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Volumn 9, Issue , 2009, Pages 80-

Monodispersity of recombinant Cre recombinase correlates with its effectiveness in vivo

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION INDEX; BACTERIAL ENDOTOXINS; CELL UPTAKE; CHROMATOGRAPHIC CONDITIONS; CRE RECOMBINASE; CRITICAL STEPS; DATA COMPARISONS; ENZYME DELIVERY; IN-VITRO; IN-VIVO; MONO-DISPERSED; MONODISPERSITY; MULTI-STEP PURIFICATION; OPTIMAL ALTERNATIVE; PURIFICATION PROTOCOL; RECOMBINASE ACTIVITY; REPORTER PROTEIN; SPECIFIC ACTIVITY; SPECTROFLUORIMETRIC; STRONG CORRELATION; TARGET GENES;

EID: 70350726751     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-9-80     Document Type: Article
Times cited : (6)

References (25)
  • 1
    • 0029860719 scopus 로고    scopus 로고
    • Different thermostabilities of FLP and Cre recombinases: implications for applied site-specific recombination
    • 10.1093/nar/24.21.4256, 146240, 8932381
    • Buchholz F, Ringrose L, Angrand P-O, Rossi F, Stewart AF. Different thermostabilities of FLP and Cre recombinases: implications for applied site-specific recombination. Nucleic Acids Res 1996, 24:4256-4262. 10.1093/nar/24.21.4256, 146240, 8932381.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4256-4262
    • Buchholz, F.1    Ringrose, L.2    Angrand, P.-.O.3    Rossi, F.4    Stewart, A.F.5
  • 2
    • 0036438816 scopus 로고    scopus 로고
    • Cre-loxP biochemistry
    • 10.1016/S1046-2023(02)00244-X, 12431441
    • Ghosh K, Van Duyne GD. Cre-loxP biochemistry. Methods 2002, 28:374-383. 10.1016/S1046-2023(02)00244-X, 12431441.
    • (2002) Methods , vol.28 , pp. 374-383
    • Ghosh, K.1    Van Duyne, G.D.2
  • 3
    • 0034965749 scopus 로고    scopus 로고
    • Intein-mediated rapid purification of Cre recombinase
    • Cantor EJ, Chong S. Intein-mediated rapid purification of Cre recombinase. Prot Expr Purif 2001, 22:135-140.
    • (2001) Prot Expr Purif , vol.22 , pp. 135-140
    • Cantor, E.J.1    Chong, S.2
  • 4
    • 2942739230 scopus 로고    scopus 로고
    • Flow cytometric application of helper adenovirus (HAd) containing GFP gene flanked by two parallel loxP sites to evaluation of 293 cre-complementing cell line and monitoring of HAd in Gutless Ad production
    • 10.1021/bp034248e, 15176899
    • Park MT, Hwang SJ, Lee GM. Flow cytometric application of helper adenovirus (HAd) containing GFP gene flanked by two parallel loxP sites to evaluation of 293 cre-complementing cell line and monitoring of HAd in Gutless Ad production. Biotechnol Prog 2004, 20:913-920. 10.1021/bp034248e, 15176899.
    • (2004) Biotechnol Prog , vol.20 , pp. 913-920
    • Park, M.T.1    Hwang, S.J.2    Lee, G.M.3
  • 5
    • 36148931645 scopus 로고    scopus 로고
    • Animal models for disease: knockout, knock-in, and conditional mutant mice
    • LePage DF, Conlon RA. Animal models for disease: knockout, knock-in, and conditional mutant mice. Methods Mol Med 2006, 129:41-67.
    • (2006) Methods Mol Med , vol.129 , pp. 41-67
    • LePage, D.F.1    Conlon, R.A.2
  • 6
    • 59849102702 scopus 로고    scopus 로고
    • Protein transduction revisited: novel insights into the mechanism underlying intracellular delivery of proteins
    • 10.2174/138161208786898833, 19075739
    • Edenhofer F. Protein transduction revisited: novel insights into the mechanism underlying intracellular delivery of proteins. Curr Pharm Des 2008, 14:3628-36. 10.2174/138161208786898833, 19075739.
    • (2008) Curr Pharm Des , vol.14 , pp. 3628-3636
    • Edenhofer, F.1
  • 7
    • 0037007121 scopus 로고    scopus 로고
    • Ability of the hydrophobic FGF and basic TAT peptides to promote cellular uptake of recombinant Cre recombinase: a tool for efficient genetic engineering of mammalian genomes
    • 10.1073/pnas.032068699, 123675, 11904364
    • Peitz M, Pfannkuche K, Rajewsky K, Edenhofer F. Ability of the hydrophobic FGF and basic TAT peptides to promote cellular uptake of recombinant Cre recombinase: a tool for efficient genetic engineering of mammalian genomes. Proc Natl Acad Sci USA 2002, 99:4489-4494. 10.1073/pnas.032068699, 123675, 11904364.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4489-4494
    • Peitz, M.1    Pfannkuche, K.2    Rajewsky, K.3    Edenhofer, F.4
  • 9
    • 13244251060 scopus 로고    scopus 로고
    • Enhanced cell-permeant Cre protein for site-specific recombination in cultured cells
    • 10.1186/1472-6750-4-25, 529453, 15500682
    • Lin Q, Jo D, Gebre-Amlak KD, Ruley HE. Enhanced cell-permeant Cre protein for site-specific recombination in cultured cells. BMC Biotechnol 2004, 4:25. 10.1186/1472-6750-4-25, 529453, 15500682.
    • (2004) BMC Biotechnol , vol.4 , pp. 25
    • Lin, Q.1    Jo, D.2    Gebre-Amlak, K.D.3    Ruley, H.E.4
  • 10
    • 0034956228 scopus 로고    scopus 로고
    • A strategy for optimizing the monodispersity of fusion proteins: application to purification of recombinant HPV E6 oncoprotein
    • Nominé Y, Ristriani T, Laurent C, Lefevre J-F, Weiss E, Travé G. A strategy for optimizing the monodispersity of fusion proteins: application to purification of recombinant HPV E6 oncoprotein. Prot Engineer 2001, 14:297-305.
    • (2001) Prot Engineer , vol.14 , pp. 297-305
    • Nominé, Y.1    Ristriani, T.2    Laurent, C.3    Lefevre, J.-.F.4    Weiss, E.5    Travé, G.6
  • 11
    • 23044456332 scopus 로고    scopus 로고
    • Characterization of the aggregates formed during recombinant protein expression in bacteria
    • 10.1186/1471-2091-6-10, 1175841, 15927061
    • Schrödel A, de Marco A. Characterization of the aggregates formed during recombinant protein expression in bacteria. BMC Biochem 2005, 6:10. 10.1186/1471-2091-6-10, 1175841, 15927061.
    • (2005) BMC Biochem , vol.6 , pp. 10
    • Schrödel, A.1    de Marco, A.2
  • 12
    • 35348924357 scopus 로고    scopus 로고
    • Enhanced purification of cell-permeant Cre and germline transmission after transduction into mouse embryonic stem cells
    • 10.1002/dvg.20321, 17661398
    • Peitz M, Jäger R, Patsch C, Jäger A, Egert A, Schorle H, Edenhofer F. Enhanced purification of cell-permeant Cre and germline transmission after transduction into mouse embryonic stem cells. Genesis 2007, 45:508-517. 10.1002/dvg.20321, 17661398.
    • (2007) Genesis , vol.45 , pp. 508-517
    • Peitz, M.1    Jäger, R.2    Patsch, C.3    Jäger, A.4    Egert, A.5    Schorle, H.6    Edenhofer, F.7
  • 14
    • 57649104748 scopus 로고    scopus 로고
    • Factors affecting endotoxin removal from recombinant therapeutic proteins by anion exchange chromatography
    • Chen RH, Huang C-J, Newton BS, Ritter G, Old LJ, Batt CA. Factors affecting endotoxin removal from recombinant therapeutic proteins by anion exchange chromatography. Prot Expr Purif 2009, 64:76-81.
    • (2009) Prot Expr Purif , vol.64 , pp. 76-81
    • Chen, R.H.1    Huang, C.-.J.2    Newton, B.S.3    Ritter, G.4    Old, L.J.5    Batt, C.A.6
  • 15
    • 33748742268 scopus 로고    scopus 로고
    • Is any measurement method optimal for all aggregate sizes and types?
    • 10.1208/aapsj080365, 17025274
    • Philo JS. Is any measurement method optimal for all aggregate sizes and types?. AAPS J 2006, 8:E564-E571. 10.1208/aapsj080365, 17025274.
    • (2006) AAPS J , vol.8
    • Philo, J.S.1
  • 17
    • 58149477054 scopus 로고    scopus 로고
    • Effect of trehalose on protein structure
    • Jain NK, Roy I. Effect of trehalose on protein structure. Protein Sci 2009, 18:24-36.
    • (2009) Protein Sci , vol.18 , pp. 24-36
    • Jain, N.K.1    Roy, I.2
  • 18
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • 10.1038/nm996, 14770178
    • Wadia JS, Stan RV, Dowdy SF. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nature Medicine 2004, 10:310-315. 10.1038/nm996, 14770178.
    • (2004) Nature Medicine , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 19
    • 0018763480 scopus 로고
    • Inhibition of the lysosomal pathway of protein degradation in isolated rat hepatocytes by ammonia, methylamine, chloroquine and leupeptin
    • 10.1111/j.1432-1033.1979.tb12956.x, 456353
    • Seglen PO, Grinde B, Solheim AE. Inhibition of the lysosomal pathway of protein degradation in isolated rat hepatocytes by ammonia, methylamine, chloroquine and leupeptin. Eur J Biochem 1979, 95:215-225. 10.1111/j.1432-1033.1979.tb12956.x, 456353.
    • (1979) Eur J Biochem , vol.95 , pp. 215-225
    • Seglen, P.O.1    Grinde, B.2    Solheim, A.E.3
  • 20
    • 2442670068 scopus 로고    scopus 로고
    • Endosome disruption enhances the functional nuclear delivery of Tat-fusion proteins
    • 10.1016/j.bbrc.2004.04.180, 15158435
    • Caron NJ, Quenneville SP, Tremblay JP. Endosome disruption enhances the functional nuclear delivery of Tat-fusion proteins. Biochem Biophys Res Commun 2004, 319:12-20. 10.1016/j.bbrc.2004.04.180, 15158435.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 12-20
    • Caron, N.J.1    Quenneville, S.P.2    Tremblay, J.P.3
  • 21
    • 80055110670 scopus 로고    scopus 로고
    • Principles of site-specific recombinase (SSR) technology
    • Buchholtz F. Principles of site-specific recombinase (SSR) technology. J Vis Exp 2008, 15.
    • (2008) J Vis Exp , vol.15
    • Buchholtz, F.1
  • 22
    • 44449122857 scopus 로고    scopus 로고
    • Conditional transgenesis using Dimerizable Cre (DiCre)
    • 10.1371/journal.pone.0001355, 2131782, 18159238
    • Jullien N, Goddard I, Selmi-Ruby S, Fina JL, Cremer H, Herman JP. Conditional transgenesis using Dimerizable Cre (DiCre). PLoS One 2007, 2:e1355. 10.1371/journal.pone.0001355, 2131782, 18159238.
    • (2007) PLoS One , vol.2
    • Jullien, N.1    Goddard, I.2    Selmi-Ruby, S.3    Fina, J.L.4    Cremer, H.5    Herman, J.P.6
  • 23
    • 42249107316 scopus 로고    scopus 로고
    • Spatially directed assembly of a heterotetrameric Cre-Lox synapse restricts recombination specificity
    • 10.1016/j.jmb.2008.02.058, 2418607, 18374357
    • Gelato KA, Martin SS, Liu PH, Saunders AA, Baldwin EP. Spatially directed assembly of a heterotetrameric Cre-Lox synapse restricts recombination specificity. J Mol Biol 2008, 378:653-665. 10.1016/j.jmb.2008.02.058, 2418607, 18374357.
    • (2008) J Mol Biol , vol.378 , pp. 653-665
    • Gelato, K.A.1    Martin, S.S.2    Liu, P.H.3    Saunders, A.A.4    Baldwin, E.P.5
  • 24
    • 57449089183 scopus 로고    scopus 로고
    • A chimeric Cre recombinase with regulated directionality
    • 10.1073/pnas.0809949105, 2587618, 19011106
    • Warren D, Laxmikanthan G, Landy A. A chimeric Cre recombinase with regulated directionality. Proc Natl Acad Sci USA 2008, 105:18278-18283. 10.1073/pnas.0809949105, 2587618, 19011106.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18278-18283
    • Warren, D.1    Laxmikanthan, G.2    Landy, A.3
  • 25
    • 67649280374 scopus 로고    scopus 로고
    • Light-activated Cre recombinase as a tool for the spatial and temporal control of gene function in mammalian cells
    • 10.1021/cb900041s, 19413301
    • Edwards WF, Young DD, Deiters A. Light-activated Cre recombinase as a tool for the spatial and temporal control of gene function in mammalian cells. ACS Chem Biol 2009, 4:441-445. 10.1021/cb900041s, 19413301.
    • (2009) ACS Chem Biol , vol.4 , pp. 441-445
    • Edwards, W.F.1    Young, D.D.2    Deiters, A.3


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