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Volumn 78, Issue 2, 2011, Pages 113-119

Production of recombinant peptides as fusions with SUMO

Author keywords

Amyloidogenic A 42; Fusion protein; Hydrolase; SUMO

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); HYBRID PROTEIN; OMPA OUTER MEMBRANE PROTEINS; OUTER MEMBRANE PROTEIN; PEPTIDE; PEPTIDE FRAGMENT; PEPTIDE HYDROLASE; SIGNAL PEPTIDE; SUMO 1 PROTEIN;

EID: 79958768615     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.04.015     Document Type: Article
Times cited : (56)

References (38)
  • 1
    • 0032844656 scopus 로고    scopus 로고
    • Methods for exploring early events in protein folding
    • DOI 10.1016/S0959-440X(99)00015-9
    • H. Roder, M.R. Shastry, Methods for exploring early events in protein folding, Curr. Opin. Struct. Biol. 9 (1999) 620-626. (Pubitemid 29460590)
    • (1999) Current Opinion in Structural Biology , vol.9 , Issue.5 , pp. 620-626
    • Roder, H.1    Shastry, M.R.2
  • 2
  • 3
    • 0033855775 scopus 로고    scopus 로고
    • Review: Model peptides and the physicochemical approach to beta-amyloids
    • D.G. Lynn, S.C. Meredith, Review: Model peptides and the physicochemical approach to beta-amyloids, J. Struct. Biol. 130 (2000) 153-173.
    • (2000) J. Struct. Biol. , vol.130 , pp. 153-173
    • Lynn, D.G.1    Meredith, S.C.2
  • 4
    • 0036897817 scopus 로고    scopus 로고
    • Design of nanostructured biological materials through self-assembly of peptides and proteins
    • DOI 10.1016/S1367-5931(02)00391-5
    • S.G. Zhang, D.M. Marini, W. Hwang, S. Santoso, Design of nanostructured biological materials through self-assembly of peptides and proteins, Curr. Opin. Chem. Biol. 6 (2002) 865-871. (Pubitemid 35449349)
    • (2002) Current Opinion in Chemical Biology , vol.6 , Issue.6 , pp. 865-871
    • Zhang, S.1    Marini, D.M.2    Hwang, W.3    Santoso, S.4
  • 5
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesized in Escherichia coli
    • F.A. O Marston, 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.O.1
  • 6
    • 0006530907 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • G. Hannig, S.C. Makrides, Strategies for optimizing heterologous protein expression in Escherichia coli, TIBTECH 16 (1998) 2-9.
    • (1998) TIBTECH , vol.16 , pp. 2-9
    • Hannig, G.1    Makrides, S.C.2
  • 7
    • 31044435481 scopus 로고    scopus 로고
    • Expression and purification of human antimicrobial peptide, dermcidin, in Escherichia coli
    • DOI 10.1016/j.pep.2005.07.002, PII S1046592805002299
    • I. Cipakova, J. Gasperik, E. Hostinova, Expression and purification of human antimicrobial peptide, dermcidin, in Escherichia coli, Protein Express. Purif. 45 (2006) 269-274. (Pubitemid 43120431)
    • (2006) Protein Expression and Purification , vol.45 , Issue.2 , pp. 269-274
    • Cipakova, I.1    Gasperik, J.2    Hostinova, E.3
  • 8
    • 33645404559 scopus 로고    scopus 로고
    • Expression and purification of a fusion-typed pediocin PA-1 in Escherichia coli and recovery of biologically active pediocin PA-1
    • G.S. Moon, Y.R. Pyun, W.J. Kim, Expression and purification of a fusion-typed pediocin PA-1 in Escherichia coli and recovery of biologically active pediocin PA-1, Int. J. Food Microbiol. 108 (2006) 136-140.
    • (2006) Int. J. Food Microbiol. , vol.108 , pp. 136-140
    • Moon, G.S.1    Pyun, Y.R.2    Kim, W.J.3
  • 9
    • 0036215113 scopus 로고    scopus 로고
    • Cloning and expression of human beta-defensin-2 gene in Escherichia coli
    • DOI 10.2174/0929866023409011
    • X.M. Fang, L. Peng, Z.N. Xu, J.M. Wu, P.L. Cen, Cloning and expression of β-defensin- 2 gene in Escherichia coli, Prot. Pep. Lett. 9 (2002) 31-37. (Pubitemid 34293914)
    • (2002) Protein and Peptide Letters , vol.9 , Issue.1 , pp. 31-37
    • Fang, X.1    Peng, L.2    Xu, Z.3    Wu, J.4    Cen, P.5
  • 10
    • 23444455293 scopus 로고    scopus 로고
    • Production and purification of a novel antibiotic peptide, adenoregulin, from a recombinant Escherichia coli
    • DOI 10.1007/s10529-005-5361-2
    • Y.X. Zhou, W. Cao, Q.P. Luo, Y.S. Ma, J.Z. Wang, D.Z. Wei, Production and purification of a novel antibiotic peptide, adenoregulin, from a recombinant Escherichia coli, Biotechnol. Lett. 27 (2005) 725-730. (Pubitemid 41110932)
    • (2005) Biotechnology Letters , vol.27 , Issue.10 , pp. 725-730
    • Zhou, Y.-X.1    Cao, W.2    Luo, Q.-P.3    Ma, Y.-S.4    Wang, J.-Z.5    Wei, D.-Z.6
  • 11
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • K. Terpe, Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems, Appl. Microb. Biotechnol. 60 (2003) 523-533. (Pubitemid 36169526)
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.5 , pp. 523-533
    • Terpe, K.1
  • 12
    • 0023806075 scopus 로고    scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • D.B. Smith, K.S. Johnson, Single-step purification of polypeptides expressed In Escherichia coli as fusions with glutathione S-transferase, Gene 67 (1998) 31-40.
    • (1998) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 13
    • 0028825817 scopus 로고
    • Gene fusion expression systems in Escherichia coli
    • E.R. LaVallie, J.M. McCoy, Gene fusion expression systems in Escherichia coli, Curr. Opin. Biotechnol. 6 (1995) 501-506.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 501-506
    • LaVallie, E.R.1    McCoy, J.M.2
  • 14
    • 0031214792 scopus 로고    scopus 로고
    • High-level expression of soluble protein in Escherichia coli using a His(6)-tag and maltose-binding-protein double-affinity fusion system
    • K.D. Pryor, B. Leiting, High-level expression of soluble protein in Escherichia coli using a His(6)-tag and maltose-binding-protein double-affinity fusion system, Protein Express. Purif. 10 (1997) 309-319.
    • (1997) Protein Express. Purif. , vol.10 , pp. 309-319
    • Pryor, K.D.1    Leiting, B.2
  • 15
    • 0020602654 scopus 로고
    • Gene fusion vectors based on the gene for staphylococcal protein A
    • DOI 10.1016/0378-1119(83)90025-2
    • M.B. Uhlen, B. Nilsson, B. Guss, M. Lindberg, S. Gatenbeck, L. Philipson, Gene fusion vectors based on the gene for Staphylococcal protein-A, Gene 23 (1983) 369-378. (Pubitemid 13009986)
    • (1983) Gene , vol.23 , Issue.3 , pp. 369-378
    • Uhlen, M.1    Nillson, B.2    Guss, B.3
  • 16
    • 0021169719 scopus 로고
    • One-step purification of hybrid proteins which have beta-galactosidase activity
    • A. Ullmann, One-step purification of hybrid proteins which have beta-galactosidase activity, Gene 29 (1984) 27-31. (Pubitemid 14030929)
    • (1984) Gene , vol.29 , Issue.1-2 , pp. 27-31
    • Ullmann, A.1
  • 17
    • 1942537173 scopus 로고    scopus 로고
    • An efficient system for high-level expression and easy purification of authentic recombinant proteins
    • DOI 10.1110/ps.04618904
    • A.M. Catanzariti, T.A. Soboleva, D.A. Jans, P.G. Board, R.T. Baker, An efficient system for high-level expression and easy purification of authentic recombinant proteins, Prot. Sci. 13 (2004) 1331-1339. (Pubitemid 38526098)
    • (2004) Protein Science , vol.13 , Issue.5 , pp. 1331-1339
    • Catanzariti, A.-M.1    Soboleva, T.A.2    Jans, D.A.3    Board, P.G.4    Baker, R.T.5
  • 19
    • 0028834866 scopus 로고
    • Purification of human matrilysin produced in Escherichia coli and characterization using a new optimized fluorogenic peptide substrate
    • A.R. Welch, C.M. Holman, M.F. Browner, M.R. Gehring, C.C. Kan, H.E. Van Wart, Purification of human matrilysin produced in Escherichia coli and characterization using a new optimized fluorogenic peptide substrate, Arch. Biochem. Biophys. 324 (1995) 59-64.
    • (1995) Arch. Biochem. Biophys. , vol.324 , pp. 59-64
    • Welch, A.R.1    Holman, C.M.2    Browner, M.F.3    Gehring, M.R.4    Kan, C.C.5    Van Wart, H.E.6
  • 21
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
    • DOI 10.1038/nbt0293-187
    • E.R. LaVallie, E.A. DiBlasio, S. Kovacic, K.L. Grant, P.F. Schendel, J.M. McCoy, A thioredoxin gene fusion expression system that circumvents inclusion body formation in the Escherichia coli cytoplasm, Bio./Technology 11 (1993) 187-193. (Pubitemid 23056045)
    • (1993) Bio/Technology , vol.11 , Issue.2 , pp. 187-193
    • LaVallie, E.R.1    DiBlasio, E.A.2    Kovacic, S.3    Grant, K.L.4    Schendel, P.F.5    McCoy, J.M.6
  • 22
    • 0030272645 scopus 로고    scopus 로고
    • Protein expression using ubiquitin fusion and cleavage
    • R.T. Baker, Protein expression using ubiquitin fusion and cleavage, Curr. Opin. Biotechnol. 7 (1996) 541-546.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 541-546
    • Baker, R.T.1
  • 23
    • 0036237383 scopus 로고    scopus 로고
    • Versatile protein tag, SUMO: Its enzymology and biological function
    • DOI 10.1002/jcp.10100
    • K.I. Kim, S.H. Baek, S.H. Chung, Versatile protein tag, SUMO: Its enzymology and biological function, J. Cellul. Physiol. 191 (2002) 257-268. (Pubitemid 34462476)
    • (2002) Journal of Cellular Physiology , vol.191 , Issue.3 , pp. 257-268
    • Kim, K.I.L.1    Baek, S.H.2    Chung, C.H.3
  • 26
    • 33847163530 scopus 로고    scopus 로고
    • Ligating independent cloning vectors for expression of SUMO fusions
    • S.D. Weeks, M. Drinker, P.J. Loll, Ligating independent cloning vectors for expression of SUMO fusions, Protein Express. Purif. 53 (2007) 40-50.
    • (2007) Protein Express. Purif. , vol.53 , pp. 40-50
    • Weeks, S.D.1    Drinker, M.2    Loll, P.J.3
  • 27
    • 34247324364 scopus 로고    scopus 로고
    • Systematic analysis of fusion and affinity tags using human aspartyl-tRNA synthetase expressed in E. coli
    • DOI 10.1016/j.pep.2007.03.001, PII S1046592807000654
    • C.M. Guzzo, D.C.H. Yang, Systematic analysis of fusion and affinity tags using human-aspartyl-tRNA synthetase expressed in E. Coli, Protein Express. Purif. 54 (2007) 166-175. (Pubitemid 46636330)
    • (2007) Protein Expression and Purification , vol.54 , Issue.1 , pp. 166-175
    • Guzzo, C.M.1    Yang, D.C.H.2
  • 28
    • 38349110223 scopus 로고    scopus 로고
    • High yield production of recombinant native and modified peptides exemplified by ligands for G-protein coupled receptors
    • E. Bosse-Doenecke, U. Weininger, M. Gopalswamy, J. Balbach, S.M. Knudsen, R. Rudolph, High yield production of recombinant native and modified peptides exemplified by ligands for G-protein coupled receptors, Protein Express. Purif. 58 (2008) 114-121.
    • (2008) Protein Express. Purif. , vol.58 , pp. 114-121
    • Bosse-Doenecke, E.1    Weininger, U.2    Gopalswamy, M.3    Balbach, J.4    Knudsen, S.M.5    Rudolph, R.6
  • 29
    • 39149114403 scopus 로고    scopus 로고
    • Expression and purification of human urodilatin by small ubiquitin-related modifier fusion in Escherichia Coli
    • Z. Sun, Z. Xia, J-N. Liu, Expression and purification of human urodilatin by small ubiquitin-related modifier fusion in Escherichia Coli, Appl. Microbiol. Biotechnol. 78 (2008) 495-502.
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 495-502
    • Sun, Z.1    Xia, Z.2    Liu, J.-N.3
  • 31
    • 0032484702 scopus 로고    scopus 로고
    • Recombinant production and purification of novel antisense antimicrobial peptide in Escherichia coli
    • C. Haught, G.D. Davis, R. Subramanian, K.W. Jackson, R.G. Harrison, Recombinant production and purification of novel antisense antimicrobial peptide in Escherichia coli, Biotechnol. Bioeng. 57 (1998) 55-61.
    • (1998) Biotechnol. Bioeng. , vol.57 , pp. 55-61
    • Haught, C.1    Davis, G.D.2    Subramanian, R.3    Jackson, K.W.4    Harrison, R.G.5
  • 32
    • 0034597709 scopus 로고    scopus 로고
    • High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies
    • J.H. Lee, J.H. Kim, S.W. Hwang, W.J. Lee, H.K. Yoon, H.S. Lee, S.S. Hong, High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies, Biochem. Biophys. Res. Comm. 277 (2000) 575-580.
    • (2000) Biochem. Biophys. Res. Comm. , vol.277 , pp. 575-580
    • Lee, J.H.1    Kim, J.H.2    Hwang, S.W.3    Lee, W.J.4    Yoon, H.K.5    Lee, H.S.6    Hong, S.S.7
  • 34
    • 13844256497 scopus 로고    scopus 로고
    • Production of recombinant amyloid-β peptide 42 as an ubiquitin extension
    • E.K. Lee, J.H. Hwang, D.Y. Shin, D.I. Kim, Y.J. Yoo, Production of recombinant amyloid-β peptide 42 as an ubiquitin extension, Protein Express. Purif. 40 (2005) 183-189.
    • (2005) Protein Express. Purif. , vol.40 , pp. 183-189
    • Lee, E.K.1    Hwang, J.H.2    Shin, D.Y.3    Kim, D.I.4    Yoo, Y.J.5
  • 35
    • 0031958566 scopus 로고    scopus 로고
    • Erratum: Production of active chimeric pediocin AcH in Escherichia coil in the absence of processing and secretion genes from the Pediococcus pap operon (Applied and Environmental Microbiology 64:1 (20))
    • K.W. Miller, R. Schamber, Y.L. Chen, B. Ray, Production of active chimeric pediocin AcH in Escherichia coli in the absence of processing and secretion genes from the Pediococcus pap operon, Appl. Environ. Microbiol. 64 (1998) 1587. (Pubitemid 28188440)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.4 , pp. 1587
    • Miller, K.W.1    Schamber, R.2    Chen, Y.3    Ray, B.4
  • 37
    • 0031940586 scopus 로고    scopus 로고
    • Isolation of recombinant secretory proteins by limited induction and quantitative harvest
    • H.F. Rosenberg, Isolation of recombinant secretory proteins by limited induction and quantitative harvest, Biotechniques 24 (1998) 188-189.
    • (1998) Biotechniques , vol.24 , pp. 188-189
    • Rosenberg, H.F.1
  • 38
    • 0036192267 scopus 로고    scopus 로고
    • Growth rate-dependent changes in Escherichia coli membrane structure and protein leakage
    • DOI 10.1007/s00253-001-0889-0
    • A. Shokri, A.M. Sanden, G. Larsson, Growth rate-dependent changes in Escherichia coli membrane structure and protein leakage, Appl. Microb. Biotechnol. 58 (2002) 386-392. (Pubitemid 34185585)
    • (2002) Applied Microbiology and Biotechnology , vol.58 , Issue.3 , pp. 386-392
    • Shokri, A.1    Sanden, A.M.2    Larsson, G.3


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