines and inactivating creatine kinase and glyceraldehyde-3-phosphate dehydrogenase
    • Peskin A.V., Winterbourn C.C. Taurine chloramine is more selective than hypochlorous acid at targeting critical cysteines and inactivating creatine kinase and glyceraldehyde-3-phosphate dehydrogenase. Free Radical Biology & Medicine 2006, 40:45-53.
    • (2006) Free Radical Biology & Medicine , vol.40 , pp. 45-53
    • Peskin, A.V.1    Winterbourn, C.C.2
  • 81
    • 69449097954 scopus 로고    scopus 로고
    • Glutathione transferases kappa 1 and kappa 2 localize in peroxisomes and mitochondria, respectively, and are involved in lipid metabolism and respiration in Caenorhabditis elegans
    • Petit E., Michelet X., Rauch C., Bertrand-Michel J., Terce F., Legouis R., et al. Glutathione transferases kappa 1 and kappa 2 localize in peroxisomes and mitochondria, respectively, and are involved in lipid metabolism and respiration in Caenorhabditis elegans. The FEBS Journal 2009, 276:5030-5040.
    • (2009) The FEBS Journal , vol.276 , pp. 5030-5040
    • Petit, E.1    Michelet, X.2    Rauch, C.3    Bertrand-Michel, J.4    Terce, F.5    Legouis, R.6
  • 82
    • 0035894563 scopus 로고    scopus 로고
    • Heterodimers of glutathione S-transferase can form between isoenzyme classes pi and mu
    • Pettigrew N.E., Colman R.F. Heterodimers of glutathione S-transferase can form between isoenzyme classes pi and mu. Archives of Biochemistry and Biophysics 2001, 396:225-230.
    • (2001) Archives of Biochemistry and Biophysics , vol.396 , pp. 225-230
    • Pettigrew, N.E.1    Colman, R.F.2
  • 83
    • 0028209437 scopus 로고
    • Reversible conjugation of ethacrynic acid with glutathione and human glutathione S-transferase p11
    • Ploemen J.H., Van Schanke A., Van Ommen B., Van Bladeren P.J. Reversible conjugation of ethacrynic acid with glutathione and human glutathione S-transferase p11. Cancer Research 1994, 54:915-919.
    • (1994) Cancer Research , vol.54 , pp. 915-919
    • Ploemen, J.H.1    Van Schanke, A.2    Van Ommen, B.3    Van Bladeren, P.J.4
  • 85
    • 30744437425 scopus 로고    scopus 로고
    • Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes
    • Ralat L.A., Manevich Y., Fisher A.B., Colman R.F. Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes. Biochemistry 2006, 45:360-372.
    • (2006) Biochemistry , vol.45 , pp. 360-372
    • Ralat, L.A.1    Manevich, Y.2    Fisher, A.B.3    Colman, R.F.4
  • 87
    • 80255127115 scopus 로고    scopus 로고
    • Dual localization of glutathione S-transferase in the cytosol and mitochondria: Implications in oxidative stress, toxicity and disease
    • Raza H. Dual localization of glutathione S-transferase in the cytosol and mitochondria: Implications in oxidative stress, toxicity and disease. The FEBS Journal 2011, 278:4243-4251.
    • (2011) The FEBS Journal , vol.278 , pp. 4243-4251
    • Raza, H.1
  • 88
    • 67651167047 scopus 로고    scopus 로고
    • Phase 1-2a multicenter dose-escalation study of ezatiostat hydrochloride liposomes for injection (Telintra, TLK199), a novel glutathione analog prodrug in patients with myelodysplastic syndrome
    • Raza A., Galili N., Callander N., Ochoa L., Piro L., Emanuel P., et al. Phase 1-2a multicenter dose-escalation study of ezatiostat hydrochloride liposomes for injection (Telintra, TLK199), a novel glutathione analog prodrug in patients with myelodysplastic syndrome. Journal of Hematology & Oncology 2009, 2:20.
    • (2009) Journal of Hematology & Oncology , vol.2 , pp. 20
    • Raza, A.1    Galili, N.2    Callander, N.3    Ochoa, L.4    Piro, L.5    Emanuel, P.6
  • 90
    • 22544436117 scopus 로고    scopus 로고
    • 7-Nitro-2,1,3-benzoxadiazole derivatives, a new class of suicide inhibitors for glutathione S-transferases. Mechanism of action of potential anticancer drugs
    • Ricci G., De Maria F., Antonini G., Turella P., Bullo A., Stella L., et al. 7-Nitro-2,1,3-benzoxadiazole derivatives, a new class of suicide inhibitors for glutathione S-transferases. Mechanism of action of potential anticancer drugs. The Journal of Biological Chemistry 2005, 280:26397-26405.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 26397-26405
    • Ricci, G.1    De Maria, F.2    Antonini, G.3    Turella, P.4    Bullo, A.5    Stella, L.6
  • 91
    • 78650249967 scopus 로고    scopus 로고
    • Inhibition of GST-pi nuclear transfer increases mantle cell lymphoma sensitivity to cisplatin, cytarabine, gemcitabine, bortezomib and doxorubicin
    • Rolland D., Raharijaona M., Barbarat A., Houlgatte R., Thieblemont C. Inhibition of GST-pi nuclear transfer increases mantle cell lymphoma sensitivity to cisplatin, cytarabine, gemcitabine, bortezomib and doxorubicin. Anticancer Research 2010, 30:3951-3957.
    • (2010) Anticancer Research , vol.30 , pp. 3951-3957
    • Rolland, D.1    Raharijaona, M.2    Barbarat, A.3    Houlgatte, R.4    Thieblemont, C.5
  • 92
    • 33751115477 scopus 로고    scopus 로고
    • Human GSTA1-1 reduces c-Jun N-terminal kinase signalling and apoptosis in Caco-2 cells
    • Romero L., Andrews K., Ng L., O'Rourke K., Maslen A., Kirby G. Human GSTA1-1 reduces c-Jun N-terminal kinase signalling and apoptosis in Caco-2 cells. The Biochemical Journal 2006, 400:135-141.
    • (2006) The Biochemical Journal , vol.400 , pp. 135-141
    • Romero, L.1    Andrews, K.2    Ng, L.3    O'Rourke, K.4    Maslen, A.5    Kirby, G.6
  • 94
    • 31044449239 scopus 로고    scopus 로고
    • PABA/NO as an anticancer lead: Analogue synthesis, structure revision, solution chemistry, reactivity toward glutathione, and in vitro activity
    • Saavedra J.E., Srinivasan A., Buzard G.S., Davies K.M., Waterhouse D.J., Inami K., et al. PABA/NO as an anticancer lead: Analogue synthesis, structure revision, solution chemistry, reactivity toward glutathione, and in vitro activity. Journal of Medicinal Chemistry 2006, 49:1157-1164.
    • (2006) Journal of Medicinal Chemistry , vol.49 , pp. 1157-1164
    • Saavedra, J.E.1    Srinivasan, A.2    Buzard, G.S.3    Davies, K.M.4    Waterhouse, D.J.5    Inami, K.6
  • 95
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • Saitoh M., Nishitoh H., Fujii M., Takeda K., Tobiume K., Sawada Y., et al. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. The EMBO Journal 1998, 17:2596-2606.
    • (1998) The EMBO Journal , vol.17 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3    Takeda, K.4    Tobiume, K.5    Sawada, Y.6
  • 97
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: Role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation
    • Shelton M.D., Chock P.B., Mieyal J.J. Glutaredoxin: Role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxidants & Redox Signaling 2005, 7:348-366.
    • (2005) Antioxidants & Redox Signaling , vol.7 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 100
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamler J.S., Singel D.J., Loscalzo J. Biochemistry of nitric oxide and its redox-activated forms. Science 1992, 258:1898-1902.
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 101
    • 0030988217 scopus 로고    scopus 로고
    • Structure-function aspects in the nitric oxide synthases
    • Stuehr D.J. Structure-function aspects in the nitric oxide synthases. Annual Review of Pharmacology and Toxicology 1997, 37:339-359.
    • (1997) Annual Review of Pharmacology and Toxicology , vol.37 , pp. 339-359
    • Stuehr, D.J.1
  • 102
    • 33646130621 scopus 로고    scopus 로고
    • Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase p1-1
    • Tellez-Sanz R., Cesareo E., Nuccetelli M., Aguilera A.M., Baron C., Parker L.J., et al. Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase p1-1. Protein Science 2006, 15:1093-1105.
    • (2006) Protein Science , vol.15 , pp. 1093-1105
    • Tellez-Sanz, R.1    Cesareo, E.2    Nuccetelli, M.3    Aguilera, A.M.4    Baron, C.5    Parker, L.J.6
  • 103
    • 0028106016 scopus 로고
    • Glutathione-associated enzymes in anticancer drug resistance
    • Tew K.D. Glutathione-associated enzymes in anticancer drug resistance. Cancer Research 1994, 54:4313-4320.
    • (1994) Cancer Research , vol.54 , pp. 4313-4320
    • Tew, K.D.1
  • 104
    • 79851510296 scopus 로고    scopus 로고
    • Redox platforms in cancer drug discovery and development
    • Tew K.D., Townsend D.M. Redox platforms in cancer drug discovery and development. Current Opinion in Chemical Biology 2011, 15:156-161.
    • (2011) Current Opinion in Chemical Biology , vol.15 , pp. 156-161
    • Tew, K.D.1    Townsend, D.M.2
  • 105
    • 79954617745 scopus 로고    scopus 로고
    • Regulatory functions of glutathione S-transferase P1-1 unrelated to detoxification
    • Tew K.D., Townsend D.M. Regulatory functions of glutathione S-transferase P1-1 unrelated to detoxification. Drug Metabolism Reviews 2011, 43:179-193.
    • (2011) Drug Metabolism Reviews , vol.43 , pp. 179-193
    • Tew, K.D.1    Townsend, D.M.2
  • 106
    • 79954495990 scopus 로고    scopus 로고
    • GST pi modulates JNK activity through a direct interaction with JNK substrate, ATF2
    • Thevenin A.F., Zony C.L., Bahnson B.J., Colman R.F. GST pi modulates JNK activity through a direct interaction with JNK substrate, ATF2. Protein Science 2011, 20:834-848.
    • (2011) Protein Science , vol.20 , pp. 834-848
    • Thevenin, A.F.1    Zony, C.L.2    Bahnson, B.J.3    Colman, R.F.4
  • 107
    • 38349049487 scopus 로고    scopus 로고
    • S-glutathionylation: Indicator of cell stress and regulator of the unfolded protein response
    • Townsend D.M. S-glutathionylation: Indicator of cell stress and regulator of the unfolded protein response. Molecular Interventions 2007, 7:313-324.
    • (2007) Molecular Interventions , vol.7 , pp. 313-324
    • Townsend, D.M.1
  • 108
    • 31044436627 scopus 로고    scopus 로고
    • A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins
    • Townsend D.M., Findlay V.J., Fazilev F., Ogle M., Fraser J., Saavedra J.E., et al. A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins. Molecular Pharmacology 2006, 69:501-508.
    • (2006) Molecular Pharmacology , vol.69 , pp. 501-508
    • Townsend, D.M.1    Findlay, V.J.2    Fazilev, F.3    Ogle, M.4    Fraser, J.5    Saavedra, J.E.6
  • 109
    • 58649100268 scopus 로고    scopus 로고
    • Novel role for glutathione S-transferase pi. Regulator of protein S-Glutathionylation following oxidative and nitrosative stress
    • Townsend D.M., Manevich Y., He L., Hutchens S., Pazoles C.J., Tew K.D. Novel role for glutathione S-transferase pi. Regulator of protein S-Glutathionylation following oxidative and nitrosative stress. The Journal of Biological Chemistry 2009, 284:436-445.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 436-445
    • Townsend, D.M.1    Manevich, Y.2    He, L.3    Hutchens, S.4    Pazoles, C.J.5    Tew, K.D.6
  • 110
    • 58649100268 scopus 로고    scopus 로고
    • Novel role for glutathione S-transferase pi. Regulator of protein S-Glutathionylation following oxidative and nitrosative stress
    • Townsend D.M., Manevich Y., He L., Hutchens S., Pazoles C.J., Tew K.D. Novel role for glutathione S-transferase pi. Regulator of protein S-Glutathionylation following oxidative and nitrosative stress. The Journal of Biological Chemistry 2009, 284:436-445.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 436-445
    • Townsend, D.M.1    Manevich, Y.2    He, L.3    Hutchens, S.4    Pazoles, C.J.5    Tew, K.D.6
  • 111
    • 0038345017 scopus 로고    scopus 로고
    • Cancer drugs, genetic variation and the glutathione-S-transferase gene family
    • Townsend D., Tew K. Cancer drugs, genetic variation and the glutathione-S-transferase gene family. American Journal of Pharmacogenomics 2003, 3:157-172.
    • (2003) American Journal of Pharmacogenomics , vol.3 , pp. 157-172
    • Townsend, D.1    Tew, K.2
  • 114
    • 67649781729 scopus 로고    scopus 로고
    • Dinitrosyl iron complexes with thiolate ligands: Physico-chemistry, biochemistry and physiology
    • Vanin A.F. Dinitrosyl iron complexes with thiolate ligands: Physico-chemistry, biochemistry and physiology. Nitric Oxide 2009, 21:1-13.
    • (2009) Nitric Oxide , vol.21 , pp. 1-13
    • Vanin, A.F.1
  • 115
    • 79952819524 scopus 로고    scopus 로고
    • The many faces of glutathione transferase pi
    • Vasieva O. The many faces of glutathione transferase pi. Current Molecular Medicine 2011, 11:129-139.
    • (2011) Current Molecular Medicine , vol.11 , pp. 129-139
    • Vasieva, O.1
  • 116
    • 68749089764 scopus 로고    scopus 로고
    • Phase 3 randomised study of canfosfamide (Telcyta, TLK286) versus pegylated liposomal doxorubicin or topotecan as third-line therapy in patients with platinum-refractory or -resistant ovarian cancer
    • Vergote I., Finkler N., del Campo J., Lohr A., Hunter J., Matei D., et al. Phase 3 randomised study of canfosfamide (Telcyta, TLK286) versus pegylated liposomal doxorubicin or topotecan as third-line therapy in patients with platinum-refractory or -resistant ovarian cancer. European Journal of Cancer 2009, 45:2324-2332.
    • (2009) European Journal of Cancer , vol.45 , pp. 2324-2332
    • Vergote, I.1    Finkler, N.2    del Campo, J.3    Lohr, A.4    Hunter, J.5    Matei, D.6
  • 117
    • 0035877779 scopus 로고    scopus 로고
    • Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus
    • Wang T., Arifoglu P., Ronai Z., Tew K.D. Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus. The Journal of Biological Chemistry 2001, 276:20999-21003.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 20999-21003
    • Wang, T.1    Arifoglu, P.2    Ronai, Z.3    Tew, K.D.4
  • 118
    • 0031878594 scopus 로고    scopus 로고
    • Human glutathione S-transferase P1 polymorphisms: Relationship to lung tissue enzyme activity and population frequency distribution
    • Watson M.A., Stewart R.K., Smith G.B., Massey T.E., Bell D.A. Human glutathione S-transferase P1 polymorphisms: Relationship to lung tissue enzyme activity and population frequency distribution. Carcinogenesis 1998, 19:275-280.
    • (1998) Carcinogenesis , vol.19 , pp. 275-280
    • Watson, M.A.1    Stewart, R.K.2    Smith, G.B.3    Massey, T.E.4    Bell, D.A.5
  • 119
    • 33845600791 scopus 로고    scopus 로고
    • Protein glutathiolation by nitric oxide: An intracellular mechanism regulating redox protein modification
    • West M.B., Hill B.G., Xuan Y.T., Bhatnagar A. Protein glutathiolation by nitric oxide: An intracellular mechanism regulating redox protein modification. The FASEB Journal 2006, 20:1715-1717.
    • (2006) The FASEB Journal , vol.20 , pp. 1715-1717
    • West, M.B.1    Hill, B.G.2    Xuan, Y.T.3    Bhatnagar, A.4
  • 121
    • 33748919803 scopus 로고    scopus 로고
    • Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals
    • Wu Y., Fan Y., Xue B., Luo L., Shen J., Zhang S., et al. Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals. Oncogene 2006, 25:5787-5800.
    • (2006) Oncogene , vol.25 , pp. 5787-5800
    • Wu, Y.1    Fan, Y.2    Xue, B.3    Luo, L.4    Shen, J.5    Zhang, S.6
  • 123
    • 22544480556 scopus 로고    scopus 로고
    • Regulation of lipopolysaccharide-induced inflammatory response by glutathione S-transferase P1 in RAW264.7 cells
    • Xue B., Wu Y., Yin Z., Zhang H., Sun S., Yi T., et al. Regulation of lipopolysaccharide-induced inflammatory response by glutathione S-transferase P1 in RAW264.7 cells. FEBS Letters 2005, 579:4081-4087.
    • (2005) FEBS Letters , vol.579 , pp. 4081-4087
    • Xue, B.1    Wu, Y.2    Yin, Z.3    Zhang, H.4    Sun, S.5    Yi, T.6
  • 124
    • 0028088048 scopus 로고
    • Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties
    • Zimniak P., Nanduri B., Pikula S., Bandorowicz-Pikula J., Singhal S.S., Srivastava S.K., et al. Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties. European Journal of Biochemistry 1994, 224:893-899.
    • (1994) European Journal of Biochemistry , vol.224 , pp. 893-899
    • Zimniak, P.1    Nanduri, B.2    Pikula, S.3    Bandorowicz-Pikula, J.4    Singhal, S.S.5    Srivastava, S.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.