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Volumn 7, Issue 11, 2012, Pages

Position-Specific Analysis and Prediction for Protein Lysine Acetylation Based on Multiple Features

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE;

EID: 84869217522     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049108     Document Type: Article
Times cited : (75)

References (62)
  • 1
    • 79952613335 scopus 로고    scopus 로고
    • Computational refinement of post-translational modifications predicted from tandem mass spectrometry
    • Chung C, Liu J, Emili A, Frey BJ, (2011) Computational refinement of post-translational modifications predicted from tandem mass spectrometry. Bioinformatics 27: 797-806.
    • (2011) Bioinformatics , vol.27 , pp. 797-806
    • Chung, C.1    Liu, J.2    Emili, A.3    Frey, B.J.4
  • 2
    • 7044250740 scopus 로고    scopus 로고
    • Lysine acetylation and the bromodomain: a new partnership for signaling
    • Yang XJ, (2004) Lysine acetylation and the bromodomain: a new partnership for signaling. Bioessays 26: 1076-1087.
    • (2004) Bioessays , vol.26 , pp. 1076-1087
    • Yang, X.J.1
  • 3
    • 0014430407 scopus 로고
    • Chemical studies of histone acetylation. The distribution of epsilon-N-acetyllysine in calf thymus histones
    • Vidali G, Gershey EL, Allfrey VG, (1968) Chemical studies of histone acetylation. The distribution of epsilon-N-acetyllysine in calf thymus histones. The Journal of biological chemistry 243: 6361-6366.
    • (1968) The Journal of Biological Chemistry , vol.243 , pp. 6361-6366
    • Vidali, G.1    Gershey, E.L.2    Allfrey, V.G.3
  • 5
    • 33847258674 scopus 로고    scopus 로고
    • Discovery and development of SAHA as an anticancer agent
    • Marks PA, (2007) Discovery and development of SAHA as an anticancer agent. Oncogene 26: 1351-1356.
    • (2007) Oncogene , vol.26 , pp. 1351-1356
    • Marks, P.A.1
  • 6
    • 0035032345 scopus 로고    scopus 로고
    • A tale of histone modifications
    • Grant PA, (2001) A tale of histone modifications. Genome Biology 2: REVIEWS0003.
    • (2001) Genome Biology , vol.2
    • Grant, P.A.1
  • 7
    • 0032518442 scopus 로고    scopus 로고
    • Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase
    • Verreault A, Kaufman PD, Kobayashi R, Stillman B, (1998) Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. Current Biology 8: 96-108.
    • (1998) Current Biology , vol.8 , pp. 96-108
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 9
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: codified crosstalk with other post-translational modifications
    • Yang XJ, Seto E, (2008) Lysine acetylation: codified crosstalk with other post-translational modifications. Molecular Cell 31: 449-461.
    • (2008) Molecular Cell , vol.31 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 10
    • 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
  • 12
    • 0023733887 scopus 로고
    • Amino-terminal alanine functions in a calcium-specific process essential for membrane-binding by prothrombin fragment-1
    • Welsch DJ, Nelsestuen GL, (1988) Amino-terminal alanine functions in a calcium-specific process essential for membrane-binding by prothrombin fragment-1. Biochemistry 27: 4939-4945.
    • (1988) Biochemistry , vol.27 , pp. 4939-4945
    • Welsch, D.J.1    Nelsestuen, G.L.2
  • 13
    • 5444223019 scopus 로고    scopus 로고
    • Site-specific analysis of histone methylation and acetylation
    • Umlauf D, Goto Y, Feil R, (2004) Site-specific analysis of histone methylation and acetylation. Methods in Molecular Biology 287: 99-120.
    • (2004) Methods in Molecular Biology , vol.287 , pp. 99-120
    • Umlauf, D.1    Goto, Y.2    Feil, R.3
  • 15
    • 77954181419 scopus 로고    scopus 로고
    • Predicting post-translational lysine acetylation using support vector machines
    • Gnad F, Ren SB, Choudhary C, Cox J, Mann M, (2010) Predicting post-translational lysine acetylation using support vector machines. Bioinformatics 26: 1666-1668.
    • (2010) Bioinformatics , vol.26 , pp. 1666-1668
    • Gnad, F.1    Ren, S.B.2    Choudhary, C.3    Cox, J.4    Mann, M.5
  • 16
    • 45449094954 scopus 로고    scopus 로고
    • Predicting N-terminal acetylation based on feature selection method
    • Cai YD, Lu L, (2008) Predicting N-terminal acetylation based on feature selection method. Biochemical and Biophysical Research Communications 372: 862-865.
    • (2008) Biochemical and Biophysical Research Communications , vol.372 , pp. 862-865
    • Cai, Y.D.1    Lu, L.2
  • 17
    • 78149461454 scopus 로고    scopus 로고
    • N-Ace: Using Solvent Accessibility and Physicochemical Properties to Identify Protein N-Acetylation Sites
    • Lee TY, Hsu JBK, Lin FM, Chang WC, Hsu PC, et al. (2010) N-Ace: Using Solvent Accessibility and Physicochemical Properties to Identify Protein N-Acetylation Sites. Journal of Computational Chemistry 31: 2759-2771.
    • (2010) Journal of Computational Chemistry , vol.31 , pp. 2759-2771
    • Lee, T.Y.1    Hsu, J.B.K.2    Lin, F.M.3    Chang, W.C.4    Hsu, P.C.5
  • 18
    • 77649234126 scopus 로고    scopus 로고
    • Lysine acetylation sites prediction using an ensemble of support vector machine classifiers
    • Xu Y, Wang X-B, Ding J, Wu L-Y, Deng N-Y, (2010) Lysine acetylation sites prediction using an ensemble of support vector machine classifiers. Journal of Theoretical Biology 264: 130-135.
    • (2010) Journal of Theoretical Biology , vol.264 , pp. 130-135
    • Xu, Y.1    Wang, X.-B.2    Ding, J.3    Wu, L.-Y.4    Deng, N.-Y.5
  • 19
    • 68949108329 scopus 로고    scopus 로고
    • Improved Prediction of Lysine Acetylation by Support Vector Machines
    • Li SL, Li H, Li MF, Shyr Y, Xie L, et al. (2009) Improved Prediction of Lysine Acetylation by Support Vector Machines. Protein and Peptide Letters 16: 977-983.
    • (2009) Protein and Peptide Letters , vol.16 , pp. 977-983
    • Li, S.L.1    Li, H.2    Li, M.F.3    Shyr, Y.4    Xie, L.5
  • 21
    • 0034968667 scopus 로고    scopus 로고
    • Structure and function of histone acetyltransferases
    • Marmorstein R, (2001) Structure and function of histone acetyltransferases. Cellular and Molecular Life Sciences 58: 693-703.
    • (2001) Cellular and Molecular Life Sciences , vol.58 , pp. 693-703
    • Marmorstein, R.1
  • 22
    • 0035902781 scopus 로고    scopus 로고
    • Structure of histone acetyltransferases
    • Marmorstein R, (2001) Structure of histone acetyltransferases. Journal of Molecular Biology 311: 433-444.
    • (2001) Journal of Molecular Biology , vol.311 , pp. 433-444
    • Marmorstein, R.1
  • 23
    • 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 WSR, et al. (2011) Proteome-wide mapping of the drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Science Signaling 4.
    • (2011) Science Signaling , vol.4
    • Weinert, B.T.1    Wagner, S.A.2    Horn, H.3    Henriksen, P.4    Liu, W.S.R.5
  • 24
    • 34249699005 scopus 로고    scopus 로고
    • Prediction of flexible/rigid regions from protein sequences using k-spaced amino acid pairs
    • Chen K, Kurgan LA, Ruan JS (2007) Prediction of flexible/rigid regions from protein sequences using k-spaced amino acid pairs. BMC Structural Biology 7.
    • (2007) BMC Structural Biology , vol.7
    • Chen, K.1    Kurgan, L.A.2    Ruan, J.S.3
  • 25
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer JC, Cantley LC, Yaffe MB, (2003) Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Research 31: 3635-3641.
    • (2003) Nucleic Acids Research , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 27
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck PV, Kornhauser JM, Tkachev S, Zhang B, Skrzypek E, et al. (2012) PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Research 40: D261-D270.
    • (2012) Nucleic Acids Research , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5
  • 29
    • 71049118572 scopus 로고    scopus 로고
    • SysPTM: A Systematic Resource for Proteomic Research on Post-translational Modifications
    • Li H, Xing XB, Ding GH, Li QR, Wang C, et al. (2009) SysPTM: A Systematic Resource for Proteomic Research on Post-translational Modifications. Molecular & Cellular Proteomics 8: 1839-1849.
    • (2009) Molecular & Cellular Proteomics , vol.8 , pp. 1839-1849
    • Li, H.1    Xing, X.B.2    Ding, G.H.3    Li, Q.R.4    Wang, C.5
  • 30
    • 33745634395 scopus 로고    scopus 로고
    • Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences
    • Li WZ, Godzik A, (2006) Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences. Bioinformatics 22: 1658-1659.
    • (2006) Bioinformatics , vol.22 , pp. 1658-1659
    • Li, W.Z.1    Godzik, A.2
  • 31
    • 0031178951 scopus 로고    scopus 로고
    • The mathematical theory of communication (Reprinted)
    • Shannon CE, (1997) The mathematical theory of communication (Reprinted). M D Computing 14: 306-317.
    • (1997) M D Computing , vol.14 , pp. 306-317
    • Shannon, C.E.1
  • 32
    • 80053607468 scopus 로고    scopus 로고
    • An information entropy-based approach to outlier detection in rough sets
    • Feng J, Yuefei S, Cungen C, (2010) An information entropy-based approach to outlier detection in rough sets. Expert Systems with Applications 37: 6338-6344.
    • (2010) Expert Systems with Applications , vol.37 , pp. 6338-6344
    • Feng, J.1    Yuefei, S.2    Cungen, C.3
  • 33
    • 58149269554 scopus 로고    scopus 로고
    • Prediction of integral membrane protein type by collocated hydrophobic amino acid pairs
    • Ke C, Yingfu J, Li D, Kurgan L, (2009) Prediction of integral membrane protein type by collocated hydrophobic amino acid pairs. Journal of Computational Chemistry 30: 163-172172.
    • (2009) Journal of Computational Chemistry , vol.30 , pp. 163-172172
    • Ke, C.1    Yingfu, J.2    Li, D.3    Kurgan, L.4
  • 34
    • 33748150984 scopus 로고    scopus 로고
    • Fuzzy KNN for predicting membrane protein types from pseudo-amino acid composition
    • Shen HB, Yang J, Chou KC, (2006) Fuzzy KNN for predicting membrane protein types from pseudo-amino acid composition. Journal of Theoretical Biology 240: 9-13.
    • (2006) Journal of Theoretical Biology , vol.240 , pp. 9-13
    • Shen, H.B.1    Yang, J.2    Chou, K.C.3
  • 35
    • 28544439958 scopus 로고    scopus 로고
    • An effective refinement strategy for KNN text classifier
    • Tan SB, (2006) An effective refinement strategy for KNN text classifier. Expert Systems with Applications 30: 290-298.
    • (2006) Expert Systems with Applications , vol.30 , pp. 290-298
    • Tan, S.B.1
  • 36
    • 78650153738 scopus 로고    scopus 로고
    • Musite, a Tool for Global Prediction of General and Kinase-specific Phosphorylation Sites
    • Gao JJ, Thelen JJ, Dunker AK, Xu D, (2010) Musite, a Tool for Global Prediction of General and Kinase-specific Phosphorylation Sites. Molecular & Cellular Proteomics 9: 2586-2600.
    • (2010) Molecular & Cellular Proteomics , vol.9 , pp. 2586-2600
    • Gao, J.J.1    Thelen, J.J.2    Dunker, A.K.3    Xu, D.4
  • 37
    • 48249145694 scopus 로고    scopus 로고
    • Computational identification of ubiquitylation sites from protein sequences
    • Tung CW, Ho SY (2008) Computational identification of ubiquitylation sites from protein sequences. BMC Bioinformatics 9.
    • (2008) BMC Bioinformatics , vol.9
    • Tung, C.W.1    Ho, S.Y.2
  • 38
    • 0029922443 scopus 로고    scopus 로고
    • Analysis of amino acid indices and mutation matrices for sequence comparison and structure prediction of proteins
    • Tomii K, Kanehisa M, (1996) Analysis of amino acid indices and mutation matrices for sequence comparison and structure prediction of proteins. Protein Engineering 9: 27-36.
    • (1996) Protein Engineering , vol.9 , pp. 27-36
    • Tomii, K.1    Kanehisa, M.2
  • 39
    • 0024046665 scopus 로고
    • Cluster analysis of amino acid indices for prediction of protein structure and function
    • Nakai K, Kidera A, Kanehisa M, (1988) Cluster analysis of amino acid indices for prediction of protein structure and function. Protein Engineering 2: 93-100.
    • (1988) Protein Engineering , vol.2 , pp. 93-100
    • Nakai, K.1    Kidera, A.2    Kanehisa, M.3
  • 41
    • 0018115846 scopus 로고
    • Conformation of amino acid side-chains in proteins
    • Janin J, Wodak S, (1978) Conformation of amino acid side-chains in proteins. Journal Of Molecular Biology 125: 357-386.
    • (1978) Journal Of Molecular Biology , vol.125 , pp. 357-386
    • Janin, J.1    Wodak, S.2
  • 42
    • 34548606295 scopus 로고    scopus 로고
    • Recent progress in protein subcellular location prediction
    • Chou KC, Shen HB, (2007) Recent progress in protein subcellular location prediction. Analytical Biochemistry 370: 1-16.
    • (2007) Analytical Biochemistry , vol.370 , pp. 1-16
    • Chou, K.C.1    Shen, H.B.2
  • 44
    • 33846285258 scopus 로고    scopus 로고
    • Temperature dependence of binding and catalysis for the Cdc25B phosphatase
    • Sohn J, Rudolph J, (2007) Temperature dependence of binding and catalysis for the Cdc25B phosphatase. Biophysical Chemistry 125: 549-555.
    • (2007) Biophysical Chemistry , vol.125 , pp. 549-555
    • Sohn, J.1    Rudolph, J.2
  • 45
    • 34247621230 scopus 로고    scopus 로고
    • Thermodynamic characterization of the protein-protein interaction in the heteromeric Bacillus subtilis pyridoxalphosphate synthase
    • Neuwirth M, Flicker K, Strohmeier M, Tews I, Macheroux P, (2007) Thermodynamic characterization of the protein-protein interaction in the heteromeric Bacillus subtilis pyridoxalphosphate synthase. Biochemistry 46: 5131-5139.
    • (2007) Biochemistry , vol.46 , pp. 5131-5139
    • Neuwirth, M.1    Flicker, K.2    Strohmeier, M.3    Tews, I.4    Macheroux, P.5
  • 46
    • 34250885126 scopus 로고    scopus 로고
    • The P-glycoprotein (ABCB1) linker domain encodes high-affinity binding sequences to alpha- and beta-tubulins
    • Georges E, (2007) The P-glycoprotein (ABCB1) linker domain encodes high-affinity binding sequences to alpha- and beta-tubulins. Biochemistry 46: 7337-7342.
    • (2007) Biochemistry , vol.46 , pp. 7337-7342
    • Georges, E.1
  • 47
    • 33749527976 scopus 로고    scopus 로고
    • Lipid-protein interaction of the MscS mechanosensitive channel examined by scanning mutagenesis
    • Nomura T, Sokabe M, Yoshimura K, (2006) Lipid-protein interaction of the MscS mechanosensitive channel examined by scanning mutagenesis. Biophysical Journal 91: 2874-2881.
    • (2006) Biophysical Journal , vol.91 , pp. 2874-2881
    • Nomura, T.1    Sokabe, M.2    Yoshimura, K.3
  • 48
    • 11144345726 scopus 로고    scopus 로고
    • The change in Gibbs free energy for hydrophobic association - Derivation and evaluation by means of inverse temperature transitions
    • Urry DW, (2004) The change in Gibbs free energy for hydrophobic association- Derivation and evaluation by means of inverse temperature transitions. Chemical Physics Letters 399: 177-183.
    • (2004) Chemical Physics Letters , vol.399 , pp. 177-183
    • Urry, D.W.1
  • 49
    • 33745622868 scopus 로고    scopus 로고
    • Two Sample Logo: a graphical representation of the differences between two sets of sequence alignments
    • Vacic V, Iakoucheva LM, Radivojac P, (2006) Two Sample Logo: a graphical representation of the differences between two sets of sequence alignments. Bioinformatics 22: 1536-1537.
    • (2006) Bioinformatics , vol.22 , pp. 1536-1537
    • Vacic, V.1    Iakoucheva, L.M.2    Radivojac, P.3
  • 50
    • 34249301302 scopus 로고    scopus 로고
    • Surface accessibility of protein post-translational modifications
    • Pang CNI, Hayen A, Wilkins MR, (2007) Surface accessibility of protein post-translational modifications. Journal of Proteome Research 6: 1833-1845.
    • (2007) Journal of Proteome Research , vol.6 , pp. 1833-1845
    • Pang, C.N.I.1    Hayen, A.2    Wilkins, M.R.3
  • 51
    • 84857518627 scopus 로고    scopus 로고
    • Biological Sequence Motif Discovery Using motif-x
    • Unit13
    • Chou MF, Schwartz D, (2011) Biological Sequence Motif Discovery Using motif-x. Current protocols in bioinformatics/editoral board, Andreas D Baxevanis [et al] Chapter 13: Unit13.15.
    • (2011) Current Protocols in Bioinformatics , vol.13 , pp. 15
    • Chou, M.F.1    Schwartz, D.2
  • 52
    • 17644391197 scopus 로고    scopus 로고
    • A rapid method for determining protein kinase phosphorylation specificity
    • Hutti JE, Jarrell ET, Chang JD, Abbott DW, Storz P, et al. (2004) A rapid method for determining protein kinase phosphorylation specificity. Nature Methods 1: 27-29.
    • (2004) Nature Methods , vol.1 , pp. 27-29
    • Hutti, J.E.1    Jarrell, E.T.2    Chang, J.D.3    Abbott, D.W.4    Storz, P.5
  • 53
    • 82555170600 scopus 로고    scopus 로고
    • Bioinformatic Analysis and Post-Translational Modification Crosstalk Prediction of Lysine Acetylation
    • Lu ZK, Cheng ZY, Zhao YM, Volchenboum SL (2011) Bioinformatic Analysis and Post-Translational Modification Crosstalk Prediction of Lysine Acetylation. Plos One 6.
    • (2011) Plos One , vol.6
    • Lu, Z.K.1    Cheng, Z.Y.2    Zhao, Y.M.3    Volchenboum, S.L.4
  • 54
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of Cellular Metabolism by Protein Lysine Acetylation
    • Zhao SM, Xu W, Jiang WQ, 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.M.1    Xu, W.2    Jiang, W.Q.3    Yu, W.4    Lin, Y.5
  • 55
    • 0033635283 scopus 로고    scopus 로고
    • Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases
    • Yan Y, Barlev NA, Haley RH, Berger SL, Marmorstein R, (2000) Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases. Molecular Cell 6: 1195-1205.
    • (2000) Molecular Cell , vol.6 , pp. 1195-1205
    • Yan, Y.1    Barlev, N.A.2    Haley, R.H.3    Berger, S.L.4    Marmorstein, R.5
  • 56
    • 0030954208 scopus 로고    scopus 로고
    • GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein
    • Neuwald AF, Landsman D, (1997) GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends In Biochemical Sciences 22: 154-155.
    • (1997) Trends In Biochemical Sciences , vol.22 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 57
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim SC, Sprung R, Chen Y, Xu YD, Ball H, et al. (2006) Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Molecular Cell 23: 607-618.
    • (2006) Molecular Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3    Xu, Y.D.4    Ball, H.5
  • 60
    • 0033517354 scopus 로고    scopus 로고
    • Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide
    • Rojas JR, Trievel RC, Zhou JX, Mo Y, Li XM, et al. (1999) Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide. Nature 401: 93-98.
    • (1999) Nature , vol.401 , pp. 93-98
    • Rojas, J.R.1    Trievel, R.C.2    Zhou, J.X.3    Mo, Y.4    Li, X.M.5


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