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Volumn 85, Issue 2, 2012, Pages 239-245

Cloning, expression, and purification of a recombinant Tat-HA-NR2B9c peptide

Author keywords

Cerebral ischemic injury; Cloning; Expression; Neuroprotection; Purification; Tat HA NR2B9c

Indexed keywords

HYBRID PROTEIN; INFLUENZA VIRUS HEMAGGLUTININ; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PEPTIDE; PROTECTIVE AGENT; TRANSACTIVATOR PROTEIN;

EID: 84866147051     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2012.08.011     Document Type: Article
Times cited : (8)

References (24)
  • 2
    • 64149091118 scopus 로고    scopus 로고
    • Emergent cerebrovascular disease risk factor weighting: is transient ischemic attack an imminent threat?
    • Gállego, J., Muñoz, R., Martínez-Vila, E., Emergent cerebrovascular disease risk factor weighting: is transient ischemic attack an imminent threat?. Cerebrovasc. Dis. 27 (2009), 88–96.
    • (2009) Cerebrovasc. Dis. , vol.27 , pp. 88-96
    • Gállego, J.1    Muñoz, R.2    Martínez-Vila, E.3
  • 3
    • 0033546347 scopus 로고    scopus 로고
    • Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein
    • Sattler, R., Xiong, Z., Lu, W.Y., Hafner, M., MacDonald, J.F., Tymianski, M., Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein. Science 284 (1999), 1845–1848.
    • (1999) Science , vol.284 , pp. 1845-1848
    • Sattler, R.1    Xiong, Z.2    Lu, W.Y.3    Hafner, M.4    MacDonald, J.F.5    Tymianski, M.6
  • 4
    • 78649983743 scopus 로고    scopus 로고
    • Treatment of cerebral ischemia by disrupting ischemia-induced interaction of nNOS with PSD-95
    • Zhou, L., Li, F., Xu, H.B., Luo, C.X., Wu, H.Y., Zhu, M.M., Lu, W., Ji, X., Zhou, Q.G., Zhu, D.Y., Treatment of cerebral ischemia by disrupting ischemia-induced interaction of nNOS with PSD-95. Nat. Med. 16 (2010), 1439–1443.
    • (2010) Nat. Med. , vol.16 , pp. 1439-1443
    • Zhou, L.1    Li, F.2    Xu, H.B.3    Luo, C.X.4    Wu, H.Y.5    Zhu, M.M.6    Lu, W.7    Ji, X.8    Zhou, Q.G.9    Zhu, D.Y.10
  • 5
    • 0033951941 scopus 로고    scopus 로고
    • Selfotel in acute ischemic stroke: possible neurotoxic effects of an NMDA antagonist
    • Davis, S.M., Lees, K.R., Albers, G.W., Diener, H.C., Markabi, S., Karlsson, G., Norris, J., Selfotel in acute ischemic stroke: possible neurotoxic effects of an NMDA antagonist. Stroke 31 (2000), 347–354.
    • (2000) Stroke , vol.31 , pp. 347-354
    • Davis, S.M.1    Lees, K.R.2    Albers, G.W.3    Diener, H.C.4    Markabi, S.5    Karlsson, G.6    Norris, J.7
  • 6
    • 33846456236 scopus 로고    scopus 로고
    • Differential roles of NR2A- and NR2B-containing NMDA receptors in activity-dependent brain derived neurotrophic factor gene regulation and limbic epileptogenesis
    • Chen, Q., He, S., Hu, X.L., Yu, J., Zhou, Y., Zheng, J., Zhang, S., Zhang, C., Duan, W.H., Xiong, Z.Q., Differential roles of NR2A- and NR2B-containing NMDA receptors in activity-dependent brain derived neurotrophic factor gene regulation and limbic epileptogenesis. J. Neurosci., 2007, 542–552.
    • (2007) J. Neurosci. , pp. 542-552
    • Chen, Q.1    He, S.2    Hu, X.L.3    Yu, J.4    Zhou, Y.5    Zheng, J.6    Zhang, S.7    Zhang, C.8    Duan, W.H.9    Xiong, Z.Q.10
  • 8
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H.C., Schenker, L.T., Kennedy, M.B., Seeburg, P.H., Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269 (1995), 1737–1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 12
    • 34247868094 scopus 로고    scopus 로고
    • Recombinant production of antimicrobial peptides in heterologous microbial systems
    • Ingham, A.B., Moore, R.J., Recombinant production of antimicrobial peptides in heterologous microbial systems. Biotechnol. Appl. Biochem. 47 (2007), 1–9.
    • (2007) Biotechnol. Appl. Biochem. , vol.47 , pp. 1-9
    • Ingham, A.B.1    Moore, R.J.2
  • 13
    • 67349210667 scopus 로고    scopus 로고
    • A novel human parathyroid hormone (1–34) analog for the treatment of osteoporosis
    • Feng, J., Liu, Y., Xing, Y., Wang, H., Li, T., Liu, J., Fan, H., Cao, R., A novel human parathyroid hormone (1–34) analog for the treatment of osteoporosis. Peptides 30 (2009), 1173–1180.
    • (2009) Peptides , vol.30 , pp. 1173-1180
    • Feng, J.1    Liu, Y.2    Xing, Y.3    Wang, H.4    Li, T.5    Liu, J.6    Fan, H.7    Cao, R.8
  • 14
    • 56649106249 scopus 로고    scopus 로고
    • RAPD: a database of recombinantly-produced antimicrobial peptides
    • Li, Y., Chen, Z., RAPD: a database of recombinantly-produced antimicrobial peptides. FEMS Microbiol. Lett. 289 (2008), 126–129.
    • (2008) FEMS Microbiol. Lett. , vol.289 , pp. 126-129
    • Li, Y.1    Chen, Z.2
  • 15
    • 84860792807 scopus 로고    scopus 로고
    • Production of the catalytic core of human peptidylglycine α-hydroxylating monooxygenase (hPHMcc) in Escherichia coli
    • Handa, S., Spradling, T.J., Dempsey, D.R., Merkler, D.J., Production of the catalytic core of human peptidylglycine α-hydroxylating monooxygenase (hPHMcc) in Escherichia coli. Protein Expr. Purif. 84 (2012), 9–13.
    • (2012) Protein Expr. Purif. , vol.84 , pp. 9-13
    • Handa, S.1    Spradling, T.J.2    Dempsey, D.R.3    Merkler, D.J.4
  • 16
    • 0037855839 scopus 로고    scopus 로고
    • Low temperature and glucose enhanced T7 RNA polymerase-based plasmid stability for increasing expression of glucagon-like peptide-2 in Escherichia coli
    • Zhang, Y., Taiming, L., Liu, J., Low temperature and glucose enhanced T7 RNA polymerase-based plasmid stability for increasing expression of glucagon-like peptide-2 in Escherichia coli. Protein Expr. Purif. 29 (2003), 132–139.
    • (2003) Protein Expr. Purif. , vol.29 , pp. 132-139
    • Zhang, Y.1    Taiming, L.2    Liu, J.3
  • 17
    • 8844262654 scopus 로고    scopus 로고
    • High level recombinant protein expression in Ralstonia eutropha using T7 RNA polymerase based amplification
    • Barnard, G.C., Henderson, G.E., Srinivasan, S., Gerngross, T.U., High level recombinant protein expression in Ralstonia eutropha using T7 RNA polymerase based amplification. Protein Expr. Purif. 38 (2004), 264–271.
    • (2004) Protein Expr. Purif. , vol.38 , pp. 264-271
    • Barnard, G.C.1    Henderson, G.E.2    Srinivasan, S.3    Gerngross, T.U.4
  • 18
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesized in Escherichia coli
    • Marston, F.A., The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem. J. 240 (1986), 1–12.
    • (1986) Biochem. J. , vol.240 , pp. 1-12
    • Marston, F.A.1
  • 19
    • 0025953577 scopus 로고
    • Predicting the solubility of recombinant proteins in Escherichia coli
    • Wilkinson, D.L., Harrison, R.G., Predicting the solubility of recombinant proteins in Escherichia coli. Biotechnology (NY) 9 (1991), 443–448.
    • (1991) Biotechnology (NY) , vol.9 , pp. 443-448
    • Wilkinson, D.L.1    Harrison, R.G.2
  • 20
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: delivery of a biologically active protein into the mouse
    • Schwarze, S.R., Ho, A., Vocero-Akbani, A., Dowdy, S.F., In vivo protein transduction: delivery of a biologically active protein into the mouse. Science 285 (1999), 1569–1572.
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 21
    • 33645998425 scopus 로고    scopus 로고
    • Evaluation of epitope tags for protein detection after in vivo CNS gene transfer
    • Shevtsova, Z., Malik, J.M., Michel, U., Schöll, U., Bähr, M., Kügler, S., Evaluation of epitope tags for protein detection after in vivo CNS gene transfer. Eur. J. Neurosci. 23 (2006), 1961–1969.
    • (2006) Eur. J. Neurosci. , vol.23 , pp. 1961-1969
    • Shevtsova, Z.1    Malik, J.M.2    Michel, U.3    Schöll, U.4    Bähr, M.5    Kügler, S.6
  • 22
    • 33750797498 scopus 로고    scopus 로고
    • Cloning, expression, and purification of a highly immunogenic recombinant gonadotropin-releasing hormone (GnRH) chimeric peptide
    • Xu, J., Zhu, Z., Duan, P., Li, W., Zhang, Y., Wu, J., Hu, Z., Roque, R.S., Liu, J., Cloning, expression, and purification of a highly immunogenic recombinant gonadotropin-releasing hormone (GnRH) chimeric peptide. Protein Expr. Purif. 50 (2006), 163–170.
    • (2006) Protein Expr. Purif. , vol.50 , pp. 163-170
    • Xu, J.1    Zhu, Z.2    Duan, P.3    Li, W.4    Zhang, Y.5    Wu, J.6    Hu, Z.7    Roque, R.S.8    Liu, J.9
  • 23
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacryl-amide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., von Jagow, G., Tricine-sodium dodecyl sulfate-polyacryl-amide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987), 368–379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2


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