메뉴 건너뛰기




Volumn 14, Issue 8, 2015, Pages 3252-3262

Quantification of SAHA-Dependent Changes in Histone Modifications Using Data-Independent Acquisition Mass Spectrometry

Author keywords

acetylation; data independent acquisition; DIA; epigenetics; Histone PTM; mass spectrometry; methylation; proteomics; SAHA

Indexed keywords

HISTONE H3; HISTONE H4; VORINOSTAT; HISTONE; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; PEPTIDE;

EID: 84938810497     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/acs.jproteome.5b00245     Document Type: Article
Times cited : (47)

References (38)
  • 1
    • 79951481957 scopus 로고    scopus 로고
    • Initial impact of the sequencing of the human genome
    • Lander, E. S. Initial impact of the sequencing of the human genome Nature 2011, 470, 187-197 10.1038/nature09792
    • (2011) Nature , vol.470 , pp. 187-197
    • Lander, E.S.1
  • 3
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K.; Mäder, A. W.; Richmond, R. K.; Sargent, D. F.; Richmond, T. J. Crystal structure of the nucleosome core particle at 2.8 A resolution Nature 1997, 389, 251-260 10.1038/38444
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 4
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T.; Allis, C. D. Translating the histone code Science 2001, 293, 1074-1080 10.1126/science.1063127
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 6
    • 79151470871 scopus 로고    scopus 로고
    • Influence of Combinatorial Histone Modifications on Antibody and Effector Protein Recognition
    • Fuchs, S. M.; Krajewski, K.; Baker, R. W.; Miller, V. L.; Strahl, B. D. Influence of Combinatorial Histone Modifications on Antibody and Effector Protein Recognition Curr. Biol. 2011, 21, 53-58 10.1016/j.cub.2010.11.058
    • (2011) Curr. Biol. , vol.21 , pp. 53-58
    • Fuchs, S.M.1    Krajewski, K.2    Baker, R.W.3    Miller, V.L.4    Strahl, B.D.5
  • 8
    • 84861174704 scopus 로고    scopus 로고
    • Quantitative assessment of chromatin immunoprecipitation grade antibodies directed against histone modifications reveals patterns of co-occurring marks on histone protein molecules
    • Peach, S. E.; Rudomin, E. L.; Udeshi, N. D.; Carr, S. A.; Jaffe, J. D. Quantitative assessment of chromatin immunoprecipitation grade antibodies directed against histone modifications reveals patterns of co-occurring marks on histone protein molecules Mol. Cell. Proteomics 2012, 11, 128-137 10.1074/mcp.M111.015941
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 128-137
    • Peach, S.E.1    Rudomin, E.L.2    Udeshi, N.D.3    Carr, S.A.4    Jaffe, J.D.5
  • 9
    • 84869237494 scopus 로고    scopus 로고
    • Broad Ranges of Affinity and Specificity of Anti-Histone Antibodies Revealed by a Quantitative Peptide Immunoprecipitation Assay
    • Nishikori, S.; Hattori, T.; Fuchs, S. M.; Yasui, N.; Wojcik, J.; Koide, A.; Strahl, B. D.; Koide, S. Broad Ranges of Affinity and Specificity of Anti-Histone Antibodies Revealed by a Quantitative Peptide Immunoprecipitation Assay J. Mol. Biol. 2012, 424, 391-399 10.1016/j.jmb.2012.09.022
    • (2012) J. Mol. Biol. , vol.424 , pp. 391-399
    • Nishikori, S.1    Hattori, T.2    Fuchs, S.M.3    Yasui, N.4    Wojcik, J.5    Koide, A.6    Strahl, B.D.7    Koide, S.8
  • 10
    • 84896784289 scopus 로고    scopus 로고
    • The top-down, middle-down, and bottom-up mass spectrometry approaches for characterization of histone variants and their post-translational modifications
    • Moradian, A.; Kalli, A.; Sweredoski, M. J.; Hess, S. The top-down, middle-down, and bottom-up mass spectrometry approaches for characterization of histone variants and their post-translational modifications Proteomics 2014, 14, 489-497 10.1002/pmic.201300256
    • (2014) Proteomics , vol.14 , pp. 489-497
    • Moradian, A.1    Kalli, A.2    Sweredoski, M.J.3    Hess, S.4
  • 11
    • 59449086329 scopus 로고    scopus 로고
    • Analysis of histones in Xenopus laevis. II. Mass spectrometry reveals an index of cell type-specific modifications on H3 and H4
    • Nicklay, J. J.; Shechter, D.; Chitta, R. K.; Garcia, B. A.; Shabanowitz, J.; Allis, C. D.; Hunt, D. F. Analysis of histones in Xenopus laevis. II. mass spectrometry reveals an index of cell type-specific modifications on H3 and H4 J. Biol. Chem. 2009, 284, 1075-1085 10.1074/jbc.M807274200
    • (2009) J. Biol. Chem. , vol.284 , pp. 1075-1085
    • Nicklay, J.J.1    Shechter, D.2    Chitta, R.K.3    Garcia, B.A.4    Shabanowitz, J.5    Allis, C.D.6    Hunt, D.F.7
  • 12
    • 47249157351 scopus 로고    scopus 로고
    • Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry
    • Pesavento, J. J.; Bullock, C. R.; LeDuc, R. D.; Mizzen, C. A.; Kelleher, N. L. Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry J. Biol. Chem. 2008, 283, 14927-14937 10.1074/jbc.M709796200
    • (2008) J. Biol. Chem. , vol.283 , pp. 14927-14937
    • Pesavento, J.J.1    Bullock, C.R.2    LeDuc, R.D.3    Mizzen, C.A.4    Kelleher, N.L.5
  • 14
    • 84869233177 scopus 로고    scopus 로고
    • Parallel reaction monitoring for high resolution and high mass accuracy quantitative, targeted proteomics
    • Peterson, A. C.; Russell, J. D.; Bailey, D. J.; Westphall, M. S.; Coon, J. J. Parallel reaction monitoring for high resolution and high mass accuracy quantitative, targeted proteomics Mol. Cell. Proteomics 2012, 11, 1475-1488 10.1074/mcp.O112.020131
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1475-1488
    • Peterson, A.C.1    Russell, J.D.2    Bailey, D.J.3    Westphall, M.S.4    Coon, J.J.5
  • 15
    • 84887873381 scopus 로고    scopus 로고
    • Recent advances in mass spectrometry: Data independent analysis and hyper reaction monitoring
    • Law, K. P.; Lim, Y. P. Recent advances in mass spectrometry: data independent analysis and hyper reaction monitoring Expert Rev. Proteomics 2013, 10, 551-566 10.1586/14789450.2013.858022
    • (2013) Expert Rev. Proteomics , vol.10 , pp. 551-566
    • Law, K.P.1    Lim, Y.P.2
  • 17
    • 14744293536 scopus 로고    scopus 로고
    • Automated approach for quantitative analysis of complex peptide mixtures from tandem mass spectra
    • Venable, J. D.; Dong, M.-Q.; Wohlschlegel, J.; Dillin, A.; Yates, J. R. Automated approach for quantitative analysis of complex peptide mixtures from tandem mass spectra Nat. Methods 2004, 1, 39-45 10.1038/nmeth705
    • (2004) Nat. Methods , vol.1 , pp. 39-45
    • Venable, J.D.1    Dong, M.-Q.2    Wohlschlegel, J.3    Dillin, A.4    Yates, J.R.5
  • 18
    • 76149113930 scopus 로고    scopus 로고
    • Deconvolution of mixture spectra from ion-trap data-independent-acquisition tandem mass spectrometry
    • Bern, M.; Finney, G.; Hoopmann, M. R.; Merrihew, G.; Toth, M. J.; MacCoss, M. J. Deconvolution of mixture spectra from ion-trap data-independent-acquisition tandem mass spectrometry Anal. Chem. 2010, 82, 833-841 10.1021/ac901801b
    • (2010) Anal. Chem. , vol.82 , pp. 833-841
    • Bern, M.1    Finney, G.2    Hoopmann, M.R.3    Merrihew, G.4    Toth, M.J.5    MacCoss, M.J.6
  • 19
    • 84861860481 scopus 로고    scopus 로고
    • Targeted data extraction of the MS/MS spectra generated by data-independent acquisition: A new concept for consistent and accurate proteome analysis
    • Gillet, L. C.; Navarro, P.; Tate, S.; Röst, H.; Selevsek, N.; Reiter, L.; Bonner, R.; Aebersold, R. Targeted data extraction of the MS/MS spectra generated by data-independent acquisition: a new concept for consistent and accurate proteome analysis Mol. Cell. Proteomics 2012, 11, O111.016717 10.1074/mcp.O111.016717
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 111016717
    • Gillet, L.C.1    Navarro, P.2    Tate, S.3    Röst, H.4    Selevsek, N.5    Reiter, L.6    Bonner, R.7    Aebersold, R.8
  • 22
    • 0035577768 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells
    • Munster, P. N.; Troso-Sandoval, T.; Rosen, N.; Rifkind, R.; Marks, P. A.; Richon, V. M. The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells Cancer Res. 2001, 61, 8492-8497
    • (2001) Cancer Res. , vol.61 , pp. 8492-8497
    • Munster, P.N.1    Troso-Sandoval, T.2    Rosen, N.3    Rifkind, R.4    Marks, P.A.5    Richon, V.M.6
  • 23
    • 84865337735 scopus 로고    scopus 로고
    • Examining histone posttranslational modification patterns by high-resolution mass spectrometry
    • Lin, S.; Garcia, B. A. Examining histone posttranslational modification patterns by high-resolution mass spectrometry Methods Enzymol. 2012, 512, 3-28
    • (2012) Methods Enzymol. , vol.512 , pp. 3-28
    • Lin, S.1    Garcia, B.A.2
  • 24
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J.; Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification Nat. Biotechnol. 2008, 26, 1367-1372 10.1038/nbt.1511
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 29
    • 84907195499 scopus 로고    scopus 로고
    • Stable-isotope-labeled histone peptide library for histone post-translational modification and variant quantification by mass spectrometry
    • Lin, S.; Wein, S.; Gonzales-Cope, M.; Otte, G. L.; Yuan, Z.-F.; Afjehi-Sadat, L.; Maile, T.; Berger, S. L.; Rush, J.; Lill, J. R. Stable-isotope-labeled histone peptide library for histone post-translational modification and variant quantification by mass spectrometry Mol. Cell. Proteomics 2014, 13, 2450-2466 10.1074/mcp.O113.036459
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2450-2466
    • Lin, S.1    Wein, S.2    Gonzales-Cope, M.3    Otte, G.L.4    Yuan, Z.-F.5    Afjehi-Sadat, L.6    Maile, T.7    Berger, S.L.8    Rush, J.9    Lill, J.R.10
  • 30
    • 84895071750 scopus 로고    scopus 로고
    • Drift time-specific collision energies enable deep-coverage data-independent acquisition proteomics
    • Distler, U.; Kuharev, J.; Navarro, P.; Levin, Y.; Schild, H.; Tenzer, S. Drift time-specific collision energies enable deep-coverage data-independent acquisition proteomics Nat. Methods 2013, 11, 167-170 10.1038/nmeth.2767
    • (2013) Nat. Methods , vol.11 , pp. 167-170
    • Distler, U.1    Kuharev, J.2    Navarro, P.3    Levin, Y.4    Schild, H.5    Tenzer, S.6
  • 31
    • 84929660250 scopus 로고    scopus 로고
    • Automated Validation of Results and Removal of Fragment Ion Interferences in Targeted Analysis of Data Independent Acquisition MS using SWATHProphet
    • Keller, A.; Bader, S. L.; Shteynberg, D.; Hood, L.; Moritz, R. L. Automated Validation of Results and Removal of Fragment Ion Interferences in Targeted Analysis of Data Independent Acquisition MS using SWATHProphet Mol. Cell. Proteomics 2015, 14, 1411-1418 10.1074/mcp.O114.044917
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 1411-1418
    • Keller, A.1    Bader, S.L.2    Shteynberg, D.3    Hood, L.4    Moritz, R.L.5
  • 32
    • 67049117495 scopus 로고    scopus 로고
    • Directed sample interrogation utilizing an accurate mass exclusion-based data-dependent acquisition strategy (AMEx)
    • Rudomin, E. L.; Carr, S. A.; Jaffe, J. D. Directed sample interrogation utilizing an accurate mass exclusion-based data-dependent acquisition strategy (AMEx) J. Proteome Res. 2009, 8, 3154-3160 10.1021/pr801017a
    • (2009) J. Proteome Res. , vol.8 , pp. 3154-3160
    • Rudomin, E.L.1    Carr, S.A.2    Jaffe, J.D.3
  • 35
    • 84907830955 scopus 로고    scopus 로고
    • SAHA Regulates Histone Acetylation, Butyrylation, and Protein Expression in Neuroblastoma
    • Xu, G.; Wang, J.; Wu, Z.; Qian, L.; Dai, L.; Wan, X.; Tan, M.; Zhao, Y.; Wu, Y. SAHA Regulates Histone Acetylation, Butyrylation, and Protein Expression in Neuroblastoma J. Proteome Res. 2014, 13, 4211-4219 10.1021/pr500497e
    • (2014) J. Proteome Res. , vol.13 , pp. 4211-4219
    • Xu, G.1    Wang, J.2    Wu, Z.3    Qian, L.4    Dai, L.5    Wan, X.6    Tan, M.7    Zhao, Y.8    Wu, Y.9
  • 36
    • 84883750603 scopus 로고    scopus 로고
    • SAHA treatment reveals the link between histone lysine acetylation and proteome in nonsmall cell lung cancer A549 Cells
    • Wu, Q.; Xu, W.; Cao, L.; Li, X.; He, T.; Wu, Z.; Li, W. SAHA treatment reveals the link between histone lysine acetylation and proteome in nonsmall cell lung cancer A549 Cells J. Proteome Res. 2013, 12, 4064-4073 10.1021/pr4004079
    • (2013) J. Proteome Res. , vol.12 , pp. 4064-4073
    • Wu, Q.1    Xu, W.2    Cao, L.3    Li, X.4    He, T.5    Wu, Z.6    Li, W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.