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Volumn 9, Issue 5, 2014, Pages

Characterization of protein phosphatase 5 from three lepidopteran insects: Helicoverpa armigera, Mythimna separata and Plutella xylostella

Author keywords

[No Author keywords available]

Indexed keywords

ARACHIDONIC ACID; CANTHARIDIN; COMPLEMENTARY DNA; OKADAIC ACID; PHOSPHATASE; PROTEIN PHOSPHATASE 5; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; DICARBOXYLIC ACID; ENDOTHALL; NUCLEAR PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PRIMER DNA;

EID: 84901265355     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0097437     Document Type: Article
Times cited : (7)

References (25)
  • 1
    • 0032988329 scopus 로고    scopus 로고
    • Protein phosphorylation and signal transduction
    • DOI 10.1016/S0163-7258(98)00056-4, PII S0163725898000564
    • Graves JD, Krebs EG (1999) Protein phosphorylation and signal transduction. Pharmacol Therapeut 82(2): 111-121. (Pubitemid 29255908)
    • (1999) Pharmacology and Therapeutics , vol.82 , Issue.2-3 , pp. 111-121
    • Graves, J.D.1    Krebs, E.G.2
  • 2
    • 17044391680 scopus 로고    scopus 로고
    • Overview of protein serine/threonine phosphatase
    • J Arino ed. (Berlin: Springer)
    • Cohen PTW (2004) Overview of protein serine/threonine phosphatase. In Protein Phosphatases, J Arino ed. (Berlin: Springer), 1-20.
    • (2004) Protein Phosphatases , pp. 1-20
    • Cohen, P.T.W.1
  • 3
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi Y (2009) Serine/threonine phosphatases: mechanism through structure. Cell 139(3): 468-484.
    • (2009) Cell , vol.139 , Issue.3 , pp. 468-484
    • Shi, Y.1
  • 4
    • 0031015069 scopus 로고    scopus 로고
    • Activation of protein phosphatase 5 by limited proteolysis or the binding of polyunsaturated fatty acids to the TPR domain
    • DOI 10.1016/S0014-5793(96)01427-5, PII S0014579396014275
    • Chen MX, Cohen PTW (1997) Activation of protein phosphatase 5 by limited proteolysis or the binding of polyunsaturated fatty acids to the TPR domain. FEBS Letters 400(1): 136-140. (Pubitemid 27046837)
    • (1997) FEBS Letters , vol.400 , Issue.1 , pp. 136-140
    • Chen, M.X.1    Cohen, P.T.W.2
  • 6
    • 0035807022 scopus 로고    scopus 로고
    • Identification of amino acids in the tetratricopeptide repeat and C-terminal domains of protein phosphatase 5 involved in autoinhibition and lipid activation
    • DOI 10.1021/bi010999i
    • Kang H, Sayner SL, Gross KL, Russell LC, Chinkers M (2001) Identification of amino acids in the tetratricopeptide repeat and C-terminal domains of protein phosphatase 5 involved in autoinhibition and lipid activation. Biochemistry 40(35): 10485-10490. (Pubitemid 32816658)
    • (2001) Biochemistry , vol.40 , Issue.35 , pp. 10485-10490
    • Kang, H.1    Sayner, S.L.2    Gross, K.L.3    Russell, L.C.4    Chinkers, M.5
  • 7
    • 13544267438 scopus 로고    scopus 로고
    • Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506
    • DOI 10.1021/bi048503v
    • Davies TH, Ning YM, Sánchez ER (2005) Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506. Biochemistry 44(6): 2030-2038. (Pubitemid 40223631)
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 2030-2038
    • Davies, T.H.1    Ning, Y.-M.2    Sanchez, E.R.3
  • 8
    • 43049097815 scopus 로고    scopus 로고
    • The role of serine/threonine protein phosphatase type 5 (PP5) in the regulation of stress-induced signaling networks and cancer
    • Golden T, Swingle M, Honkanen RE (2008) The role of serine/threonine protein phosphatase type 5 (PP5) in the regulation of stress-induced signaling networks and cancer. Cancer Metast Rev 27(2): 169-178.
    • (2008) Cancer Metast Rev , vol.27 , Issue.2 , pp. 169-178
    • Golden, T.1    Swingle, M.2    Honkanen, R.E.3
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72(1): 248-254.
    • (1976) Anal Biochem , vol.72 , Issue.1 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0025877838 scopus 로고
    • Inhibitory effect of okadaic acid on the p-nitrophenyl phosphate phosphatase activity of protein phosphatases
    • Takai A, Mieskes G (1991) Inhibitory effect of okadaic acid on the p-nitrophenyl phosphate phosphatase activity of protein phosphatases. Biochem J 275: 233-239.
    • (1991) Biochem J , vol.275 , pp. 233-239
    • Takai, A.1    Mieskes, G.2
  • 12
    • 84891457322 scopus 로고    scopus 로고
    • Cantharidin impedes the activity of protein serine/threonine phosphatase in Plutella xylostella
    • Chen X, Liu J, Zhang Y (2014) Cantharidin impedes the activity of protein serine/threonine phosphatase in Plutella xylostella. Mol BioSyst 10(2): 240-250.
    • (2014) Mol BioSyst , vol.10 , Issue.2 , pp. 240-250
    • Chen, X.1    Liu, J.2    Zhang, Y.3
  • 13
    • 0027944142 scopus 로고
    • Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis
    • Zhuo S, Clemens JC, Stone RL, Dixon JE (1994) Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis. J Biol Chem 269(42): 26234-26238.
    • (1994) J Biol Chem , vol.269 , Issue.42 , pp. 26234-26238
    • Zhuo, S.1    Clemens, J.C.2    Stone, R.L.3    Dixon, J.E.4
  • 14
    • 0029784483 scopus 로고    scopus 로고
    • Interactions between a minimal protein serine/threonine phosphatase and its phosphopeptide substrate sequence
    • DOI 10.1074/jbc.271.40.24401
    • Ansai T, Dupuy LC, Barik S (1996) Interactions between a minimal protein serine/threonine phosphatase and its phosphopeptides substrate sequence. J Biol Chem 271(40): 24401-24407. (Pubitemid 26333172)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.40 , pp. 24401-24407
    • Ansai, T.1    Dupuy, L.C.2    Barik, S.3
  • 15
    • 0034710179 scopus 로고    scopus 로고
    • Drosophila protein phosphatase 5 is encoded by a single gene that is most highly expressed during embryonic development
    • DOI 10.1016/S0167-4781(00)00105-6, PII S0167478100001056
    • Brown L, Borthwick EB, Cohen PTW (2000) Drosophila protein phosphatase 5 is encoded by a single gene that is most highly expressed during embryonic development. Biochim Biophys Acta 1492(2): 470-476. (Pubitemid 30427361)
    • (2000) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1492 , Issue.2-3 , pp. 470-476
    • Brown, L.1    Borthwick, E.B.2    Cohen, P.T.W.3
  • 16
    • 84890466192 scopus 로고    scopus 로고
    • Identification and biochemical characterization of protein phosphatase 5 from the cantharidin-producing blister beetle, Epicauta chinensis
    • Chen X, Lü S, Zhang Y (2013) Identification and biochemical characterization of protein phosphatase 5 from the cantharidin-producing blister beetle, Epicauta chinensis. Int J Mol Sci 14(12): 24501-24513.
    • (2013) Int J Mol Sci , vol.14 , Issue.12 , pp. 24501-24513
    • Chen, X.1    Lü, S.2    Zhang, Y.3
  • 17
    • 57749209868 scopus 로고    scopus 로고
    • Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: A novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors
    • Kelker MS, Page R, Peti W (2009) Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: A novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors. J Mol Biol 385(1): 11-21.
    • (2009) J Mol Biol , vol.385 , Issue.1 , pp. 11-21
    • Kelker, M.S.1    Page, R.2    Peti, W.3
  • 18
    • 0030928118 scopus 로고    scopus 로고
    • Purification of a fatty acid-stimulated protein-serine/threonine phosphatase from bovine brain and its identification as a homolog of protein phosphatase 5
    • DOI 10.1074/jbc.272.36.22464
    • Skinner J, Sinclair C, Romeo C, Armstrong D, Charbonneau H, et al. (1997) Purification of a fatty acid-stimulated protein-serine/threonine phosphatase from bovine brain and its identification as a homolog of protein phosphatase 5. J Biol Chem 272(36): 22464-22471. (Pubitemid 27386055)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.36 , pp. 22464-22471
    • Skinner, J.1    Sinclair, C.2    Romeo, C.3    Armstrong, D.4    Charbonneau, H.5    Rossie, S.6
  • 19
    • 0037046101 scopus 로고    scopus 로고
    • Identification and biochemical characterisation of a Protein Phosphatase 5 homologue from Plasmodium falciparum
    • PII S0166685102000075
    • Lindenthal C, Klinkert MQ (2002) Identification and biochemical characterisation of a protein phosphatase 5 homologue from Plasmodium falciparum. Mol Biochem Parasitol 120(2): 257-268. (Pubitemid 34233790)
    • (2002) Molecular and Biochemical Parasitology , vol.120 , Issue.2 , pp. 257-268
    • Lindenthal, C.1    Klinkert, M.-Q.2
  • 20
    • 0035925658 scopus 로고    scopus 로고
    • Cloning and characterization of a novel serine/threonine protein phosphatase type 5 from Trypanosoma brucei
    • Chaudhuri M (2001) Cloning and characterization of a novel serine/threonine protein phosphatase type 5 from Trypanosoma brucei. Gene 266(1): 1-13.
    • (2001) Gene , vol.266 , Issue.1 , pp. 1-13
    • Chaudhuri, M.1
  • 21
    • 4043101125 scopus 로고    scopus 로고
    • Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5
    • DOI 10.1074/jbc.M402855200
    • Swingle MR, Honkanen RE, Ciszak EM (2004) Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5. J Biol Chem 279(32): 33992-33999. (Pubitemid 39063050)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.32 , pp. 33992-33999
    • Swingle, M.R.1    Honkanen, R.E.2    Ciszak, E.M.3
  • 22
    • 0036032778 scopus 로고    scopus 로고
    • Regulators of serine/threonine protein phosphatases at the dawn of a clinical era
    • Honkanen RE, Golden T (2002) Regulators of serine/threonine protein phosphatases at the dawn of a clinical era? Curr Med Chem 9(22): 2055-2075. (Pubitemid 35256504)
    • (2002) Current Medicinal Chemistry , vol.9 , Issue.22 , pp. 2055-2075
    • Honkanen, R.E.1    Golden, T.2
  • 23
    • 84155167961 scopus 로고    scopus 로고
    • Validation of serine/threonine protein phosphatase as the herbicide target site of endothall
    • Bajsa J, Pan Z, Dayan FE, Owens DK, Duke SO (2012) Validation of serine/threonine protein phosphatase as the herbicide target site of endothall. Pestic Biochem Phys 102(1): 38-44.
    • (2012) Pestic Biochem Phys , vol.102 , Issue.1 , pp. 38-44
    • Bajsa, J.1    Pan, Z.2    Dayan, F.E.3    Owens, D.K.4    Duke, S.O.5
  • 24
    • 80052551301 scopus 로고    scopus 로고
    • Transcriptional responses to cantharidin, a protein phosphatase inhibitor, in Arabidopsis thaliana reveal the involvement of multiple signal transduction pathways
    • Bajsa J, Pan Z, Duke SO (2013) Transcriptional responses to cantharidin, a protein phosphatase inhibitor, in Arabidopsis thaliana reveal the involvement of multiple signal transduction pathways. Physiol Plantarum 143(2): 188-205.
    • (2013) Physiol Plantarum , vol.143 , Issue.2 , pp. 188-205
    • Bajsa, J.1    Pan, Z.2    Duke, S.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.