메뉴 건너뛰기




Volumn 396, Issue 1, 2010, Pages 13-22

Unambiguous determination of isobaric histone modifications by reversed-phase retention time and high-mass accuracy

Author keywords

Acetylation; High mass accuracy; Methylation; Retention; Trimethylation

Indexed keywords

ALKYLATION; AMINO ACIDS; MASS SPECTROMETRY; METHYLATION; PEPTIDES; TRANSCRIPTION; YEAST;

EID: 70449624833     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.08.027     Document Type: Article
Times cited : (18)

References (54)
  • 1
    • 15744396813 scopus 로고    scopus 로고
    • The key to development: interpreting the histone code?
    • Margueron R., Trojer P., and Reinberg D. The key to development: interpreting the histone code?. Curr. Opin. Genet. Dev. 15 (2005) 163-176
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 163-176
    • Margueron, R.1    Trojer, P.2    Reinberg, D.3
  • 2
    • 26444446597 scopus 로고    scopus 로고
    • Histone modifications as a platform for cancer therapy
    • Espino P.S., Drobic B., Dunn K.L., and Davie J.R. Histone modifications as a platform for cancer therapy. J. Cell. Biochem. 94 (2005) 1088-1102
    • (2005) J. Cell. Biochem. , vol.94 , pp. 1088-1102
    • Espino, P.S.1    Drobic, B.2    Dunn, K.L.3    Davie, J.R.4
  • 4
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin C., and Zhang Y. The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 6 (2005) 838-849
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 5
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner D.E., and Berger S.L. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 64 (2000) 435-459
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 6
    • 33747609801 scopus 로고    scopus 로고
    • Genome-wide patterns of histone modifications in yeast
    • Millar C.B., and Grunstein M. Genome-wide patterns of histone modifications in yeast. Nat. Rev. Mol. Cell Biol. 7 (2006) 657-666
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 657-666
    • Millar, C.B.1    Grunstein, M.2
  • 7
    • 0037672689 scopus 로고    scopus 로고
    • An epigenetic road map for histone lysine methylation
    • Lachner M., O'Sullivan R.J., and Jenuwein T. An epigenetic road map for histone lysine methylation. J. Cell Sci. 116 (2003) 2117-2124
    • (2003) J. Cell Sci. , vol.116 , pp. 2117-2124
    • Lachner, M.1    O'Sullivan, R.J.2    Jenuwein, T.3
  • 8
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung P., Tanner K.G., Cheung W.L., Sassone-Corsi P., Denu J.M., and Allis C.D. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol. Cell 5 (2000) 905-915
    • (2000) Mol. Cell , vol.5 , pp. 905-915
    • Cheung, P.1    Tanner, K.G.2    Cheung, W.L.3    Sassone-Corsi, P.4    Denu, J.M.5    Allis, C.D.6
  • 9
    • 0033638105 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14
    • Lo W.S., Trievel R.C., Rojas J.R., Duggan L., Hsu J.Y., Allis C.D., Marmorstein R., and Berger S.L. Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Mol. Cell 5 (2000) 917-926
    • (2000) Mol. Cell , vol.5 , pp. 917-926
    • Lo, W.S.1    Trievel, R.C.2    Rojas, J.R.3    Duggan, L.4    Hsu, J.Y.5    Allis, C.D.6    Marmorstein, R.7    Berger, S.L.8
  • 13
    • 5644231221 scopus 로고    scopus 로고
    • Characterization of Tetrahymena histone H2B variants and posttranslational populations by electron capture dissociation (ECD) Fourier transform ion cyclotron mass spectrometry (FT-ICR MS)
    • Medzihradszky K.F., Zhang X., Chalkley R.J., Guan S., McFarland M.A., Chalmers M.J., Marshall A.G., Diaz R.L., Allis C.D., and Burlingame A.L. Characterization of Tetrahymena histone H2B variants and posttranslational populations by electron capture dissociation (ECD) Fourier transform ion cyclotron mass spectrometry (FT-ICR MS). Mol. Cell. Proteomics 3 (2004) 872-886
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 872-886
    • Medzihradszky, K.F.1    Zhang, X.2    Chalkley, R.J.3    Guan, S.4    McFarland, M.A.5    Chalmers, M.J.6    Marshall, A.G.7    Diaz, R.L.8    Allis, C.D.9    Burlingame, A.L.10
  • 14
    • 7544229161 scopus 로고    scopus 로고
    • Application of mass spectrometry to the identification and quantification of histone post-translational modifications
    • Freitas M.A., Sklenar A.R., and Parthun M.R. Application of mass spectrometry to the identification and quantification of histone post-translational modifications. J. Cell. Biochem. 92 (2004) 691-700
    • (2004) J. Cell. Biochem. , vol.92 , pp. 691-700
    • Freitas, M.A.1    Sklenar, A.R.2    Parthun, M.R.3
  • 16
    • 33846604580 scopus 로고    scopus 로고
    • Histone H4 N-terminal acetylation in Kasumi-1 cells treated with depsipeptide determined by acetic acid-urea polyacrylamide gel electrophoresis, amino acid coded mass tagging, and mass spectrometry
    • Zhang L., Su X., Liu S., Knapp A.R., Parthun M.R., Marcucci G., and Freitas M.A. Histone H4 N-terminal acetylation in Kasumi-1 cells treated with depsipeptide determined by acetic acid-urea polyacrylamide gel electrophoresis, amino acid coded mass tagging, and mass spectrometry. J. Proteome Res. 6 (2007) 81-88
    • (2007) J. Proteome Res. , vol.6 , pp. 81-88
    • Zhang, L.1    Su, X.2    Liu, S.3    Knapp, A.R.4    Parthun, M.R.5    Marcucci, G.6    Freitas, M.A.7
  • 17
    • 34247337729 scopus 로고    scopus 로고
    • Lysine trimethylation of retinoic acid receptor-α: a novel means to regulate receptor function
    • Huq M.D., Tsai N.P., Khan S.A., and Wei L.N. Lysine trimethylation of retinoic acid receptor-α: a novel means to regulate receptor function. Mol. Cell. Proteomics 6 (2007) 677-688
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 677-688
    • Huq, M.D.1    Tsai, N.P.2    Khan, S.A.3    Wei, L.N.4
  • 18
    • 0141483484 scopus 로고    scopus 로고
    • Identification of novel histone post-translational modifications by peptide mass fingerprinting
    • Zhang L., Eugeni E.E., Parthun M.R., and Freitas M.A. Identification of novel histone post-translational modifications by peptide mass fingerprinting. Chromosoma 112 (2003) 77-86
    • (2003) Chromosoma , vol.112 , pp. 77-86
    • Zhang, L.1    Eugeni, E.E.2    Parthun, M.R.3    Freitas, M.A.4
  • 19
    • 0942276237 scopus 로고    scopus 로고
    • Differentiation between peptides containing acetylated or tri-methylated lysines by mass spectrometry: an application for determining lysine 9 acetylation and methylation of histone H3
    • Zhang K., Yau P.M., Chandrasekhar B., New R., Kondrat R., Imai B.S., and Bradbury M.E. Differentiation between peptides containing acetylated or tri-methylated lysines by mass spectrometry: an application for determining lysine 9 acetylation and methylation of histone H3. Proteomics 4 (2004) 1-10
    • (2004) Proteomics , vol.4 , pp. 1-10
    • Zhang, K.1    Yau, P.M.2    Chandrasekhar, B.3    New, R.4    Kondrat, R.5    Imai, B.S.6    Bradbury, M.E.7
  • 20
    • 0037402422 scopus 로고    scopus 로고
    • Mass spectrometric quantification of acetylation at specific lysines within the amino-terminal tail of histone H4
    • Smith C.M., Gafken P.R., Zhang Z., Gottschling D.E., Smith J.B., and Smith D.L. Mass spectrometric quantification of acetylation at specific lysines within the amino-terminal tail of histone H4. Anal. Biochem. 316 (2003) 23-33
    • (2003) Anal. Biochem. , vol.316 , pp. 23-33
    • Smith, C.M.1    Gafken, P.R.2    Zhang, Z.3    Gottschling, D.E.4    Smith, J.B.5    Smith, D.L.6
  • 21
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong S.E., Mittler G., and Mann M. Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat. Methods 1 (2004) 119-126
    • (2004) Nat. Methods , vol.1 , pp. 119-126
    • Ong, S.E.1    Mittler, G.2    Mann, M.3
  • 22
    • 70449630064 scopus 로고    scopus 로고
    • Simultaneous metabolic labeling of cell with multiple amino acids: localization and dynamics of histone acetylation and methylation
    • Ren C., Liu S., Ghoshal K., Hsu P.H., Jacob S.T., Marcucci G., and Freitas M.A. Simultaneous metabolic labeling of cell with multiple amino acids: localization and dynamics of histone acetylation and methylation. Proteomics Clin. Appl. 1 (2007) 130-142
    • (2007) Proteomics Clin. Appl. , vol.1 , pp. 130-142
    • Ren, C.1    Liu, S.2    Ghoshal, K.3    Hsu, P.H.4    Jacob, S.T.5    Marcucci, G.6    Freitas, M.A.7
  • 24
    • 15444377466 scopus 로고    scopus 로고
    • SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1
    • Bouras T., Fu M., Sauve A.A., Wang F., Quong A.A., Perkins N.D., Hay R.T., Gu W., and Pestell R.G. SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1. J. Biol. Chem. 280 (2005) 10264-10276
    • (2005) J. Biol. Chem. , vol.280 , pp. 10264-10276
    • Bouras, T.1    Fu, M.2    Sauve, A.A.3    Wang, F.4    Quong, A.A.5    Perkins, N.D.6    Hay, R.T.7    Gu, W.8    Pestell, R.G.9
  • 26
    • 0031962612 scopus 로고    scopus 로고
    • Mass spectrometry and the age of the proteome
    • Yates III J.R. Mass spectrometry and the age of the proteome. J. Mass Spectrom. 33 (1998) 1-19
    • (1998) J. Mass Spectrom. , vol.33 , pp. 1-19
    • Yates III, J.R.1
  • 27
    • 0037204639 scopus 로고    scopus 로고
    • Effect of the mobile phase composition on the separation and detection of intact proteins by reversed-phase liquid chromatography-electrospray mass spectrometry
    • Garcia M.C., Hogenboom A.C., Zappey H., and Irth H. Effect of the mobile phase composition on the separation and detection of intact proteins by reversed-phase liquid chromatography-electrospray mass spectrometry. J. Chromatogr. A 957 (2002) 187-199
    • (2002) J. Chromatogr. A , vol.957 , pp. 187-199
    • Garcia, M.C.1    Hogenboom, A.C.2    Zappey, H.3    Irth, H.4
  • 28
    • 0042887140 scopus 로고    scopus 로고
    • Proteome analyses using accurate mass and elution time peptide tags with capillary LC time-of-flight mass spectrometry
    • Strittmatter E.F., Ferguson P.L., Tang K., and Smith R.D. Proteome analyses using accurate mass and elution time peptide tags with capillary LC time-of-flight mass spectrometry. J. Am. Soc. Mass Spectrom. 14 (2003) 980-991
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 980-991
    • Strittmatter, E.F.1    Ferguson, P.L.2    Tang, K.3    Smith, R.D.4
  • 29
    • 25144460509 scopus 로고    scopus 로고
    • Peptide mass mapping of acetylated isoforms of histone H4 from mouse lymphosarcoma cells treated with histone deacetylase (HDACs) inhibitors
    • Ren C., Zhang L., Freitas M.A., Ghoshal K., Parthun M.R., and Jacob S.T. Peptide mass mapping of acetylated isoforms of histone H4 from mouse lymphosarcoma cells treated with histone deacetylase (HDACs) inhibitors. J. Am. Soc. Mass Spectrom. 16 (2005) 1641-1653
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 1641-1653
    • Ren, C.1    Zhang, L.2    Freitas, M.A.3    Ghoshal, K.4    Parthun, M.R.5    Jacob, S.T.6
  • 30
    • 0018990802 scopus 로고
    • Prediction of peptide retention times in high-pressure liquid chromatography on the basis of amino acid composition
    • Meek J.L. Prediction of peptide retention times in high-pressure liquid chromatography on the basis of amino acid composition. Proc. Natl. Acad. Sci. USA 77 (1980) 1632-1636
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1632-1636
    • Meek, J.L.1
  • 31
    • 0022455435 scopus 로고
    • Prediction of peptide retention times in reversed-phase high-performance liquid chromatography: II. Correlation of observed and predicted peptide retention times factors influencing the retention times of peptides
    • Guo D., Mant C.T., Taneja A.K., and Hodges R.S. Prediction of peptide retention times in reversed-phase high-performance liquid chromatography: II. Correlation of observed and predicted peptide retention times factors influencing the retention times of peptides. J. Chromatogr. 359 (1986) 519-532
    • (1986) J. Chromatogr. , vol.359 , pp. 519-532
    • Guo, D.1    Mant, C.T.2    Taneja, A.K.3    Hodges, R.S.4
  • 32
    • 0022452397 scopus 로고
    • Prediction of peptide retention times in reversed-phase high-performance liquid chromatography: I. Determination of retention coefficients of amino acid residues of model synthetic peptides
    • Guo D., Mant C.T., Taneja A.K., Parker J.M.R., and Hodges R.S. Prediction of peptide retention times in reversed-phase high-performance liquid chromatography: I. Determination of retention coefficients of amino acid residues of model synthetic peptides. J. Chromatogr. 359 (1986) 499-518
    • (1986) J. Chromatogr. , vol.359 , pp. 499-518
    • Guo, D.1    Mant, C.T.2    Taneja, A.K.3    Parker, J.M.R.4    Hodges, R.S.5
  • 33
    • 0024295556 scopus 로고
    • Effect of peptide chain length on peptide retention behaviour in reversed-phase chromatography
    • Mant C.T., Burke T.W., Black J.A., and Hodges R.S. Effect of peptide chain length on peptide retention behaviour in reversed-phase chromatography. J. Chromatogr. 458 (1988) 193-205
    • (1988) J. Chromatogr. , vol.458 , pp. 193-205
    • Mant, C.T.1    Burke, T.W.2    Black, J.A.3    Hodges, R.S.4
  • 34
    • 0037112383 scopus 로고    scopus 로고
    • Prediction of chromatographic retention and protein identification in liquid chromatography/mass spectrometry
    • Palmblad M., Ramstrom M., Markides K.E., Hakansson P., and Bergquist J. Prediction of chromatographic retention and protein identification in liquid chromatography/mass spectrometry. Anal. Chem. 74 (2002) 5826-5830
    • (2002) Anal. Chem. , vol.74 , pp. 5826-5830
    • Palmblad, M.1    Ramstrom, M.2    Markides, K.E.3    Hakansson, P.4    Bergquist, J.5
  • 36
    • 33751208935 scopus 로고    scopus 로고
    • Sequence-specific retention calculator: algorithm for peptide retention prediction in ion-pair RP-HPLC-application to 300- and 100-Å pore size C18 sorbents
    • Krokhin O.V. Sequence-specific retention calculator: algorithm for peptide retention prediction in ion-pair RP-HPLC-application to 300- and 100-Å pore size C18 sorbents. Anal. Chem. 78 (2006) 7785-7795
    • (2006) Anal. Chem. , vol.78 , pp. 7785-7795
    • Krokhin, O.V.1
  • 37
    • 31644439146 scopus 로고    scopus 로고
    • Phosphorylation analysis by mass spectrometry: myths, facts, and the consequences for qualitative and quantitative measurements
    • Steen H., Jebanathirajah J.A., Rush J., Morrice N., and Kirschner M.W. Phosphorylation analysis by mass spectrometry: myths, facts, and the consequences for qualitative and quantitative measurements. Mol. Cell. Proteomics 5 (2006) 172-181
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 172-181
    • Steen, H.1    Jebanathirajah, J.A.2    Rush, J.3    Morrice, N.4    Kirschner, M.W.5
  • 40
    • 43249091345 scopus 로고    scopus 로고
    • Distinctive core histone post-translational modification patterns in Arabidopsis thaliana
    • Zhang K., Sridhar V.V., Zhu J., Kapoor A., and Zhu J.-K. Distinctive core histone post-translational modification patterns in Arabidopsis thaliana. PLoS ONE 2 (2007) e1210
    • (2007) PLoS ONE , vol.2
    • Zhang, K.1    Sridhar, V.V.2    Zhu, J.3    Kapoor, A.4    Zhu, J.-K.5
  • 43
    • 2442623186 scopus 로고    scopus 로고
    • A combination of different mass spectroscopic techniques for the analysis of dynamic changes of histone modifications
    • Bonaldi T., Imhof A., and Regula J.T. A combination of different mass spectroscopic techniques for the analysis of dynamic changes of histone modifications. Proteomics 4 (2004) 1382-1396
    • (2004) Proteomics , vol.4 , pp. 1382-1396
    • Bonaldi, T.1    Imhof, A.2    Regula, J.T.3
  • 46
    • 34247110340 scopus 로고    scopus 로고
    • Mass spectrometry-based strategies for characterization of histones and their post-translational modifications
    • Su X., Ren C., and Freitas M.A. Mass spectrometry-based strategies for characterization of histones and their post-translational modifications. Expert Rev. Proteomics 4 (2007) 211-225
    • (2007) Expert Rev. Proteomics , vol.4 , pp. 211-225
    • Su, X.1    Ren, C.2    Freitas, M.A.3
  • 48
    • 34249094851 scopus 로고    scopus 로고
    • A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data
    • Xu H., and Freitas M.A. A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data. BMC Bioinformatics 8 (2007) 133
    • (2007) BMC Bioinformatics , vol.8 , pp. 133
    • Xu, H.1    Freitas, M.A.2
  • 50
    • 2942518343 scopus 로고    scopus 로고
    • Mapping global histone acetylation patterns to gene expression
    • Kurdistani S.K., Tavazoie S., and Grunstein M. Mapping global histone acetylation patterns to gene expression. Cell 117 (2004) 721-733
    • (2004) Cell , vol.117 , pp. 721-733
    • Kurdistani, S.K.1    Tavazoie, S.2    Grunstein, M.3
  • 52
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • Xu F., Zhang K., and Grunstein M. Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell 121 (2005) 375-385
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 53
    • 36549022132 scopus 로고    scopus 로고
    • Qualitative and quantitative analysis of lysine acetylation and methylation in yeast histone H3
    • Zhang K. Qualitative and quantitative analysis of lysine acetylation and methylation in yeast histone H3. Int. J. Mass Spectrom. 269 (2008) 101-111
    • (2008) Int. J. Mass Spectrom. , vol.269 , pp. 101-111
    • Zhang, K.1
  • 54
    • 2442429471 scopus 로고    scopus 로고
    • Comparison of peptide mass mapping and electron capture dissociation as assays for histone posttranslational modifications
    • Zhang L., and Freitas M.A. Comparison of peptide mass mapping and electron capture dissociation as assays for histone posttranslational modifications. Int. J. Mass Spectrom. 234 (2004) 213-225
    • (2004) Int. J. Mass Spectrom. , vol.234 , pp. 213-225
    • Zhang, L.1    Freitas, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.