메뉴 건너뛰기




Volumn 23, Issue 1, 2010, Pages 20-25

A large-scale quantitative proteomic approach to identifying sulfur mustard-induced protein phosphorylation cascades

Author keywords

[No Author keywords available]

Indexed keywords

MUSTARD GAS; PHOSPHOPEPTIDE;

EID: 75149198790     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx900265z     Document Type: Article
Times cited : (13)

References (31)
  • 1
    • 67849131217 scopus 로고    scopus 로고
    • Signaling molecules in sulfur mustard-induced cutaneous injury
    • Ruff, A. L., and Dillman, J. F. (2007) Signaling molecules in sulfur mustard-induced cutaneous injury. Eplasty 8, e2.
    • (2007) Eplasty , vol.8
    • Ruff, A.L.1    Dillman, J.F.2
  • 2
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 4
    • 4043141477 scopus 로고    scopus 로고
    • Quantitative cancer proteomics: Stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research
    • Everley, P. A., Krijgsveld, J., Zetter, B. R., and Gygi, S. P. (2004) Quantitative cancer proteomics: Stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research. Mol. Cell. Proteomics 3, 729-735.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 729-735
    • Everley, P.A.1    Krijgsveld, J.2    Zetter, B.R.3    Gygi, S.P.4
  • 5
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann, M. (2006) Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 7, 952-958.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 952-958
    • Mann, M.1
  • 6
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 8
    • 44649142564 scopus 로고    scopus 로고
    • Proteomic assessment of sulfur mustard-induced protein adducts and other protein modifications in human epidermal keratinocytes
    • Mol, M. A., van den Berg, R. M., and Benschop, H. P. (2008) Proteomic assessment of sulfur mustard-induced protein adducts and other protein modifications in human epidermal keratinocytes. Toxicol. Appl. Pharmacol. 230, 97-108.
    • (2008) Toxicol. Appl. Pharmacol , vol.230 , pp. 97-108
    • Mol, M.A.1    van den Berg, R.M.2    Benschop, H.P.3
  • 9
    • 0023852747 scopus 로고
    • Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line
    • Boukamp, P., Petrussevska, R. T., Breitkreutz, D., Hornung, J., Markham, A., and Fusenig, N. E. (1988) Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line. J. Cell Biol. 106, 761-771.
    • (1988) J. Cell Biol , vol.106 , pp. 761-771
    • Boukamp, P.1    Petrussevska, R.T.2    Breitkreutz, D.3    Hornung, J.4    Markham, A.5    Fusenig, N.E.6
  • 10
    • 33947397515 scopus 로고    scopus 로고
    • Bifunctional alkylating agent-induced p53 and nonclassical nuclear factor kappaB responses and cell death are altered by caffeic acid phenethyl ester: A potential role for antioxidant/electrophilic response-element signaling
    • Minsavage, G. D., and Dillman, J. F., 3rd (2007) Bifunctional alkylating agent-induced p53 and nonclassical nuclear factor kappaB responses and cell death are altered by caffeic acid phenethyl ester: A potential role for antioxidant/electrophilic response-element signaling. J. Pharmacol. Exp. Ther. 321, 202-212.
    • (2007) J. Pharmacol. Exp. Ther , vol.321 , pp. 202-212
    • Minsavage, G.D.1    Dillman 3rd, J.F.2
  • 11
    • 3142644823 scopus 로고    scopus 로고
    • An inhibitor of p38 MAP kinase downregulates cytokine release induced by sulfur mustard exposure in human epidermal keratinocytes
    • Dillman, J. F., 3rd, McGary, K. L., and Schlager, J. J. (2004) An inhibitor of p38 MAP kinase downregulates cytokine release induced by sulfur mustard exposure in human epidermal keratinocytes. Toxicol. In Vitro 18, 593-599.
    • (2004) Toxicol. In Vitro , vol.18 , pp. 593-599
    • Dillman 3rd, J.F.1    McGary, K.L.2    Schlager, J.J.3
  • 13
    • 84984933087 scopus 로고    scopus 로고
    • The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
    • Villen, J., and Gygi, S. P. (2008) The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry. Nat. Protoc. 3, 1630-1638.
    • (2008) Nat. Protoc , vol.3 , pp. 1630-1638
    • Villen, J.1    Gygi, S.P.2
  • 15
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., McCormack, A. L., and Yates, J. R., III (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989.
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 16
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E., and Gygi, S. P. (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4, 207-214.
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 17
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil, S. A., Villen, J., Gerber, S. A., Rush, J., and Gygi, S. P. (2006) A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat. Biotechnol. 24, 1285-1292.
    • (2006) Nat. Biotechnol , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 18
    • 58149401890 scopus 로고    scopus 로고
    • The impact of peptide abundance and dynamic range on stable-isotope-based quantitative proteomic analyses
    • Bakalarski, C. E., Elias, J. E., Villen, J., Haas, W., Gerber, S. A., Everley, P. A., and Gygi, S. P. (2008) The impact of peptide abundance and dynamic range on stable-isotope-based quantitative proteomic analyses. J. Proteome Res. 7, 4756-4765.
    • (2008) J. Proteome Res , vol.7 , pp. 4756-4765
    • Bakalarski, C.E.1    Elias, J.E.2    Villen, J.3    Haas, W.4    Gerber, S.A.5    Everley, P.A.6    Gygi, S.P.7
  • 19
    • 0030851775 scopus 로고    scopus 로고
    • The 90-kDa ribosomal S6 kinase (pp90rsk) phosphorylates the N-terminal regulatory domain of IkappaBalpha and stimulates its degradation in vitro
    • Ghoda, L., Lin, X., and Greene, W. C. (1997) The 90-kDa ribosomal S6 kinase (pp90rsk) phosphorylates the N-terminal regulatory domain of IkappaBalpha and stimulates its degradation in vitro. J. Biol. Chem. 272, 21281-21288.
    • (1997) J. Biol. Chem , vol.272 , pp. 21281-21288
    • Ghoda, L.1    Lin, X.2    Greene, W.C.3
  • 20
    • 33646871568 scopus 로고    scopus 로고
    • DNA ligase I is an in vivo substrate of DNA-dependent protein kinase and is activated by phosphorylation in response to DNA double-strand breaks
    • Bhat, K. R., Benton, B. J., and Ray, R. (2006) DNA ligase I is an in vivo substrate of DNA-dependent protein kinase and is activated by phosphorylation in response to DNA double-strand breaks. Biochemistry 45, 6522-6528.
    • (2006) Biochemistry , vol.45 , pp. 6522-6528
    • Bhat, K.R.1    Benton, B.J.2    Ray, R.3
  • 22
    • 0034570675 scopus 로고    scopus 로고
    • Calmodulin, poly(ADP-ribose-)polymerase and p53 are targets for modulating the effects of sulfur mustard
    • Rosenthal, D. S., Simbulan-Rosenthal, C. M., Iyer, S., Smith, W. J., Ray, R., and Smulson, M. E. (2000) Calmodulin, poly(ADP-ribose-)polymerase and p53 are targets for modulating the effects of sulfur mustard. J. Appl. Toxicol. 20 (Suppl. 1), S43-49.
    • (2000) J. Appl. Toxicol , vol.20 , Issue.SUPPL. 1
    • Rosenthal, D.S.1    Simbulan-Rosenthal, C.M.2    Iyer, S.3    Smith, W.J.4    Ray, R.5    Smulson, M.E.6
  • 23
    • 0035951850 scopus 로고    scopus 로고
    • Negative cell cycle regulation and DNA damage-inducible phosphorylation of the BRCT protein 53BP1
    • Xia, Z., Morales, J. C., Dunphy, W. G., and Carpenter, P. B. (2001) Negative cell cycle regulation and DNA damage-inducible phosphorylation of the BRCT protein 53BP1. J. Biol. Chem. 276, 2708-2718.
    • (2001) J. Biol. Chem , vol.276 , pp. 2708-2718
    • Xia, Z.1    Morales, J.C.2    Dunphy, W.G.3    Carpenter, P.B.4
  • 24
    • 37549051733 scopus 로고    scopus 로고
    • Protein kinase C delta induces transcription of the TP53 tumor suppressor gene by controlling death-promoting factor Btf in the apoptotic response to DNA damage
    • Liu, H., Lu, Z. G., Miki, Y., and Yoshida, K. (2007) Protein kinase C delta induces transcription of the TP53 tumor suppressor gene by controlling death-promoting factor Btf in the apoptotic response to DNA damage. Mol. Cell. Biol. 27, 8480-8491.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 8480-8491
    • Liu, H.1    Lu, Z.G.2    Miki, Y.3    Yoshida, K.4
  • 25
    • 0026713875 scopus 로고
    • Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15
    • Gu, Y., Rosenblatt, J., and Morgan, D. O. (1992) Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15. EMBO J. 11, 3995-4005.
    • (1992) EMBO J , vol.11 , pp. 3995-4005
    • Gu, Y.1    Rosenblatt, J.2    Morgan, D.O.3
  • 26
    • 0142135133 scopus 로고    scopus 로고
    • Differential contribution of inhibitory phosphorylation of CDC2 and CDK2 for unperturbed cell cycle control and DNA integrity checkpoints
    • Chow, J. P., Siu, W. Y., Ho, H. T., Ma, K. H., Ho, C. C., and Poon, R. Y. (2003) Differential contribution of inhibitory phosphorylation of CDC2 and CDK2 for unperturbed cell cycle control and DNA integrity checkpoints. J. Biol. Chem. 278, 40815-40828.
    • (2003) J. Biol. Chem , vol.278 , pp. 40815-40828
    • Chow, J.P.1    Siu, W.Y.2    Ho, H.T.3    Ma, K.H.4    Ho, C.C.5    Poon, R.Y.6
  • 27
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville, S., and Hall, A. (2002) Rho GTPases in cell biology. Nature 420, 629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 28
    • 0028139020 scopus 로고
    • Requiem: A novel zinc finger gene essential for apoptosis in myeloid cells
    • Gabig, T. G., Mantel, P. L., Rosli, R., and Crean, C. D. (1994) Requiem: A novel zinc finger gene essential for apoptosis in myeloid cells. J. Biol. Chem. 269, 29515-29519.
    • (1994) J. Biol. Chem , vol.269 , pp. 29515-29519
    • Gabig, T.G.1    Mantel, P.L.2    Rosli, R.3    Crean, C.D.4
  • 30
    • 0003264585 scopus 로고    scopus 로고
    • N-acetylcysteine and endothelial cell injury by sulfur mustard
    • Atkins, K. B., Lodhi, I. J., Hurley, L. L., and Hinshaw, D. B. (2000) N-acetylcysteine and endothelial cell injury by sulfur mustard. J. Appl. Toxicol. 20 (Suppl. 1), S125-S128.
    • (2000) J. Appl. Toxicol , vol.20 , Issue.SUPPL. 1
    • Atkins, K.B.1    Lodhi, I.J.2    Hurley, L.L.3    Hinshaw, D.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.