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Volumn 5, Issue 6, 2013, Pages 673-685

Selenium mediated arsenic toxicity modifies cytotoxicity, reactive oxygen species and phosphorylated proteins

Author keywords

[No Author keywords available]

Indexed keywords

CONCENTRATION-DEPENDENT MANNERS; ENZYMATIC DIGESTIONS; MODULATING FUNCTIONS; PHOSPHORYLATED PEPTIDES; PHOSPHORYLATED PROTEINS; PROTEIN PHOSPHORYLATION; REACTIVE OXYGEN SPECIES; SELENOMETHIONINE (SEMET);

EID: 84878799179     PISSN: 17565901     EISSN: 1756591X     Source Type: Journal    
DOI: 10.1039/c3mt20213e     Document Type: Article
Times cited : (22)

References (82)
  • 1
    • 48749096008 scopus 로고    scopus 로고
    • Carcinogenic metal compounds: Recent insight into molecular and cellular mechanisms
    • D. Beyersmann A. Hartwig Carcinogenic metal compounds: recent insight into molecular and cellular mechanisms Arch. Toxicol. 2008 82 8 493 512
    • (2008) Arch. Toxicol. , vol.82 , Issue.8 , pp. 493-512
    • Beyersmann, D.1    Hartwig, A.2
  • 2
    • 0037150538 scopus 로고    scopus 로고
    • Public health. Arsenic epidemiology and drinking water standards
    • A. H. Smith P. A. Lopipero M. N. Bates C. M. Steinmaus Public health. Arsenic epidemiology and drinking water standards Science 2002 296 5576 2145 2146
    • (2002) Science , vol.296 , Issue.5576 , pp. 2145-2146
    • Smith, A.H.1    Lopipero, P.A.2    Bates, M.N.3    Steinmaus, C.M.4
  • 5
    • 0038346303 scopus 로고    scopus 로고
    • Difference in uptake and toxicity of trivalent and pentavalent inorganic arsenic in rat heart microvessel endothelial cells
    • S. Hirano X. Cui S. Li S. Kanno Y. Kobayashi T. Hayakawa A. Shraim Difference in uptake and toxicity of trivalent and pentavalent inorganic arsenic in rat heart microvessel endothelial cells Arch. Toxicol. 2003 77 6 305 312
    • (2003) Arch. Toxicol. , vol.77 , Issue.6 , pp. 305-312
    • Hirano, S.1    Cui, X.2    Li, S.3    Kanno, S.4    Kobayashi, Y.5    Hayakawa, T.6    Shraim, A.7
  • 6
    • 18544371009 scopus 로고    scopus 로고
    • Metals, toxicity and oxidative stress
    • M. Valko H. Morris M. T. Cronin Metals, toxicity and oxidative stress Curr. Med. Chem. 2005 12 10 1161 1208
    • (2005) Curr. Med. Chem. , vol.12 , Issue.10 , pp. 1161-1208
    • Valko, M.1    Morris, H.2    Cronin, M.T.3
  • 8
    • 77049126844 scopus 로고    scopus 로고
    • Arsenic-induced carcinogenesis-oxidative stress as a possible mode of action and future research needs for more biologically based risk assessment
    • K. T. Kitchin R. Conolly Arsenic-induced carcinogenesis-oxidative stress as a possible mode of action and future research needs for more biologically based risk assessment Chem. Res. Toxicol. 2010 23 2 327 335
    • (2010) Chem. Res. Toxicol. , vol.23 , Issue.2 , pp. 327-335
    • Kitchin, K.T.1    Conolly, R.2
  • 10
    • 0035860357 scopus 로고    scopus 로고
    • Oral exposure of dimethylarsinic acid, a main metabolite of inorganic arsenics, in mice leads to an increase in 8-oxo-2′-deoxyguanosine level, specifically in the target organs for arsenic carcinogenesis
    • K. Yamanaka F. Takabayashi M. Mizoi Y. An A. Hasegawa S. Okada Oral exposure of dimethylarsinic acid, a main metabolite of inorganic arsenics, in mice leads to an increase in 8-oxo-2′-deoxyguanosine level, specifically in the target organs for arsenic carcinogenesis Biochem. Biophys. Res. Commun. 2001 287 1 66 70
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , Issue.1 , pp. 66-70
    • Yamanaka, K.1    Takabayashi, F.2    Mizoi, M.3    An, Y.4    Hasegawa, A.5    Okada, S.6
  • 11
    • 33646080824 scopus 로고    scopus 로고
    • Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products
    • W. L. Neeley J. M. Essigmann Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products Chem. Res. Toxicol. 2006 19 4 491 505
    • (2006) Chem. Res. Toxicol. , vol.19 , Issue.4 , pp. 491-505
    • Neeley, W.L.1    Essigmann, J.M.2
  • 12
    • 45949112003 scopus 로고    scopus 로고
    • Attenuation of DNA damage-induced p53 expression by arsenic: A possible mechanism for arsenic co-carcinogenesis
    • S. Shen J. Lee M. Weinfeld X. C. Le Attenuation of DNA damage-induced p53 expression by arsenic: a possible mechanism for arsenic co-carcinogenesis Mol. Carcinog. 2008 47 7 508 518
    • (2008) Mol. Carcinog. , vol.47 , Issue.7 , pp. 508-518
    • Shen, S.1    Lee, J.2    Weinfeld, M.3    Le, X.C.4
  • 13
    • 84859750422 scopus 로고    scopus 로고
    • Biologically relevant oxidants cause bound proteins to readily oxidatively cross-link at guanine
    • M. J. Solivio D. B. Nemera L. Sallans E. J. Merino Biologically relevant oxidants cause bound proteins to readily oxidatively cross-link at guanine Chem. Res. Toxicol. 2012 25 2 326 336
    • (2012) Chem. Res. Toxicol. , vol.25 , Issue.2 , pp. 326-336
    • Solivio, M.J.1    Nemera, D.B.2    Sallans, L.3    Merino, E.J.4
  • 14
    • 49649083174 scopus 로고    scopus 로고
    • Arsenite alters global histone H3 methylation
    • X. Zhou H. Sun T. P. Ellen H. Chen M. Costa Arsenite alters global histone H3 methylation Carcinogenesis 2008 29 9 1831 1836
    • (2008) Carcinogenesis , vol.29 , Issue.9 , pp. 1831-1836
    • Zhou, X.1    Sun, H.2    Ellen, T.P.3    Chen, H.4    Costa, M.5
  • 15
    • 39049190270 scopus 로고    scopus 로고
    • Genetic and epigenetic changes induced by chronic low dose exposure to arsenic of mouse testicular Leydig cells
    • K. P. Singh J. W. DuMond, Jr. Genetic and epigenetic changes induced by chronic low dose exposure to arsenic of mouse testicular Leydig cells Int. J. Oncol. 2007 30 1 253 260
    • (2007) Int. J. Oncol. , vol.30 , Issue.1 , pp. 253-260
    • Singh, K.P.1    Dumond, Jr.J.W.2
  • 16
    • 34547644483 scopus 로고    scopus 로고
    • Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide
    • J. Lu E. H. Chew A. Holmgren Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide Proc. Natl. Acad. Sci. U. S. A. 2007 104 30 12288 12293
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , Issue.30 , pp. 12288-12293
    • Lu, J.1    Chew, E.H.2    Holmgren, A.3
  • 17
    • 79959363492 scopus 로고    scopus 로고
    • Arsenic-induced oxidative stress and its reversibility
    • S. J. Flora Arsenic-induced oxidative stress and its reversibility Free Radical Biol. Med. 2011 51 2 257 281
    • (2011) Free Radical Biol. Med. , vol.51 , Issue.2 , pp. 257-281
    • Flora, S.J.1
  • 18
    • 0034662094 scopus 로고    scopus 로고
    • The importance of selenium to human health
    • M. P. Rayman The importance of selenium to human health Lancet 2000 356 9225 233 241
    • (2000) Lancet , vol.356 , Issue.9225 , pp. 233-241
    • Rayman, M.P.1
  • 19
    • 77956402478 scopus 로고    scopus 로고
    • Evaluation of cytotoxicity and oxidative DNA damaging effects of di(2-ethylhexyl)-phthalate (DEHP) and mono(2-ethylhexyl)-phthalate (MEHP) on MA-10 Leydig cells and protection by selenium
    • P. Erkekoglu W. Rachidi O. G. Yuzugullu B. Giray A. Favier M. Ozturk F. Hincal Evaluation of cytotoxicity and oxidative DNA damaging effects of di(2-ethylhexyl)-phthalate (DEHP) and mono(2-ethylhexyl)-phthalate (MEHP) on MA-10 Leydig cells and protection by selenium Toxicol. Appl. Pharmacol. 2010 248 1 52 62
    • (2010) Toxicol. Appl. Pharmacol. , vol.248 , Issue.1 , pp. 52-62
    • Erkekoglu, P.1    Rachidi, W.2    Yuzugullu, O.G.3    Giray, B.4    Favier, A.5    Ozturk, M.6    Hincal, F.7
  • 21
    • 34047164947 scopus 로고    scopus 로고
    • Arsenic-selenium and mercury-selenium bonds in biology
    • J. Gailer Arsenic-selenium and mercury-selenium bonds in biology Coord. Chem. Rev. 2007 251 234 254
    • (2007) Coord. Chem. Rev. , vol.251 , pp. 234-254
    • Gailer, J.1
  • 22
    • 84858438033 scopus 로고    scopus 로고
    • Arsenic-glutathione conjugate transport by the human multidrug resistance proteins (MRPs/ABCCs)
    • E. M. Leslie Arsenic-glutathione conjugate transport by the human multidrug resistance proteins (MRPs/ABCCs) J. Inorg. Biochem. 2012 108 141 149
    • (2012) J. Inorg. Biochem. , vol.108 , pp. 141-149
    • Leslie, E.M.1
  • 27
    • 78049324544 scopus 로고    scopus 로고
    • Arsenic-induced protein phosphorylation changes in HeLa cells
    • O. Alp E. J. Merino J. A. Caruso Arsenic-induced protein phosphorylation changes in HeLa cells Anal. Bioanal. Chem. 2010 398 5 2099 2107
    • (2010) Anal. Bioanal. Chem. , vol.398 , Issue.5 , pp. 2099-2107
    • Alp, O.1    Merino, E.J.2    Caruso, J.A.3
  • 28
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • J. V. Olsen B. Blagoev F. Gnad B. Macek C. Kumar P. Mortensen M. Mann Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 2006 127 3 635 648
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    MacEk, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 29
    • 77953218034 scopus 로고    scopus 로고
    • Phosphorylation of conserved PIN motifs directs Arabidopsis PIN1 polarity and auxin transport
    • F. Huang M. K. Zago L. Abas A. van Marion C. S. Galvan-Ampudia R. Offringa Phosphorylation of conserved PIN motifs directs Arabidopsis PIN1 polarity and auxin transport Plant Cell 2010 22 4 1129 1142
    • (2010) Plant Cell , vol.22 , Issue.4 , pp. 1129-1142
    • Huang, F.1    Zago, M.K.2    Abas, L.3    Van Marion, A.4    Galvan-Ampudia, C.S.5    Offringa, R.6
  • 30
    • 41249087147 scopus 로고    scopus 로고
    • Reversible tyrosine protein phosphorylation regulates large conductance voltage- and calcium-activated potassium channels via cortactin
    • L. Tian H. McClafferty L. Chen M. J. Shipston Reversible tyrosine protein phosphorylation regulates large conductance voltage- and calcium-activated potassium channels via cortactin J. Biol. Chem. 2008 283 6 3067 3076
    • (2008) J. Biol. Chem. , vol.283 , Issue.6 , pp. 3067-3076
    • Tian, L.1    McClafferty, H.2    Chen, L.3    Shipston, M.J.4
  • 31
    • 0032577051 scopus 로고    scopus 로고
    • The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: Its role in cell growth and disease
    • T. Hunter The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease Philos. Trans. R. Soc. London, Ser. B 1998 353 1368 583 605
    • (1998) Philos. Trans. R. Soc. London, Ser. B , vol.353 , Issue.1368 , pp. 583-605
    • Hunter, T.1
  • 32
    • 0037214522 scopus 로고    scopus 로고
    • Determination of serine/threonine protein phosphatase type 2B PP2B in lymphocytes by HPLC
    • B. Blanchet A. Hulin C. Duvoux A. Astier Determination of serine/threonine protein phosphatase type 2B PP2B in lymphocytes by HPLC Anal. Biochem. 2003 312 1 1 6
    • (2003) Anal. Biochem. , vol.312 , Issue.1 , pp. 1-6
    • Blanchet, B.1    Hulin, A.2    Duvoux, C.3    Astier, A.4
  • 33
    • 33646178365 scopus 로고    scopus 로고
    • Identification of in vivo phosphorylation sites on human deoxycytidine kinase. Role of Ser-74 in the control of enzyme activity
    • C. Smal D. Vertommen L. Bertrand S. Ntamashimikiro M. H. Rider E. Van Den Neste F. Bontemps Identification of in vivo phosphorylation sites on human deoxycytidine kinase. Role of Ser-74 in the control of enzyme activity J. Biol. Chem. 2006 281 8 4887 4893
    • (2006) J. Biol. Chem. , vol.281 , Issue.8 , pp. 4887-4893
    • Smal, C.1    Vertommen, D.2    Bertrand, L.3    Ntamashimikiro, S.4    Rider, M.H.5    Van Den Neste, E.6    Bontemps, F.7
  • 34
    • 52049083485 scopus 로고    scopus 로고
    • Phosphoproteomics: Unraveling the signaling web
    • P. H. Huang F. M. White Phosphoproteomics: unraveling the signaling web Mol. Cell 2008 31 6 777 781
    • (2008) Mol. Cell , vol.31 , Issue.6 , pp. 777-781
    • Huang, P.H.1    White, F.M.2
  • 35
    • 1642464045 scopus 로고    scopus 로고
    • Phosphorylation regulates nucleophosmin targeting to the centrosome during mitosis as detected by cross-reactive phosphorylation-specific MKK1/MKK2 antibodies
    • H. Cha C. Hancock S. Dangi D. Maiguel F. Carrier P. Shapiro Phosphorylation regulates nucleophosmin targeting to the centrosome during mitosis as detected by cross-reactive phosphorylation-specific MKK1/MKK2 antibodies Biochem. J. 2004 378 Pt 3 857 865
    • (2004) Biochem. J. , vol.378 , Issue.PART 3 , pp. 857-865
    • Cha, H.1    Hancock, C.2    Dangi, S.3    Maiguel, D.4    Carrier, F.5    Shapiro, P.6
  • 37
    • 79955676532 scopus 로고    scopus 로고
    • Selenium effects on arsenic cytotoxicity and protein phosphorylation in human kidney cells using chip-based nanoLC-MS/MS
    • O. Alp Y. Zhang E. J. Merino J. A. Caruso Selenium effects on arsenic cytotoxicity and protein phosphorylation in human kidney cells using chip-based nanoLC-MS/MS Metallomics 2011 3 5 482 490
    • (2011) Metallomics , vol.3 , Issue.5 , pp. 482-490
    • Alp, O.1    Zhang, Y.2    Merino, E.J.3    Caruso, J.A.4
  • 38
    • 58149377768 scopus 로고    scopus 로고
    • Studying phosphorylation in cerebrospinal fluid with capLC-ICPMS for 31P specific detection and nanoLC-chip/ITMS for identification
    • J. Ellis R. Grimm J. F. Clark G. J. Pyne-Geithman S. Wilbur J. A. Caruso Studying phosphorylation in cerebrospinal fluid with capLC-ICPMS for 31P specific detection and nanoLC-chip/ITMS for identification J. Proteome Res. 2008 7 4736 4742
    • (2008) J. Proteome Res. , vol.7 , pp. 4736-4742
    • Ellis, J.1    Grimm, R.2    Clark, J.F.3    Pyne-Geithman, G.J.4    Wilbur, S.5    Caruso, J.A.6
  • 40
    • 41149098111 scopus 로고    scopus 로고
    • Absolute and site-specific quantification of protein phosphorylation using integrated elemental and molecular mass spectrometry: Its potential to assess phosphopeptide enrichment procedures
    • A. P. Navaza J. R. Encinar M. Carrascal J. Abian A. Sanz-Medel Absolute and site-specific quantification of protein phosphorylation using integrated elemental and molecular mass spectrometry: its potential to assess phosphopeptide enrichment procedures Anal. Chem. 2008 80 5 1777 1787
    • (2008) Anal. Chem. , vol.80 , Issue.5 , pp. 1777-1787
    • Navaza, A.P.1    Encinar, J.R.2    Carrascal, M.3    Abian, J.4    Sanz-Medel, A.5
  • 41
    • 67649995540 scopus 로고    scopus 로고
    • Capillary HPLC-ICPMS and tyrosine iodination for the absolute quantification of peptides using generic standards
    • A. P. Navaza J. R. Encinar A. Ballesteros J. M. Gonzalez A. Sanz-Medel Capillary HPLC-ICPMS and tyrosine iodination for the absolute quantification of peptides using generic standards Anal. Chem. 2009 81 13 5390 5399
    • (2009) Anal. Chem. , vol.81 , Issue.13 , pp. 5390-5399
    • Navaza, A.P.1    Encinar, J.R.2    Ballesteros, A.3    Gonzalez, J.M.4    Sanz-Medel, A.5
  • 42
    • 77952950498 scopus 로고    scopus 로고
    • Metal labeling for quantitative protein and proteome analysis using inductively-coupled plasma mass spectrometry
    • A. Tholey D. Schaumlöffel Metal labeling for quantitative protein and proteome analysis using inductively-coupled plasma mass spectrometry TrAC, Trends Anal. Chem. 2010 29 5 399 408
    • (2010) TrAC, Trends Anal. Chem. , vol.29 , Issue.5 , pp. 399-408
    • Tholey, A.1    Schaumlöffel, D.2
  • 43
    • 78651306084 scopus 로고    scopus 로고
    • Implications of using the fluorescent probes, dihydrorhodamine 123 and 2′,7′-dichlorodihydrofluorescein diacetate, for the detection of UVA-induced reactive oxygen species
    • S. Boulton A. Anderson H. Swalwell J. R. Henderson P. Manning M. A. Birch-Machin Implications of using the fluorescent probes, dihydrorhodamine 123 and 2′,7′-dichlorodihydrofluorescein diacetate, for the detection of UVA-induced reactive oxygen species Free Radical Res. 2011 45 2 139 146
    • (2011) Free Radical Res. , vol.45 , Issue.2 , pp. 139-146
    • Boulton, S.1    Anderson, A.2    Swalwell, H.3    Henderson, J.R.4    Manning, P.5    Birch-Machin, M.A.6
  • 44
    • 17844380283 scopus 로고    scopus 로고
    • Overexpression of alpha enolase in hepatitis C virus-related hepatocellular carcinoma: Association with tumor progression as determined by proteomic analysis
    • M. Takashima Y. Kuramitsu Y. Yokoyama N. Iizuka M. Fujimoto T. Nishisaka K. Okita M. Oka K. Nakamura Overexpression of alpha enolase in hepatitis C virus-related hepatocellular carcinoma: association with tumor progression as determined by proteomic analysis Proteomics 2005 5 6 1686 1692
    • (2005) Proteomics , vol.5 , Issue.6 , pp. 1686-1692
    • Takashima, M.1    Kuramitsu, Y.2    Yokoyama, Y.3    Iizuka, N.4    Fujimoto, M.5    Nishisaka, T.6    Okita, K.7    Oka, M.8    Nakamura, K.9
  • 45
    • 79952830765 scopus 로고    scopus 로고
    • Alpha-enolase: A promising therapeutic and diagnostic tumor target
    • M. Capello S. Ferri-Borgogno P. Cappello F. Novelli alpha-enolase: a promising therapeutic and diagnostic tumor target FEBS J. 2011 278 7 1064 1074
    • (2011) FEBS J. , vol.278 , Issue.7 , pp. 1064-1074
    • Capello, M.1    Ferri-Borgogno, S.2    Cappello, P.3    Novelli, F.4
  • 46
    • 61449134122 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of apoptosis
    • M. Broemer P. Meier Ubiquitin-mediated regulation of apoptosis Trends Cell Biol. 2009 19 3 130 140
    • (2009) Trends Cell Biol. , vol.19 , Issue.3 , pp. 130-140
    • Broemer, M.1    Meier, P.2
  • 47
  • 49
    • 33644756933 scopus 로고    scopus 로고
    • Differential expression of eIF5A-1 and eIF5A-2 in human cancer cells
    • P. M. Clement H. E. Johansson E. C. Wolff M. H. Park Differential expression of eIF5A-1 and eIF5A-2 in human cancer cells FEBS J. 2006 273 6 1102 1114
    • (2006) FEBS J. , vol.273 , Issue.6 , pp. 1102-1114
    • Clement, P.M.1    Johansson, H.E.2    Wolff, E.C.3    Park, M.H.4
  • 50
    • 0344304422 scopus 로고    scopus 로고
    • Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells
    • E. Tzima J. S. Reader M. Irani-Tehrani K. L. Ewalt M. A. Schwartz P. Schimmel Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells Proc. Natl. Acad. Sci. U. S. A. 2003 100 25 14903 14907
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , Issue.25 , pp. 14903-14907
    • Tzima, E.1    Reader, J.S.2    Irani-Tehrani, M.3    Ewalt, K.L.4    Schwartz, M.A.5    Schimmel, P.6
  • 51
    • 42949090556 scopus 로고    scopus 로고
    • The spectrin cytoskeleton influences the surface expression and activation of human transient receptor potential channel 4 channels
    • A. F. Odell D. F. Van Helden J. L. Scott The spectrin cytoskeleton influences the surface expression and activation of human transient receptor potential channel 4 channels J. Biol. Chem. 2008 283 7 4395 4407
    • (2008) J. Biol. Chem. , vol.283 , Issue.7 , pp. 4395-4407
    • Odell, A.F.1    Van Helden, D.F.2    Scott, J.L.3
  • 53
    • 12844265993 scopus 로고    scopus 로고
    • Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205
    • S. Ganguly J. L. Weller A. Ho P. Chemineau B. Malpaux D. C. Klein Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205 Proc. Natl. Acad. Sci. U. S. A. 2005 102 4 1222 1227
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.4 , pp. 1222-1227
    • Ganguly, S.1    Weller, J.L.2    Ho, A.3    Chemineau, P.4    Malpaux, B.5    Klein, D.C.6
  • 55
    • 70350462371 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T Cell receptor signaling reveals system-wide modulation of protein-protein interactions
    • 10.1126/scisignal.2000007
    • V. Mayya D. H. Lundgren S. L. L. Hwang K. Rezaul L. Wu J. K. Eng V. Rodionov D. K. Han Quantitative phosphoproteomic analysis of T Cell receptor signaling reveals system-wide modulation of protein-protein interactions Sci. Signaling 2009 2 84 10.1126/scisignal.2000007
    • (2009) Sci. Signaling , vol.2 , Issue.84
    • Mayya, V.1    Lundgren, D.H.2    Hwang, S.L.L.3    Rezaul, K.4    Wu, L.5    Eng, J.K.6    Rodionov, V.7    Han, D.K.8
  • 58
    • 0030794277 scopus 로고    scopus 로고
    • Identification of putative c-Myc-responsive genes: Characterization of rcl, a novel growth-related gene
    • B. C. Lewis H. Shim Q. Li C. S. Wu L. A. Lee A. Maity C. V. Dang Identification of putative c-Myc-responsive genes: characterization of rcl, a novel growth-related gene Mol. Cell. Biol. 1997 17 9 4967 4978
    • (1997) Mol. Cell. Biol. , vol.17 , Issue.9 , pp. 4967-4978
    • Lewis, B.C.1    Shim, H.2    Li, Q.3    Wu, C.S.4    Lee, L.A.5    Maity, A.6    Dang, C.V.7
  • 59
    • 70449534068 scopus 로고    scopus 로고
    • Solution structure of RCL, a novel 2′-deoxyribonucleoside 5′-monophosphate N-glycosidase
    • K. Doddapaneni B. Mahler R. Pavlovicz A. Haushalter C. Yuan Z. Wu Solution structure of RCL, a novel 2′-deoxyribonucleoside 5′-monophosphate N-glycosidase J. Mol. Biol. 2009 394 3 423 434
    • (2009) J. Mol. Biol. , vol.394 , Issue.3 , pp. 423-434
    • Doddapaneni, K.1    Mahler, B.2    Pavlovicz, R.3    Haushalter, A.4    Yuan, C.5    Wu, Z.6
  • 60
    • 32144435113 scopus 로고    scopus 로고
    • The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice
    • F. Cui Y. Wang J. Wang K. Wei J. Hu F. Liu H. Wang X. Zhao X. Zhang X. Yang The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice Proteomics 2006 6 2 498 504
    • (2006) Proteomics , vol.6 , Issue.2 , pp. 498-504
    • Cui, F.1    Wang, Y.2    Wang, J.3    Wei, K.4    Hu, J.5    Liu, F.6    Wang, H.7    Zhao, X.8    Zhang, X.9    Yang, X.10
  • 63
    • 1842457755 scopus 로고    scopus 로고
    • Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel pathway for triggering apoptosis
    • X. B. Qiu S. L. Markant J. Yuan A. L. Goldberg Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel pathway for triggering apoptosis EMBO J. 2004 23 4 800 810
    • (2004) EMBO J. , vol.23 , Issue.4 , pp. 800-810
    • Qiu, X.B.1    Markant, S.L.2    Yuan, J.3    Goldberg, A.L.4
  • 64
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • N. A. Thornberry Y. Lazebnik Caspases: enemies within Science 1998 281 5381 1312 1316
    • (1998) Science , vol.281 , Issue.5381 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 67
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • D. D. Mosser A. W. Caron L. Bourget C. Denis-Larose B. Massie Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis Mol. Cell. Biol. 1997 17 9 5317 5327
    • (1997) Mol. Cell. Biol. , vol.17 , Issue.9 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 68
    • 0031793127 scopus 로고    scopus 로고
    • Heat shock protein 70 kDa: Molecular biology, biochemistry, and physiology
    • J. G. Kiang G. C. Tsokos Heat shock protein 70 kDa: molecular biology, biochemistry, and physiology Pharmacol. Ther. 1998 80 2 183 201
    • (1998) Pharmacol. Ther. , vol.80 , Issue.2 , pp. 183-201
    • Kiang, J.G.1    Tsokos, G.C.2
  • 69
    • 68949202516 scopus 로고    scopus 로고
    • Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders
    • M. Wang S. Wey Y. Zhang R. Ye A. S. Lee Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders Antioxid. Redox Signaling 2009 11 9 2307 2316
    • (2009) Antioxid. Redox Signaling , vol.11 , Issue.9 , pp. 2307-2316
    • Wang, M.1    Wey, S.2    Zhang, Y.3    Ye, R.4    Lee, A.S.5
  • 70
    • 79960400840 scopus 로고    scopus 로고
    • Novel mechanism of anti-apoptotic function of 78-kDa glucose-regulated protein (GRP78): Endocrine resistance factor in breast cancer, through release of B-cell lymphoma 2 (BCL-2) from BCL-2-interacting killer (BIK)
    • H. Zhou Y. Zhang Y. Fu L. Chan A. S. Lee Novel mechanism of anti-apoptotic function of 78-kDa glucose-regulated protein (GRP78): endocrine resistance factor in breast cancer, through release of B-cell lymphoma 2 (BCL-2) from BCL-2-interacting killer (BIK) J. Biol. Chem. 2011 286 29 25687 25696
    • (2011) J. Biol. Chem. , vol.286 , Issue.29 , pp. 25687-25696
    • Zhou, H.1    Zhang, Y.2    Fu, Y.3    Chan, L.4    Lee, A.S.5
  • 72
    • 80053376304 scopus 로고    scopus 로고
    • Redox signalling via the cellular thiolstat
    • C. Jacob Redox signalling via the cellular thiolstat Biochem. Soc. Trans. 2011 39 5 1247 1253
    • (2011) Biochem. Soc. Trans. , vol.39 , Issue.5 , pp. 1247-1253
    • Jacob, C.1
  • 73
    • 19444381651 scopus 로고    scopus 로고
    • Direct association of hepatopoietin with thioredoxin constitutes a redox signal transduction in activation of AP-1/NF-kappaB
    • Y. Li W. Liu G. Xing C. Tian Y. Zhu F. He Direct association of hepatopoietin with thioredoxin constitutes a redox signal transduction in activation of AP-1/NF-kappaB Cell. Signalling 2005 17 8 985 996
    • (2005) Cell. Signalling , vol.17 , Issue.8 , pp. 985-996
    • Li, Y.1    Liu, W.2    Xing, G.3    Tian, C.4    Zhu, Y.5    He, F.6
  • 74
    • 67649840689 scopus 로고    scopus 로고
    • Regulation of superoxide dismutase genes: Implications in disease
    • L. Miao D. K. St. Clair Regulation of superoxide dismutase genes: implications in disease Free Radical Biol. Med. 2009 47 4 344 356
    • (2009) Free Radical Biol. Med. , vol.47 , Issue.4 , pp. 344-356
    • Miao, L.1    St. Clair, D.K.2
  • 75
    • 53549103598 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 5 suppresses the transcription of the RB family of tumor suppressors in leukemia and lymphoma cells
    • L. Wang S. Pal S. Sif Protein arginine methyltransferase 5 suppresses the transcription of the RB family of tumor suppressors in leukemia and lymphoma cells Mol. Cell. Biol. 2008 28 20 6262 6277
    • (2008) Mol. Cell. Biol. , vol.28 , Issue.20 , pp. 6262-6277
    • Wang, L.1    Pal, S.2    Sif, S.3
  • 76
    • 67649968054 scopus 로고    scopus 로고
    • The protein arginine methyltransferase family: An update about function, new perspectives and the physiological role in humans
    • S. S. Wolf The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans Cell. Mol. Life Sci. 2009 66 13 2109 2121
    • (2009) Cell. Mol. Life Sci. , vol.66 , Issue.13 , pp. 2109-2121
    • Wolf, S.S.1
  • 77
    • 77958471611 scopus 로고    scopus 로고
    • Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation
    • H. Iwasaki J. C. Kovacic M. Olive J. K. Beers T. Yoshimoto M. F. Crook L. H. Tonelli E. G. Nabel Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation Circ. Res. 2010 107 8 992 1001
    • (2010) Circ. Res. , vol.107 , Issue.8 , pp. 992-1001
    • Iwasaki, H.1    Kovacic, J.C.2    Olive, M.3    Beers, J.K.4    Yoshimoto, T.5    Crook, M.F.6    Tonelli, L.H.7    Nabel, E.G.8
  • 78
    • 51349135008 scopus 로고    scopus 로고
    • The involvement of c-Abl and D40 (AF15q14/CASC5) proteins in the regulation of cell proliferation and cancer
    • K. V. Bogdanov M. Takimoto The involvement of c-Abl and D40 (AF15q14/CASC5) proteins in the regulation of cell proliferation and cancer Tsitologiya 2008 50 7 590 596
    • (2008) Tsitologiya , vol.50 , Issue.7 , pp. 590-596
    • Bogdanov, K.V.1    Takimoto, M.2
  • 79
    • 58949091294 scopus 로고    scopus 로고
    • Involvement of c-Abl, p53 and the MAP kinase JNK in the cell death program initiated in A2E-laden ARPE-19 cells by exposure to blue light
    • B. S. Westlund B. Cai J. Zhou J. R. Sparrow Involvement of c-Abl, p53 and the MAP kinase JNK in the cell death program initiated in A2E-laden ARPE-19 cells by exposure to blue light Apoptosis 2009 14 1 31 41
    • (2009) Apoptosis , vol.14 , Issue.1 , pp. 31-41
    • Westlund, B.S.1    Cai, B.2    Zhou, J.3    Sparrow, J.R.4
  • 80
    • 78650086228 scopus 로고    scopus 로고
    • C-Abl tyrosine kinase in the DNA damage response: Cell death and more
    • V. Meltser M. Ben-Yehoyada Y. Shaul c-Abl tyrosine kinase in the DNA damage response: cell death and more Cell Death Differ. 2011 18 1 2 4
    • (2011) Cell Death Differ. , vol.18 , Issue.1 , pp. 2-4
    • Meltser, V.1    Ben-Yehoyada, M.2    Shaul, Y.3
  • 81
    • 77951213966 scopus 로고    scopus 로고
    • A novel LZAP-binding protein, NLBP, inhibits cell invasion
    • J. Kwon H. J. Cho S. H. Han J. G. No J. Y. Kwon H. Kim A novel LZAP-binding protein, NLBP, inhibits cell invasion J. Biol. Chem. 2010 285 16 12232 12240
    • (2010) J. Biol. Chem. , vol.285 , Issue.16 , pp. 12232-12240
    • Kwon, J.1    Cho, H.J.2    Han, S.H.3    No, J.G.4    Kwon, J.Y.5    Kim, H.6


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