메뉴 건너뛰기




Volumn 21, Issue 1, 2010, Pages 9-17

Simultaneous protein expression and modification: An efficient approach for production of unphosphorylated and biotinylated receptor tyrosine kinases by triple infection in the baculovirus expression system

Author keywords

Biotin; Phosphatase; Phosphorylation

Indexed keywords

BIOTIN; BIOTIN LIGASE; INSULIN RECEPTOR; LIGASE; PHOSPHATASE; PHOSPHATASE YOPH; PHOSPHOTRANSFERASE; PROTEIN KINASE; PROTEIN LIGASE BIRA; SOMATOMEDIN C RECEPTOR; TYROSINE KINASE RECEPTOR; UNCLASSIFIED DRUG;

EID: 77953652923     PISSN: 15240215     EISSN: 19434731     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (35)
  • 1
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S. The protein kinase complement of the human genome. Science 2002; 298: 1912-1934. (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 2
    • 0037392444 scopus 로고    scopus 로고
    • Issues and progress with protein kinase inhibitors for cancer treatment
    • Dancey J, Sausville EA. Issues and progress with protein kinase inhibitors for cancer treatment. Nat Rev Drug Discov 2003; 2: 296-313. (Pubitemid 37361688)
    • (2003) Nature Reviews Drug Discovery , vol.2 , Issue.4 , pp. 296-313
    • Dancey, J.1    Sausville, E.A.2
  • 3
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases - The major drug targets of the twenty-first century?
    • Cohen P. Protein kinases - the major drug targets of the twenty- first century? Nat Rev Drug Discov 2002; 1: 309-315. (Pubitemid 37361447)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.4 , pp. 309-315
    • Cohen, P.1
  • 4
    • 44649180430 scopus 로고    scopus 로고
    • Challenges in design of biochemical assays for the identification ofsmall molecules to target multiple conformations of protein kinases
    • Chene P. Challenges in design of biochemical assays for the identification ofsmall molecules to target multiple conformations of protein kinases. Drug Discov Today 2008; 13: 522-529.
    • (2008) Drug Discov Today , vol.13 , pp. 522-529
    • Chene, P.1
  • 5
    • 34548825448 scopus 로고    scopus 로고
    • Targeting protein multiple conformations: A structure-based strategy for kinase drug design
    • DOI 10.2174/156802607781696783
    • Liao JJ, Andrews RC. Targeting protein multiple conformations: A structure-based strategy for kinase drug design. Curr Top Med Chem 2007; 7: 1394-1407. (Pubitemid 47471237)
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , Issue.14 , pp. 1394-1407
    • Liao, J.J.-L.1    Andrews, R.C.2
  • 6
    • 33644889108 scopus 로고    scopus 로고
    • Allosteric inhibitors of Bcr-abl- dependent cell proliferation
    • Adrian FJ, Ding Q, Sim T, et al. Allosteric inhibitors of Bcr-abl- dependent cell proliferation. Nat Chem Biol 2006; 2: 95-102.
    • (2006) Nat Chem Biol , vol.2 , pp. 95-102
    • Adrian, F.J.1    Ding, Q.2    Sim, T.3
  • 7
    • 34547817154 scopus 로고    scopus 로고
    • A new paradigm for protein kinase inhibition: Blocking phosphorylation without directly targeting atp binding
    • Bogoyevitch MA, Fairlie DP. A new paradigm for protein kinase inhibition: Blocking phosphorylation without directly targeting ATP binding. Drug Discov Today 2007; 12: 622-633.
    • (2007) Drug Discov Today , vol.12 , pp. 622-633
    • Bogoyevitch, M.A.1    Fairlie, D.P.2
  • 8
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang J, Yang PL, Gray NS. Targeting cancer with small molecule kinase inhibitors. Nat Rev Cancer 2009; 9: 28-39.
    • (2009) Nat Rev Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 9
    • 77953680445 scopus 로고    scopus 로고
    • Version 8.2, April 2009
    • Phospho.ELM Database Version 8.2, April 2009. http://phospho.elm.eu.org/ 2009.
    • (2009) Phospho.ELM Database
  • 10
    • 0029955955 scopus 로고    scopus 로고
    • Src phosphorylates the insulin-like growth factor type I receptor on the autophosphorylation sites. Requirement for transformation by src
    • DOI 10.1074/jbc.271.49.31562
    • Peterson JE, Kulik G, Jelinek T, Reuter CW, Shannon JA, Weber MJ. Src phosphorylates the insulin-like growth factor type I receptor on the autophosphorylation sites. Requirement for transformation bysrc. J Biol Chem 1996; 271: 31562-31571. (Pubitemid 26408616)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.49 , pp. 31562-31571
    • Peterson, J.E.1    Kulik, G.2    Jelinek, T.3    Reuter, C.W.M.4    Shannon, J.A.5    Weber, M.J.6
  • 11
    • 0028085078 scopus 로고
    • The insulin signaling system
    • White MF, Kahn CR. The insulin signaling system. J Biol Chem 1994; 269: 1-4.
    • (1994) J Biol Chem , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 12
    • 0029671423 scopus 로고    scopus 로고
    • Effects of tyrosine mutations on the kinase activity and transforming potential of an oncogenic human insulin-like growth factor I receptor
    • DOI 10.1074/jbc.271.1.160
    • Jiang Y, Chan JL, Zong CS, Wang LH. Effect of tyrosine mutations on the kinase activity and transforming potential of an oncogenic human insulin-like growth factor I receptor. J Biol Chem 1996; 271: 160-167. (Pubitemid 3027736)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.1 , pp. 160-167
    • Jiang Yixing1    Chan, J.L.2    Zong Cong, -S.3    Wang Lu-Hai4
  • 13
    • 0028577981 scopus 로고
    • A mutant insulin receptor induces formation of a shc-growth factor receptor bound protein 2 (Grb2) complex and p21ras-GTP without detectable interaction of insulin receptor substrate 1 (IRS1) with Grb2. evidence for irs1-independent p21ras-GTP formation
    • Ouwens DM, van der Zon GC, Pronk GJ, et al. A mutant insulin receptor induces formation of a Shc-growth factor receptor bound protein 2 (Grb2) complex and p21ras-GTP without detectable interaction of insulin receptor substrate 1 (IRS1) with Grb2. Evidence for IRS1-independent p21ras-GTP formation. JBiol Chem 1994; 269: 33116-33122.
    • (1994) J Biol Chem , vol.269 , pp. 33116-33122
    • Ouwens, D.M.1    Van Der Zon, G.C.2    Pronk, G.J.3
  • 14
    • 0035185571 scopus 로고    scopus 로고
    • Structure and autoregulation of the insulin-like growth factor 1 receptor kinase
    • DOI 10.1038/nsb721
    • Favelyukis S, Till JH, Hubbard SR, Miller WT. Structure and autoregulation ofthe insulin-like growth factor 1 receptor kinase. Nat Struct Biol 2001; 8: 1058-1063. (Pubitemid 33101627)
    • (2001) Nature Structural Biology , vol.8 , Issue.12 , pp. 1058-1063
    • Favelyukis, S.1    Till, J.H.2    Hubbard, S.R.3    Miller, W.T.4
  • 15
    • 27644553625 scopus 로고    scopus 로고
    • Phosphorylation ofserine residues in histidine-tag sequences attached to recombinant protein kinases: A cause of heterogeneity in mass and complications in function
    • Du P, Loulakis P, Luo C, et al. Phosphorylation ofserine residues in histidine-tag sequences attached to recombinant protein kinases: A cause of heterogeneity in mass and complications in function. Protein Expr Purif 2005; 44: 121-129.
    • (2005) Protein Expr Purif , vol.44 , pp. 121-129
    • Du, P.1    Loulakis, P.2    Luo, C.3
  • 16
    • 58749091073 scopus 로고    scopus 로고
    • Chaperone Over- expression in escherichia coli: Apparent increased yields ofsoluble recombinant protein kinases are due mainly to soluble aggregates
    • Haacke A, Fendrich G, Ramage P, Geiser, M. Chaperone Over- expression in Escherichia coli: Apparent increased yields ofsoluble recombinant protein kinases are due mainly to soluble aggregates. Protein Expr Purif 2009; 64: 185-193.
    • (2009) Protein Expr Purif , vol.64 , pp. 185-193
    • Haacke, A.1    Fendrich, G.2    Ramage, P.3    Geiser, M.4
  • 17
    • 34247337692 scopus 로고    scopus 로고
    • Mouse Aurora A: Expression in escherichia coli and purification
    • Elling RA, Tangonan BT, Penny DM, et al. Mouse Aurora A: expression in Escherichia coli and purification. Protein Expr Purif 2007; 54: 139-146.
    • (2007) Protein Expr Purif , vol.54 , pp. 139-146
    • Elling, R.A.1    Tangonan, B.T.2    Penny, D.M.3
  • 18
    • 50049093962 scopus 로고    scopus 로고
    • High yield expression of non-phosphorylated protein tyrosine kinases in insect cells
    • Wang L, Foster M, Zhang Y, et al. High yield expression of non-phosphorylated protein tyrosine kinases in insect cells. Protein Expr Purif 2008; 61: 204-211.
    • (2008) Protein Expr Purif , vol.61 , pp. 204-211
    • Wang, L.1    Foster, M.2    Zhang, Y.3
  • 19
    • 33846415054 scopus 로고    scopus 로고
    • Expression and purification of phosphorylated and non-phosphor-ylated human MEK1
    • Smith CK, CarrD, MayhoodTW, Jin W, Gray K, Windsor WT. Expression and purification of phosphorylated and non-phosphor- ylated human MEK1. Protein Expr Purif2007; 52: 446-456.
    • (2007) Protein Expr Purif , vol.52 , pp. 446-456
    • Smith, C.K.1    Mayhoodtw, C.2    Jin, W.3    Gray, K.4    Windsor, W.T.5
  • 20
    • 0033954827 scopus 로고    scopus 로고
    • Loss of elisa specificity due to biotinylation of monoclonal antibodies
    • Høyer-Hansen G, Hamers MJ, Pedersen AN, et al. Loss of ELISA specificity due to biotinylation of monoclonal antibodies. J Immunol Methods 2000; 235: 91-99.
    • (2000) J Immunol Methods , vol.235 , pp. 91-99
    • Høyer-Hansen, G.1    Hamers, M.J.2    Pedersen, A.N.3
  • 21
    • 0347634531 scopus 로고    scopus 로고
    • Production of a biotinylated single- chain antibody fragment in the cytoplasm of
    • Santala V, Lamminmaki U. Production of a biotinylated single- chain antibody fragment in the cytoplasm of Escherichia coli. J Immunol Methods 2004; 284: 165-175.
    • (2004) Escherichia Coli. J Immunol Methods , vol.284 , pp. 165-175
    • Santala, V.1    Lamminmaki, U.2
  • 22
    • 0033621510 scopus 로고    scopus 로고
    • In vivo enzymatic protein biotinylation
    • Chapman-Smith A, Cronan Jr. JE. In vivo enzymatic protein biotinylation. Biomol Eng 1999; 16: 119-125.
    • (1999) Biomol Eng , vol.16 , pp. 119-125
    • Chapman-Smith, A.1    Cronan Jr., J.E.2
  • 23
    • 12144285705 scopus 로고    scopus 로고
    • In vivo antitumor activity of nvp-aew541 - A novel, potent, and selective inhibitor of the IGF-IR kinase
    • Garcia-Echeverria C, Pearson MA, Marti A, et al. In vivo antitu- mor activity of NVP-AEW541 - a novel, potent, and selective inhibitor of the IGF-IR kinase. Cancer Cell 2004; 5: 231-239.
    • (2004) Cancer Cell , vol.5 , pp. 231-239
    • Garcia-Echeverria, C.1    Pearson, M.A.2    Marti, A.3
  • 24
    • 0039310043 scopus 로고
    • Use ofpeptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation
    • Schatz PJ. Use ofpeptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology (NY) 1993; 11: 1138-1143.
    • (1993) Escherichia Coli. Biotechnology (NY) , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 25
    • 34249072595 scopus 로고    scopus 로고
    • TIPS: Titerless infected-cells preservation and scale-up
    • Wasilko DJ, Lee SE. TIPS: Titerless Infected-Cells Preservation and Scale-up. Bio Process J 2006; 5: 29-32.
    • (2006) Bio Process J , vol.5 , pp. 29-32
    • Wasilko, D.J.1    Lee, S.E.2
  • 26
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the Bradford protein assay increases its sensitivity: Theoretical and experimental studies
    • Zor T, Selinger Z. Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal Biochem 1996; 236: 302-308.
    • (1996) Anal Biochem , vol.236 , pp. 302-308
    • Zor, T.1    Selinger, Z.2
  • 27
    • 77953657966 scopus 로고    scopus 로고
    • Study of the selectivity of type i insulin-like growth factor receptor (IGF1R) inhibitors, in press
    • Chene P. Study of the selectivity of type I insulin-like growth factor receptor (IGF1R) inhibitors, in press, Open Enz Lnh J.
    • Open Enz Lnh J
    • Chene, P.1
  • 28
    • 0026471741 scopus 로고
    • The yersinia tyrosine phosphatase: Specificity of a bacterial virulence determinant for phosphoproteins in the J 774A.1 macrophage
    • Bliska JB, Clemens JC, Dixon JE, Falkow S. The Yersinia tyrosine phosphatase: Specificity of a bacterial virulence determinant for phosphoproteins in the J 774A.1 macrophage. J Exp Med 1992; 176: 1625-1630.
    • (1992) J Exp Med , vol.176 , pp. 1625-1630
    • Bliska, J.B.1    Clemens, J.C.2    Dixon, J.E.3    Falkow, S.4
  • 29
    • 0025024995 scopus 로고
    • Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia
    • Guan KL, Dixon JE. Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science 1990; 249: 553-556. (Pubitemid 120031646)
    • (1990) Science , vol.249 , Issue.4968 , pp. 553-556
    • Guan, K.1    Dixon, J.E.2
  • 30
    • 0027058169 scopus 로고
    • Expression, purification, and physicochemical characterization of a recombinant yersinia protein tyrosine phosphatase
    • Zhang ZY, Clemens JC, Schubert HL, et al. Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase. J Biol Chem 1992; 267: 23759-23766.
    • (1992) J Biol Chem , vol.267 , pp. 23759-23766
    • Zhang, Z.Y.1    Clemens, J.C.2    Schubert, H.L.3
  • 32
    • 0025293361 scopus 로고
    • Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins
    • Cronan Jr. J.E. Biotination of proteins in vivo. A post-transla- tional modification to label, purify, and study proteins. J Biol Chem 1990; 265: 10327-10333. (Pubitemid 20212756)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.18 , pp. 10327-10333
    • Cronan Jr., J.E.1
  • 33
    • 0033199782 scopus 로고    scopus 로고
    • The enzymatic biotinylation of proteins: A post-translational modification of exceptional specificity
    • DOI 10.1016/S0968-0004(99)01438-3, PII S0968000499014383
    • Chapman-Smith A, Cronan Jr. JE. The enzymatic biotinylation of proteins: A post-translational modification of exceptional specificity. Trends Biochem Sci 1999; 24: 359-363. (Pubitemid 29421812)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 359-363
    • Chapman-Smith, A.1    Cronan Jr., J.E.2
  • 34
    • 0032520638 scopus 로고    scopus 로고
    • A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli
    • DOI 10.1093/nar/26.6.1414
    • Smith, PA, Tripp BC, DiBlasio-Smith EA, Lu Z, LaVallie ER, McCoy JM. A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli. Nucleic Acids Res 1998; 26: 1414-1420. (Pubitemid 28291615)
    • (1998) Nucleic Acids Research , vol.26 , Issue.6 , pp. 1414-1420
    • Smith, P.A.1    Tripp, B.C.2    DiBlasio-Smith, E.A.3    Lu, Z.4    LaVallie, E.R.5    McCoy, J.M.6
  • 35
    • 4043084175 scopus 로고    scopus 로고
    • In vivo biotinylation of the major histocompatibility complex (MHC) class II/peptide complex by coexpression of BirA enzyme for the generation of MHC class II/tetramers
    • DOI 10.1016/j.humimm.2004.04.001, PII S0198885904000837
    • YangJ, Jaramillo A, Shi R, KwokWW, MohanakumarT. In vivo biotinylation of the major histocompatibility complex (MHC) class Il/peptide complex by coexpression of BirA enzyme for the generation of MHC class II/tetramers. Hum Immunol 2004; 65: 692-699. (Pubitemid 39061165)
    • (2004) Human Immunology , vol.65 , Issue.7 , pp. 692-699
    • Yang, J.1    Jaramillo, A.2    Shi, R.3    Kwok, W.W.4    Mohanakumar, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.