메뉴 건너뛰기




Volumn 6, Issue 12, 2011, Pages

Bioinformatic analysis and post-translational modification crosstalk prediction of lysine acetylation

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; LYSINE; UBIQUITIN;

EID: 82555170600     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0028228     Document Type: Article
Times cited : (54)

References (64)
  • 1
    • 36749010218 scopus 로고    scopus 로고
    • The age of crosstalk: phosphorylation, ubiquitination, and beyond
    • Hunter T, (2007) The age of crosstalk: phosphorylation, ubiquitination, and beyond. Mol Cell 28: 730-738.
    • (2007) Mol Cell , vol.28 , pp. 730-738
    • Hunter, T.1
  • 2
    • 37049252376 scopus 로고
    • Structural Modifications of Histones and their Possible Role in the Regulation of RNA Synthesis
    • Allfrey VG, Mirsky AE, (1964) Structural Modifications of Histones and their Possible Role in the Regulation of RNA Synthesis. Science 144: 559.
    • (1964) Science , vol.144 , pp. 559
    • Allfrey, V.G.1    Mirsky, A.E.2
  • 3
    • 0030916336 scopus 로고    scopus 로고
    • What's up and down with histone deacetylation and transcription?
    • Pazin MJ, Kadonaga JT, (1997) What's up and down with histone deacetylation and transcription? Cell 89: 325-328.
    • (1997) Cell , vol.89 , pp. 325-328
    • Pazin, M.J.1    Kadonaga, J.T.2
  • 4
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim SC, Sprung R, Chen Y, Xu Y, Ball H, et al. (2006) Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 23: 607-618.
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3    Xu, Y.4    Ball, H.5
  • 5
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, et al. (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325: 834-840.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5
  • 6
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • Zhao S, Xu W, Jiang W, Yu W, Lin Y, et al. (2010) Regulation of cellular metabolism by protein lysine acetylation. Science 327: 1000-1004.
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3    Yu, W.4    Lin, Y.5
  • 7
    • 77449116892 scopus 로고    scopus 로고
    • Acetylation goes global: the emergence of acetylation biology
    • Norris KL, Lee J-Y, Yao T-P, (2009) Acetylation goes global: the emergence of acetylation biology. Sci Signal 2: pe76.
    • (2009) Sci Signal , vol.2
    • Norris, K.L.1    Lee, J.-Y.2    Yao, T.-P.3
  • 8
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: a regulatory modification to rival phosphorylation?
    • Kouzarides T, (2000) Acetylation: a regulatory modification to rival phosphorylation? EMBO J 19: 1176-1179.
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 9
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation
    • Brooks CL, Gu W, (2003) Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr Opin Cell Biol 15: 164-171.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 10
    • 9244247669 scopus 로고    scopus 로고
    • Regulation of p53 activity through lysine methylation
    • Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, et al. (2004) Regulation of p53 activity through lysine methylation. Nature 432: 353-360.
    • (2004) Nature , vol.432 , pp. 353-360
    • Chuikov, S.1    Kurash, J.K.2    Wilson, J.R.3    Xiao, B.4    Justin, N.5
  • 11
    • 20744448187 scopus 로고    scopus 로고
    • Functional analysis of the roles of posttranslational modifications at the p53 C terminus in regulating p53 stability and activity
    • Feng L, Lin T, Uranishi H, Gu W, Xu Y, (2005) Functional analysis of the roles of posttranslational modifications at the p53 C terminus in regulating p53 stability and activity. Mol Cell Biol 25: 5389-5395.
    • (2005) Mol Cell Biol , vol.25 , pp. 5389-5395
    • Feng, L.1    Lin, T.2    Uranishi, H.3    Gu, W.4    Xu, Y.5
  • 12
    • 0032530486 scopus 로고    scopus 로고
    • DNA damage activates p53 through a phosphorylation-acetylation cascade
    • Sakaguchi K, Herrera JE, Saito S, Miki T, Bustin M, et al. (1998) DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev 12: 2831-2841.
    • (1998) Genes Dev , vol.12 , pp. 2831-2841
    • Sakaguchi, K.1    Herrera, J.E.2    Saito, S.3    Miki, T.4    Bustin, M.5
  • 13
    • 34248640428 scopus 로고    scopus 로고
    • Lysine propionylation and butyrylation are novel post-translational modifications in histones
    • Chen Y, Sprung R, Tang Y, Ball H, Sangras B, et al. (2007) Lysine propionylation and butyrylation are novel post-translational modifications in histones. Mol Cell Proteomics 6: 812-819.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 812-819
    • Chen, Y.1    Sprung, R.2    Tang, Y.3    Ball, H.4    Sangras, B.5
  • 14
    • 17844385784 scopus 로고    scopus 로고
    • Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability
    • Caron C, Boyault C, Khochbin S, (2005) Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability. Bioessays 27: 408-415.
    • (2005) Bioessays , vol.27 , pp. 408-415
    • Caron, C.1    Boyault, C.2    Khochbin, S.3
  • 15
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: codified crosstalk with other posttranslational modifications
    • Yang X-J, Seto E, (2008) Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol Cell 31: 449-461.
    • (2008) Mol Cell , vol.31 , pp. 449-461
    • Yang, X.-J.1    Seto, E.2
  • 16
  • 17
    • 33847768829 scopus 로고    scopus 로고
    • Long-distance combinatorial linkage between methylation and acetylation on histone H3 N termini
    • Taverna SD, Ueberheide BM, Liu Y, Tackett AJ, Diaz RL, et al. (2007) Long-distance combinatorial linkage between methylation and acetylation on histone H3 N termini. Proc Natl Acad Sci USA 104: 2086-2091.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2086-2091
    • Taverna, S.D.1    Ueberheide, B.M.2    Liu, Y.3    Tackett, A.J.4    Diaz, R.L.5
  • 18
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary C, Mann M, (2010) Decoding signalling networks by mass spectrometry-based proteomics. Nat Rev Mol Cell Biol 11: 427-439.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 19
    • 14844361808 scopus 로고    scopus 로고
    • Multisite protein modification and intramolecular signaling
    • Yang X-J, (2005) Multisite protein modification and intramolecular signaling. Oncogene 24: 1653-1662.
    • (2005) Oncogene , vol.24 , pp. 1653-1662
    • Yang, X.-J.1
  • 20
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung P, Tanner KG, Cheung WL, Sassone-Corsi P, Denu JM, et al. (2000) Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol Cell 5: 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
  • 21
    • 0034604354 scopus 로고    scopus 로고
    • Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes
    • Hsu JY, Sun ZW, Li X, Reuben M, Tatchell K, et al. (2000) Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell 102: 279-291.
    • (2000) Cell , vol.102 , pp. 279-291
    • Hsu, J.Y.1    Sun, Z.W.2    Li, X.3    Reuben, M.4    Tatchell, K.5
  • 22
    • 35848936709 scopus 로고    scopus 로고
    • Cross-regulation of histone modifications
    • Latham JA, Dent SYR, (2007) Cross-regulation of histone modifications. Nat Struct Mol Biol 14: 1017-1024.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1017-1024
    • Latham, J.A.1    Dent, S.Y.R.2
  • 23
    • 0037119438 scopus 로고    scopus 로고
    • Site-specific loss of acetylation upon phosphorylation of histone H3
    • Edmondson DG, Davie JK, Zhou J, Mirnikjoo B, Tatchell K, et al. (2002) Site-specific loss of acetylation upon phosphorylation of histone H3. J Biol Chem 277: 29496-29502.
    • (2002) J Biol Chem , vol.277 , pp. 29496-29502
    • Edmondson, D.G.1    Davie, J.K.2    Zhou, J.3    Mirnikjoo, B.4    Tatchell, K.5
  • 24
    • 77950644139 scopus 로고    scopus 로고
    • PhosSNP for systematic analysis of genetic polymorphisms that influence protein phosphorylation
    • Ren J, Jiang C, Gao X, Liu Z, Yuan Z, et al. (2010) PhosSNP for systematic analysis of genetic polymorphisms that influence protein phosphorylation. Mol Cell Proteomics 9: 623-634.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 623-634
    • Ren, J.1    Jiang, C.2    Gao, X.3    Liu, Z.4    Yuan, Z.5
  • 25
    • 2942598149 scopus 로고    scopus 로고
    • PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation
    • Hornbeck PV, Chabra I, Kornhauser JM, Skrzypek E, Zhang B, (2004) PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation. Proteomics 4: 1551-1561.
    • (2004) Proteomics , vol.4 , pp. 1551-1561
    • Hornbeck, P.V.1    Chabra, I.2    Kornhauser, J.M.3    Skrzypek, E.4    Zhang, B.5
  • 27
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • Consortium U, (2010) The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res 38: D142-148.
    • (2010) Nucleic Acids Res , vol.38
    • Consortium, U.1
  • 30
    • 61649089277 scopus 로고    scopus 로고
    • Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli
    • Zhang J, Sprung R, Pei J, Tan X, Kim S, et al. (2009) Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics 8: 215-225.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 215-225
    • Zhang, J.1    Sprung, R.2    Pei, J.3    Tan, X.4    Kim, S.5
  • 31
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
    • Yang X-J, Seto E, (2008) The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nat Rev Mol Cell Biol 9: 206-218.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 206-218
    • Yang, X.-J.1    Seto, E.2
  • 37
    • 73249149751 scopus 로고    scopus 로고
    • HDAC6 regulates androgen receptor hypersensitivity and nuclear localization via modulating Hsp90 acetylation in castration-resistant prostate cancer
    • Ai J, Wang Y, Dar JA, Liu J, Liu L, et al. (2009) HDAC6 regulates androgen receptor hypersensitivity and nuclear localization via modulating Hsp90 acetylation in castration-resistant prostate cancer. Mol Endocrinol 23: 1963-1972.
    • (2009) Mol Endocrinol , vol.23 , pp. 1963-1972
    • Ai, J.1    Wang, Y.2    Dar, J.A.3    Liu, J.4    Liu, L.5
  • 38
    • 33846014703 scopus 로고    scopus 로고
    • An acetylation site in the middle domain of Hsp90 regulates chaperone function
    • Scroggins BT, Robzyk K, Wang D, Marcu MG, Tsutsumi S, et al. (2007) An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol Cell 25: 151-159.
    • (2007) Mol Cell , vol.25 , pp. 151-159
    • Scroggins, B.T.1    Robzyk, K.2    Wang, D.3    Marcu, M.G.4    Tsutsumi, S.5
  • 39
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C, (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 40
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N, Gammeltoft S, Brunak S, (1999) Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 294: 1351-1362.
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 41
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • Blom N, Sicheritz-Pontén T, Gupta R, Gammeltoft S, Brunak S, (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4: 1633-1649.
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Pontén, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, S.5
  • 42
    • 62849118051 scopus 로고    scopus 로고
    • Computational identification of protein methylation sites through bi-profile Bayes feature extraction
    • Shao J, Xu D, Tsai S-N, Wang Y, Ngai S-M, (2009) Computational identification of protein methylation sites through bi-profile Bayes feature extraction. PLoS ONE 4: e4920.
    • (2009) PLoS ONE , vol.4
    • Shao, J.1    Xu, D.2    Tsai, S.-N.3    Wang, Y.4    Ngai, S.-M.5
  • 43
    • 77449103113 scopus 로고    scopus 로고
    • Identification, analysis, and prediction of protein ubiquitination sites
    • Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, et al. (2010) Identification, analysis, and prediction of protein ubiquitination sites. Proteins 78: 365-380.
    • (2010) Proteins , vol.78 , pp. 365-380
    • Radivojac, P.1    Vacic, V.2    Haynes, C.3    Cocklin, R.R.4    Mohan, A.5
  • 44
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang Q, Zhang Y, Yang C, Xiong H, Lin Y, et al. (2010) Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 327: 1004-1007.
    • (2010) Science , vol.327 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3    Xiong, H.4    Lin, Y.5
  • 46
    • 0025297458 scopus 로고
    • Effect of lysine modification on the secondary structure of ovalbumin
    • Batra PP, Roebuck MA, Uetrecht D, (1990) Effect of lysine modification on the secondary structure of ovalbumin. J Protein Chem 9: 37-44.
    • (1990) J Protein Chem , vol.9 , pp. 37-44
    • Batra, P.P.1    Roebuck, M.A.2    Uetrecht, D.3
  • 47
    • 0028812386 scopus 로고
    • Helix formation in model peptides based on nucleolin TPAKK motifs
    • Xu X, Cooper LG, DiMario PJ, Nelson JW, (1994) Helix formation in model peptides based on nucleolin TPAKK motifs. Biopolymers 35: 93-102.
    • (1994) Biopolymers , vol.35 , pp. 93-102
    • Xu, X.1    Cooper, L.G.2    DiMario, P.J.3    Nelson, J.W.4
  • 48
    • 0031876314 scopus 로고    scopus 로고
    • Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III
    • Tse C, Sera T, Wolffe AP, Hansen JC, (1998) Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III. Mol Cell Biol 18: 4629-4638.
    • (1998) Mol Cell Biol , vol.18 , pp. 4629-4638
    • Tse, C.1    Sera, T.2    Wolffe, A.P.3    Hansen, J.C.4
  • 50
    • 33846026402 scopus 로고    scopus 로고
    • Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation
    • Karanam B, Jiang L, Wang L, Kelleher NL, Cole PA, (2006) Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation. J Biol Chem 281: 40292-40301.
    • (2006) J Biol Chem , vol.281 , pp. 40292-40301
    • Karanam, B.1    Jiang, L.2    Wang, L.3    Kelleher, N.L.4    Cole, P.A.5
  • 51
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, et al. (1999) Structure and ligand of a histone acetyltransferase bromodomain. Nature 399: 491-496.
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C.1    Carlson, J.E.2    Zeng, L.3    He, C.4    Aggarwal, A.K.5
  • 53
    • 34948883324 scopus 로고    scopus 로고
    • SIRT1 deacetylates and positively regulates the nuclear receptor LXR
    • Li X, Zhang S, Blander G, Tse JG, Krieger M, et al. (2007) SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol Cell 28: 91-106.
    • (2007) Mol Cell , vol.28 , pp. 91-106
    • Li, X.1    Zhang, S.2    Blander, G.3    Tse, J.G.4    Krieger, M.5
  • 54
    • 38949178369 scopus 로고    scopus 로고
    • Methylation of p53 by Set7/9 mediates p53 acetylation and activity in vivo
    • Kurash JK, Lei H, Shen Q, Marston WL, Granda BW, et al. (2008) Methylation of p53 by Set7/9 mediates p53 acetylation and activity in vivo. Mol Cell 29: 392-400.
    • (2008) Mol Cell , vol.29 , pp. 392-400
    • Kurash, J.K.1    Lei, H.2    Shen, Q.3    Marston, W.L.4    Granda, B.W.5
  • 55
    • 62549126959 scopus 로고    scopus 로고
    • Genome-wide analysis to predict protein sequence variations that change phosphorylation sites or their corresponding kinases
    • Ryu G-M, Song P, Kim K-W, Oh K-S, Park K-J, et al. (2009) Genome-wide analysis to predict protein sequence variations that change phosphorylation sites or their corresponding kinases. Nucleic Acids Res 37: 1297-1307.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1297-1307
    • Ryu, G.-M.1    Song, P.2    Kim, K.-W.3    Oh, K.-S.4    Park, K.-J.5
  • 56
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of ubiquitin-modified proteome
    • Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, et al. (2011) Systematic and quantitative assessment of ubiquitin-modified proteome. Mol Cell 44: 325-340.
    • (2011) Mol Cell , vol.44 , pp. 325-340
    • Kim, W.1    Bennett, E.J.2    Huttlin, E.L.3    Guo, A.4    Li, J.5
  • 57
    • 80054033461 scopus 로고    scopus 로고
    • A proteome-wide quantative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
    • epub ahead of print
    • Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, et al. (2011) A proteome-wide quantative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol Cell Proteomics 10 epub ahead of print.
    • (2011) Mol Cell Proteomics , vol.10
    • Wagner, S.A.1    Beli, P.2    Weinert, B.T.3    Nielsen, M.L.4    Cox, J.5
  • 58
    • 23844485211 scopus 로고    scopus 로고
    • Acetylation of Foxo1 alters its DNA-binding ability and sensitivity to phosphorylation
    • Matsuzaki H, Daitoku H, Hatta M, Aoyama H, Yoshimochi K, et al. (2005) Acetylation of Foxo1 alters its DNA-binding ability and sensitivity to phosphorylation. Proc Natl Acad Sci USA 102: 11278-11283.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11278-11283
    • Matsuzaki, H.1    Daitoku, H.2    Hatta, M.3    Aoyama, H.4    Yoshimochi, K.5
  • 59
    • 0037961625 scopus 로고    scopus 로고
    • P300 transcriptional repression is mediated by SUMO modification
    • Girdwood D, Bumpass D, Vaughan OA, Thain A, Anderson LA, et al. (2003) P300 transcriptional repression is mediated by SUMO modification. Mol Cell 11: 1043-1054.
    • (2003) Mol Cell , vol.11 , pp. 1043-1054
    • Girdwood, D.1    Bumpass, D.2    Vaughan, O.A.3    Thain, A.4    Anderson, L.A.5
  • 60
    • 33750032892 scopus 로고    scopus 로고
    • CDK2-dependent phosphorylation of FOXO1 as an apoptotic response to DNA damage
    • Huang H, Regan KM, Lou Z, Chen J, Tindall DJ, (2006) CDK2-dependent phosphorylation of FOXO1 as an apoptotic response to DNA damage. Science (New York, NY) 314: 294-297.
    • (2006) Science (New York, NY) , vol.314 , pp. 294-297
    • Huang, H.1    Regan, K.M.2    Lou, Z.3    Chen, J.4    Tindall, D.J.5
  • 61
    • 0035724042 scopus 로고    scopus 로고
    • Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP
    • Vo N, Fjeld C, Goodman RH, (2001) Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP. Mol Cell Biol 21: 6181-6188.
    • (2001) Mol Cell Biol , vol.21 , pp. 6181-6188
    • Vo, N.1    Fjeld, C.2    Goodman, R.H.3
  • 62
    • 79960797509 scopus 로고    scopus 로고
    • Proteome-Wide Mapping of the Drosophila Acetylome Demonstrates a High Degree of Conservation of Lysine Acetylation
    • Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, et al. (2011) Proteome-Wide Mapping of the Drosophila Acetylome Demonstrates a High Degree of Conservation of Lysine Acetylation. Sci Signal 4: ra48.
    • (2011) Sci Signal , vol.4
    • Weinert, B.T.1    Wagner, S.A.2    Horn, H.3    Henriksen, P.4    Liu, W.R.5
  • 63
    • 33746986063 scopus 로고    scopus 로고
    • Transcriptional pausing caused by NELF plays a dual role in regulating immediate-early expression of the junB gene
    • Aida M, Chen Y, Nakajima K, Yamaguchi Y, Wada T, et al. (2006) Transcriptional pausing caused by NELF plays a dual role in regulating immediate-early expression of the junB gene. Mol Cell Biol 26: 6094-6104.
    • (2006) Mol Cell Biol , vol.26 , pp. 6094-6104
    • Aida, M.1    Chen, Y.2    Nakajima, K.3    Yamaguchi, Y.4    Wada, T.5
  • 64
    • 34247510199 scopus 로고    scopus 로고
    • Type I diabetes mellitus in human and chimpanzee: a comparison of kyoto encyclopedia of genes and genomes pathway
    • Wiwanitkit V, (2007) Type I diabetes mellitus in human and chimpanzee: a comparison of kyoto encyclopedia of genes and genomes pathway. Diabetes Technol Ther 9: 145-148.
    • (2007) Diabetes Technol Ther , vol.9 , pp. 145-148
    • Wiwanitkit, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.