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Volumn 1824, Issue 12, 2012, Pages 1366-1373

Investigation on PLK2 and PLK3 substrate recognition

Author keywords

CK2; Kinase; PLK1; PLK2; PLK3

Indexed keywords

AMINO ACID; BETA TUBULIN; CALRETICULIN; CALUMENIN; CASEIN KINASE II; GLUCOSE REGULATED PROTEIN 94; HEAT SHOCK PROTEIN 90; PHOSPHOPROTEIN; PHOSPHOPROTEOME; PHOSPHOTRANSFERASE; POLO LIKE KINASE 1; POLO LIKE KINASE 2; POLO LIKE KINASE 3; PROTEIN 14 3 3; PROTEIN 14 3 3 EPSILON; PROTEOME; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 84867668373     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.07.003     Document Type: Article
Times cited : (32)

References (32)
  • 1
    • 33750456519 scopus 로고    scopus 로고
    • Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • J.V. Olsen, B. Blagoev, F. Gnad, B. Macek, C. Kumar, P. Mortensen, and M. Mann Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 127 2006 635 648 (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 2
    • 78650156323 scopus 로고    scopus 로고
    • Variable contribution of protein kinases to the generation of the human phosphoproteome: A global weblogo analysis
    • M. Salvi, L. Cesaro, and L.A. Pinna Variable contribution of protein kinases to the generation of the human phosphoproteome: a global weblogo analysis Biomol. Concepts 2 2010 185 196
    • (2010) Biomol. Concepts , vol.2 , pp. 185-196
    • Salvi, M.1    Cesaro, L.2    Pinna, L.A.3
  • 3
    • 67349211782 scopus 로고    scopus 로고
    • Extraordinary pleiotropy of protein kinase CK2 revealed by weblogo phosphoproteome analysis
    • M. Salvi, S. Sarno, L. Cesaro, H. Nakamura, and L.A. Pinna Extraordinary pleiotropy of protein kinase CK2 revealed by weblogo phosphoproteome analysis Biochim. Biophys. Acta 1793 2009 847 859
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 847-859
    • Salvi, M.1    Sarno, S.2    Cesaro, L.3    Nakamura, H.4    Pinna, L.A.5
  • 4
    • 0030581751 scopus 로고    scopus 로고
    • How do protein kinases recognize their substrates?
    • L.A. Pinna, and M. Ruzzene How do protein kinases recognize their substrates? Biochim. Biophys. Acta 1314 1996 191 225
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 191-225
    • Pinna, L.A.1    Ruzzene, M.2
  • 5
    • 34548058372 scopus 로고    scopus 로고
    • Pharmacological and functional comparison of the polo-like kinase family: Insight into inhibitor and substrate specificity
    • DOI 10.1021/bi7008745
    • E.F. Johnson, K.D. Stewart, K.W. Woods, V.L. Giranda, and Y. Luo Pharmacological and functional comparison of the polo-like kinase family: insight into inhibitor and substrate specificity Biochemistry 46 2007 9551 9563 (Pubitemid 47291962)
    • (2007) Biochemistry , vol.46 , Issue.33 , pp. 9551-9563
    • Johnson, E.F.1    Stewart, K.D.2    Woods, K.W.3    Giranda, V.L.4    Luo, Y.5
  • 7
    • 79952607437 scopus 로고    scopus 로고
    • The substrates of Plk1, beyond the functions in mitosis
    • X.S. Liu, B. Song, and X. Liu The substrates of Plk1, beyond the functions in mitosis Protein Cell 1 2010 999 1010
    • (2010) Protein Cell , vol.1 , pp. 999-1010
    • Liu, X.S.1    Song, B.2    Liu, X.3
  • 8
    • 79959696118 scopus 로고    scopus 로고
    • PLK1 as an oncology target: Current status and future potential
    • C. McInnes, and M.D. Wyatt PLK1 as an oncology target: current status and future potential Drug Discov. Today 16 2011 619 625
    • (2011) Drug Discov. Today , vol.16 , pp. 619-625
    • McInnes, C.1    Wyatt, M.D.2
  • 9
    • 84859815885 scopus 로고    scopus 로고
    • Combination of chemical genetics and phosphoproteomics for kinase signaling analysis enables confident identification of cellular downstream targets
    • O111.012351
    • F.S. Oppermann, K. Grundner-Culemann, C. Kumar, O.J. Gruss, P.V. Jallepalli, and H. Daub Combination of chemical genetics and phosphoproteomics for kinase signaling analysis enables confident identification of cellular downstream targets Mol. Cell. Proteomics 11 2012 O111.012351
    • (2012) Mol. Cell. Proteomics , vol.11
    • Oppermann, F.S.1    Grundner-Culemann, K.2    Kumar, C.3    Gruss, O.J.4    Jallepalli, P.V.5    Daub, H.6
  • 10
    • 62849123093 scopus 로고    scopus 로고
    • Polo-like kinases: Conservation and divergence in their functions and regulation
    • V. Archambault, and D.M. Glover Polo-like kinases: conservation and divergence in their functions and regulation Nat. Rev. Mol. Cell Biol. 10 2009 265 275
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 265-275
    • Archambault, V.1    Glover, D.M.2
  • 11
    • 13244249573 scopus 로고    scopus 로고
    • Polo-like kinases in the nervous system
    • DOI 10.1038/sj.onc.1208277
    • D.P. Seeburg, D. Pak, and M. Sheng Polo-like kinases in the nervous system Oncogene 24 2005 292 298 (Pubitemid 40188610)
    • (2005) Oncogene , vol.24 , Issue.2 , pp. 292-298
    • Seeburg, D.P.1    Pak, D.2    Sheng, M.3
  • 12
    • 77955167321 scopus 로고    scopus 로고
    • Multifaceted polo-like kinases: Drug targets and antitargets for cancer therapy
    • K. Strebhardt Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy Nat. Rev. Drug Discov. 9 2010 643 660
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 643-660
    • Strebhardt, K.1
  • 13
    • 84856507495 scopus 로고    scopus 로고
    • Superiority of PLK-2 as α-synuclein phosphorylating agent relies on unique specificity determinants
    • M. Salvi, E. Trashi, O. Marin, A. Negro, S. Sarno, and L.A. Pinna Superiority of PLK-2 as α-synuclein phosphorylating agent relies on unique specificity determinants Biochem. Biophys. Res. Commun. 418 2012 156 160
    • (2012) Biochem. Biophys. Res. Commun. , vol.418 , pp. 156-160
    • Salvi, M.1    Trashi, E.2    Marin, O.3    Negro, A.4    Sarno, S.5    Pinna, L.A.6
  • 15
    • 33744955439 scopus 로고    scopus 로고
    • Mutations affecting β-tubulin folding and degradation
    • DOI 10.1074/jbc.M513730200
    • Y. Wang, G. Tian, N.J. Cowan, and F. Cabral Mutations affecting beta-tubulin folding and degradation J. Biol. Chem. 281 2006 13628 13635 (Pubitemid 43855278)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.19 , pp. 13628-13635
    • Wang, Y.1    Tian, G.2    Cowan, N.J.3    Cabral, F.4
  • 16
    • 54949129419 scopus 로고    scopus 로고
    • ProteoWizard: Open source software for rapid proteomics tools development
    • D. Kessner, M. Chambers, R. Burke, D. Agus, and P. Mallick ProteoWizard: open source software for rapid proteomics tools development Bioinformatics 24 2008 2534 2536
    • (2008) Bioinformatics , vol.24 , pp. 2534-2536
    • Kessner, D.1    Chambers, M.2    Burke, R.3    Agus, D.4    Mallick, P.5
  • 17
    • 34248640261 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides using titanium dioxide
    • DOI 10.1038/nprot.2006.185, PII NPROT.2006.185
    • T.E. Thingholm, T.J. Jorgensen, O.N. Jensen, and M.R. Larsen Highly selective enrichment of phosphorylated peptides using titanium dioxide Nat. Protoc. 1 2006 1929 1935 (Pubitemid 46773313)
    • (2006) Nature Protocols , vol.1 , Issue.4 , pp. 1929-1935
    • Thingholm, T.E.1    Jorgensen, T.J.D.2    Jensen, O.L.3    Larsen, M.R.4
  • 19
    • 38049184709 scopus 로고    scopus 로고
    • Elucidation of the ribonuclease A aggregation process mediated by 3D domain swapping: A computational approach reveals possible new multimeric structures
    • G. Cozza, S. Moro, and G. Gotte Elucidation of the ribonuclease A aggregation process mediated by 3D domain swapping: a computational approach reveals possible new multimeric structures Biopolymers 89 2008 26 39
    • (2008) Biopolymers , vol.89 , pp. 26-39
    • Cozza, G.1    Moro, S.2    Gotte, G.3
  • 20
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • DOI 10.1006/jmbi.1999.3091
    • D.T. Jones Protein secondary structure prediction based on position-specific scoring matrices J. Mol. Biol. 292 1999 195 202 (Pubitemid 29435759)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 22
    • 30044441052 scopus 로고    scopus 로고
    • KESTREL: A powerful method for identifying the physiological substrates of protein kinases
    • DOI 10.1042/BJ20051545
    • P. Cohen, and A. Knebel KESTREL: a powerful method for identifying the physiological substrates of protein kinases Biochem. J. 393 2006 1 6 (Pubitemid 43049297)
    • (2006) Biochemical Journal , vol.393 , Issue.1 , pp. 1-6
    • Cohen, P.1    Knebelt, A.2
  • 23
    • 36549017624 scopus 로고    scopus 로고
    • Identification of the flavoprotein of succinate dehydrogenase and aconitase as in vitro mitochondrial substrates of Fgr tyrosine kinase
    • DOI 10.1016/j.febslet.2007.11.005, PII S0014579307011350
    • M. Salvi, N.A. Morrice, A.M. Brunati, and A. Toninello Identification of the flavoprotein of succinate dehydrogenase and aconitase as in vitro mitochondrial substrates of Fgr tyrosine kinase FEBS Lett. 581 2007 5579 5585 (Pubitemid 350179765)
    • (2007) FEBS Letters , vol.581 , Issue.29 , pp. 5579-5585
    • Salvi, M.1    Morrice, N.A.2    Brunati, A.M.3    Toninello, A.4
  • 24
    • 23944477376 scopus 로고    scopus 로고
    • Searching for biomarkers of Aurora-A kinase activity: Identification of in vitro substrates through a modified KESTREL approach
    • DOI 10.1021/pr050018e
    • S. Troiani, M. Uggeri, J. Moll, A. Isacchi, H.M. Kalisz, L. Rusconi, and B. Valsasina Searching for biomarkers of Aurora-A kinase activity: identification of in vitro substrates through a modified KESTREL approach J. Proteome Res. 4 2005 1296 1303 (Pubitemid 41208684)
    • (2005) Journal of Proteome Research , vol.4 , Issue.4 , pp. 1296-1303
    • Troiani, S.1    Uggeri, M.2    Moll, J.3    Isacchi, A.4    Kalisz, H.M.5    Rusconi, L.6    Valsasina, B.7
  • 25
    • 13244249573 scopus 로고    scopus 로고
    • Polo-like kinases in the nervous system
    • DOI 10.1038/sj.onc.1208277
    • D.P. Seeburg, D. Pak, and M. Sheng Polo-like kinases in the nervous system Oncogene 24 2005 292 298 (Pubitemid 40188610)
    • (2005) Oncogene , vol.24 , Issue.2 , pp. 292-298
    • Seeburg, D.P.1    Pak, D.2    Sheng, M.3
  • 27
    • 0033561274 scopus 로고    scopus 로고
    • Association of polo-like kinase with α-, β- and γ-tubulins in a stable complex
    • DOI 10.1042/0264-6021:3390435
    • Y. Feng, D.R. Hodge, G. Palmieri, D.L. Chase, D.L. Longo, and D.K. Ferris Association of polo-like kinase with alpha-, beta- and gamma-tubulins in a stable complex Biochem. J. 339 1999 435 442 (Pubitemid 29209976)
    • (1999) Biochemical Journal , vol.339 , Issue.2 , pp. 435-442
    • Feng, Y.1    Hodge, D.R.2    Palmieri, G.3    Chase, D.L.4    Longo, D.L.5    Ferris, D.K.6
  • 29
    • 0023036184 scopus 로고
    • Site specificity of casein kinase-2 (TS) from rat liver cytosol. A study with model peptide substrates
    • DOI 10.1111/j.1432-1033.1986.tb09962.x
    • O. Marin, F. Meggio, F. Marchiori, G. Borin, and L.A. Pinna Site specificity of casein kinase-2 (TS) from rat liver cytosol. A study with model peptide substrates Eur. J. Biochem. 160 1986 239 244 (Pubitemid 17070502)
    • (1986) European Journal of Biochemistry , vol.160 , Issue.2 , pp. 239-244
    • Marin, O.1    Meggio, F.2    Marchiori, F.3
  • 31
    • 17544377840 scopus 로고    scopus 로고
    • Protein kinase CK2 mutants defective in substrate recognition: Purification and kinetic analysis
    • DOI 10.1074/jbc.271.18.10595
    • S. Sarno, P. Vaglio, F. Meggio, O.G. Issinger, and L.A. Pinna Protein kinase CK2 mutants defective in substrate recognition. Purification and kinetic analysis J. Biol. Chem. 271 1996 10595 10601 (Pubitemid 26145793)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.18 , pp. 10595-10601
    • Sarno, S.1    Vaglio, P.2    Meggio, F.3    Issinger, O.-G.4    Pinna, L.A.5
  • 32
    • 0030817009 scopus 로고    scopus 로고
    • Mutational analysis of residues implicated in the interaction between protein kinase CK2 and peptide substrates
    • DOI 10.1021/bi9705772
    • S. Sarno, P. Vaglio, O. Marin, O.G. Issinger, K. Ruffato, and L.A. Pinna Mutational analysis of residues implicated in the interaction between protein kinase CK2 and peptide substrates Biochemistry 36 1997 11717 11724 (Pubitemid 27424096)
    • (1997) Biochemistry , vol.36 , Issue.39 , pp. 11717-11724
    • Sarno, S.1    Vaglio, P.2    Marin, O.3    Issinger, O.-G.4    Ruffato, K.5    Pinna, L.A.6


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