메뉴 건너뛰기




Volumn 15, Issue 5-6, 2015, Pages 1051-1074

Proteomics in mechanistic toxicology: History, concepts, achievements, caveats, and potential

Author keywords

Cell biology; Toxicology

Indexed keywords

DRUG; INDUSTRIAL CHEMICAL; METAL; METALLOID; NANOFIBER; NANOPARTICLE; NATURAL PRODUCT; PROTEIN; PROTEOME; TOXIC SUBSTANCE;

EID: 84924598514     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400288     Document Type: Review
Times cited : (46)

References (237)
  • 1
    • 0019212386 scopus 로고
    • Induction of 4 proteins in chick-embryo cells by sodium arsenite
    • Johnston, D., Oppermann, H., Jackson, J., Levinson, W., Induction of 4 proteins in chick-embryo cells by sodium arsenite. J. Biol. Chem. 1980, 255, 6975-6980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6975-6980
    • Johnston, D.1    Oppermann, H.2    Jackson, J.3    Levinson, W.4
  • 2
    • 0020538318 scopus 로고
    • Arsenate induces stress proteins in cultured rat myoblasts
    • Kim, Y. J., Shuman, J., Sette, M., Przybyla, A., Arsenate induces stress proteins in cultured rat myoblasts. J. Cell Biol. 1983, 96, 393-400.
    • (1983) J. Cell Biol. , vol.96 , pp. 393-400
    • Kim, Y.J.1    Shuman, J.2    Sette, M.3    Przybyla, A.4
  • 3
    • 0021611140 scopus 로고
    • Protein-pattern changes and morphological effects due to methionine starvation or treatment with 5-azacytidine of the phorbol-ester-sensitive cell lines HL-60, CCL-119, and U-937
    • Anderson, N. L., Gemmell, M. A., Protein-pattern changes and morphological effects due to methionine starvation or treatment with 5-azacytidine of the phorbol-ester-sensitive cell lines HL-60, CCL-119, and U-937. Clin. Chem. 1984, 30, 1956-1964.
    • (1984) Clin. Chem. , vol.30 , pp. 1956-1964
    • Anderson, N.L.1    Gemmell, M.A.2
  • 4
    • 0022624795 scopus 로고
    • Effects of Aroclor-1254 on proteins of mouse liver-application of two-dimensional electrophoretic protein mapping
    • Anderson, N. L., Swanson, M., Giere, F. A., Tollaksen, S. et al., Effects of Aroclor-1254 on proteins of mouse liver-application of two-dimensional electrophoretic protein mapping. Electrophoresis 1986, 7, 44-48.
    • (1986) Electrophoresis , vol.7 , pp. 44-48
    • Anderson, N.L.1    Swanson, M.2    Giere, F.A.3    Tollaksen, S.4
  • 5
    • 77957175441 scopus 로고
    • Effects of toxic agents at the protein level-quantitative measurement of 213 mouse-liver proteins following xenobiotic treatment
    • Anderson, N. L., Giere, F. A., Nance, S. L., Gemmell, M. A. et al., Effects of toxic agents at the protein level-quantitative measurement of 213 mouse-liver proteins following xenobiotic treatment. Fund. Appl. Toxicol. 1987, 8, 39-50.
    • (1987) Fund. Appl. Toxicol. , vol.8 , pp. 39-50
    • Anderson, N.L.1    Giere, F.A.2    Nance, S.L.3    Gemmell, M.A.4
  • 6
    • 84924584504 scopus 로고
    • Determination of perfluoro-normal-decanoic acid toxicity invitro and invivo via two-dimensional polyacrylamide-gel electrophoresis
    • Witzmann, F. A., Bale, S. S., London, S. A., Determination of perfluoro-normal-decanoic acid toxicity invitro and invivo via two-dimensional polyacrylamide-gel electrophoresis. Electrophoresis 1988, 9, 641-641.
    • (1988) Electrophoresis , vol.9 , pp. 641-641
    • Witzmann, F.A.1    Bale, S.S.2    London, S.A.3
  • 7
    • 0019721087 scopus 로고
    • Isolation and characterization of desmosome-associated tonofilaments from rat intestinal brush border
    • Franke, W. W., Winter, S., Grund, C., Schmid, E. et al., Isolation and characterization of desmosome-associated tonofilaments from rat intestinal brush border. J. Cell Biol. 1981, 90, 116-127.
    • (1981) J. Cell Biol. , vol.90 , pp. 116-127
    • Franke, W.W.1    Winter, S.2    Grund, C.3    Schmid, E.4
  • 8
    • 0020423061 scopus 로고
    • Polypeptide patterns of hepatic microsomes from long-evans rats treated with different xenobiotics
    • Vlasuk, G. P., Ryan, D. E., Thomas, P. E., Levin, W., Walz, F. G., Polypeptide patterns of hepatic microsomes from long-evans rats treated with different xenobiotics. Biochemistry 1982, 21, 6288-6292.
    • (1982) Biochemistry , vol.21 , pp. 6288-6292
    • Vlasuk, G.P.1    Ryan, D.E.2    Thomas, P.E.3    Levin, W.4    Walz, F.G.5
  • 9
    • 0028231844 scopus 로고
    • Induction of enoyl-coa hydratase by Ld(50) exposure to perfluorocarboxylic acids detected by 2-dimensional electrophoresis
    • Witzmann, F. A., Parker, D. N., Jarnot, B. M., Induction of enoyl-coa hydratase by Ld(50) exposure to perfluorocarboxylic acids detected by 2-dimensional electrophoresis. Toxicol. Lett. 1994, 71, 271-277.
    • (1994) Toxicol. Lett. , vol.71 , pp. 271-277
    • Witzmann, F.A.1    Parker, D.N.2    Jarnot, B.M.3
  • 10
    • 0030019866 scopus 로고    scopus 로고
    • Cyclosporine A decreases the protein level of the calcium-binding protein calbindin-D 28kDa in rat kidney
    • Steiner, S., Aicher, L., Raymackers, J., Meheus, L. et al., Cyclosporine A decreases the protein level of the calcium-binding protein calbindin-D 28kDa in rat kidney. Biochem. Pharmacol. 1996, 51, 253-258.
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 253-258
    • Steiner, S.1    Aicher, L.2    Raymackers, J.3    Meheus, L.4
  • 11
    • 0031823995 scopus 로고    scopus 로고
    • New insights into cyclosporine A nephrotoxicity by proteome analysis
    • Aicher, L., Wahl, D., Arce, A., Grenet, O., Steiner, S., New insights into cyclosporine A nephrotoxicity by proteome analysis. Electrophoresis 1998, 19, 1998-2003.
    • (1998) Electrophoresis , vol.19 , pp. 1998-2003
    • Aicher, L.1    Wahl, D.2    Arce, A.3    Grenet, O.4    Steiner, S.5
  • 12
    • 33750591821 scopus 로고    scopus 로고
    • Proteomics as a route to identification of toxicity targets in environmental toxicology
    • Dowling, V. A., Sheehan, D., Proteomics as a route to identification of toxicity targets in environmental toxicology. Proteomics 2006, 6, 5597-5604.
    • (2006) Proteomics , vol.6 , pp. 5597-5604
    • Dowling, V.A.1    Sheehan, D.2
  • 13
    • 0034653417 scopus 로고    scopus 로고
    • Expression profiling in toxicology-potentials and limitations
    • Steiner, S., Anderson, N. L., Expression profiling in toxicology-potentials and limitations. Toxicol. Lett. 2000, 112, 467-471.
    • (2000) Toxicol. Lett. , vol.112 , pp. 467-471
    • Steiner, S.1    Anderson, N.L.2
  • 14
    • 0035124707 scopus 로고    scopus 로고
    • Analysis of genetic and epigenetic mechanisms of toxicity: potential roles of toxicogenomics and proteomics in toxicology
    • Burchiel, S. W., Knall, C. M., Davis, J. W., Paules, R. S. et al., Analysis of genetic and epigenetic mechanisms of toxicity: potential roles of toxicogenomics and proteomics in toxicology. Toxicol. Sci. 2001, 59, 193-195.
    • (2001) Toxicol. Sci. , vol.59 , pp. 193-195
    • Burchiel, S.W.1    Knall, C.M.2    Davis, J.W.3    Paules, R.S.4
  • 15
    • 0035819883 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis: a powerful method to elucidate cellular responses to toxic compounds
    • Moller, A., Soldan, M., Volker, U., Maser, E., Two-dimensional gel electrophoresis: a powerful method to elucidate cellular responses to toxic compounds. Toxicology 2001, 160, 129-138.
    • (2001) Toxicology , vol.160 , pp. 129-138
    • Moller, A.1    Soldan, M.2    Volker, U.3    Maser, E.4
  • 16
    • 1842766389 scopus 로고    scopus 로고
    • Application of proteomic technologies in the drug development process
    • Walgren, J. L., Thompson, D. C., Application of proteomic technologies in the drug development process. Toxicol. Lett. 2004, 149, 377-385.
    • (2004) Toxicol. Lett. , vol.149 , pp. 377-385
    • Walgren, J.L.1    Thompson, D.C.2
  • 17
    • 8544277251 scopus 로고    scopus 로고
    • Toxicoproteomics: proteomics applied to toxicology and pathology
    • Wetmore, B. A., Merrick, B. A., Toxicoproteomics: proteomics applied to toxicology and pathology. Toxicol. Pathol. 2004, 32, 619-642.
    • (2004) Toxicol. Pathol. , vol.32 , pp. 619-642
    • Wetmore, B.A.1    Merrick, B.A.2
  • 19
    • 63249128015 scopus 로고    scopus 로고
    • The role of toxicoproteomics in assessing organ specific toxicity
    • Merrick, B. A., Witzmann, F. A., The role of toxicoproteomics in assessing organ specific toxicity. EXS 2009, 99, 367-400.
    • (2009) EXS , vol.99 , pp. 367-400
    • Merrick, B.A.1    Witzmann, F.A.2
  • 22
    • 77952552373 scopus 로고    scopus 로고
    • The discovery and development of proteomic safety biomarkers for the detection of drug-induced liver toxicity
    • Amacher, D. E., The discovery and development of proteomic safety biomarkers for the detection of drug-induced liver toxicity. Toxicol. Appl. Pharmacol. 2010, 245, 134-142.
    • (2010) Toxicol. Appl. Pharmacol. , vol.245 , pp. 134-142
    • Amacher, D.E.1
  • 23
    • 79551480069 scopus 로고    scopus 로고
    • Protein expression profiling in chemical carcinogenesis: a proteomic-based approach
    • Schmitz-Spanke, S., Rettenmeier, A. W., Protein expression profiling in chemical carcinogenesis: a proteomic-based approach. Proteomics 2011, 11, 644-656.
    • (2011) Proteomics , vol.11 , pp. 644-656
    • Schmitz-Spanke, S.1    Rettenmeier, A.W.2
  • 24
    • 79960983894 scopus 로고    scopus 로고
    • Drug target deconvolution by chemical proteomics
    • Raida, M., Drug target deconvolution by chemical proteomics. Curr. Opin. Chem. Biol. 2011, 15, 570-575.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 570-575
    • Raida, M.1
  • 25
    • 81055157545 scopus 로고    scopus 로고
    • Pesticides and cancer: insights into toxicoproteomic-based findings
    • George, J., Shukla, Y., Pesticides and cancer: insights into toxicoproteomic-based findings. J. Proteomics 2011, 74, 2713-2722.
    • (2011) J. Proteomics , vol.74 , pp. 2713-2722
    • George, J.1    Shukla, Y.2
  • 27
    • 84872745833 scopus 로고    scopus 로고
    • The emerging field of chemo- and pharmacoproteomics
    • Hess, S., The emerging field of chemo- and pharmacoproteomics. Proteomics Clin. Appl. 2013, 7, 171-180.
    • (2013) Proteomics Clin. Appl. , vol.7 , pp. 171-180
    • Hess, S.1
  • 28
    • 84862844613 scopus 로고    scopus 로고
    • Review on proteomic analyses of benzo[a]pyrene toxicity
    • Verma, N., Pink, M., Rettenmeier, A. W., Schmitz-Spanke, S., Review on proteomic analyses of benzo[a]pyrene toxicity. Proteomics 2012, 12, 1731-1755.
    • (2012) Proteomics , vol.12 , pp. 1731-1755
    • Verma, N.1    Pink, M.2    Rettenmeier, A.W.3    Schmitz-Spanke, S.4
  • 29
    • 0037192320 scopus 로고    scopus 로고
    • Toxicology and genetic toxicology in the new era of "toxicogenomics": impact of "-omics" technologies
    • Aardema, M. J., MacGregor, J. T., Toxicology and genetic toxicology in the new era of "toxicogenomics": impact of "-omics" technologies. Mutat. Res. 2002, 499, 13-25.
    • (2002) Mutat. Res. , vol.499 , pp. 13-25
    • Aardema, M.J.1    MacGregor, J.T.2
  • 30
    • 24644475376 scopus 로고    scopus 로고
    • Complementary gene and protein expression studies and integrative approaches in toxicogenomics
    • Merrick, B. A., Madenspacher, J. H., Complementary gene and protein expression studies and integrative approaches in toxicogenomics. Toxicol. Appl. Pharmacol. 2005, 207, 189-194.
    • (2005) Toxicol. Appl. Pharmacol. , vol.207 , pp. 189-194
    • Merrick, B.A.1    Madenspacher, J.H.2
  • 31
    • 56749122303 scopus 로고    scopus 로고
    • Systems biology and functional genomics approaches for the identification of cellular responses to drug toxicity
    • Harrill, A. H., Rusyn, I., Systems biology and functional genomics approaches for the identification of cellular responses to drug toxicity. Expert Opin. Drug Metab. Toxicol. 2008, 4, 1379-1389.
    • (2008) Expert Opin. Drug Metab. Toxicol. , vol.4 , pp. 1379-1389
    • Harrill, A.H.1    Rusyn, I.2
  • 32
    • 0032522873 scopus 로고    scopus 로고
    • Incidence of adverse drug reactions in hospitalized patients: a meta-analysis of prospective studies
    • Lazarou, J., Pomeranz, B. H., Corey, P. N., Incidence of adverse drug reactions in hospitalized patients: a meta-analysis of prospective studies. J. Am. Med. Assoc. 1998, 279, 1200-1205.
    • (1998) J. Am. Med. Assoc. , vol.279 , pp. 1200-1205
    • Lazarou, J.1    Pomeranz, B.H.2    Corey, P.N.3
  • 33
    • 0033920278 scopus 로고    scopus 로고
    • Two-dimensional database of mouse liver proteins: changes in hepatic protein levels following treatment with acetaminophen or its nontoxic regioisomer 3-acetamidophenol
    • Fountoulakis, M., Berndt, P., Boelsterli, U. A., Crameri, F. et al., Two-dimensional database of mouse liver proteins: changes in hepatic protein levels following treatment with acetaminophen or its nontoxic regioisomer 3-acetamidophenol. Electrophoresis 2000, 21, 2148-2161.
    • (2000) Electrophoresis , vol.21 , pp. 2148-2161
    • Fountoulakis, M.1    Berndt, P.2    Boelsterli, U.A.3    Crameri, F.4
  • 34
    • 61349141840 scopus 로고    scopus 로고
    • 9-Aminoacridine-based anticancer drugs target the PI3K/AKT/mTOR, NF-kappa B and p53 pathways
    • Guo, C., Gasparian, A. V., Zhuang, Z., Bosykh, D. A. et al., 9-Aminoacridine-based anticancer drugs target the PI3K/AKT/mTOR, NF-kappa B and p53 pathways. Oncogene 2009, 28, 1151-1161.
    • (2009) Oncogene , vol.28 , pp. 1151-1161
    • Guo, C.1    Gasparian, A.V.2    Zhuang, Z.3    Bosykh, D.A.4
  • 35
    • 84867333345 scopus 로고    scopus 로고
    • Cell type-dependent effects of andrographolide on human cancer cell lines
    • Cheung, M. T. W., Ramalingam, R., Lau, K. K. K., Chiang, M. W. L. et al., Cell type-dependent effects of andrographolide on human cancer cell lines. Life Sci. 2012, 91, 751-760.
    • (2012) Life Sci. , vol.91 , pp. 751-760
    • Cheung, M.T.W.1    Ramalingam, R.2    Lau, K.K.K.3    Chiang, M.W.L.4
  • 36
    • 84898827374 scopus 로고    scopus 로고
    • Proteomic analysis of A2780/S ovarian cancer cell response to the cytotoxic organogold(III) compound Aubipy
    • Gamberi, T., Massai, L., Magherini, F., Landini, I. et al., Proteomic analysis of A2780/S ovarian cancer cell response to the cytotoxic organogold(III) compound Aubipy. J. Proteomics 2014, 103, 103-120.
    • (2014) J. Proteomics , vol.103 , pp. 103-120
    • Gamberi, T.1    Massai, L.2    Magherini, F.3    Landini, I.4
  • 37
    • 0346458828 scopus 로고    scopus 로고
    • Proteomic analysis of pancreatic ductal carcinoma cells treated with 5-aza-2 '-deoxycytidine
    • Cecconi, D., Astner, H., Donadelli, M., Palmieri, M. et al., Proteomic analysis of pancreatic ductal carcinoma cells treated with 5-aza-2 '-deoxycytidine. Electrophoresis 2003, 24, 4291-4303.
    • (2003) Electrophoresis , vol.24 , pp. 4291-4303
    • Cecconi, D.1    Astner, H.2    Donadelli, M.3    Palmieri, M.4
  • 38
    • 84878814234 scopus 로고    scopus 로고
    • Azacytidine induces necrosis of multiple myeloma cells through oxidative stress
    • Tian, E. B., Tang, H. P., Xu, R. H., Liu, C. D. et al., Azacytidine induces necrosis of multiple myeloma cells through oxidative stress. Proteome Sci. 2013, 11, 24. doi:10.1186/1477-5956-11-24.
    • (2013) Proteome Sci. , vol.11 , pp. 24
    • Tian, E.B.1    Tang, H.P.2    Xu, R.H.3    Liu, C.D.4
  • 39
    • 84872375658 scopus 로고    scopus 로고
    • Quantitative proteomic analysis to decipher the differential apoptotic response of bortezomib-treated APL cells before and after retinoic acid differentiation reveals involvement of protein toxicity mechanisms
    • Uttenweiler-Joseph, S., Bouyssie, D., Calligaris, D., Lutz, P. G. et al., Quantitative proteomic analysis to decipher the differential apoptotic response of bortezomib-treated APL cells before and after retinoic acid differentiation reveals involvement of protein toxicity mechanisms. Proteomics 2013, 13, 37-47.
    • (2013) Proteomics , vol.13 , pp. 37-47
    • Uttenweiler-Joseph, S.1    Bouyssie, D.2    Calligaris, D.3    Lutz, P.G.4
  • 40
    • 79957561774 scopus 로고    scopus 로고
    • Quantitative proteomic and interaction network analysis of cisplatin resistance in HeLa cells
    • Chavez, J. D., Hoopmann, M. R., Weisbrod, C. R., Takara, K., Bruce, J. E., Quantitative proteomic and interaction network analysis of cisplatin resistance in HeLa cells. PLoS One 2011, 6, e19892.
    • (2011) PLoS One , vol.6 , pp. e19892
    • Chavez, J.D.1    Hoopmann, M.R.2    Weisbrod, C.R.3    Takara, K.4    Bruce, J.E.5
  • 41
    • 84862951708 scopus 로고    scopus 로고
    • In-depth identification of pathways related to cisplatin-induced hepatotoxicity through an integrative method based on an informatics-assisted label-free protein quantitation and microarray gene expression approach
    • M11010884
    • Cho, Y. E., Singh, T. S. K., Lee, H. C., Moon, P. G. et al., In-depth identification of pathways related to cisplatin-induced hepatotoxicity through an integrative method based on an informatics-assisted label-free protein quantitation and microarray gene expression approach. Mol. Cell. Proteomics 2012, 11, M11.010884.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Cho, Y.E.1    Singh, T.S.K.2    Lee, H.C.3    Moon, P.G.4
  • 42
    • 84866125839 scopus 로고    scopus 로고
    • Mitochondrial proteomic analysis of cisplatin resistance in ovarian cancer
    • Chappell, N. P., Teng, P. N., Hood, B. L., Wang, G. et al., Mitochondrial proteomic analysis of cisplatin resistance in ovarian cancer. J. Proteome Res. 2012, 11, 4605-4614.
    • (2012) J. Proteome Res. , vol.11 , pp. 4605-4614
    • Chappell, N.P.1    Teng, P.N.2    Hood, B.L.3    Wang, G.4
  • 43
    • 82355181112 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of cyclosporine-induced toxicity in a human kidney cell line and comparison with tacrolimus
    • Lamoureux, F., Mestre, E., Essig, M., Sauvage, F. L. et al., Quantitative proteomic analysis of cyclosporine-induced toxicity in a human kidney cell line and comparison with tacrolimus. J. Proteomics 2011, 75, 677-694.
    • (2011) J. Proteomics , vol.75 , pp. 677-694
    • Lamoureux, F.1    Mestre, E.2    Essig, M.3    Sauvage, F.L.4
  • 44
    • 84864081270 scopus 로고    scopus 로고
    • Cardiac phosphoproteome reveals cell signaling events involved in doxorubicin cardiotoxicity
    • Gratia, S., Kay, L., Michelland, S., Seve, M. et al., Cardiac phosphoproteome reveals cell signaling events involved in doxorubicin cardiotoxicity. J. Proteomics 2012, 75, 4705-4716.
    • (2012) J. Proteomics , vol.75 , pp. 4705-4716
    • Gratia, S.1    Kay, L.2    Michelland, S.3    Seve, M.4
  • 45
    • 79959990528 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of dexamethasone-induced effects on osteoblast differentiation, proliferation, and apoptosis in MC3T3-E1 cells using SILAC
    • Hong, D., Chen, H. X., Yu, H. Q., Wang, C. et al., Quantitative proteomic analysis of dexamethasone-induced effects on osteoblast differentiation, proliferation, and apoptosis in MC3T3-E1 cells using SILAC. Osteoporosis Int. 2011, 22, 2175-2186.
    • (2011) Osteoporosis Int. , vol.22 , pp. 2175-2186
    • Hong, D.1    Chen, H.X.2    Yu, H.Q.3    Wang, C.4
  • 46
    • 45249097366 scopus 로고    scopus 로고
    • Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine
    • Dukes, A. A., Van Laar, V. S., Cascio, M., Hastings, T. G., Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine. J. Neurochem. 2008, 106, 333-346.
    • (2008) J. Neurochem. , vol.106 , pp. 333-346
    • Dukes, A.A.1    Van Laar, V.S.2    Cascio, M.3    Hastings, T.G.4
  • 48
    • 33846599777 scopus 로고    scopus 로고
    • Proteomic analysis of rat cortical neurons after fluoxetine treatment
    • Cecconi, D., Mion, S., Astner, H., Domenici, E. et al., Proteomic analysis of rat cortical neurons after fluoxetine treatment. Brain Res. 2007, 1135, 41-51.
    • (2007) Brain Res. , vol.1135 , pp. 41-51
    • Cecconi, D.1    Mion, S.2    Astner, H.3    Domenici, E.4
  • 49
    • 34347228727 scopus 로고    scopus 로고
    • Correlation between protein accumulation profiles and conventional toxicological findings using a model antiandrogenic compound, flutamide
    • Friry-Santini, C., Rouquie, D., Kennel, P., Tinwell, H. et al., Correlation between protein accumulation profiles and conventional toxicological findings using a model antiandrogenic compound, flutamide. Toxicol. Sci. 2007, 97, 81-93.
    • (2007) Toxicol. Sci. , vol.97 , pp. 81-93
    • Friry-Santini, C.1    Rouquie, D.2    Kennel, P.3    Tinwell, H.4
  • 50
    • 0035977914 scopus 로고    scopus 로고
    • Cholesterol biosynthesis regulation and protein changes in rat liver following treatment with fluvastatin
    • Steiner, S., Gatlin, C. L., Lennon, J. J., McGrath, A. M. et al., Cholesterol biosynthesis regulation and protein changes in rat liver following treatment with fluvastatin. Toxicol. Lett. 2001, 120, 369-377.
    • (2001) Toxicol. Lett. , vol.120 , pp. 369-377
    • Steiner, S.1    Gatlin, C.L.2    Lennon, J.J.3    McGrath, A.M.4
  • 51
    • 77950491441 scopus 로고    scopus 로고
    • Shotgun approach based comparative proteomic analysis of levo-tetrahydropalmatine-induced apoptosis in hepatocytes
    • Wang, C., Zhou, J. R., Wang, S. W., Ye, M. L. et al., Shotgun approach based comparative proteomic analysis of levo-tetrahydropalmatine-induced apoptosis in hepatocytes. Toxicol. Lett. 2010, 194, 8-15.
    • (2010) Toxicol. Lett. , vol.194 , pp. 8-15
    • Wang, C.1    Zhou, J.R.2    Wang, S.W.3    Ye, M.L.4
  • 52
    • 0033920189 scopus 로고    scopus 로고
    • Proteomics to display lovastatin-induced protein and pathway regulation in rat liver
    • Steiner, S., Gatlin, C. L., Lennon, J. J., McGrath, A. M. et al., Proteomics to display lovastatin-induced protein and pathway regulation in rat liver. Electrophoresis 2000, 21, 2129-2137.
    • (2000) Electrophoresis , vol.21 , pp. 2129-2137
    • Steiner, S.1    Gatlin, C.L.2    Lennon, J.J.3    McGrath, A.M.4
  • 53
    • 77954086163 scopus 로고    scopus 로고
    • Unexpected common mechanistic pathways for embryotoxicity of warfarin and lovastatin
    • Groebe, K., Hayess, K., Klemm-Manns, M., Schwall, G. et al., Unexpected common mechanistic pathways for embryotoxicity of warfarin and lovastatin. Reprod. Toxicol. 2010, 30, 121-130.
    • (2010) Reprod. Toxicol. , vol.30 , pp. 121-130
    • Groebe, K.1    Hayess, K.2    Klemm-Manns, M.3    Schwall, G.4
  • 54
    • 77951909679 scopus 로고    scopus 로고
    • Proteomic analysis to identify early molecular targets of pregabalin in C6 glial cells
    • Park, S., Lee, J., Proteomic analysis to identify early molecular targets of pregabalin in C6 glial cells. Cell Biol. Int. 2010, 34, 27-33.
    • (2010) Cell Biol. Int. , vol.34 , pp. 27-33
    • Park, S.1    Lee, J.2
  • 55
    • 34249079109 scopus 로고    scopus 로고
    • Proteomic changes of PC12 cells treated with proteasomal inhibitor PSI
    • Zhang, L., Chang, M., Li, H. J., Hou, S. et al., Proteomic changes of PC12 cells treated with proteasomal inhibitor PSI. Brain Res. 2007, 1153, 196-203.
    • (2007) Brain Res. , vol.1153 , pp. 196-203
    • Zhang, L.1    Chang, M.2    Li, H.J.3    Hou, S.4
  • 56
    • 84876315066 scopus 로고    scopus 로고
    • Integrative analysis of proteomic and transcriptomic data for identification of pathways related to simvastatin-induced hepatotoxicity
    • Cho, Y. E., Moon, P. G., Lee, J. E., Singh, T. S. et al., Integrative analysis of proteomic and transcriptomic data for identification of pathways related to simvastatin-induced hepatotoxicity. Proteomics 2013, 13, 1257-1275.
    • (2013) Proteomics , vol.13 , pp. 1257-1275
    • Cho, Y.E.1    Moon, P.G.2    Lee, J.E.3    Singh, T.S.4
  • 57
    • 63049126568 scopus 로고    scopus 로고
    • Differential genomic and proteomic profiling of glioblastoma cells exposed to terpyridineplatinum(II) complexes
    • Koncarevic, S., Urig, S., Steiner, K., Rahlfs, S. et al., Differential genomic and proteomic profiling of glioblastoma cells exposed to terpyridineplatinum(II) complexes. Free Radic. Biol.Med. 2009, 46, 1096-1108.
    • (2009) Free Radic. Biol.Med. , vol.46 , pp. 1096-1108
    • Koncarevic, S.1    Urig, S.2    Steiner, K.3    Rahlfs, S.4
  • 58
    • 84866866554 scopus 로고    scopus 로고
    • Proteome profiling of tolbutamide-treated rat primary hepatocytes using nano LC-MS/MS and label-free protein quantitation
    • Cho, Y. E., Kim, S. H., Baek, M. C., Proteome profiling of tolbutamide-treated rat primary hepatocytes using nano LC-MS/MS and label-free protein quantitation. Electrophoresis 2012, 33, 2806-2817.
    • (2012) Electrophoresis , vol.33 , pp. 2806-2817
    • Cho, Y.E.1    Kim, S.H.2    Baek, M.C.3
  • 59
    • 13644268145 scopus 로고    scopus 로고
    • Chaperone proteins involved in troglitazone-induced toxicity in human hepatoma cell lines
    • Maniratanachote, R., Minami, K., Katoh, M., Nakajima, M., Yokoi, T., Chaperone proteins involved in troglitazone-induced toxicity in human hepatoma cell lines. Toxicol. Sci. 2005, 83, 293-302.
    • (2005) Toxicol. Sci. , vol.83 , pp. 293-302
    • Maniratanachote, R.1    Minami, K.2    Katoh, M.3    Nakajima, M.4    Yokoi, T.5
  • 60
    • 84879329299 scopus 로고    scopus 로고
    • Integrative toxicoproteomics implicates impaired mitochondrial glutathione import as an off-target effect of troglitazone
    • Lee, Y. H., Bin Goh, W. W., Ng, C. K., Raida, M. et al., Integrative toxicoproteomics implicates impaired mitochondrial glutathione import as an off-target effect of troglitazone. J. Proteome Res. 2013, 12, 2933-2945.
    • (2013) J. Proteome Res. , vol.12 , pp. 2933-2945
    • Lee, Y.H.1    Bin Goh, W.W.2    Ng, C.K.3    Raida, M.4
  • 61
    • 74849088209 scopus 로고    scopus 로고
    • Proteomic analysis in NSAIDs-treated primary cardiomyocytes
    • Baek, S. M., Ahn, J. S., Noh, H. S., Park, J. et al., Proteomic analysis in NSAIDs-treated primary cardiomyocytes. J. Proteomics 2010, 73, 721-732.
    • (2010) J. Proteomics , vol.73 , pp. 721-732
    • Baek, S.M.1    Ahn, J.S.2    Noh, H.S.3    Park, J.4
  • 62
    • 79953685509 scopus 로고    scopus 로고
    • Cross-study and cross-omics comparisons of three nephrotoxic compounds reveal mechanistic insights and new candidate biomarkers
    • Matheis, K. A., Com, E., Gautier, J. C., Guerreiro, N. et al., Cross-study and cross-omics comparisons of three nephrotoxic compounds reveal mechanistic insights and new candidate biomarkers. Toxicol. Appl. Pharmacol. 2011, 252, 112-122.
    • (2011) Toxicol. Appl. Pharmacol. , vol.252 , pp. 112-122
    • Matheis, K.A.1    Com, E.2    Gautier, J.C.3    Guerreiro, N.4
  • 63
    • 0036859006 scopus 로고    scopus 로고
    • Protein expression analysis of drug-mediated hepatotoxicity in the Sprague-Dawley rat
    • Man, W. J., White, I. R., Bryant, D., Bugelski, P. et al., Protein expression analysis of drug-mediated hepatotoxicity in the Sprague-Dawley rat. Proteomics 2002, 2, 1577-1585.
    • (2002) Proteomics , vol.2 , pp. 1577-1585
    • Man, W.J.1    White, I.R.2    Bryant, D.3    Bugelski, P.4
  • 64
    • 0142244529 scopus 로고    scopus 로고
    • Toward the identification of liver toxicity markers: a proteome study in human cell culture and rats
    • Thome-Kromer, B., Bonk, I., Klatt, M., Nebrich, G. et al., Toward the identification of liver toxicity markers: a proteome study in human cell culture and rats. Proteomics 2003, 3, 1835-1862.
    • (2003) Proteomics , vol.3 , pp. 1835-1862
    • Thome-Kromer, B.1    Bonk, I.2    Klatt, M.3    Nebrich, G.4
  • 65
    • 79952091052 scopus 로고    scopus 로고
    • Proteomics investigations of drug-induced hepatotoxicity in HepG2 cells
    • Van Summeren, A., Renes, J., Bouwman, F. G., Noben, J. P. et al., Proteomics investigations of drug-induced hepatotoxicity in HepG2 cells. Toxicol. Sci. 2011, 120, 109-122.
    • (2011) Toxicol. Sci. , vol.120 , pp. 109-122
    • Van Summeren, A.1    Renes, J.2    Bouwman, F.G.3    Noben, J.P.4
  • 66
    • 84890505890 scopus 로고    scopus 로고
    • Quercetin-induced cardioprotection against doxorubicin cytotoxicity
    • Chen, J. Y., Hu, R. Y., Chou, H. C., Quercetin-induced cardioprotection against doxorubicin cytotoxicity. J. Biomed. Sci. 2013, 20, 95. doi:10.1186/1423-0127-20-95.
    • (2013) J. Biomed. Sci. , vol.20 , pp. 95
    • Chen, J.Y.1    Hu, R.Y.2    Chou, H.C.3
  • 67
    • 84878322096 scopus 로고    scopus 로고
    • Proteomic profiling reveals that resveratrol inhibits HSP27 expression and sensitizes breast cancer cells to doxorubicin therapy
    • Diaz-Chavez, J., Fonseca-Sanchez, M. A., Arechaga-Ocampo, E., Flores-Perez, A. et al., Proteomic profiling reveals that resveratrol inhibits HSP27 expression and sensitizes breast cancer cells to doxorubicin therapy. PLoS One 2013, 8, e64378.
    • (2013) PLoS One , vol.8 , pp. e64378
    • Diaz-Chavez, J.1    Fonseca-Sanchez, M.A.2    Arechaga-Ocampo, E.3    Flores-Perez, A.4
  • 68
    • 84855870106 scopus 로고    scopus 로고
    • Comparative 2D-DIGE proteomic analysis of ovarian carcinoma cells: toward a reorientation of biosynthesis pathways associated with acquired platinum resistance
    • Lincet, H., Guevel, B., Pineau, C., Allouche, S. et al., Comparative 2D-DIGE proteomic analysis of ovarian carcinoma cells: toward a reorientation of biosynthesis pathways associated with acquired platinum resistance. J. Proteomics 2012, 75, 1157-1169.
    • (2012) J. Proteomics , vol.75 , pp. 1157-1169
    • Lincet, H.1    Guevel, B.2    Pineau, C.3    Allouche, S.4
  • 69
    • 53149138610 scopus 로고    scopus 로고
    • Proteomic investigation of taxol and taxotere resistance and invasiveness in a squamous lung carcinoma cell line
    • Murphy, L., Henry, M., Meleady, P., Clynes, M., Keenan, J., Proteomic investigation of taxol and taxotere resistance and invasiveness in a squamous lung carcinoma cell line. Biochim. Biophys. Acta 2008, 1784, 1184-1191.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1184-1191
    • Murphy, L.1    Henry, M.2    Meleady, P.3    Clynes, M.4    Keenan, J.5
  • 70
    • 14644412367 scopus 로고    scopus 로고
    • A proteomic investigation into etoposide chemo-resistance of neuroblastoma cell lines
    • Urbani, A., Poland, J., Bernardini, S., Bellincampi, L. et al., A proteomic investigation into etoposide chemo-resistance of neuroblastoma cell lines. Proteomics 2005, 5, 796-804.
    • (2005) Proteomics , vol.5 , pp. 796-804
    • Urbani, A.1    Poland, J.2    Bernardini, S.3    Bellincampi, L.4
  • 71
    • 33748446959 scopus 로고    scopus 로고
    • Overexpression of sorcin in multidrug resistant human leukemia cells and its role in regulating cell apoptosis
    • Qi, J., Liu, N., Zhou, Y., Tan, Y. H. et al., Overexpression of sorcin in multidrug resistant human leukemia cells and its role in regulating cell apoptosis. Biochem. Biophys. Res. Commun. 2006, 349, 303-309.
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 303-309
    • Qi, J.1    Liu, N.2    Zhou, Y.3    Tan, Y.H.4
  • 72
    • 58149178732 scopus 로고    scopus 로고
    • A proteomic approach to paclitaxel chemoresistance in ovarian cancer cell lines
    • Di Michele, M., Della Corte, A., Cicchillitti, L., Del Boccio, P. et al., A proteomic approach to paclitaxel chemoresistance in ovarian cancer cell lines. Biochim. Biophys. Acta 2009, 1794, 225-236.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 225-236
    • Di Michele, M.1    Della Corte, A.2    Cicchillitti, L.3    Del Boccio, P.4
  • 73
    • 79953682796 scopus 로고    scopus 로고
    • A proteomic investigation into adriamycin chemo-resistance of human leukemia K562 cells
    • Peng, X. C., Gong, F. M., Xie, G., Zhao, Y. W. et al., A proteomic investigation into adriamycin chemo-resistance of human leukemia K562 cells. Mol. Cell. Biochem. 2011, 351, 233-241.
    • (2011) Mol. Cell. Biochem. , vol.351 , pp. 233-241
    • Peng, X.C.1    Gong, F.M.2    Xie, G.3    Zhao, Y.W.4
  • 74
    • 4444234110 scopus 로고    scopus 로고
    • Investigation of doxorubicin resistance in MCF-7 breast cancer cells using shot-gun comparative proteomics with proteolytic O-18 labeling
    • Brown, K. J., Fenselau, C., Investigation of doxorubicin resistance in MCF-7 breast cancer cells using shot-gun comparative proteomics with proteolytic O-18 labeling. J. Proteome Res. 2004, 3, 455-462.
    • (2004) J. Proteome Res. , vol.3 , pp. 455-462
    • Brown, K.J.1    Fenselau, C.2
  • 75
    • 0242695141 scopus 로고    scopus 로고
    • Study of the development of chemoresistance in melanoma cell lines using proteome analysis
    • Sinha, P., Poland, J., Kohl, S., Schnolzer, M. et al., Study of the development of chemoresistance in melanoma cell lines using proteome analysis. Electrophoresis 2003, 24, 2386-2404.
    • (2003) Electrophoresis , vol.24 , pp. 2386-2404
    • Sinha, P.1    Poland, J.2    Kohl, S.3    Schnolzer, M.4
  • 76
    • 5644294264 scopus 로고    scopus 로고
    • A proteomic approach to cisplatin resistance in the cervix squamous cell carcinoma cell line A431
    • Castagna, A., Antonioli, P., Astner, H., Hamdan, M. et al., A proteomic approach to cisplatin resistance in the cervix squamous cell carcinoma cell line A431. Proteomics 2004, 4, 3246-3267.
    • (2004) Proteomics , vol.4 , pp. 3246-3267
    • Castagna, A.1    Antonioli, P.2    Astner, H.3    Hamdan, M.4
  • 77
    • 0035489609 scopus 로고    scopus 로고
    • Proteomics for studying cancer cells and the development of chemoresistance
    • Hutter, G., Sinha, P., Proteomics for studying cancer cells and the development of chemoresistance. Proteomics 2001, 1, 1233-1248.
    • (2001) Proteomics , vol.1 , pp. 1233-1248
    • Hutter, G.1    Sinha, P.2
  • 78
    • 0345516042 scopus 로고    scopus 로고
    • Increased expression of annexin I and thioredoxin detected by two-dimensional gel electrophoresis of drug resistant human stomach cancer cells
    • Sinha, P., Hutter, G., Kottgen, E., Dietel, M. et al., Increased expression of annexin I and thioredoxin detected by two-dimensional gel electrophoresis of drug resistant human stomach cancer cells. J. Biochem. Biophys. Methods 1998, 37, 105-116.
    • (1998) J. Biochem. Biophys. Methods , vol.37 , pp. 105-116
    • Sinha, P.1    Hutter, G.2    Kottgen, E.3    Dietel, M.4
  • 79
    • 0344131934 scopus 로고    scopus 로고
    • Increased expression of epidermal fatty acid binding protein, cofilin, and 14-3-3-sigma (stratifin) detected by two-dimensional gel electrophoresis, mass spectrometry and microsequencing of drug-resistant human adenocarcinoma of the pancreas
    • Sinha, P., Hutter, G., Kottgen, E., Dietel, M. et al., Increased expression of epidermal fatty acid binding protein, cofilin, and 14-3-3-sigma (stratifin) detected by two-dimensional gel electrophoresis, mass spectrometry and microsequencing of drug-resistant human adenocarcinoma of the pancreas. Electrophoresis 1999, 20, 2952-2960.
    • (1999) Electrophoresis , vol.20 , pp. 2952-2960
    • Sinha, P.1    Hutter, G.2    Kottgen, E.3    Dietel, M.4
  • 80
    • 63649141239 scopus 로고    scopus 로고
    • Proteomic response of human neuroblastoma cells to azaspiracid-1
    • Kellmann, R., Schaffner, C. A. M., Gronset, T. A., Satake, M. et al., Proteomic response of human neuroblastoma cells to azaspiracid-1. J. Proteomics 2009, 72, 695-707.
    • (2009) J. Proteomics , vol.72 , pp. 695-707
    • Kellmann, R.1    Schaffner, C.A.M.2    Gronset, T.A.3    Satake, M.4
  • 81
    • 77951675685 scopus 로고    scopus 로고
    • A proteomic approach to the bilirubin-induced toxicity in neuronal cells reveals a protective function of DJ-1 protein
    • Deganuto, M., Cesaratto, L., Bellarosa, C., Calligaris, R. et al., A proteomic approach to the bilirubin-induced toxicity in neuronal cells reveals a protective function of DJ-1 protein. Proteomics 2010, 10, 1645-1657.
    • (2010) Proteomics , vol.10 , pp. 1645-1657
    • Deganuto, M.1    Cesaratto, L.2    Bellarosa, C.3    Calligaris, R.4
  • 82
    • 79953687423 scopus 로고    scopus 로고
    • Butyrate-induced apoptosis in HCT116 colorectal cancer cells includes induction of a cell stress response
    • Fung, K. Y. C., Brierley, G. V., Henderson, S., Hoffmann, P. et al., Butyrate-induced apoptosis in HCT116 colorectal cancer cells includes induction of a cell stress response. J. Proteome Res. 2011, 10, 1860-1869.
    • (2011) J. Proteome Res. , vol.10 , pp. 1860-1869
    • Fung, K.Y.C.1    Brierley, G.V.2    Henderson, S.3    Hoffmann, P.4
  • 83
    • 84881045284 scopus 로고    scopus 로고
    • ER stress-mediated apoptosis induced by celastrol in cancer cells and important role of glycogen synthase kinase-3 beta in the signal network
    • Feng, L., Zhang, D., Fan, C., Ma, C. et al., ER stress-mediated apoptosis induced by celastrol in cancer cells and important role of glycogen synthase kinase-3 beta in the signal network. Cell Death Dis. 2013, 4, e715.
    • (2013) Cell Death Dis. , vol.4 , pp. e715
    • Feng, L.1    Zhang, D.2    Fan, C.3    Ma, C.4
  • 84
    • 80055034613 scopus 로고    scopus 로고
    • Quantitative proteomics reveals cellular targets of celastrol
    • Hansen, J., Palmfeldt, J., Vang, S., Corydon, T. J. et al., Quantitative proteomics reveals cellular targets of celastrol. Plos One 2011, 6, e26634.
    • (2011) Plos One , vol.6 , pp. e26634
    • Hansen, J.1    Palmfeldt, J.2    Vang, S.3    Corydon, T.J.4
  • 85
    • 79955750184 scopus 로고    scopus 로고
    • Proteomic analysis of the effects of the immunomodulatory mycotoxin deoxynivalenol
    • Nogueira da Costa, A., Mijal, R. S., Keen, J. N., Findlay, J. B., Wild, C. P., Proteomic analysis of the effects of the immunomodulatory mycotoxin deoxynivalenol. Proteomics 2011, 11, 1903-1914.
    • (2011) Proteomics , vol.11 , pp. 1903-1914
    • Nogueira da Costa, A.1    Mijal, R.S.2    Keen, J.N.3    Findlay, J.B.4    Wild, C.P.5
  • 86
    • 54049149896 scopus 로고    scopus 로고
    • Comparative proteomics analysis reveals role of heat shock protein 60 in digoxin-induced toxicity in human endothelial cells
    • Qiu, J., Gao, H. Q., Liang, Y., Yu, H., Zhou, R. H., Comparative proteomics analysis reveals role of heat shock protein 60 in digoxin-induced toxicity in human endothelial cells. Biochim. Biophys. Acta 2008, 1784, 1857-1864.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1857-1864
    • Qiu, J.1    Gao, H.Q.2    Liang, Y.3    Yu, H.4    Zhou, R.H.5
  • 87
    • 84864569270 scopus 로고    scopus 로고
    • Proteomic characterization of the possible molecular targets of pyrrolizidine alkaloid isoline-induced hepatotoxicity
    • Wang, Z. Y., Kang, H., Ji, L. L., Yang, Y. Q. et al., Proteomic characterization of the possible molecular targets of pyrrolizidine alkaloid isoline-induced hepatotoxicity. Environ. Toxicol. Pharmacol. 2012, 34, 608-617.
    • (2012) Environ. Toxicol. Pharmacol. , vol.34 , pp. 608-617
    • Wang, Z.Y.1    Kang, H.2    Ji, L.L.3    Yang, Y.Q.4
  • 88
    • 73849141896 scopus 로고    scopus 로고
    • The cytotoxic pathway triggered by palytoxin involves a change in the cellular pool of stress response proteins
    • Sala, G. L., Bellocci, M., Rossini, G. P., The cytotoxic pathway triggered by palytoxin involves a change in the cellular pool of stress response proteins. Chem. Res. Toxicol. 2009, 22, 2009-2016.
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 2009-2016
    • Sala, G.L.1    Bellocci, M.2    Rossini, G.P.3
  • 89
    • 77956778648 scopus 로고    scopus 로고
    • Toxicoproteomic analysis of phalloidin-induced cholestasis in mouse liver
    • Heo, S. H., Oh, J. H., Park, H. J., Kwon, M. S. et al., Toxicoproteomic analysis of phalloidin-induced cholestasis in mouse liver. Mol. Cell. Toxicol. 2010, 6, 87-95.
    • (2010) Mol. Cell. Toxicol. , vol.6 , pp. 87-95
    • Heo, S.H.1    Oh, J.H.2    Park, H.J.3    Kwon, M.S.4
  • 90
    • 49749104260 scopus 로고    scopus 로고
    • Proteomic and transcriptomic study on the action of a cytotoxic saponin (Polyphyllin D): induction of endoplasmic reticulum stress and mitochondria-mediated apoptotic pathways
    • Siu, F. M., Ma, D. L., Cheung, Y. W., Lok, C. N. et al., Proteomic and transcriptomic study on the action of a cytotoxic saponin (Polyphyllin D): induction of endoplasmic reticulum stress and mitochondria-mediated apoptotic pathways. Proteomics 2008, 8, 3105-3117.
    • (2008) Proteomics , vol.8 , pp. 3105-3117
    • Siu, F.M.1    Ma, D.L.2    Cheung, Y.W.3    Lok, C.N.4
  • 91
    • 80051634012 scopus 로고    scopus 로고
    • Resveratrol suppresses human colon cancer cell proliferation and induces apoptosis via targeting the pentose phosphate and the talin-FAK signaling pathways-a proteomic approach
    • Vanamala, J., Radhakrishnan, S., Reddivari, L., Bhat, V. B., Ptitsyn, A., Resveratrol suppresses human colon cancer cell proliferation and induces apoptosis via targeting the pentose phosphate and the talin-FAK signaling pathways-a proteomic approach. Proteome Sci. 2011, 9, 49. doi:10.1186/1477-5956-9-49.
    • (2011) Proteome Sci. , vol.9 , pp. 49
    • Vanamala, J.1    Radhakrishnan, S.2    Reddivari, L.3    Bhat, V.B.4    Ptitsyn, A.5
  • 92
    • 34748902479 scopus 로고    scopus 로고
    • Apoptosis induced by staurosporine alters chaperone and endoplasmic reticulum proteins: identification by quantitative proteornics
    • Short, D. M., Heron, I. D., Birse-Archbold, J. L. A., Kerr, L. E. et al., Apoptosis induced by staurosporine alters chaperone and endoplasmic reticulum proteins: identification by quantitative proteornics. Proteomics 2007, 7, 3085-3096.
    • (2007) Proteomics , vol.7 , pp. 3085-3096
    • Short, D.M.1    Heron, I.D.2    Birse-Archbold, J.L.A.3    Kerr, L.E.4
  • 93
    • 84890298665 scopus 로고    scopus 로고
    • Proteomic analysis reveals tanshinone IIA enhances apoptosis of advanced cervix carcinoma CaSki cells through mitochondria intrinsic and endoplasmic reticulum stress pathways
    • Pan, T. L., Wang, P. W., Hung, Y. C., Huang, C. H., Rau, K. M., Proteomic analysis reveals tanshinone IIA enhances apoptosis of advanced cervix carcinoma CaSki cells through mitochondria intrinsic and endoplasmic reticulum stress pathways. Proteomics 2013, 13, 3411-3423.
    • (2013) Proteomics , vol.13 , pp. 3411-3423
    • Pan, T.L.1    Wang, P.W.2    Hung, Y.C.3    Huang, C.H.4    Rau, K.M.5
  • 94
    • 84870804257 scopus 로고    scopus 로고
    • Proteome-wide study of endoplasmic reticulum stress induced by thapsigargin in N2a neuroblastoma cells
    • Foldi, I., Toth, A. M., Szabo, Z., Mozes, E. et al., Proteome-wide study of endoplasmic reticulum stress induced by thapsigargin in N2a neuroblastoma cells. Neurochem. Int. 2013, 62, 58-69.
    • (2013) Neurochem. Int. , vol.62 , pp. 58-69
    • Foldi, I.1    Toth, A.M.2    Szabo, Z.3    Mozes, E.4
  • 95
    • 65249174521 scopus 로고    scopus 로고
    • Tubeimoside-1 exerts cytotoxicity in HeLa cells through mitochondrial dysfunction and endoplasmic reticulum stress pathways
    • Xu, Y., Chiu, L. F., He, Q. Y., Chen, F., Tubeimoside-1 exerts cytotoxicity in HeLa cells through mitochondrial dysfunction and endoplasmic reticulum stress pathways. J. Proteome Res. 2009, 8, 1585-1593.
    • (2009) J. Proteome Res. , vol.8 , pp. 1585-1593
    • Xu, Y.1    Chiu, L.F.2    He, Q.Y.3    Chen, F.4
  • 96
    • 84864356096 scopus 로고    scopus 로고
    • Proteomic study on usnic-acid-induced hepatotoxicity in rats
    • Liu, Q., Zhao, X. P., Lu, X. Y., Fan, X. H., Wang, Y., Proteomic study on usnic-acid-induced hepatotoxicity in rats. J. Agric. Food Chem. 2012, 60, 7312-7317.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 7312-7317
    • Liu, Q.1    Zhao, X.P.2    Lu, X.Y.3    Fan, X.H.4    Wang, Y.5
  • 97
    • 67649184787 scopus 로고    scopus 로고
    • Generally detected proteins in comparative proteomics-a matter of cellular stress response
    • Wang, P., Bouwman, F. G., Mariman, E. C. M., Generally detected proteins in comparative proteomics-a matter of cellular stress response? Proteomics 2009, 9, 2955-2966.
    • (2009) Proteomics , vol.9 , pp. 2955-2966
    • Wang, P.1    Bouwman, F.G.2    Mariman, E.C.M.3
  • 98
    • 67649814628 scopus 로고    scopus 로고
    • Proteomic profiling of rat lung epithelial cells induced by acrolein
    • Sarkar, P., Hayes, B. E., Proteomic profiling of rat lung epithelial cells induced by acrolein. Life Sci. 2009, 85, 188-195.
    • (2009) Life Sci. , vol.85 , pp. 188-195
    • Sarkar, P.1    Hayes, B.E.2
  • 99
    • 84887044953 scopus 로고    scopus 로고
    • Subtoxic and toxic concentrations of benzene and toluene induce Nrf2-mediated antioxidative stress response and affect the central carbon metabolism in lung epithelial cells A549
    • Murugesan, K., Baumann, S., Wissenbach, D. K., Kliemt, S. et al., Subtoxic and toxic concentrations of benzene and toluene induce Nrf2-mediated antioxidative stress response and affect the central carbon metabolism in lung epithelial cells A549. Proteomics 2013, 13, 3211-3221.
    • (2013) Proteomics , vol.13 , pp. 3211-3221
    • Murugesan, K.1    Baumann, S.2    Wissenbach, D.K.3    Kliemt, S.4
  • 100
    • 8744258677 scopus 로고    scopus 로고
    • Effects of benzo(a)pyrene on protein expression in Jurkat T-cells
    • Oh, S., Im, H., Oh, E., Lee, J. et al., Effects of benzo(a)pyrene on protein expression in Jurkat T-cells. Proteomics 2004, 4, 3514-3526.
    • (2004) Proteomics , vol.4 , pp. 3514-3526
    • Oh, S.1    Im, H.2    Oh, E.3    Lee, J.4
  • 101
    • 84878176386 scopus 로고    scopus 로고
    • Benzo[a]pyrene-mediated toxicity in primary pig bladder epithelial cells: a proteomic approach
    • Verma, N., Pink, M., Rettenmeier, A. W., Schmitz-Spanke, S., Benzo[a]pyrene-mediated toxicity in primary pig bladder epithelial cells: a proteomic approach. J. Proteomics 2013, 85, 53-64.
    • (2013) J. Proteomics , vol.85 , pp. 53-64
    • Verma, N.1    Pink, M.2    Rettenmeier, A.W.3    Schmitz-Spanke, S.4
  • 102
    • 84863548653 scopus 로고    scopus 로고
    • Altered carcinogenesis and proteome in mammary glands of rats after prepubertal exposures to the hormonally active chemicals bisphenol a and genistein
    • Betancourt, A. M., Wang, J., Jenkins, S., Mobley, J. et al., Altered carcinogenesis and proteome in mammary glands of rats after prepubertal exposures to the hormonally active chemicals bisphenol a and genistein. J. Nutr. 2012, 142, 1382S-S1388.
    • (2012) J. Nutr. , vol.142 , pp. 1382S-S1388
    • Betancourt, A.M.1    Wang, J.2    Jenkins, S.3    Mobley, J.4
  • 103
    • 4544317005 scopus 로고    scopus 로고
    • Analysis of differentially regulated proteins in TM4 cells treated with bisphenol A
    • Lee, D. Y., Lee, S. S., Joo, W. A., Lee, E. J., Kim, C. W., Analysis of differentially regulated proteins in TM4 cells treated with bisphenol A. Biosci. Biotechnol.Biochem. 2004, 68, 1201-1208.
    • (2004) Biosci. Biotechnol.Biochem. , vol.68 , pp. 1201-1208
    • Lee, D.Y.1    Lee, S.S.2    Joo, W.A.3    Lee, E.J.4    Kim, C.W.5
  • 104
    • 67349228396 scopus 로고    scopus 로고
    • Early alterations in protein and gene expression in rat kidney following bromate exposure
    • Ahlborn, G. J., Delker, D. A., Roop, B. C., Geter, D. R. et al., Early alterations in protein and gene expression in rat kidney following bromate exposure. Food Chem. Toxicol. 2009, 47, 1154-1160.
    • (2009) Food Chem. Toxicol. , vol.47 , pp. 1154-1160
    • Ahlborn, G.J.1    Delker, D.A.2    Roop, B.C.3    Geter, D.R.4
  • 105
    • 84880099343 scopus 로고    scopus 로고
    • Proteomic-based identification of multiple pathways underlying n-butylidenephthalide-induced apoptosis in LNCaP human prostate cancer cells
    • Pang, C. Y., Chiu, S. C., Harn, H. J., Zhai, W. J. et al., Proteomic-based identification of multiple pathways underlying n-butylidenephthalide-induced apoptosis in LNCaP human prostate cancer cells. Food Chem. Toxicol. 2013, 59, 281-288.
    • (2013) Food Chem. Toxicol. , vol.59 , pp. 281-288
    • Pang, C.Y.1    Chiu, S.C.2    Harn, H.J.3    Zhai, W.J.4
  • 106
    • 0036384164 scopus 로고    scopus 로고
    • Modulation of gene and protein expression by carbon tetrachloride in the rat liver
    • Fountoulakis, M., de Vera, M. C., Crameri, F., Boess, F. et al., Modulation of gene and protein expression by carbon tetrachloride in the rat liver. Toxicol. Appl. Pharmacol. 2002, 183, 71-80.
    • (2002) Toxicol. Appl. Pharmacol. , vol.183 , pp. 71-80
    • Fountoulakis, M.1    de Vera, M.C.2    Crameri, F.3    Boess, F.4
  • 107
    • 79955414547 scopus 로고    scopus 로고
    • Chlorinated benzenes cause concomitantly oxidative stress and induction of apoptotic markers in lung epithelial cells (A549) at nonacute toxic concentrations
    • Morbt, N., Tomm, J., Feltens, R., Mogel, I. et al., Chlorinated benzenes cause concomitantly oxidative stress and induction of apoptotic markers in lung epithelial cells (A549) at nonacute toxic concentrations. J. Proteome Res. 2011, 10, 363-378.
    • (2011) J. Proteome Res. , vol.10 , pp. 363-378
    • Morbt, N.1    Tomm, J.2    Feltens, R.3    Mogel, I.4
  • 108
    • 53149134254 scopus 로고    scopus 로고
    • Proteomic analysis of proteins associated with tt-DDE induced toxicity in BEAS-2B cells
    • Lin, P. P., Yang, M. H., Liao, P. C., Wu, H. Y. et al., Proteomic analysis of proteins associated with tt-DDE induced toxicity in BEAS-2B cells. Biochem. Biophys. Res. Commun. 2008, 376, 519-524.
    • (2008) Biochem. Biophys. Res. Commun. , vol.376 , pp. 519-524
    • Lin, P.P.1    Yang, M.H.2    Liao, P.C.3    Wu, H.Y.4
  • 109
    • 70349233759 scopus 로고    scopus 로고
    • Proteomic analysis of differentiating neuroblastoma cells treated with sub-lethal neurite inhibitory concentrations of diazinon: identification of novel biomarkers of effect
    • Harris, W., Sachana, M., Flaskos, J., Hargreaves, A. J., Proteomic analysis of differentiating neuroblastoma cells treated with sub-lethal neurite inhibitory concentrations of diazinon: identification of novel biomarkers of effect. Toxicol. Appl. Pharmacol. 2009, 240, 159-165.
    • (2009) Toxicol. Appl. Pharmacol. , vol.240 , pp. 159-165
    • Harris, W.1    Sachana, M.2    Flaskos, J.3    Hargreaves, A.J.4
  • 110
    • 84878968685 scopus 로고    scopus 로고
    • Differential expression of peroxiredoxin 6, annexin A5 and ubiquitin carboxyl-terminal hydrolase isozyme L1 in testis of rat fetuses after maternal exposure to di-n-butyl phthalate
    • Shen, H., Liao, K., Zhang, W., Wu, H. et al., Differential expression of peroxiredoxin 6, annexin A5 and ubiquitin carboxyl-terminal hydrolase isozyme L1 in testis of rat fetuses after maternal exposure to di-n-butyl phthalate. Reprod. Toxicol. 2013, 39, 76-84.
    • (2013) Reprod. Toxicol. , vol.39 , pp. 76-84
    • Shen, H.1    Liao, K.2    Zhang, W.3    Wu, H.4
  • 111
    • 34548856483 scopus 로고    scopus 로고
    • Differential expression of peroxiredoxin 6 in fetal rat testis following in utero exposure to di(nbuty1) phthalate
    • Zhang, W., Shen, H., Ma, L., Shen, B. X. et al., Differential expression of peroxiredoxin 6 in fetal rat testis following in utero exposure to di(nbuty1) phthalate. Toxicology 2007, 240, 86-95.
    • (2007) Toxicology , vol.240 , pp. 86-95
    • Zhang, W.1    Shen, H.2    Ma, L.3    Shen, B.X.4
  • 112
    • 77956644515 scopus 로고    scopus 로고
    • Protein thiol oxidation in murine airway epithelial cells in response to naphthalene or diethyl maleate
    • Spiess, P. C., Morin, D., Williams, C. R., Buckpittl, A. R., Protein thiol oxidation in murine airway epithelial cells in response to naphthalene or diethyl maleate. Am. J. Resp. Cell Mol. Biol. 2010, 43, 316-325.
    • (2010) Am. J. Resp. Cell Mol. Biol. , vol.43 , pp. 316-325
    • Spiess, P.C.1    Morin, D.2    Williams, C.R.3    Buckpittl, A.R.4
  • 113
    • 34447638890 scopus 로고    scopus 로고
    • Proteomic investigation of 1,6-dimethoxyhexane testicular toxicity
    • Pelletier, G., Masson, S., Wang, Y. L., Wade, M. G. et al., Proteomic investigation of 1, 6-dimethoxyhexane testicular toxicity. Environ. Toxicol. Pharmacol. 2007, 24, 129-133.
    • (2007) Environ. Toxicol. Pharmacol. , vol.24 , pp. 129-133
    • Pelletier, G.1    Masson, S.2    Wang, Y.L.3    Wade, M.G.4
  • 114
    • 84888154160 scopus 로고    scopus 로고
    • Genomic and proteomic analyses of 1,3-dinitrobenzene-induced testicular toxicity in Sprague-Dawley rats
    • Oh, J. H., Heo, S. H., Park, H. J., Choi, M. S. et al., Genomic and proteomic analyses of 1, 3-dinitrobenzene-induced testicular toxicity in Sprague-Dawley rats. Reprod. Toxicol. 2014, 43, 45-55.
    • (2014) Reprod. Toxicol. , vol.43 , pp. 45-55
    • Oh, J.H.1    Heo, S.H.2    Park, H.J.3    Choi, M.S.4
  • 115
    • 41749097203 scopus 로고    scopus 로고
    • Differential signatures of protein glycosylation and phosphorylation in human Chang liver cells induced by TCDD treatment
    • Kim, J. H., In, Y. J., Kim, W. K., Bae, K. H. et al., Differential signatures of protein glycosylation and phosphorylation in human Chang liver cells induced by TCDD treatment. Toxicol. Lett. 2008, 178, 20-28.
    • (2008) Toxicol. Lett. , vol.178 , pp. 20-28
    • Kim, J.H.1    In, Y.J.2    Kim, W.K.3    Bae, K.H.4
  • 116
    • 33646252021 scopus 로고    scopus 로고
    • Quantitative analysis of 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced proteome alterations in 5L rat hepatoma cells using isotope-coded protein labels
    • Sarioglu, H., Brandner, S., Jacobsen, C., Meindl, T. et al., Quantitative analysis of 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin-induced proteome alterations in 5L rat hepatoma cells using isotope-coded protein labels. Proteomics 2006, 6, 2407-2421.
    • (2006) Proteomics , vol.6 , pp. 2407-2421
    • Sarioglu, H.1    Brandner, S.2    Jacobsen, C.3    Meindl, T.4
  • 117
    • 0035056118 scopus 로고    scopus 로고
    • Proteome analysis of the effects of 2,3,7,8-tetrachlorodibenzo-p-dioxin on murine testicular Leydig and Sertoli cells
    • Uchida, T., Ohashi, Y., Morikawa, E., Tsugita, A., Takeda, K., Proteome analysis of the effects of 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin on murine testicular Leydig and Sertoli cells. J. Health Sci. 2001, 47, 136-144.
    • (2001) J. Health Sci. , vol.47 , pp. 136-144
    • Uchida, T.1    Ohashi, Y.2    Morikawa, E.3    Tsugita, A.4    Takeda, K.5
  • 118
    • 0142024970 scopus 로고    scopus 로고
    • JP-8 jet fuel exposure alters protein expression in the lung
    • Drake, M. G., Witzmann, F. A., Hyde, J., Witten, M. L., JP-8 jet fuel exposure alters protein expression in the lung. Toxicology 2003, 191, 199-210.
    • (2003) Toxicology , vol.191 , pp. 199-210
    • Drake, M.G.1    Witzmann, F.A.2    Hyde, J.3    Witten, M.L.4
  • 119
    • 77249107555 scopus 로고    scopus 로고
    • Studies on glyphosate-induced carcinogenicity in mouse skin: a proteomic approach
    • George, J., Prasad, S., Mahmood, Z., Shukla, Y., Studies on glyphosate-induced carcinogenicity in mouse skin: a proteomic approach. J. Proteomics 2010, 73, 951-964.
    • (2010) J. Proteomics , vol.73 , pp. 951-964
    • George, J.1    Prasad, S.2    Mahmood, Z.3    Shukla, Y.4
  • 120
    • 1542720668 scopus 로고    scopus 로고
    • Mechanisms of hydrazine toxicity in rat liver investigated by proteomics and multivariate data analysis
    • Kleno, T. G., Leonardsen, L. R., Kjeldal, H. O., Laursen, S. M. et al., Mechanisms of hydrazine toxicity in rat liver investigated by proteomics and multivariate data analysis. Proteomics 2004, 4, 868-880.
    • (2004) Proteomics , vol.4 , pp. 868-880
    • Kleno, T.G.1    Leonardsen, L.R.2    Kjeldal, H.O.3    Laursen, S.M.4
  • 121
    • 29144521756 scopus 로고    scopus 로고
    • Expressions of galectin-3, glutathione S-transferase A2 and peroxiredoxin-1 by nonylphenol-incubated Caco-2 cells and reduction in transepithelial electrical resistance by nonylphenol
    • Isoda, H., Talorete, T. P. N., Han, J., Nakamura, K., Expressions of galectin-3, glutathione S-transferase A2 and peroxiredoxin-1 by nonylphenol-incubated Caco-2 cells and reduction in transepithelial electrical resistance by nonylphenol. Toxicol. In Vitro 2006, 20, 63-70.
    • (2006) Toxicol. In Vitro , vol.20 , pp. 63-70
    • Isoda, H.1    Talorete, T.P.N.2    Han, J.3    Nakamura, K.4
  • 122
    • 84886303120 scopus 로고    scopus 로고
    • Perfluorooctanoic acid induces apoptosis through the p53-dependent mitochondrial pathway in human hepatic cells: a proteomic study
    • Huang, Q. Y., Zhang, J., Martin, F. L., Peng, S. Y. et al., Perfluorooctanoic acid induces apoptosis through the p53-dependent mitochondrial pathway in human hepatic cells: a proteomic study. Toxicol. Lett. 2013, 223, 211-220.
    • (2013) Toxicol. Lett. , vol.223 , pp. 211-220
    • Huang, Q.Y.1    Zhang, J.2    Martin, F.L.3    Peng, S.Y.4
  • 123
    • 80855147547 scopus 로고    scopus 로고
    • Aroclor 1254, a developmental neurotoxicant, alters energy metabolism- and intracellular signaling-associated protein networks in rat cerebellum and hippocampus
    • Kodavanti, P. R. S., Osorio, C., Royland, J. E., Ramabhadran, R., Alzate, O., Aroclor 1254, a developmental neurotoxicant, alters energy metabolism- and intracellular signaling-associated protein networks in rat cerebellum and hippocampus. Toxicol. Appl. Pharmacol. 2011, 256, 290-299.
    • (2011) Toxicol. Appl. Pharmacol. , vol.256 , pp. 290-299
    • Kodavanti, P.R.S.1    Osorio, C.2    Royland, J.E.3    Ramabhadran, R.4    Alzate, O.5
  • 124
    • 80052461778 scopus 로고    scopus 로고
    • Cerebellum proteomics addressing the cognitive deficit of rats perinatally exposed to the food-relevant polychlorinated biphenyl 138
    • Campagna, R., Brunelli, L., Airoldi, L., Fanelli, R. et al., Cerebellum proteomics addressing the cognitive deficit of rats perinatally exposed to the food-relevant polychlorinated biphenyl 138. Toxicol. Sci. 2011, 123, 170-179.
    • (2011) Toxicol. Sci. , vol.123 , pp. 170-179
    • Campagna, R.1    Brunelli, L.2    Airoldi, L.3    Fanelli, R.4
  • 125
    • 84859264960 scopus 로고    scopus 로고
    • Insight into the neuroproteomics effects of the food-contaminant non-dioxin like polychlorinated biphenyls
    • Brunelli, L., Llansola, M., Felipo, V., Campagna, R. et al., Insight into the neuroproteomics effects of the food-contaminant non-dioxin like polychlorinated biphenyls. J. Proteomics 2012, 75, 2417-2430.
    • (2012) J. Proteomics , vol.75 , pp. 2417-2430
    • Brunelli, L.1    Llansola, M.2    Felipo, V.3    Campagna, R.4
  • 126
    • 10644250718 scopus 로고    scopus 로고
    • A proteomic analysis of thioacetamide-induced hepatotoxicity and cirrhosis in rat livers
    • Low, T. Y., Leow, C. K., Salto-Tellez, M., Chung, M. C., A proteomic analysis of thioacetamide-induced hepatotoxicity and cirrhosis in rat livers. Proteomics 2004, 4, 3960-3974.
    • (2004) Proteomics , vol.4 , pp. 3960-3974
    • Low, T.Y.1    Leow, C.K.2    Salto-Tellez, M.3    Chung, M.C.4
  • 127
    • 44649118594 scopus 로고    scopus 로고
    • Proteomic analysis of MCF-7 cells treated with benzo[a]pyrene, dibenzo[a,l]pyrene, coal tar extract, and diesel exhaust extract
    • Hooven, L. A., Baird, W. M., Proteomic analysis of MCF-7 cells treated with benzo[a]pyrene, dibenzo[a, l]pyrene, coal tar extract, and diesel exhaust extract. Toxicology 2008, 249, 1-10.
    • (2008) Toxicology , vol.249 , pp. 1-10
    • Hooven, L.A.1    Baird, W.M.2
  • 128
    • 84872686346 scopus 로고    scopus 로고
    • Proteomic profiling of expression of proteasomal subunits from livers of mice treated with diethylnitrosamine
    • Yuan, F. Q., Lu, J., You, P., Yang, Z. M. et al., Proteomic profiling of expression of proteasomal subunits from livers of mice treated with diethylnitrosamine. Proteomics 2013, 13, 389-397.
    • (2013) Proteomics , vol.13 , pp. 389-397
    • Yuan, F.Q.1    Lu, J.2    You, P.3    Yang, Z.M.4
  • 129
    • 34250704249 scopus 로고    scopus 로고
    • Proteomic analysis of alternative protein tyrosine phosphorylation in 1,2-dichlorovinyl-cysteine-induced cytotoxicity in primary cultured rat renal proximal tubular cells
    • de Graauw, M., Le Devedec, S., Tijdens, I., Smeets, M. B. et al., Proteomic analysis of alternative protein tyrosine phosphorylation in 1, 2-dichlorovinyl-cysteine-induced cytotoxicity in primary cultured rat renal proximal tubular cells. J. Pharmacol. Exp. Ther. 2007, 322, 89-100.
    • (2007) J. Pharmacol. Exp. Ther. , vol.322 , pp. 89-100
    • de Graauw, M.1    Le Devedec, S.2    Tijdens, I.3    Smeets, M.B.4
  • 130
    • 79955106392 scopus 로고    scopus 로고
    • Proteomics as a tool for examining the toxicity of heavy metals
    • Luque-Garcia, J. L., Cabezas-Sanchez, P., Camara, C., Proteomics as a tool for examining the toxicity of heavy metals. Trends Anal. Chem. 2011, 30, 703-716.
    • (2011) Trends Anal. Chem. , vol.30 , pp. 703-716
    • Luque-Garcia, J.L.1    Cabezas-Sanchez, P.2    Camara, C.3
  • 131
    • 67049115481 scopus 로고    scopus 로고
    • Proteomic and functional analyses reveal a dual molecular mechanism underlying arsenic-induced apoptosis in human multiple myeloma cells
    • Ge, F., Lu, X. P., Zeng, H. L., He, Q. Y. et al., Proteomic and functional analyses reveal a dual molecular mechanism underlying arsenic-induced apoptosis in human multiple myeloma cells. J. Proteome Res. 2009, 8, 3006-3019.
    • (2009) J. Proteome Res. , vol.8 , pp. 3006-3019
    • Ge, F.1    Lu, X.P.2    Zeng, H.L.3    He, Q.Y.4
  • 132
    • 76149138039 scopus 로고    scopus 로고
    • Quantitative proteomic analysis reveals the perturbation of multiple cellular pathways in HL-60 cells induced by arsenite treatment
    • Xiong, L., Wang, Y., Quantitative proteomic analysis reveals the perturbation of multiple cellular pathways in HL-60 cells induced by arsenite treatment. J. Proteome Res. 2010, 9, 1129-1137.
    • (2010) J. Proteome Res. , vol.9 , pp. 1129-1137
    • Xiong, L.1    Wang, Y.2
  • 133
    • 65349114116 scopus 로고    scopus 로고
    • Proteomic analysis of low dose arsenic and ionizing radiation exposure on keratinocytes
    • Berglund, S. R., Santana, A. R., Li, D., Rice, R. H. et al., Proteomic analysis of low dose arsenic and ionizing radiation exposure on keratinocytes. Proteomics 2009, 9, 1925-1938.
    • (2009) Proteomics , vol.9 , pp. 1925-1938
    • Berglund, S.R.1    Santana, A.R.2    Li, D.3    Rice, R.H.4
  • 134
    • 34247225990 scopus 로고    scopus 로고
    • Down-regulation of glutaminase C in human hepatocarcinoma cell by diphenylarsinic acid, a degradation product of chemical warfare agents
    • Kita, K., Suzuki, T., Ochi, T., Down-regulation of glutaminase C in human hepatocarcinoma cell by diphenylarsinic acid, a degradation product of chemical warfare agents. Toxicol. Appl. Pharmacol. 2007, 220, 262-270.
    • (2007) Toxicol. Appl. Pharmacol. , vol.220 , pp. 262-270
    • Kita, K.1    Suzuki, T.2    Ochi, T.3
  • 135
    • 58149389515 scopus 로고    scopus 로고
    • Proteomic analysis of calcium oxalate monohydrate crystal-induced cytotoxicity in distal renal tubular cells
    • Thongboonkerd, V., Semangoen, T., Sinchaikul, S., Chen, S. T., Proteomic analysis of calcium oxalate monohydrate crystal-induced cytotoxicity in distal renal tubular cells. J. Proteome Res. 2008, 7, 4689-4700.
    • (2008) J. Proteome Res. , vol.7 , pp. 4689-4700
    • Thongboonkerd, V.1    Semangoen, T.2    Sinchaikul, S.3    Chen, S.T.4
  • 136
    • 77955456260 scopus 로고    scopus 로고
    • Proteome changes in human monocytes upon interaction with calcium oxalate monohydrate crystals
    • Singhto, N., Sintiprungrat, K., Sinchaikul, S., Chen, S. T., Thongboonkerd, V., Proteome changes in human monocytes upon interaction with calcium oxalate monohydrate crystals. J. Proteome Res. 2010, 9, 3980-3988.
    • (2010) J. Proteome Res. , vol.9 , pp. 3980-3988
    • Singhto, N.1    Sintiprungrat, K.2    Sinchaikul, S.3    Chen, S.T.4    Thongboonkerd, V.5
  • 137
    • 84881124761 scopus 로고    scopus 로고
    • Alterations in macrophage cellular proteome induced by calcium oxalate crystals: the association of HSP90 and F-actin is important for phagosome formation
    • Singhto, N., Sintiprungrat, K., Thongboonkerd, V., Alterations in macrophage cellular proteome induced by calcium oxalate crystals: the association of HSP90 and F-actin is important for phagosome formation. J. Proteome Res. 2013, 12, 3561-3572.
    • (2013) J. Proteome Res. , vol.12 , pp. 3561-3572
    • Singhto, N.1    Sintiprungrat, K.2    Thongboonkerd, V.3
  • 138
    • 46049115518 scopus 로고    scopus 로고
    • Zinc adaptation and resistance to cadmium toxicity in mammalian cells: molecular insight by proteomic analysis
    • Rousselet, E., Martelli, A., Chevallet, M., Diemer, H. et al., Zinc adaptation and resistance to cadmium toxicity in mammalian cells: molecular insight by proteomic analysis. Proteomics 2008, 8, 2244-2255.
    • (2008) Proteomics , vol.8 , pp. 2244-2255
    • Rousselet, E.1    Martelli, A.2    Chevallet, M.3    Diemer, H.4
  • 139
    • 78650431341 scopus 로고    scopus 로고
    • Genomic and proteomic profiling of the cadmium cytotoxic response in human lung epithelial cells
    • Choi, K. M., Youn, H. S., Lee, M. Y., Genomic and proteomic profiling of the cadmium cytotoxic response in human lung epithelial cells. Mol. Cell. Toxicol. 2009, 5, 198-206.
    • (2009) Mol. Cell. Toxicol. , vol.5 , pp. 198-206
    • Choi, K.M.1    Youn, H.S.2    Lee, M.Y.3
  • 140
    • 79960697168 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase and cAMP are associated with cadmium-mediated Leydig cell damage
    • Zhang, Q. H., Zou, P., Zhan, H. C., Zhang, M. J. et al., Dihydrolipoamide dehydrogenase and cAMP are associated with cadmium-mediated Leydig cell damage. Toxicol. Lett. 2011, 205, 183-189.
    • (2011) Toxicol. Lett. , vol.205 , pp. 183-189
    • Zhang, Q.H.1    Zou, P.2    Zhan, H.C.3    Zhang, M.J.4
  • 141
    • 84863033409 scopus 로고    scopus 로고
    • Functional proteomics reveals hepatotoxicity and the molecular mechanisms of different forms of chromium delivered by skin administration
    • Pan, T. L., Wang, P. W., Chen, C. C., Fang, J. Y., Sintupisut, N., Functional proteomics reveals hepatotoxicity and the molecular mechanisms of different forms of chromium delivered by skin administration. Proteomics 2012, 12, 477-489.
    • (2012) Proteomics , vol.12 , pp. 477-489
    • Pan, T.L.1    Wang, P.W.2    Chen, C.C.3    Fang, J.Y.4    Sintupisut, N.5
  • 142
    • 48249095483 scopus 로고    scopus 로고
    • Proteomic analysis of chromium cytotoxicity in cultured rat lung epithelial cells
    • Lei, T., He, Q. Y., Cai, Z., Zhou, Y. et al., Proteomic analysis of chromium cytotoxicity in cultured rat lung epithelial cells. Proteomics 2008, 8, 2420-2429.
    • (2008) Proteomics , vol.8 , pp. 2420-2429
    • Lei, T.1    He, Q.Y.2    Cai, Z.3    Zhou, Y.4
  • 143
    • 70949090258 scopus 로고    scopus 로고
    • Elucidation of the percutaneous absorption of chromium compounds by functional proteomics
    • Pan, T. L., Wang, P. W., Huang, C. M., Chen, C. C., Fang, J. Y., Elucidation of the percutaneous absorption of chromium compounds by functional proteomics. Proteomics 2009, 9, 5120-5131.
    • (2009) Proteomics , vol.9 , pp. 5120-5131
    • Pan, T.L.1    Wang, P.W.2    Huang, C.M.3    Chen, C.C.4    Fang, J.Y.5
  • 144
    • 75149159544 scopus 로고    scopus 로고
    • Changes in protein expression associated with chronic in vitro exposure of hexavalent chromium to osteoblasts and monocytes: a proteomic approach
    • Raghunathan, V. K., Grant, M. H., Ellis, E. M., Changes in protein expression associated with chronic in vitro exposure of hexavalent chromium to osteoblasts and monocytes: a proteomic approach. J. Biomed. Mater. Res. Part A 2010, 92A, 615-625.
    • (2010) J. Biomed. Mater. Res. Part A , vol.92 A , pp. 615-625
    • Raghunathan, V.K.1    Grant, M.H.2    Ellis, E.M.3
  • 145
    • 77952957835 scopus 로고    scopus 로고
    • Heavy metals chromium and neodymium reduced phosphorylation level of heat shock protein 27 in human keratinocytes
    • Zhang, Q., Zhang, L., Xiao, X., Su, Z. et al., Heavy metals chromium and neodymium reduced phosphorylation level of heat shock protein 27 in human keratinocytes. Toxicol. In Vitro 2010, 24, 1098-1104.
    • (2010) Toxicol. In Vitro , vol.24 , pp. 1098-1104
    • Zhang, Q.1    Zhang, L.2    Xiao, X.3    Su, Z.4
  • 146
    • 84865003637 scopus 로고    scopus 로고
    • Proteomic analysis of the copper ion-induced stress response in a human embryonic carcinoma cell line
    • Han, D. M., Choi, M. R., Jung, K. H., Lee, H. T. et al., Proteomic analysis of the copper ion-induced stress response in a human embryonic carcinoma cell line. Int. J. Toxicol. 2012, 31, 397-406.
    • (2012) Int. J. Toxicol. , vol.31 , pp. 397-406
    • Han, D.M.1    Choi, M.R.2    Jung, K.H.3    Lee, H.T.4
  • 148
    • 84865481324 scopus 로고    scopus 로고
    • Differential protein expression of hepatic cells associated with MeHg exposure: deepening into the molecular mechanisms of toxicity
    • Cuello, S., Ramos, S., Madrid, Y., Luque-Garcia, J. L., Camara, C., Differential protein expression of hepatic cells associated with MeHg exposure: deepening into the molecular mechanisms of toxicity. Anal. Bioanal. Chem. 2012, 404, 315-324.
    • (2012) Anal. Bioanal. Chem. , vol.404 , pp. 315-324
    • Cuello, S.1    Ramos, S.2    Madrid, Y.3    Luque-Garcia, J.L.4    Camara, C.5
  • 149
    • 10044233716 scopus 로고    scopus 로고
    • Changes in the brain mitochondrial proteome of male Sprague-Dawley rats treated with manganese chloride
    • Zhang, S. R., Fu, J. L., Zhou, Z. C., Changes in the brain mitochondrial proteome of male Sprague-Dawley rats treated with manganese chloride. Toxicol. Appl. Pharmacol. 2005, 202, 13-17.
    • (2005) Toxicol. Appl. Pharmacol. , vol.202 , pp. 13-17
    • Zhang, S.R.1    Fu, J.L.2    Zhou, Z.C.3
  • 150
    • 0035925095 scopus 로고    scopus 로고
    • Nickel-induced proteins in human HaCaT keratinocytes: annexin II and phosphoglycerate kinase
    • Acevedo, F., Serra, M. A., Ermolli, M., Clerici, L., Vesterberg, O., Nickel-induced proteins in human HaCaT keratinocytes: annexin II and phosphoglycerate kinase. Toxicology 2001, 159, 33-41.
    • (2001) Toxicology , vol.159 , pp. 33-41
    • Acevedo, F.1    Serra, M.A.2    Ermolli, M.3    Clerici, L.4    Vesterberg, O.5
  • 151
    • 77953810222 scopus 로고    scopus 로고
    • Skin toxicology of lead species evaluated by their permeability and proteomic profiles: a comparison of organic and inorganic lead
    • Pan, T. L., Wang, P. W., Al-Suwayeh, S. A., Chen, C. C., Fang, J. Y., Skin toxicology of lead species evaluated by their permeability and proteomic profiles: a comparison of organic and inorganic lead. Toxicol. Lett. 2010, 197, 19-28.
    • (2010) Toxicol. Lett. , vol.197 , pp. 19-28
    • Pan, T.L.1    Wang, P.W.2    Al-Suwayeh, S.A.3    Chen, C.C.4    Fang, J.Y.5
  • 152
    • 13244255293 scopus 로고    scopus 로고
    • Transcriptomic and proteomic responses of human renal HEK293 cells to uranium toxicity
    • Prat, O., Berenguer, F., Malard, V., Tavan, E. et al., Transcriptomic and proteomic responses of human renal HEK293 cells to uranium toxicity. Proteomics 2005, 5, 297-306.
    • (2005) Proteomics , vol.5 , pp. 297-306
    • Prat, O.1    Berenguer, F.2    Malard, V.3    Tavan, E.4
  • 153
    • 28444482820 scopus 로고    scopus 로고
    • Proteomic analysis of the response of human lung cells to uranium
    • Malard, V., Prat, O., Darrouzet, E., Berenguer, F. et al., Proteomic analysis of the response of human lung cells to uranium. Proteomics 2005, 5, 4568-4580.
    • (2005) Proteomics , vol.5 , pp. 4568-4580
    • Malard, V.1    Prat, O.2    Darrouzet, E.3    Berenguer, F.4
  • 154
    • 18844461671 scopus 로고    scopus 로고
    • Effects of increased cellular zinc levels on gene and protein expression in HT-29 cells
    • Kindermann, B., Doring, F., Fuchs, D., Pfaffl, M. W., Daniel, H., Effects of increased cellular zinc levels on gene and protein expression in HT-29 cells. Biometals 2005, 18, 243-253.
    • (2005) Biometals , vol.18 , pp. 243-253
    • Kindermann, B.1    Doring, F.2    Fuchs, D.3    Pfaffl, M.W.4    Daniel, H.5
  • 155
    • 84555194632 scopus 로고    scopus 로고
    • Identification of the nanogold particle-induced endoplasmic reticulum stress by omic techniques and systems biology analysis
    • Tsai, Y. Y., Huang, Y. H., Chao, Y. L., Hu, K. Y. et al., Identification of the nanogold particle-induced endoplasmic reticulum stress by omic techniques and systems biology analysis. Acs Nano 2011, 5, 9354-9369.
    • (2011) Acs Nano , vol.5 , pp. 9354-9369
    • Tsai, Y.Y.1    Huang, Y.H.2    Chao, Y.L.3    Hu, K.Y.4
  • 156
    • 84871877189 scopus 로고    scopus 로고
    • Effect of labeling with iron oxide particles or nanodiamonds on the functionality of adipose-derived mesenchymal stem cells
    • Blaber, S. P., Hill, C. J., Webster, R. A., Say, J. M. et al., Effect of labeling with iron oxide particles or nanodiamonds on the functionality of adipose-derived mesenchymal stem cells. Plos One 2013, 8, e52997.
    • (2013) Plos One , vol.8 , pp. e52997
    • Blaber, S.P.1    Hill, C.J.2    Webster, R.A.3    Say, J.M.4
  • 157
    • 79952094315 scopus 로고    scopus 로고
    • Comparative proteomics and pulmonary toxicity of instilled single-walled carbon nanotubes, crocidolite asbestos, and ultrafine carbon black in mice
    • Teeguarden, J. G., Webb-Robertson, B. J., Waters, K. M., Murray, A. R. et al., Comparative proteomics and pulmonary toxicity of instilled single-walled carbon nanotubes, crocidolite asbestos, and ultrafine carbon black in mice. Toxicol. Sci. 2011, 120, 123-135.
    • (2011) Toxicol. Sci. , vol.120 , pp. 123-135
    • Teeguarden, J.G.1    Webb-Robertson, B.J.2    Waters, K.M.3    Murray, A.R.4
  • 158
    • 73449137508 scopus 로고    scopus 로고
    • Proteomics-based safety evaluation of multi-walled carbon nanotubes
    • Haniu, H., Matsuda, Y., Takeuchi, K., Kim, Y. A. et al., Proteomics-based safety evaluation of multi-walled carbon nanotubes. Toxicol. Appl. Pharmacol. 2010, 242, 256-262.
    • (2010) Toxicol. Appl. Pharmacol. , vol.242 , pp. 256-262
    • Haniu, H.1    Matsuda, Y.2    Takeuchi, K.3    Kim, Y.A.4
  • 159
    • 84891400033 scopus 로고    scopus 로고
    • A comparative study of lung toxicity in rats induced by three types of nanomaterials
    • X Z.G.
    • Lin, Z. Q., Ma, L., X, Z. G., Zhang, H. S., Lin, B. C., A comparative study of lung toxicity in rats induced by three types of nanomaterials. Nanoscale Res. Lett. 2013, 8, 521. doi:10.1186/1556-276X-8-521.
    • (2013) Nanoscale Res. Lett. , vol.8 , pp. 521
    • Lin, Z.Q.1    Ma, L.2    Zhang, H.S.3    Lin, B.C.4
  • 160
    • 80053913077 scopus 로고    scopus 로고
    • Comparative protein profile of human hepatoma HepG2 cells treated with graphene and single-walled carbon nanotubes: an iTRAQ-coupled 2D LC-MS/MS proteome analysis
    • Yuan, J., Gao, H., Ching, C. B., Comparative protein profile of human hepatoma HepG2 cells treated with graphene and single-walled carbon nanotubes: an iTRAQ-coupled 2D LC-MS/MS proteome analysis. Toxicol. Lett. 2011, 207, 213-221.
    • (2011) Toxicol. Lett. , vol.207 , pp. 213-221
    • Yuan, J.1    Gao, H.2    Ching, C.B.3
  • 161
    • 84887055915 scopus 로고    scopus 로고
    • Molecular Responses of Mouse Macrophages to Copper and Copper Oxide Nanoparticles Inferred from Proteomic Analyses
    • Triboulet, S., Aude-Garcia, C., Carriere, M., Diemer, H. et al., Molecular Responses of Mouse Macrophages to Copper and Copper Oxide Nanoparticles Inferred from Proteomic Analyses. Mol. Cell. Proteomics 2013, 12, 3108-3122.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3108-3122
    • Triboulet, S.1    Aude-Garcia, C.2    Carriere, M.3    Diemer, H.4
  • 162
    • 84883429471 scopus 로고    scopus 로고
    • Elucidation of Toxicity Pathways in Lung Epithelial Cells Induced by Silicon Dioxide Nanoparticles
    • Okoturo-Evans, O., Dybowska, A., Valsami-Jones, E., Cupitt, J., et al., Elucidation of Toxicity Pathways in Lung Epithelial Cells Induced by Silicon Dioxide Nanoparticles. Plos One 2013, 8, e72363.
    • (2013) Plos One , vol.8 , pp. e72363
    • Okoturo-Evans, O.1    Dybowska, A.2    Valsami-Jones, E.3    Cupitt, J.4
  • 163
    • 33846468452 scopus 로고    scopus 로고
    • Proteomic identification of macrophage migration-inhibitory factor upon exposure to TiO2 particles
    • Cha, M. H., Rhim, T., Kim, K. H., Jang, A. S. et al., Proteomic identification of macrophage migration-inhibitory factor upon exposure to TiO2 particles. Mol. Cell Proteomics 2007, 6, 56-63.
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 56-63
    • Cha, M.H.1    Rhim, T.2    Kim, K.H.3    Jang, A.S.4
  • 164
    • 79958150337 scopus 로고    scopus 로고
    • Proteome profiling reveals potential toxicity and detoxification pathways following exposure of BEAS-2B cells to engineered nanoparticle titanium dioxide
    • Ge, Y., Bruno, M., Wallace, K., Winnik, W., Prasad, R. Y., Proteome profiling reveals potential toxicity and detoxification pathways following exposure of BEAS-2B cells to engineered nanoparticle titanium dioxide. Proteomics 2011, 11, 2406-2422.
    • (2011) Proteomics , vol.11 , pp. 2406-2422
    • Ge, Y.1    Bruno, M.2    Wallace, K.3    Winnik, W.4    Prasad, R.Y.5
  • 165
    • 84863012351 scopus 로고    scopus 로고
    • The effects of TiO2 nanoparticles on the protein expression in mouse lung
    • Jeon, Y. M., Park, S. K., Kim, W. J., Ham, J. H., Lee, M. Y., The effects of TiO2 nanoparticles on the protein expression in mouse lung. Mol. Cell. Toxicol. 2011, 7, 283-289.
    • (2011) Mol. Cell. Toxicol. , vol.7 , pp. 283-289
    • Jeon, Y.M.1    Park, S.K.2    Kim, W.J.3    Ham, J.H.4    Lee, M.Y.5
  • 166
    • 79951686059 scopus 로고    scopus 로고
    • Proteomic profiling of the differentially expressed proteins by TiO2 nanoparticles in mouse kidney
    • Jeon, Y. M., Park, S. K., Rhee, S. K., Lee, M. Y., Proteomic profiling of the differentially expressed proteins by TiO2 nanoparticles in mouse kidney. Mol. Cell. Toxicol. 2010, 6, 419-425.
    • (2010) Mol. Cell. Toxicol. , vol.6 , pp. 419-425
    • Jeon, Y.M.1    Park, S.K.2    Rhee, S.K.3    Lee, M.Y.4
  • 167
    • 84901036283 scopus 로고    scopus 로고
    • Analysis of cellular responses of macrophages to zinc ions and zinc oxide nanoparticles: a combined targeted and proteomic approach
    • Triboulet, S., Aude-Garcia, C., Armand, L., Gerdil, A. et al., Analysis of cellular responses of macrophages to zinc ions and zinc oxide nanoparticles: a combined targeted and proteomic approach. Nanoscale 2014, 6, 6102-6114.
    • (2014) Nanoscale , vol.6 , pp. 6102-6114
    • Triboulet, S.1    Aude-Garcia, C.2    Armand, L.3    Gerdil, A.4
  • 168
    • 78651493829 scopus 로고    scopus 로고
    • Wear particles from studded tires and granite pavement induce pro-inflammatory alterations in human monocyte-derived macrophages: a proteomic study
    • Karlsson, H., Lindbom, J., Ghafouri, B., Lindahl, M. et al., Wear particles from studded tires and granite pavement induce pro-inflammatory alterations in human monocyte-derived macrophages: a proteomic study. Chem. Res. Toxicol. 2011, 24, 45-53.
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 45-53
    • Karlsson, H.1    Lindbom, J.2    Ghafouri, B.3    Lindahl, M.4
  • 169
    • 69249136243 scopus 로고    scopus 로고
    • Target profiling of small molecules by chemical proteomics
    • Rix, U., Superti-Furga, G., Target profiling of small molecules by chemical proteomics. Nat. Chem. Biol. 2009, 5, 616-624.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 616-624
    • Rix, U.1    Superti-Furga, G.2
  • 170
    • 84857911138 scopus 로고    scopus 로고
    • Chemoproteomic approaches to drug target identification and drug profiling
    • Bantscheff, M., Drewes, G., Chemoproteomic approaches to drug target identification and drug profiling. Bioorg. Med. Chem. 2012, 20, 1973-1978.
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 1973-1978
    • Bantscheff, M.1    Drewes, G.2
  • 172
    • 34948875686 scopus 로고    scopus 로고
    • Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors
    • Bantscheff, M., Eberhard, D., Abraham, Y., Bastuck, S. et al., Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors. Nat. Biotechnol. 2007, 25, 1035-1044.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1035-1044
    • Bantscheff, M.1    Eberhard, D.2    Abraham, Y.3    Bastuck, S.4
  • 173
    • 37049014938 scopus 로고    scopus 로고
    • Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets
    • Rix, U., Hantschel, O., Durnberger, G., Remsing Rix, L. L. et al., Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets. Blood 2007, 110, 4055-4063.
    • (2007) Blood , vol.110 , pp. 4055-4063
    • Rix, U.1    Hantschel, O.2    Durnberger, G.3    Remsing Rix, L.L.4
  • 174
    • 84895556422 scopus 로고    scopus 로고
    • A quantitative chemical proteomics approach to profile the specific cellular targets of andrographolide, a promising anticancer agent that suppresses tumor metastasis
    • Wang, J., Tan, X. F., Nguyen, V. S., Yang, P. et al., A quantitative chemical proteomics approach to profile the specific cellular targets of andrographolide, a promising anticancer agent that suppresses tumor metastasis. Mol. Cell. Proteomics 2014, 13, 876-886.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 876-886
    • Wang, J.1    Tan, X.F.2    Nguyen, V.S.3    Yang, P.4
  • 175
    • 62549166213 scopus 로고    scopus 로고
    • Global target profile of the kinase inhibitor bosutinib in primary chronic myeloid leukemia cells
    • Rix, L. L. R., Rix, U., Colinge, J., Hantschel, O. et al., Global target profile of the kinase inhibitor bosutinib in primary chronic myeloid leukemia cells. Leukemia 2009, 23, 477-485.
    • (2009) Leukemia , vol.23 , pp. 477-485
    • Rix, L.L.R.1    Rix, U.2    Colinge, J.3    Hantschel, O.4
  • 176
    • 46749145391 scopus 로고    scopus 로고
    • An unbiased evaluation of CK2 inhibitors by chemoproteomics: characterization of inhibitor effects on CK2 and identification of novel inhibitor targets
    • Duncan, J. S., Gyenis, L., Lenehan, J., Bretner, M. et al., An unbiased evaluation of CK2 inhibitors by chemoproteomics: characterization of inhibitor effects on CK2 and identification of novel inhibitor targets. Mol. Cell. Proteomics 2008, 7, 1077-1088.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1077-1088
    • Duncan, J.S.1    Gyenis, L.2    Lenehan, J.3    Bretner, M.4
  • 177
    • 84863116427 scopus 로고    scopus 로고
    • Cell-based proteome profiling of potential dasatinib targets by use of affinity-based probes
    • Shi, H., Zhang, C. J., Chen, G. Y., Yao, S. Q., Cell-based proteome profiling of potential dasatinib targets by use of affinity-based probes. J. Am. Chem. Soc. 2012, 134, 3001-3014.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3001-3014
    • Shi, H.1    Zhang, C.J.2    Chen, G.Y.3    Yao, S.Q.4
  • 178
    • 84901950348 scopus 로고    scopus 로고
    • Quantitative chemical proteomics identifies novel targets of the anti-cancer multi-kinase inhibitor E-3810
    • Colzani, M., Noberini, R., Romanenghi, M., Colella, G. et al., Quantitative chemical proteomics identifies novel targets of the anti-cancer multi-kinase inhibitor E-3810. Mol. Cell. Proteomics 2014, 13, 1495-1509.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 1495-1509
    • Colzani, M.1    Noberini, R.2    Romanenghi, M.3    Colella, G.4
  • 179
    • 84855874661 scopus 로고    scopus 로고
    • Dual phosphoproteomics and chemical proteomics analysis of erlotinib and gefitinib interference in acute myeloid leukemia cells
    • Weber, C., Schreiber, T. B., Daub, H., Dual phosphoproteomics and chemical proteomics analysis of erlotinib and gefitinib interference in acute myeloid leukemia cells. J. Proteomics 2012, 75, 1343-1356.
    • (2012) J. Proteomics , vol.75 , pp. 1343-1356
    • Weber, C.1    Schreiber, T.B.2    Daub, H.3
  • 180
    • 79952396960 scopus 로고    scopus 로고
    • Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes
    • Bantscheff, M., Hopf, C., Savitski, M. M., Dittmann, A. et al., Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes. Nat. Biotechnol. 2011, 29, 255-265.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 255-265
    • Bantscheff, M.1    Hopf, C.2    Savitski, M.M.3    Dittmann, A.4
  • 181
    • 74249085402 scopus 로고    scopus 로고
    • A comprehensive target selectivity survey of the BCR-ABL kinase inhibitor INNO-406 by kinase profiling and chemical proteomics in chronic myeloid leukemia cells
    • Rix, U., Rix, L. L. R., Terker, A. S., Fernbach, N. V. et al., A comprehensive target selectivity survey of the BCR-ABL kinase inhibitor INNO-406 by kinase profiling and chemical proteomics in chronic myeloid leukemia cells. Leukemia 2010, 24, 44-50.
    • (2010) Leukemia , vol.24 , pp. 44-50
    • Rix, U.1    Rix, L.L.R.2    Terker, A.S.3    Fernbach, N.V.4
  • 182
    • 84894030819 scopus 로고    scopus 로고
    • The antitumor agent PBT-1 directly targets HSP90 and hnRNP A2/B1 and inhibits lung adenocarcinoma growth and metastasis
    • Chen, C. Y., Yang, S. C., Lee, K. H., Yang, X. et al., The antitumor agent PBT-1 directly targets HSP90 and hnRNP A2/B1 and inhibits lung adenocarcinoma growth and metastasis. J. Med. Chem. 2014, 57, 677-685.
    • (2014) J. Med. Chem. , vol.57 , pp. 677-685
    • Chen, C.Y.1    Yang, S.C.2    Lee, K.H.3    Yang, X.4
  • 183
    • 4444315207 scopus 로고    scopus 로고
    • Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry
    • She, Y. M., Narindrasorasak, S., Yang, S., Spitale, N. et al., Identification of metal-binding proteins in human hepatoma lines by immobilized metal affinity chromatography and mass spectrometry. Mol. Cell. Proteomics 2003, 2, 1306-1318.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1306-1318
    • She, Y.M.1    Narindrasorasak, S.2    Yang, S.3    Spitale, N.4
  • 184
    • 4444219776 scopus 로고    scopus 로고
    • Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability
    • Smith, S. D., She, Y. M., Roberts, E. A., Sarkar, B., Using immobilized metal affinity chromatography, two-dimensional electrophoresis and mass spectrometry to identify hepatocellular proteins with copper-binding ability. J. Proteome Res. 2004, 3, 834-840.
    • (2004) J. Proteome Res. , vol.3 , pp. 834-840
    • Smith, S.D.1    She, Y.M.2    Roberts, E.A.3    Sarkar, B.4
  • 185
    • 0027221568 scopus 로고
    • Gamma-phosphate-linked ATP-sepharose for the affinity purification of protein kinases. Rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase
    • Haystead, C. M., Gregory, P., Sturgill, T. W., Haystead, T. A., Gamma-phosphate-linked ATP-sepharose for the affinity purification of protein kinases. Rapid purification to homogeneity of skeletal muscle mitogen-activated protein kinase kinase. Eur. J. Biochem. 1993, 214, 459-467.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 459-467
    • Haystead, C.M.1    Gregory, P.2    Sturgill, T.W.3    Haystead, T.A.4
  • 186
    • 33845386374 scopus 로고    scopus 로고
    • Analysis of the soluble ATP-binding proteome of plant mitochondria identifies new proteins and nucleotide triphosphate interactions within the matrix
    • Ito, J., Heazlewood, J. L., Millar, A. H., Analysis of the soluble ATP-binding proteome of plant mitochondria identifies new proteins and nucleotide triphosphate interactions within the matrix. J. Proteome Res. 2006, 5, 3459-3469.
    • (2006) J. Proteome Res. , vol.5 , pp. 3459-3469
    • Ito, J.1    Heazlewood, J.L.2    Millar, A.H.3
  • 187
    • 84885401478 scopus 로고    scopus 로고
    • Identification of differentially expressed proteins by treatment with PUGNAc in 3T3-L1 adipocytes through analysis of ATP-binding proteome
    • Lee, J. E., Park, J. H., Moon, P. G., Baek, M. C., Identification of differentially expressed proteins by treatment with PUGNAc in 3T3-L1 adipocytes through analysis of ATP-binding proteome. Proteomics 2013, 13, 2998-3012.
    • (2013) Proteomics , vol.13 , pp. 2998-3012
    • Lee, J.E.1    Park, J.H.2    Moon, P.G.3    Baek, M.C.4
  • 188
    • 0347087452 scopus 로고    scopus 로고
    • Chemical strategies for activity-based proteomics
    • Speers, A. E., Cravatt, B. F., Chemical strategies for activity-based proteomics. Chembiochem 2004, 5, 41-47.
    • (2004) Chembiochem , vol.5 , pp. 41-47
    • Speers, A.E.1    Cravatt, B.F.2
  • 189
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition
    • Speers, A. E., Adam, G. C., Cravatt, B. F., Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition. J. Am. Chem. Soc. 2003, 125, 4686-4687.
    • J. Am. Chem. Soc. 2003 , vol.125 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 190
    • 0033593013 scopus 로고    scopus 로고
    • Activity-based protein profiling: the serine hydrolases
    • Liu, Y., Patricelli, M. P., Cravatt, B. F., Activity-based protein profiling: the serine hydrolases. Proc. Natl. Acad. Sci. USA 1999, 96, 14694-14699.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14694-14699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 191
    • 0014405152 scopus 로고
    • The role of arene oxide-oxepin systems in the metabolism of aromatic substrates. 3. Formation of 1,2-naphthalene oxide from naphthalene by liver microsomes
    • Jerina, D. M., Daly, J. W., Witkop, B., Zaltzman-Nirenberg, P., Udenfriend, S., The role of arene oxide-oxepin systems in the metabolism of aromatic substrates. 3. Formation of 1, 2-naphthalene oxide from naphthalene by liver microsomes. J. Am. Chem. Soc. 1968, 90, 6525-6527.
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 6525-6527
    • Jerina, D.M.1    Daly, J.W.2    Witkop, B.3    Zaltzman-Nirenberg, P.4    Udenfriend, S.5
  • 192
    • 0014986730 scopus 로고
    • Possible mechanism of liver necrosis caused by aromatic organic compounds
    • Brodie, B. B., Reid, W. D., Cho, A. K., Sipes, G. et al., Possible mechanism of liver necrosis caused by aromatic organic compounds. Proc. Natl. Acad. Sci. USA 1971, 68, 160-164.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 160-164
    • Brodie, B.B.1    Reid, W.D.2    Cho, A.K.3    Sipes, G.4
  • 193
    • 0015071128 scopus 로고
    • In vitro transformation of rodent cells by K-region derivatives of polycyclic hydrocarbons
    • Grover, P. L., Sims, P., Huberman, E., Marquardt, H. et al., In vitro transformation of rodent cells by K-region derivatives of polycyclic hydrocarbons. Proc. Natl. Acad. Sci. USA 1971, 68, 1098-1101.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1098-1101
    • Grover, P.L.1    Sims, P.2    Huberman, E.3    Marquardt, H.4
  • 195
    • 77957181125 scopus 로고
    • Covalent protein modifications and gene expression changes in rodent liver following administration of methapyrilene: a study using two-dimensional electrophoresis
    • Anderson, N. L., Copple, D. C., Bendele, R. A., Probst, G. S., Richardson, F. C., Covalent protein modifications and gene expression changes in rodent liver following administration of methapyrilene: a study using two-dimensional electrophoresis. Fundam. Appl. Toxicol. 1992, 18, 570-580.
    • (1992) Fundam. Appl. Toxicol. , vol.18 , pp. 570-580
    • Anderson, N.L.1    Copple, D.C.2    Bendele, R.A.3    Probst, G.S.4    Richardson, F.C.5
  • 196
    • 0027393901 scopus 로고
    • Comparisons of protein-changes in human and rodent hepatocytes induced by the rat-specific carcinogen, methapyrilene
    • Richardson, F. C., Strom, S. C., Copple, D. M., Bendele, R. A. et al., Comparisons of protein-changes in human and rodent hepatocytes induced by the rat-specific carcinogen, methapyrilene. Electrophoresis 1993, 14, 157-161.
    • (1993) Electrophoresis , vol.14 , pp. 157-161
    • Richardson, F.C.1    Strom, S.C.2    Copple, D.M.3    Bendele, R.A.4
  • 197
    • 84877329557 scopus 로고    scopus 로고
    • Protein targets of acrylamide adduct formation in cultured rat dopaminergic cells
    • Martyniuk, C. J., Feswick, A., Fang, B., Koomen, J. M. et al., Protein targets of acrylamide adduct formation in cultured rat dopaminergic cells. Toxicol. Lett. 2013, 219, 279-287.
    • (2013) Toxicol. Lett. , vol.219 , pp. 279-287
    • Martyniuk, C.J.1    Feswick, A.2    Fang, B.3    Koomen, J.M.4
  • 198
    • 84870390940 scopus 로고    scopus 로고
    • Protein haptenation by amoxicillin: high resolution mass spectrometry analysis and identification of target proteins in serum
    • Ariza, A., Garzon, D., Abanades, D. R., de los Rios, V. et al., Protein haptenation by amoxicillin: high resolution mass spectrometry analysis and identification of target proteins in serum. J. Proteomics 2012, 77, 504-520.
    • (2012) J. Proteomics , vol.77 , pp. 504-520
    • Ariza, A.1    Garzon, D.2    Abanades, D.R.3    de los Rios, V.4
  • 199
    • 33947280388 scopus 로고    scopus 로고
    • Proteins identified as targets of the acyl glucuronide metabolite of mycophenolic acid in kidney tissue from mycophenolate mofetil treated rats
    • Asif, A. R., Armstrong, V. W., Voland, A., Wieland, E. et al., Proteins identified as targets of the acyl glucuronide metabolite of mycophenolic acid in kidney tissue from mycophenolate mofetil treated rats. Biochimie 2007, 89, 393-402.
    • (2007) Biochimie , vol.89 , pp. 393-402
    • Asif, A.R.1    Armstrong, V.W.2    Voland, A.3    Wieland, E.4
  • 200
    • 36849019121 scopus 로고    scopus 로고
    • Mechanisms of acrolein-induced myocardial dysfunction: implications for environmental and endogenous aldehyde exposure
    • Luo, J., Hill, B. G., Gu, Y., Cai, J. et al., Mechanisms of acrolein-induced myocardial dysfunction: implications for environmental and endogenous aldehyde exposure. Am. J. Physiol. Heart Circ. Physiol. 2007, 293, H3673-H3684.
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.293 , pp. H3673-H3684
    • Luo, J.1    Hill, B.G.2    Gu, Y.3    Cai, J.4
  • 201
    • 33947671231 scopus 로고    scopus 로고
    • A proteomic analysis of bromobenzene reactive metabolite targets in rat liver cytosol in vivo
    • Koen, Y. M., Gogichaeva, N. V., Alterman, M. A., Hanzlik, R. P., A proteomic analysis of bromobenzene reactive metabolite targets in rat liver cytosol in vivo. Chem. Res. Toxicol. 2007, 20, 511-519.
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 511-519
    • Koen, Y.M.1    Gogichaeva, N.V.2    Alterman, M.A.3    Hanzlik, R.P.4
  • 202
    • 84865264606 scopus 로고    scopus 로고
    • Liver protein targets of hepatotoxic 4-bromophenol metabolites
    • Koen, Y. M., Hajovsky, H., Liu, K., Williams, T. D. et al., Liver protein targets of hepatotoxic 4-bromophenol metabolites. Chem. Res. Toxicol. 2012, 25, 1777-1786.
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 1777-1786
    • Koen, Y.M.1    Hajovsky, H.2    Liu, K.3    Williams, T.D.4
  • 203
    • 67349280174 scopus 로고    scopus 로고
    • Proteomic identification of dopamine-conjugated proteins from isolated rat brain mitochondria and SH-SY5Y cells
    • Van Laar, V. S., Mishizen, A. J., Cascio, M., Hastings, T. G., Proteomic identification of dopamine-conjugated proteins from isolated rat brain mitochondria and SH-SY5Y cells. Neurobiol. Dis. 2009, 34, 487-500.
    • (2009) Neurobiol. Dis. , vol.34 , pp. 487-500
    • Van Laar, V.S.1    Mishizen, A.J.2    Cascio, M.3    Hastings, T.G.4
  • 204
    • 84859085369 scopus 로고    scopus 로고
    • Identification and pathway mapping of furan target proteins reveal mitochondrial energy production and redox regulation as critical targets of furan toxicity
    • Moro, S., Chipman, J. K., Antczak, P., Turan, N. et al., Identification and pathway mapping of furan target proteins reveal mitochondrial energy production and redox regulation as critical targets of furan toxicity. Toxicol. Sci. 2012, 126, 336-352.
    • (2012) Toxicol. Sci. , vol.126 , pp. 336-352
    • Moro, S.1    Chipman, J.K.2    Antczak, P.3    Turan, N.4
  • 205
    • 28444450886 scopus 로고    scopus 로고
    • Monocrotaline pyrrole targets proteins with and without cysteine residues in the cytosol and membranes of human pulmonary artery endothelial cells
    • Lame, M. W., Jones, A. D., Wilson, D. W., Segall, H. J., Monocrotaline pyrrole targets proteins with and without cysteine residues in the cytosol and membranes of human pulmonary artery endothelial cells. Proteomics 2005, 5, 4398-4413.
    • (2005) Proteomics , vol.5 , pp. 4398-4413
    • Lame, M.W.1    Jones, A.D.2    Wilson, D.W.3    Segall, H.J.4
  • 206
    • 22944478928 scopus 로고    scopus 로고
    • Identification of proteins adducted by reactive naphthalene metabolites in vitro
    • Isbell, M. A., Morin, D., Boland, B., Buckpitt, A. et al., Identification of proteins adducted by reactive naphthalene metabolites in vitro. Proteomics 2005, 5, 4197-4204.
    • (2005) Proteomics , vol.5 , pp. 4197-4204
    • Isbell, M.A.1    Morin, D.2    Boland, B.3    Buckpitt, A.4
  • 207
    • 0037390052 scopus 로고    scopus 로고
    • Protein targets of 1,4-benzoquinone and 1,4-naphthoquinone in human bronchial epithelial cells
    • Lame, M. W., Jones, A. D., Wilson, D. W., Segall, H. J., Protein targets of 1, 4-benzoquinone and 1, 4-naphthoquinone in human bronchial epithelial cells. Proteomics 2003, 3, 479-495.
    • (2003) Proteomics , vol.3 , pp. 479-495
    • Lame, M.W.1    Jones, A.D.2    Wilson, D.W.3    Segall, H.J.4
  • 208
    • 84876267247 scopus 로고    scopus 로고
    • Protein targets of thioacetamide metabolites in rat hepatocytes
    • Koen, Y. M., Sarma, D., Hajovsky, H., Galeva, N. A. et al., Protein targets of thioacetamide metabolites in rat hepatocytes. Chem. Res. Toxicol. 2013, 26, 564-574.
    • (2013) Chem. Res. Toxicol. , vol.26 , pp. 564-574
    • Koen, Y.M.1    Sarma, D.2    Hajovsky, H.3    Galeva, N.A.4
  • 209
    • 49049113052 scopus 로고    scopus 로고
    • Protein targets of reactive metabolites of thiobenzamide in rat liver in vivo
    • Ikehata, K., Duzhak, T. G., Galeva, N. A., Ji, T. et al., Protein targets of reactive metabolites of thiobenzamide in rat liver in vivo. Chem. Res. Toxicol. 2008, 21, 1432-1442.
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 1432-1442
    • Ikehata, K.1    Duzhak, T.G.2    Galeva, N.A.3    Ji, T.4
  • 210
    • 20644441336 scopus 로고    scopus 로고
    • Spot overlapping in two-dimensional maps: a serious problem ignored for much too long
    • Campostrini, N., Areces, L. B., Rappsilber, J., Pietrogrande, M. C. et al., Spot overlapping in two-dimensional maps: a serious problem ignored for much too long. Proteomics 2005, 5, 2385-2395.
    • (2005) Proteomics , vol.5 , pp. 2385-2395
    • Campostrini, N.1    Areces, L.B.2    Rappsilber, J.3    Pietrogrande, M.C.4
  • 211
    • 33645073886 scopus 로고    scopus 로고
    • Is protein overlap in two-dimensional gels a serious practical problem
    • Hunsucker, S. W., Duncan, M. W., Is protein overlap in two-dimensional gels a serious practical problem? Proteomics 2006, 6, 1374-1375.
    • (2006) Proteomics , vol.6 , pp. 1374-1375
    • Hunsucker, S.W.1    Duncan, M.W.2
  • 212
    • 84880623873 scopus 로고    scopus 로고
    • Evaluation of three-dimensional gel electrophoresis to improve quantitative profiling of complex proteomes
    • Colignon, B., Raes, M., Dieu, M., Delaive, E., Mauro, S., Evaluation of three-dimensional gel electrophoresis to improve quantitative profiling of complex proteomes. Proteomics 2013, 13, 2077-2082.
    • (2013) Proteomics , vol.13 , pp. 2077-2082
    • Colignon, B.1    Raes, M.2    Dieu, M.3    Delaive, E.4    Mauro, S.5
  • 213
    • 0033838003 scopus 로고    scopus 로고
    • Towards high performance two-dimensional gel electrophoresis using ultrazoom gels
    • Hoving, S., Voshol, H., van Oostrum, J., Towards high performance two-dimensional gel electrophoresis using ultrazoom gels. Electrophoresis 2000, 21, 2617-2621.
    • (2000) Electrophoresis , vol.21 , pp. 2617-2621
    • Hoving, S.1    Voshol, H.2    van Oostrum, J.3
  • 214
    • 0034848343 scopus 로고    scopus 로고
    • Zooming-in on the proteome: very narrow-range immobilised pH gradients reveal more protein species and isoforms
    • Westbrook, J. A., Yan, J. X., Wait, R., Welson, S. Y., Dunn, M. J., Zooming-in on the proteome: very narrow-range immobilised pH gradients reveal more protein species and isoforms. Electrophoresis 2001, 22, 2865-2871.
    • (2001) Electrophoresis , vol.22 , pp. 2865-2871
    • Westbrook, J.A.1    Yan, J.X.2    Wait, R.3    Welson, S.Y.4    Dunn, M.J.5
  • 215
    • 84891848414 scopus 로고    scopus 로고
    • Sulphoxythiocarbamates modify cysteine residues in HSP90 causing degradation of client proteins and inhibition of cancer cell proliferation
    • Zhang, Y., Dayalan Naidu, S., Samarasinghe, K., Van Hecke, G. C. et al., Sulphoxythiocarbamates modify cysteine residues in HSP90 causing degradation of client proteins and inhibition of cancer cell proliferation. Br. J. Cancer 2014, 110, 71-82.
    • (2014) Br. J. Cancer , vol.110 , pp. 71-82
    • Zhang, Y.1    Dayalan Naidu, S.2    Samarasinghe, K.3    Van Hecke, G.C.4
  • 216
    • 84900008694 scopus 로고    scopus 로고
    • Optimizing proteolytic digestion conditions for the analysis of serum albumin adducts of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine, a potential human carcinogen formed in cooked meat
    • Peng, L., Turesky, R. J., Optimizing proteolytic digestion conditions for the analysis of serum albumin adducts of 2-amino-1-methyl-6-phenylimidazo[4, 5-b]pyridine, a potential human carcinogen formed in cooked meat. J. Proteomics 2014, 103, 267-278.
    • (2014) J. Proteomics , vol.103 , pp. 267-278
    • Peng, L.1    Turesky, R.J.2
  • 217
    • 79960848478 scopus 로고    scopus 로고
    • Aniline-induced nitrosative stress in rat spleen: proteomic identification of nitrated proteins
    • Fan, X. Z., Wang, J. L., Soman, K. V., Ansari, G. A. S., Khan, M. F., Aniline-induced nitrosative stress in rat spleen: proteomic identification of nitrated proteins. Toxicol. Appl. Pharmacol. 2011, 255, 103-112.
    • (2011) Toxicol. Appl. Pharmacol. , vol.255 , pp. 103-112
    • Fan, X.Z.1    Wang, J.L.2    Soman, K.V.3    Ansari, G.A.S.4    Khan, M.F.5
  • 218
    • 65249108716 scopus 로고    scopus 로고
    • Protein carbonyl formation in response to propiconazole-induced oxidative stress
    • Bruno, M., Moore, T., Nesnow, S., Ge, Y., Protein carbonyl formation in response to propiconazole-induced oxidative stress. J. Proteome Res. 2009, 8, 2070-2078.
    • (2009) J. Proteome Res. , vol.8 , pp. 2070-2078
    • Bruno, M.1    Moore, T.2    Nesnow, S.3    Ge, Y.4
  • 219
    • 84877813802 scopus 로고    scopus 로고
    • A comparative study of protein carbonylation and mitochondrial dysfunction using the neurotoxicants 1,3-dinitrobenzene, 3-nitropropionic acid, and 3-chloropropanediol
    • Steiner, S. R., Milton, E., Philbert, M. A., A comparative study of protein carbonylation and mitochondrial dysfunction using the neurotoxicants 1, 3-dinitrobenzene, 3-nitropropionic acid, and 3-chloropropanediol. Neurotoxicology 2013, 37, 74-84.
    • (2013) Neurotoxicology , vol.37 , pp. 74-84
    • Steiner, S.R.1    Milton, E.2    Philbert, M.A.3
  • 220
    • 70350268089 scopus 로고    scopus 로고
    • Large-scale analysis of protein expression changes in human keratinocytes immortalized by human papilloma virus type 16 E6 and E7 oncogenes
    • Merkley, M. A., Hildebrandt, E., Podolsky, R. H., Arnouk, H. et al., Large-scale analysis of protein expression changes in human keratinocytes immortalized by human papilloma virus type 16 E6 and E7 oncogenes. Proteome Sci 2009, 7, 29. doi:10.1186/1477-5956-7-29.
    • (2009) Proteome Sci , vol.7 , pp. 29
    • Merkley, M.A.1    Hildebrandt, E.2    Podolsky, R.H.3    Arnouk, H.4
  • 221
    • 84876129279 scopus 로고    scopus 로고
    • Interindividual variation in the proteome of human peripheral blood mononuclear cells
    • Maes, E., Landuyt, B., Mertens, I., Schoofs, L., Interindividual variation in the proteome of human peripheral blood mononuclear cells. PLoS One 2013, 8, e61933.
    • (2013) PLoS One , vol.8 , pp. e61933
    • Maes, E.1    Landuyt, B.2    Mertens, I.3    Schoofs, L.4
  • 222
    • 39049097692 scopus 로고    scopus 로고
    • Biological variation of the platelet proteome in the elderly population and its implication for biomarker research
    • Winkler, W., Zellner, M., Diestinger, M., Babeluk, R. et al., Biological variation of the platelet proteome in the elderly population and its implication for biomarker research. Mol. Cell. Proteomics 2008, 7, 193-203.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 193-203
    • Winkler, W.1    Zellner, M.2    Diestinger, M.3    Babeluk, R.4
  • 223
    • 84864809026 scopus 로고    scopus 로고
    • Label-free quantification and shotgun analysis of complex proteomes by one-dimensional SDS-PAGE/NanoLC-MS: evaluation for the large scale analysis of inflammatory human endothelial cells
    • Gautier, V., Mouton-Barbosa, E., Bouyssie, D., Delcourt, N. et al., Label-free quantification and shotgun analysis of complex proteomes by one-dimensional SDS-PAGE/NanoLC-MS: evaluation for the large scale analysis of inflammatory human endothelial cells. Mol. Cell. Proteomics 2012, 11, 527-539.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 527-539
    • Gautier, V.1    Mouton-Barbosa, E.2    Bouyssie, D.3    Delcourt, N.4
  • 224
    • 84862923173 scopus 로고    scopus 로고
    • Comprehensive comparison of iTRAQ and label-free LC-based quantitative proteomics approaches using two Chlamydomonas reinhardtii strains of interest for biofuels engineering
    • Wang, H., Alvarez, S., Hicks, L. M., Comprehensive comparison of iTRAQ and label-free LC-based quantitative proteomics approaches using two Chlamydomonas reinhardtii strains of interest for biofuels engineering. J. Proteome Res. 2012, 11, 487-501.
    • (2012) J. Proteome Res. , vol.11 , pp. 487-501
    • Wang, H.1    Alvarez, S.2    Hicks, L.M.3
  • 225
    • 34250804871 scopus 로고    scopus 로고
    • Comparing SILAC and two-dimensional gel electrophoresis image analysis for profiling urokinase plasminogen activator signaling in ovarian cancer cells
    • Uitto, P. M., Lance, B. K., Wood, G. R., Sherman, J. et al., Comparing SILAC and two-dimensional gel electrophoresis image analysis for profiling urokinase plasminogen activator signaling in ovarian cancer cells. J. Proteome Res. 2007, 6, 2105-2112.
    • (2007) J. Proteome Res. , vol.6 , pp. 2105-2112
    • Uitto, P.M.1    Lance, B.K.2    Wood, G.R.3    Sherman, J.4
  • 226
    • 84860602480 scopus 로고    scopus 로고
    • Critical comparison of multidimensional separation methods for increasing protein expression coverage
    • Antberg, L., Cifani, P., Sandin, M., Levander, F., James, P., Critical comparison of multidimensional separation methods for increasing protein expression coverage. J. Proteome Res. 2011, 11, 2644-2652.
    • (2011) J. Proteome Res. , vol.11 , pp. 2644-2652
    • Antberg, L.1    Cifani, P.2    Sandin, M.3    Levander, F.4    James, P.5
  • 227
    • 77955462279 scopus 로고    scopus 로고
    • Addressing accuracy and precision issues in iTRAQ quantitation
    • Karp, N. A., Huber, W., Sadowski, P. G., Charles, P. D. et al., Addressing accuracy and precision issues in iTRAQ quantitation. Mol. Cell. Proteomics 2010, 9, 1885-1897.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1885-1897
    • Karp, N.A.1    Huber, W.2    Sadowski, P.G.3    Charles, P.D.4
  • 228
    • 63649124649 scopus 로고    scopus 로고
    • Influence of image-analysis software on quantitation of two-dimensional gel electrophoresis data
    • Stessl, M., Noe, C. R., Lachmann, B., Influence of image-analysis software on quantitation of two-dimensional gel electrophoresis data. Electrophoresis 2009, 30, 325-328.
    • (2009) Electrophoresis , vol.30 , pp. 325-328
    • Stessl, M.1    Noe, C.R.2    Lachmann, B.3
  • 229
    • 0030933168 scopus 로고    scopus 로고
    • Decrease in kidney calbindin-D 28kDa as a possible mechanism mediating cyclosporine A- and FK-506-induced calciuria and tubular mineralization
    • Aicher, L., Meier, G., Norcross, A. J., Jakubowski, J. et al., Decrease in kidney calbindin-D 28kDa as a possible mechanism mediating cyclosporine A- and FK-506-induced calciuria and tubular mineralization. Biochem. Pharmacol. 1997, 53, 723-731.
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 723-731
    • Aicher, L.1    Meier, G.2    Norcross, A.J.3    Jakubowski, J.4
  • 230
    • 84899050727 scopus 로고    scopus 로고
    • High cofilin-1 levels correlate with cisplatin resistance in lung adenocarcinomas
    • Becker, M., De Bastiani, M. A., Muller, C. B., Markoski, M. M. et al., High cofilin-1 levels correlate with cisplatin resistance in lung adenocarcinomas. Tumor Biol. 2014, 35, 1233-1238.
    • (2014) Tumor Biol. , vol.35 , pp. 1233-1238
    • Becker, M.1    De Bastiani, M.A.2    Muller, C.B.3    Markoski, M.M.4
  • 231
    • 84866441579 scopus 로고    scopus 로고
    • Fatty acid-binding protein 5 promotes cell proliferation and invasion in human intrahepatic cholangiocarcinoma
    • Jeong, C. Y., Hah, Y. S., Choi, B. I., Lee, S. M. et al., Fatty acid-binding protein 5 promotes cell proliferation and invasion in human intrahepatic cholangiocarcinoma. Oncol. Rep. 2012, 28, 1283-1292.
    • (2012) Oncol. Rep. , vol.28 , pp. 1283-1292
    • Jeong, C.Y.1    Hah, Y.S.2    Choi, B.I.3    Lee, S.M.4
  • 232
    • 43549094212 scopus 로고    scopus 로고
    • Deja vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins
    • Petrak, J., Ivanek, R., Toman, O., Cmejla, R. et al., Deja vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins. Proteomics 2008, 8, 1744-1749.
    • (2008) Proteomics , vol.8 , pp. 1744-1749
    • Petrak, J.1    Ivanek, R.2    Toman, O.3    Cmejla, R.4
  • 233
    • 0037478407 scopus 로고    scopus 로고
    • Human extrahepatic cytochromes P450: function in xenobiotic metabolism and tissue-selective chemical toxicity in the respiratory and gastrointestinal tracts
    • Ding, X., Kaminsky, L. S., Human extrahepatic cytochromes P450: function in xenobiotic metabolism and tissue-selective chemical toxicity in the respiratory and gastrointestinal tracts. Annu. Rev. Pharmacol.Toxicol. 2003, 43, 149-173.
    • (2003) Annu. Rev. Pharmacol.Toxicol. , vol.43 , pp. 149-173
    • Ding, X.1    Kaminsky, L.S.2
  • 234
    • 79953184690 scopus 로고    scopus 로고
    • Multiple hypothesis testing in proteomics: a strategy for experimental work
    • M110004374
    • Diz, A. P., Carvajal-Rodriguez, A., Skibinski, D. O., Multiple hypothesis testing in proteomics: a strategy for experimental work. Mol. Cell. Proteomics 2011, 10, M110.004374.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Diz, A.P.1    Carvajal-Rodriguez, A.2    Skibinski, D.O.3
  • 235
    • 84894375635 scopus 로고    scopus 로고
    • Biomarkers and human hepatocytes
    • Li, A. P., Biomarkers and human hepatocytes. Biomark. Med. 2014, 8, 173-183.
    • (2014) Biomark. Med. , vol.8 , pp. 173-183
    • Li, A.P.1
  • 236
    • 84891046750 scopus 로고    scopus 로고
    • Copper toxicity induced hepatocerebral and neurodegenerative diseases: an urgent need for prognostic biomarkers
    • Pal, A., Copper toxicity induced hepatocerebral and neurodegenerative diseases: an urgent need for prognostic biomarkers. Neurotoxicology 2014, 40, 97-101.
    • (2014) Neurotoxicology , vol.40 , pp. 97-101
    • Pal, A.1
  • 237
    • 84864810275 scopus 로고    scopus 로고
    • Development of a pharmaceutical hepatotoxicity biomarker panel using a discovery to targeted proteomics approach
    • Collins, B. C., Miller, C. A., Sposny, A., Hewitt, P. et al., Development of a pharmaceutical hepatotoxicity biomarker panel using a discovery to targeted proteomics approach. Mol. Cell. Proteomics 2012, 11, 394-410.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 394-410
    • Collins, B.C.1    Miller, C.A.2    Sposny, A.3    Hewitt, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.