메뉴 건너뛰기




Volumn 72, Issue 5, 2006, Pages 1033-1038

Functional solubilization of aggregation-prone TRAIL protein facilitated by coexpressing with protein isoaspartate methyltranferase

Author keywords

[No Author keywords available]

Indexed keywords

ANTICANCER THERAPEUTIC AGENT; INCLUSION BODIES; ISOASPARTATE METHYLTRANFERASE;

EID: 33749161697     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-006-0383-9     Document Type: Article
Times cited : (8)

References (34)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0031572828 scopus 로고    scopus 로고
    • Human erythrocyte protein L-isoaspartyl methyltransferase: Heritability of basal activity and genetic polymorphism for thermal stability
    • David CL, Szumlanski CL, DeVry CG, Park-Hah JO, Clarke S, Weinshilboum RM, Aswad DW (1997) Human erythrocyte protein L-isoaspartyl methyltransferase: heritability of basal activity and genetic polymorphism for thermal stability. Arch Biochem Biophys 346:277-286
    • (1997) Arch Biochem Biophys , vol.346 , pp. 277-286
    • David, C.L.1    Szumlanski, C.L.2    DeVry, C.G.3    Park-Hah, J.O.4    Clarke, S.5    Weinshilboum, R.M.6    Aswad, D.W.7
  • 5
    • 0035955743 scopus 로고    scopus 로고
    • Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses
    • Diamant S, Eliahu N, Rosenthal D, Goloubinoff P (2001) Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J Biol Chem 276:39586-39591
    • (2001) J Biol Chem , vol.276 , pp. 39586-39591
    • Diamant, S.1    Eliahu, N.2    Rosenthal, D.3    Goloubinoff, P.4
  • 6
    • 0037487260 scopus 로고    scopus 로고
    • Dicarboxylic amino acids and glycinebetaine regulate chaperone-mediated protein-disaggregation under stress
    • Diamant S, Rosenthal D, Azem A, Eliahu N, Ben-Zvi AP, Goloubinoff P (2003) Dicarboxylic amino acids and glycinebetaine regulate chaperone-mediated protein-disaggregation under stress. Mol Microbiol 49:401-410
    • (2003) Mol Microbiol , vol.49 , pp. 401-410
    • Diamant, S.1    Rosenthal, D.2    Azem, A.3    Eliahu, N.4    Ben-Zvi, A.P.5    Goloubinoff, P.6
  • 7
    • 0033582501 scopus 로고    scopus 로고
    • Proline isomerization is unlikely to be the cause of slow annealing and reactivation during the folding of alkaline phosphatase
    • Dirnbach E, Steel DG, Gafni A (1999) Proline isomerization is unlikely to be the cause of slow annealing and reactivation during the folding of alkaline phosphatase. J Biol Chem 274:4532-4536
    • (1999) J Biol Chem , vol.274 , pp. 4532-4536
    • Dirnbach, E.1    Steel, D.G.2    Gafni, A.3
  • 8
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M, Graber S, Gaestel M, Buchner J (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 16:221-229
    • (1997) EMBO J , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 9
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 10
    • 0032532099 scopus 로고    scopus 로고
    • A highly active protein repair enzyme from an extreme thermophile: The L-isoaspartyl methyltransferase from Thermotoga maritima
    • Ichikawa JK, Clarke S (1998) A highly active protein repair enzyme from an extreme thermophile: the L-isoaspartyl methyltransferase from Thermotoga maritima. Arch Biochem Biophys 358(2):222-231
    • (1998) Arch Biochem Biophys , vol.358 , Issue.2 , pp. 222-231
    • Ichikawa, J.K.1    Clarke, S.2
  • 11
    • 0036204976 scopus 로고    scopus 로고
    • Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli
    • Jonasson P, Liljeqvist S, Nygren PA, Stahl S (2002) Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli. Biotechnol Appl Biochem 35:91-105
    • (2002) Biotechnol Appl Biochem , vol.35 , pp. 91-105
    • Jonasson, P.1    Liljeqvist, S.2    Nygren, P.A.3    Stahl, S.4
  • 12
    • 14544277933 scopus 로고    scopus 로고
    • Protein isoaspartate methyltransferase is a multicopy suppressor of protein aggregation in Escherichia coli
    • Kern R, Malki A, Abdallah J, Liebart JC, Dubucs C, Yu MH, Richarme G (2005) Protein isoaspartate methyltransferase is a multicopy suppressor of protein aggregation in Escherichia coli. J Bacteriol 187:1377-1383
    • (2005) J Bacteriol , vol.187 , pp. 1377-1383
    • Kern, R.1    Malki, A.2    Abdallah, J.3    Liebart, J.C.4    Dubucs, C.5    Yu, M.H.6    Richarme, G.7
  • 13
    • 18144376288 scopus 로고    scopus 로고
    • Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli
    • Kim SG, Kweon DH, Lee DH, Park YC, Seo JH (2005) Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli. Protein Expr Purif 4:426-432
    • (2005) Protein Expr Purif , vol.4 , pp. 426-432
    • Kim, S.G.1    Kweon, D.H.2    Lee, D.H.3    Park, Y.C.4    Seo, J.H.5
  • 14
    • 4544242734 scopus 로고    scopus 로고
    • Death induction by recombinant native TRAIL and its prevention by a caspase 9 inhibitor in primary human esophageal epithelial cells
    • Kim SH, Kim K, Kwagh JG, Dicker DT, Herlyn M, Rustgi AK, Chen Y, El-Deiry WS (2004) Death induction by recombinant native TRAIL and its prevention by a caspase 9 inhibitor in primary human esophageal epithelial cells. J Biol Chem 279:40044-40052
    • (2004) J Biol Chem , vol.279 , pp. 40044-40052
    • Kim, S.H.1    Kim, K.2    Kwagh, J.G.3    Dicker, D.T.4    Herlyn, M.5    Rustgi, A.K.6    Chen, Y.7    El-Deiry, W.S.8
  • 15
    • 1242309283 scopus 로고    scopus 로고
    • Consortium of fold-catalyzing proteins increases soluble expression of cyclohexanone monooxygenase in recombinant Escherichia coli
    • Lee DH, Kim MD, Lee WH, Kweon DH, Seo JH (2004) Consortium of fold-catalyzing proteins increases soluble expression of cyclohexanone monooxygenase in recombinant Escherichia coli. Appl Microbiol Biotechnol 63:549-552
    • (2004) Appl Microbiol Biotechnol , vol.63 , pp. 549-552
    • Lee, D.H.1    Kim, M.D.2    Lee, W.H.3    Kweon, D.H.4    Seo, J.H.5
  • 16
    • 17144404114 scopus 로고    scopus 로고
    • Functional properties of PDIA from Aspergillus niger in renaturation of proteins
    • Liang Y, Li W, Ma Q, Zhang Y (2005) Functional properties of PDIA from Aspergillus niger in renaturation of proteins. FEMS Microbiol Lett 245:363-368
    • (2005) FEMS Microbiol Lett , vol.245 , pp. 363-368
    • Liang, Y.1    Li, W.2    Ma, Q.3    Zhang, Y.4
  • 17
    • 0035228439 scopus 로고    scopus 로고
    • A simple classification method for residual antibiotics using E. coli cells transformed by the calcium chloride method and drug resistance plasmid DNA
    • Lin SY, Kondo F (2001) A simple classification method for residual antibiotics using E. coli cells transformed by the calcium chloride method and drug resistance plasmid DNA. Microbios 104:149-158
    • (2001) Microbios , vol.104 , pp. 149-158
    • Lin, S.Y.1    Kondo, F.2
  • 18
    • 27644571313 scopus 로고    scopus 로고
    • Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system
    • Liu Y, Zhao TJ, Yan YB, Zhou HM (2005) Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system. Protein Expr Purif 44:155-161
    • (2005) Protein Expr Purif , vol.44 , pp. 155-161
    • Liu, Y.1    Zhao, T.J.2    Yan, Y.B.3    Zhou, H.M.4
  • 19
    • 29144469368 scopus 로고    scopus 로고
    • Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones
    • de Marco A, Vigh L, Diamant S, Goloubinoff P (2005) Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones. Cell Stress Chaperones 10:329-339
    • (2005) Cell Stress Chaperones , vol.10 , pp. 329-339
    • De Marco, A.1    Vigh, L.2    Diamant, S.3    Goloubinoff, P.4
  • 20
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • Middelberg AP (2002) Preparative protein refolding. Trends Biotechnol 20:437-443
    • (2002) Trends Biotechnol , vol.20 , pp. 437-443
    • Middelberg, A.P.1
  • 21
    • 0034050548 scopus 로고    scopus 로고
    • Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli
    • Nishihara K, Kanemori M, Yanagi H, Yura T (2000) Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli. Appl Environ Microbiol 66:884-889
    • (2000) Appl Environ Microbiol , vol.66 , pp. 884-889
    • Nishihara, K.1    Kanemori, M.2    Yanagi, H.3    Yura, T.4
  • 22
    • 0030762815 scopus 로고    scopus 로고
    • An antagonist decoy receptor and a death domain-containing receptor for TRAIL
    • Pan GH, Ni J, Wei YF, Yu GL, Reiner G, Vishva MD (1997) An antagonist decoy receptor and a death domain-containing receptor for TRAIL. Science 277:815-818
    • (1997) Science , vol.277 , pp. 815-818
    • Pan, G.H.1    Ni, J.2    Wei, Y.F.3    Yu, G.L.4    Reiner, G.5    Vishva, M.D.6
  • 23
    • 0028070754 scopus 로고
    • Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase
    • Rupp K, Birnbach U, Lundstrom J, Van PN, Soling HD (1994) Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase. J Biol Chem 269:2501-2507
    • (1994) J Biol Chem , vol.269 , pp. 2501-2507
    • Rupp, K.1    Birnbach, U.2    Lundstrom, J.3    Van, P.N.4    Soling, H.D.5
  • 24
    • 0033952307 scopus 로고    scopus 로고
    • Enzymes that catalyse the restructuring of proteins
    • Schiene C, Fischer G (2000) Enzymes that catalyse the restructuring of proteins. Curr Opin Struct Biol 10:40-45
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 40-45
    • Schiene, C.1    Fischer, G.2
  • 25
    • 0029842904 scopus 로고    scopus 로고
    • The effect of molecular chaperones on in vivo and in vitro folding processes
    • Schwarz E, Lilie H, Rudolph R (1996) The effect of molecular chaperones on in vivo and in vitro folding processes. Biol Chem 377(7-8):411-416
    • (1996) Biol Chem , vol.377 , Issue.7-8 , pp. 411-416
    • Schwarz, E.1    Lilie, H.2    Rudolph, R.3
  • 26
    • 0346463088 scopus 로고    scopus 로고
    • Refolding and purification of Apo2L/TRAIL produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli
    • Shen YL, Xia XX, Zhang Y, Liu JW, Wei DZ, Yang SL (2003) Refolding and purification of Apo2L/TRAIL produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli. Biotechnol Lett 25:2097-2101
    • (2003) Biotechnol Lett , vol.25 , pp. 2097-2101
    • Shen, Y.L.1    Xia, X.X.2    Zhang, Y.3    Liu, J.W.4    Wei, D.Z.5    Yang, S.L.6
  • 27
    • 16644383804 scopus 로고    scopus 로고
    • High-level production of soluble tumor necrosis factor-related apoptosis-inducing ligand (Apo2L/TRAIL) in high-density cultivation of recombinant Escherichia coli using a combined feeding strategy
    • Shen YL, Zhang Y, Sun AY, Xia XX, Wei DZ, Yang SL (2004) High-level production of soluble tumor necrosis factor-related apoptosis-inducing ligand (Apo2L/TRAIL) in high-density cultivation of recombinant Escherichia coli using a combined feeding strategy. Biotechnol Lett 26(12):981-984
    • (2004) Biotechnol Lett , vol.26 , Issue.12 , pp. 981-984
    • Shen, Y.L.1    Zhang, Y.2    Sun, A.Y.3    Xia, X.X.4    Wei, D.Z.5    Yang, S.L.6
  • 28
    • 0034435877 scopus 로고    scopus 로고
    • Crystal structure of protein isoaspartyl methyltransferase: A catalyst for protein repair
    • Skinner MM, Puvathingal JM, Walter RL, Friedman AM (2000) Crystal structure of protein isoaspartyl methyltransferase: a catalyst for protein repair. Structure 8:1189-1201
    • (2000) Structure , vol.8 , pp. 1189-1201
    • Skinner, M.M.1    Puvathingal, J.M.2    Walter, R.L.3    Friedman, A.M.4
  • 29
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sorensen HP, Mortensen KK (2005) Advanced genetic strategies for recombinant protein expression in Escherichia coli. J Biotechnol 115:113-128
    • (2005) J Biotechnol , vol.115 , pp. 113-128
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 30
    • 15844395096 scopus 로고    scopus 로고
    • Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins
    • Thomas JG, Baneyx F (1996) Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins. J Biol Chem 271:11141-11147
    • (1996) J Biol Chem , vol.271 , pp. 11141-11147
    • Thomas, J.G.1    Baneyx, F.2
  • 31
    • 31344474305 scopus 로고    scopus 로고
    • Strategies for protein coexpression in Escherichia coli
    • Tolia NH, Joshua-Tor L (2006) Strategies for protein coexpression in Escherichia coli. Nat Methods 3:55-64
    • (2006) Nat Methods , vol.3 , pp. 55-64
    • Tolia, N.H.1    Joshua-Tor, L.2
  • 32
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • Veinger L, Diamant S, Buchner J, Goloubinoff P (1998) The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J Biol Chem 273:11032-11037
    • (1998) J Biol Chem , vol.273 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.