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Volumn 2013, Issue , 2013, Pages

The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: Version 2.0 update

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOPROTEIN; PROTEOME; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84885896190     PISSN: 17580463     EISSN: None     Source Type: Journal    
DOI: 10.1093/database/bat026     Document Type: Article
Times cited : (89)

References (50)
  • 1
    • 33745813187 scopus 로고    scopus 로고
    • Reading protein modifications with interaction domains
    • Seet,B.T., Dikic,I., Zhou,M.M. et al. (2006) Reading protein modifications with interaction domains. Nat. Rev. Mol. Cell Biol., 7, 473-483.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 473-483
    • Seet, B.T.1    Dikic, I.2    Zhou, M.M.3
  • 2
    • 78651296878 scopus 로고    scopus 로고
    • PhosphoGRID: A database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae
    • Stark,C., Su,T.C., Breitkreutz,A. et al. (2010) PhosphoGRID: a database of experimentally verified in vivo protein phosphorylation sites from the budding yeast Saccharomyces cerevisiae. Database, 2010, bap026.
    • (2010) Database , vol.2010
    • Stark, C.1    Su, T.C.2    Breitkreutz, A.3
  • 3
    • 34248576306 scopus 로고    scopus 로고
    • NetPhosYeast: Prediction of protein phosphorylation sites in yeast
    • Ingrell,C.R., Miller,M.L., Jensen,O.N. et al. (2007) NetPhosYeast: prediction of protein phosphorylation sites in yeast. Bioinformatics, 23, 895-897.
    • (2007) Bioinformatics , vol.23 , pp. 895-897
    • Ingrell, C.R.1    Miller, M.L.2    Jensen, O.N.3
  • 4
    • 84858588614 scopus 로고    scopus 로고
    • Saccharomyces genome database: The genomics resource of budding yeast
    • Cherry,J.M., Hong,E.L., Amundsen,C. et al. (2012) Saccharomyces genome database: the genomics resource of budding yeast. Nucleic Acids Res., 40, D700-D705.
    • (2012) Nucleic Acids Res. , vol.40
    • Cherry, J.M.1    Hong, E.L.2    Amundsen, C.3
  • 5
    • 84857745267 scopus 로고    scopus 로고
    • Database resources of the National Center for Biotechnology Information
    • Sayers,E.W., Barrett,T., Benson,D.A. et al. (2012) Database resources of the National Center for Biotechnology Information. Nucleic Acids Res., 40, D13-D25.
    • (2012) Nucleic Acids Res. , vol.40
    • Sayers, E.W.1    Barrett, T.2    Benson, D.A.3
  • 6
    • 9144256665 scopus 로고    scopus 로고
    • Saccharomyces genome database (SGD) provides tools to identify and analyze sequences from Saccharomyces cerevisiae and related sequences from other organisms
    • Christie,K.R., Weng,S., Balakrishnan,R. et al. (2004) Saccharomyces genome database (SGD) provides tools to identify and analyze sequences from Saccharomyces cerevisiae and related sequences from other organisms. Nucleic Acids Res., 32, D311-D314.
    • (2004) Nucleic Acids Res. , vol.32
    • Christie, K.R.1    Weng, S.2    Balakrishnan, R.3
  • 7
    • 33644873683 scopus 로고    scopus 로고
    • The YEASTRACT database: A tool for the analysis of transcription regulatory associations in Saccharomyces cerevisiae
    • Teixeira,M.C., Monteiro,P., Jain,P. et al. (2006) The YEASTRACT database: a tool for the analysis of transcription regulatory associations in Saccharomyces cerevisiae. Nucleic Acids Res., 34, D446-D451.
    • (2006) Nucleic Acids Res. , vol.34
    • Teixeira, M.C.1    Monteiro, P.2    Jain, P.3
  • 8
    • 84908504908 scopus 로고    scopus 로고
    • Transparent mediation-based access to multiple yeast data sources using an ontology driven interface
    • Briache,A., Marrakchi,K., Kerzazi,A. et al. (2011) Transparent mediation-based access to multiple yeast data sources using an ontology driven interface. BMC Bioinformatics, 13 (Suppl. 1), S7.
    • (2011) BMC Bioinformatics , vol.13 , Issue.SUPPL. 1
    • Briache, A.1    Marrakchi, K.2    Kerzazi, A.3
  • 10
    • 69249240179 scopus 로고    scopus 로고
    • Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis
    • Huber,A., Bodenmiller,B., Uotila,A. et al. (2009) Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis. Genes Dev., 23, 1929-1943.
    • (2009) Genes Dev. , vol.23 , pp. 1929-1943
    • Huber, A.1    Bodenmiller, B.2    Uotila, A.3
  • 11
    • 77958031723 scopus 로고    scopus 로고
    • The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates
    • Soulard,A., Cremonesi,A., Moes,S. et al. (2010) The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates. Mol. Biol. Cell, 21, 3475-3486.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3475-3486
    • Soulard, A.1    Cremonesi, A.2    Moes, S.3
  • 12
    • 70349546862 scopus 로고    scopus 로고
    • Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution
    • Holt,L.J., Tuch,B.B., Villen,J. et al. (2009) Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science, 325, 1682-1686.
    • (2009) Science , vol.325 , pp. 1682-1686
    • Holt, L.J.1    Tuch, B.B.2    Villen, J.3
  • 13
    • 77953077420 scopus 로고    scopus 로고
    • A global protein kinase and phosphatase interaction network in yeast
    • Breitkreutz,A., Choi,H., Sharom,J.R. et al. (2010) A global protein kinase and phosphatase interaction network in yeast. Science, 328, 1043-1046.
    • (2010) Science , vol.328 , pp. 1043-1046
    • Breitkreutz, A.1    Choi, H.2    Sharom, J.R.3
  • 14
    • 70349972517 scopus 로고    scopus 로고
    • Global analysis of the yeast osmotic stress response by quantitative proteomics
    • Soufi,B., Kelstrup,C.D., Stoehr,G. et al. (2009) Global analysis of the yeast osmotic stress response by quantitative proteomics. Mol. Biosyst., 5, 1337-1346.
    • (2009) Mol. Biosyst. , vol.5 , pp. 1337-1346
    • Soufi, B.1    Kelstrup, C.D.2    Stoehr, G.3
  • 15
    • 77951219621 scopus 로고    scopus 로고
    • A proteome-wide analysis of kinase-substrate network in the DNA damage response
    • Chen,S.H., Albuquerque,C.P., Liang,J. et al. (2010) A proteome-wide analysis of kinase-substrate network in the DNA damage response. J. Biol. Chem., 285, 12803-12812.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12803-12812
    • Chen, S.H.1    Albuquerque, C.P.2    Liang, J.3
  • 16
    • 78649563648 scopus 로고    scopus 로고
    • Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels
    • Helbig,A.O., Rosati,S., Pijnappel,P.W. et al. (2011) Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels. BMC Genomics, 11, 685.
    • (2011) BMC Genomics , vol.11 , pp. 685
    • Helbig, A.O.1    Rosati, S.2    Pijnappel, P.W.3
  • 17
    • 78650632764 scopus 로고    scopus 로고
    • Phosphoproteomic analysis reveals interconnected system-wide responses to perturbations of kinases and phosphatases in yeast
    • Bodenmiller,B., Wanka,S., Kraft,C. et al. (2010) Phosphoproteomic analysis reveals interconnected system-wide responses to perturbations of kinases and phosphatases in yeast. Sci, Signal., 3, rs4.
    • (2010) Sci, Signal. , vol.3
    • Bodenmiller, B.1    Wanka, S.2    Kraft, C.3
  • 18
    • 78149462002 scopus 로고    scopus 로고
    • Mec1 is one of multiple kinases that prime the Mcm2-7 helicase for phosphorylation by Cdc7
    • Randell,J.C., Fan,A., Chan,C. et al. (2010) Mec1 is one of multiple kinases that prime the Mcm2-7 helicase for phosphorylation by Cdc7. Mol. Cell, 40, 353-363.
    • (2010) Mol. Cell , vol.40 , pp. 353-363
    • Randell, J.C.1    Fan, A.2    Chan, C.3
  • 19
    • 78649299852 scopus 로고    scopus 로고
    • Activation of Atg1 kinase in autophagy by regulated phosphorylation
    • Kijanska,M., Dohnal,I., Reiter,W. et al. (2010) Activation of Atg1 kinase in autophagy by regulated phosphorylation. Autophagy, 6, 1168-11678.
    • (2010) Autophagy , vol.6 , pp. 1168-11678
    • Kijanska, M.1    Dohnal, I.2    Reiter, W.3
  • 20
    • 79959947319 scopus 로고    scopus 로고
    • The identification and analysis of phosphorylation sites on the Atg1 protein kinase
    • Yeh,Y.Y., Shah,K.H., Chou,C.C. et al. (2011) The identification and analysis of phosphorylation sites on the Atg1 protein kinase. Autophagy, 7, 716-726.
    • (2011) Autophagy , vol.7 , pp. 716-726
    • Yeh, Y.Y.1    Shah, K.H.2    Chou, C.C.3
  • 21
    • 77957149919 scopus 로고    scopus 로고
    • Checkpoint-dependent inhibition of DNA replication initiation by Sld3 and Dbf4 phosphorylation
    • Zegerman,P. and Diffley,J.F. (2010) Checkpoint-dependent inhibition of DNA replication initiation by Sld3 and Dbf4 phosphorylation. Nature, 467, 474-478.
    • (2010) Nature , vol.467 , pp. 474-478
    • Zegerman, P.1    Diffley, J.F.2
  • 22
    • 77950560161 scopus 로고    scopus 로고
    • Rec8 phosphorylation by casein kinase 1 and Cdc7-Dbf4 kinase regulates cohesin cleavage by separase during meiosis
    • Katis,V.L., Lipp,J.J., Imre,R. et al. (2010) Rec8 phosphorylation by casein kinase 1 and Cdc7-Dbf4 kinase regulates cohesin cleavage by separase during meiosis. Dev. Cell, 18, 397-409.
    • (2010) Dev. Cell , vol.18 , pp. 397-409
    • Katis, V.L.1    Lipp, J.J.2    Imre, R.3
  • 23
    • 77953789728 scopus 로고    scopus 로고
    • Pho85 kinase, a cyclin-dependent kinase, regulates nuclear accumulation of the Rim101 transcription factor in the stress response of Saccharomyces cerevisiae
    • Nishizawa,M., Tanigawa,M., Hayashi,M. et al. (2010) Pho85 kinase, a cyclin-dependent kinase, regulates nuclear accumulation of the Rim101 transcription factor in the stress response of Saccharomyces cerevisiae. Eukaryot. Cell, 9, 943-951.
    • (2010) Eukaryot. Cell , vol.9 , pp. 943-951
    • Nishizawa, M.1    Tanigawa, M.2    Hayashi, M.3
  • 24
    • 77955476243 scopus 로고    scopus 로고
    • DNA damage signaling recruits the Rtt107-Slx4 scaffolds via Dpb11 to mediate replication stress response
    • Ohouo,P.Y., Bastos de Oliveira,F.M., Almeida,B.S. et al. (2010) DNA damage signaling recruits the Rtt107-Slx4 scaffolds via Dpb11 to mediate replication stress response. Mol. Cell, 39, 300-306.
    • (2010) Mol. Cell , vol.39 , pp. 300-306
    • Ohouo, P.Y.1    Bastos De Oliveira, F.M.2    Almeida, B.S.3
  • 25
    • 77957143899 scopus 로고    scopus 로고
    • Cyclin-dependent kinase promotes formation of the synaptonemal complex in yeast meiosis
    • Zhu,Z., Mori,S., Oshiumi,H. et al. (2010) Cyclin-dependent kinase promotes formation of the synaptonemal complex in yeast meiosis. Genes Cells, 15, 1036-1050.
    • (2010) Genes Cells , vol.15 , pp. 1036-1050
    • Zhu, Z.1    Mori, S.2    Oshiumi, H.3
  • 26
    • 79952271588 scopus 로고    scopus 로고
    • Genetic requirements and meiotic function of phosphorylation of the yeast axial element protein Red1
    • Lai,Y.J., Lin,F.M., Chuang,M.J. et al. (2010) Genetic requirements and meiotic function of phosphorylation of the yeast axial element protein Red1. Mol. Cell Biol., 31, 912-923.
    • (2010) Mol. Cell Biol. , vol.31 , pp. 912-923
    • Lai, Y.J.1    Lin, F.M.2    Chuang, M.J.3
  • 27
    • 79953192187 scopus 로고    scopus 로고
    • Casein kinase II-mediated phosphorylation of general repressor Maf1 triggers RNA polymerase III activation
    • Graczyk,D., Debski,J., Muszynska,G. et al . (2011) Casein kinase II-mediated phosphorylation of general repressor Maf1 triggers RNA polymerase III activation. Proc. Natl. Acad. Sci. USA, 108, 4926-4931.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 4926-4931
    • Graczyk, D.1    Debski, J.2    Muszynska, G.3
  • 28
    • 77957144885 scopus 로고    scopus 로고
    • Damage-induced phosphorylation of Sld3 is important to block late origin firing
    • Lopez-Mosqueda,J., Maas,N.L., Jonsson,Z.O. et al. (2010) Damage-induced phosphorylation of Sld3 is important to block late origin firing. Nature, 467, 479-483.
    • (2010) Nature , vol.467 , pp. 479-483
    • Lopez-Mosqueda, J.1    Maas, N.L.2    Jonsson, Z.O.3
  • 29
    • 77957766550 scopus 로고    scopus 로고
    • Uniform transitions of the general RNA polymerase II transcription complex
    • Mayer,A., Lidschreiber,M., Siebert,M. et al. (2010) Uniform transitions of the general RNA polymerase II transcription complex. Nat. Struct. Mol. Biol., 17, 1272-1278.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1272-1278
    • Mayer, A.1    Lidschreiber, M.2    Siebert, M.3
  • 30
    • 77957786100 scopus 로고    scopus 로고
    • Gene-specific RNA polymerase II phosphorylation and the CTD code
    • Kim,H., Erickson,B., Luo,W. et al. (2010) Gene-specific RNA polymerase II phosphorylation and the CTD code. Nat. Struct. Mol. Biol., 17, 1279-1286.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1279-1286
    • Kim, H.1    Erickson, B.2    Luo, W.3
  • 31
    • 70350389837 scopus 로고    scopus 로고
    • Phosphorylation of the yeast Rpb1 C-terminal domain at serines 2, 5, and 7
    • Kim,M., Suh,H., Cho,E.J. et al. (2009) Phosphorylation of the yeast Rpb1 C-terminal domain at serines 2, 5, and 7. J. Biol. Chem., 284, 26421-26426.
    • (2009) J. Biol. Chem. , vol.284 , pp. 26421-26426
    • Kim, M.1    Suh, H.2    Cho, E.J.3
  • 32
    • 65549156025 scopus 로고    scopus 로고
    • TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II
    • Akhtar,M.S., Heidemann,M., Tietjen,J.R. et al. (2009) TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II. Mol. Cell, 34, 387-393.
    • (2009) Mol. Cell , vol.34 , pp. 387-393
    • Akhtar, M.S.1    Heidemann, M.2    Tietjen, J.R.3
  • 33
    • 68849086180 scopus 로고    scopus 로고
    • Phosphorylation of the transcription elongation factor Spt5 by yeast Bur1 kinase stimulates recruitment of the PAF complex
    • Liu,Y., Warfield,L., Zhang,C. et al. (2009) Phosphorylation of the transcription elongation factor Spt5 by yeast Bur1 kinase stimulates recruitment of the PAF complex. Mol. Cell Biol., 29, 4852-4863.
    • (2009) Mol. Cell Biol. , vol.29 , pp. 4852-4863
    • Liu, Y.1    Warfield, L.2    Zhang, C.3
  • 34
    • 78651320816 scopus 로고    scopus 로고
    • Phospho.ELM: A database of phosphorylation sites-update 2011
    • Dinkel,H., Chica,C., Via,A. et al. (2011) Phospho.ELM: a database of phosphorylation sites-update 2011. Nucleic Acids Res., 39, D261-D267.
    • (2011) Nucleic Acids Res. , vol.39
    • Dinkel, H.1    Chica, C.2    Via, A.3
  • 35
    • 84862321080 scopus 로고    scopus 로고
    • Evaluation and properties of the budding yeast phosphoproteome
    • Amoutzias,G.D., He,Y., Lilley,K.S. et al. (2012) Evaluation and properties of the budding yeast phosphoproteome. Mol. Cell Proteomics, 11, M111 009555.
    • (2012) Mol. Cell Proteomics , vol.11
    • Amoutzias, G.D.1    He, Y.2    Lilley, K.S.3
  • 36
    • 67649972198 scopus 로고    scopus 로고
    • Evolution of phosphoregulation: Comparison of phosphorylation patterns across yeast species
    • Beltrao,P., Trinidad,J.C., Fiedler,D. et al. (2009) Evolution of phosphoregulation: comparison of phosphorylation patterns across yeast species. PLoS Biol., 7, e1000134.
    • (2009) PLoS Biol. , vol.7
    • Beltrao, P.1    Trinidad, J.C.2    Fiedler, D.3
  • 37
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami,S., Huh,W.K., Bower,K. et al. (2003) Global analysis of protein expression in yeast. Nature, 425, 737-741.
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1    Huh, W.K.2    Bower, K.3
  • 38
    • 33746631391 scopus 로고    scopus 로고
    • Evolutionary and physiological importance of hub proteins
    • Batada,N.N., Hurst,L.D. and Tyers,M. (2006) Evolutionary and physiological importance of hub proteins. PLoS Comput. Biol., 2, e88.
    • (2006) PLoS Comput. Biol. , vol.2
    • Batada, N.N.1    Hurst, L.D.2    Tyers, M.3
  • 39
    • 84856786805 scopus 로고    scopus 로고
    • Cdk8 regulates stability of the transcription factor Phd1 to control pseudohyphal differentiation of Saccharomyces cerevisiae
    • Raithatha,S., Su,T.C., Lourenco,P. et al. (2012) Cdk8 regulates stability of the transcription factor Phd1 to control pseudohyphal differentiation of Saccharomyces cerevisiae. Mol. Cell Biol., 32, 664-674.
    • (2012) Mol. Cell Biol. , vol.32 , pp. 664-674
    • Raithatha, S.1    Su, T.C.2    Lourenco, P.3
  • 40
    • 70349308508 scopus 로고    scopus 로고
    • Cell regulation: Determined to signal discrete cooperation
    • Gibson,T.J. (2009) Cell regulation: determined to signal discrete cooperation. Trends Biochem. Sci., 34, 471-482.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 471-482
    • Gibson, T.J.1
  • 41
    • 15944377809 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway
    • Gruhler,A., Olsen,J.V., Mohammed,S. et al. (2005) Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway. Mol. Cell Proteomics, 4, 310-327.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 310-327
    • Gruhler, A.1    Olsen, J.V.2    Mohammed, S.3
  • 42
    • 77952986553 scopus 로고    scopus 로고
    • Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs
    • Mok,J., Kim,P.M., Lam,H.Y. et al. (2012) Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs. Sci. Signal., 3, ra12.
    • (2012) Sci. Signal. , vol.3
    • Mok, J.1    Kim, P.M.2    Lam, H.Y.3
  • 43
    • 84872779494 scopus 로고    scopus 로고
    • Protein Ser/Thr phosphatases - The ugly ducklings of cell signalling
    • Brautigan,D.L. (2013) Protein Ser/Thr phosphatases - the ugly ducklings of cell signalling. FEBS J., 280, 324-345.
    • (2013) FEBS J. , vol.280 , pp. 324-345
    • Brautigan, D.L.1
  • 44
    • 65349155149 scopus 로고    scopus 로고
    • Weak functional constraints on phosphoproteomes
    • Landry,C.R., Levy,E.D. and Michnick,S.W. (2009) Weak functional constraints on phosphoproteomes. Trends Genet., 25, 193-197.
    • (2009) Trends Genet. , vol.25 , pp. 193-197
    • Landry, C.R.1    Levy, E.D.2    Michnick, S.W.3
  • 45
    • 0030445778 scopus 로고    scopus 로고
    • Tripping the switch fantastic: How a protein kinase cascade can convert graded inputs into switch-like outputs
    • Ferrell,J.E. Jr (1996) Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs. Trends Biochem. Sci., 21, 460-466.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 460-466
    • Ferrell Jr., J.E.1
  • 46
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation-a 25 year update
    • Cohen,P. (2000) The regulation of protein function by multisite phosphorylation-a 25 year update. Trends Biochem. Sci., 25, 596-601.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 596-601
    • Cohen, P.1
  • 47
    • 0035969550 scopus 로고    scopus 로고
    • Six steps to destruction
    • Ferrell,J.E. Jr (2001) Six steps to destruction. Nature, 414, 498-499.
    • (2001) Nature , vol.414 , pp. 498-499
    • Ferrell Jr., J.E.1
  • 48
    • 0036532226 scopus 로고    scopus 로고
    • Self-perpetuating states in signal transduction: Positive feedback, double-negative feedback and bistability
    • Ferrell,J.E. Jr (2002) Self-perpetuating states in signal transduction: positive feedback, double-negative feedback and bistability. Curr. Opin. Cell Biol., 14, 140-148.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 140-148
    • Ferrell Jr., J.E.1
  • 49
    • 33947304756 scopus 로고    scopus 로고
    • Substrate competition as a source of ultrasensitivity in the inactivation of Wee1
    • Kim,S.Y. and Ferrell,J.E. Jr (2007) Substrate competition as a source of ultrasensitivity in the inactivation of Wee1. Cell, 128, 1133-1145.
    • (2007) Cell , vol.128 , pp. 1133-1145
    • Kim, S.Y.1    Ferrell Jr., J.E.2
  • 50
    • 84857698871 scopus 로고    scopus 로고
    • Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligase
    • Tang,X., Orlicky,S., Mittag,T. et al. (2012) Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligase. Proc. Natl. Acad. Sci. USA, 109, 3287-3292.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 3287-3292
    • Tang, X.1    Orlicky, S.2    Mittag, T.3


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