메뉴 건너뛰기




Volumn 74, Issue 2, 2010, Pages 298-303

The effects of supplementing specific amino acids on the expression of elastin-like polypeptides (ELPs)

Author keywords

Amino acids supplement; Cell free protein synthesis; Elastin like polypeptide (ELP); Expression profile; Repetitive polypeptides; Repetitive protein

Indexed keywords

AMINO ACID; ELASTIN; OLIGOPEPTIDE; PEPTIDE;

EID: 77957744375     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.07.006     Document Type: Article
Times cited : (12)

References (17)
  • 1
    • 0027556206 scopus 로고
    • Synthesis of a genetically engineered repetitive polypeptide containing periodic selenomethionine residues
    • M.J. Dougherty, S. Kothakota, T.L. Mason, D.A. Tirrell, and M.J. Fournier Synthesis of a genetically engineered repetitive polypeptide containing periodic selenomethionine residues Macromolecules 26 1993 1779 1781
    • (1993) Macromolecules , vol.26 , pp. 1779-1781
    • Dougherty, M.J.1    Kothakota, S.2    Mason, T.L.3    Tirrell, D.A.4    Fournier, M.J.5
  • 2
    • 44949268630 scopus 로고
    • The biological production of protein polymers and their use
    • J. Cappello The biological production of protein polymers and their use J. Trends Biotechnol. 8 1990 309 311
    • (1990) J. Trends Biotechnol. , vol.8 , pp. 309-311
    • Cappello, J.1
  • 4
    • 0032739304 scopus 로고    scopus 로고
    • Purification of recombinant proteins by fusion with thermally-responsive polypeptides
    • D.E. Meyer, and A. Chilkoti Purification of recombinant proteins by fusion with thermally-responsive polypeptides Nat. Biotechnol. 17 11 1999 1112 1115
    • (1999) Nat. Biotechnol. , vol.17 , Issue.11 , pp. 1112-1115
    • Meyer, D.E.1    Chilkoti, A.2
  • 5
    • 0035957458 scopus 로고    scopus 로고
    • Tunable biopolymers for heavy metal removal
    • J. Kostal, A. Mulchandani, and W. Chen Tunable biopolymers for heavy metal removal Macromolecules 34 2001 2257 2261
    • (2001) Macromolecules , vol.34 , pp. 2257-2261
    • Kostal, J.1    Mulchandani, A.2    Chen, W.3
  • 6
    • 0036739152 scopus 로고    scopus 로고
    • Characterization of a genetically engineered elastin-like polypeptide for cartilaginous tissue repair
    • H. Betre, L.A. Setton, D.E. Meyer, and A. Chilkoti Characterization of a genetically engineered elastin-like polypeptide for cartilaginous tissue repair Biomacromolecules 3 5 2002 910 916
    • (2002) Biomacromolecules , vol.3 , Issue.5 , pp. 910-916
    • Betre, H.1    Setton, L.A.2    Meyer, D.E.3    Chilkoti, A.4
  • 8
    • 58849104014 scopus 로고    scopus 로고
    • Allosteric actuation of inverse phase transition of a stimulus-responsive fusion polypeptide by ligand binding
    • B. Kim, and A. Chilkoti Allosteric actuation of inverse phase transition of a stimulus-responsive fusion polypeptide by ligand binding J. Am. Chem. Soc. 130 52 2008 17867 17873
    • (2008) J. Am. Chem. Soc. , vol.130 , Issue.52 , pp. 17867-17873
    • Kim, B.1    Chilkoti, A.2
  • 9
    • 0037159267 scopus 로고    scopus 로고
    • A new cloning method for the preparation of long repetitive polypeptides without a sequence requirement
    • J.I. Won, and A.E. Barron A new cloning method for the preparation of long repetitive polypeptides without a sequence requirement Macromolecules 35 22 2002 8281 8287
    • (2002) Macromolecules , vol.35 , Issue.22 , pp. 8281-8287
    • Won, J.I.1    Barron, A.E.2
  • 10
    • 71249161487 scopus 로고    scopus 로고
    • Expression analysis of an elastin-like polypeptide (ELP) in a cell-free protein synthesis system
    • H.S. Chu, K.H. Lee, J.E. Park, D.M. Kim, B.G. Kim, and J.I. Won Expression analysis of an elastin-like polypeptide (ELP) in a cell-free protein synthesis system Enzyme Microb. Technol. 46 2010 87 91
    • (2010) Enzyme Microb. Technol. , vol.46 , pp. 87-91
    • Chu, H.S.1    Lee, K.H.2    Park, J.E.3    Kim, D.M.4    Kim, B.G.5    Won, J.I.6
  • 11
    • 33745026919 scopus 로고    scopus 로고
    • Ultra-high expression of a thermally responsive recombinant fusion protein in E. coli
    • D.C. Chow, M.R. Dreher, K. Trabbic-Carlson, and A. Chilkoti Ultra-high expression of a thermally responsive recombinant fusion protein in E. coli Biotechnol. Prog. 22 2006 638 646
    • (2006) Biotechnol. Prog. , vol.22 , pp. 638-646
    • Chow, D.C.1    Dreher, M.R.2    Trabbic-Carlson, K.3    Chilkoti, A.4
  • 12
    • 0029956987 scopus 로고    scopus 로고
    • A highly efficient cell-free protein synthesis system from E. coli
    • D.M. Kim, T. Kigawa, C.Y. Choi, and S. Yokoyama A highly efficient cell-free protein synthesis system from E. coli Eur. J. Biochem. 239 3 1996 881 886
    • (1996) Eur. J. Biochem. , vol.239 , Issue.3 , pp. 881-886
    • Kim, D.M.1    Kigawa, T.2    Choi, C.Y.3    Yokoyama, S.4
  • 13
    • 0034045838 scopus 로고    scopus 로고
    • Prolonging cell-free protein synthesis by selective reagent additions
    • D.M. Kim, and J.R. Swartz Prolonging cell-free protein synthesis by selective reagent additions Biotechnol. Prog. 16 3 2000 385 390
    • (2000) Biotechnol. Prog. , vol.16 , Issue.3 , pp. 385-390
    • Kim, D.M.1    Swartz, J.R.2
  • 14
    • 0023216021 scopus 로고
    • An increased content of protease La, the Lon gene-product, increases protein-degradation and blocks growth in E. coli
    • S.A. Goff, and A.L. Goldberg An increased content of protease La, the Lon gene-product, increases protein-degradation and blocks growth in E. coli J. Biol. Chem. 262 1987 4508 4515
    • (1987) J. Biol. Chem. , vol.262 , pp. 4508-4515
    • Goff, S.A.1    Goldberg, A.L.2
  • 15
    • 0036200174 scopus 로고    scopus 로고
    • Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: Examples from the elastin-like polypeptide system
    • D.E. Meyer, and A. Chilkoti Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: examples from the elastin-like polypeptide system Biomacromolecules 3 2002 357 367
    • (2002) Biomacromolecules , vol.3 , pp. 357-367
    • Meyer, D.E.1    Chilkoti, A.2
  • 16
    • 33750283167 scopus 로고    scopus 로고
    • Simple procedures for the construction of a robust and cost-effective cell-free protein synthesis system
    • T.W. Kim, J.W. Keum, I.S. Oh, C.Y. Choi, C.G. Park, and D.M. Kim Simple procedures for the construction of a robust and cost-effective cell-free protein synthesis system J. Biotechnol. 126 4 2006 554 561
    • (2006) J. Biotechnol. , vol.126 , Issue.4 , pp. 554-561
    • Kim, T.W.1    Keum, J.W.2    Oh, I.S.3    Choi, C.Y.4    Park, C.G.5    Kim, D.M.6
  • 17
    • 63349111721 scopus 로고    scopus 로고
    • A protocol for the production of recombinant spider silk-like proteins for artificial fiber spinning
    • F. Teulé, A.R. Cooper, W.A. Furin, D. Bittencourt, E.L. Rech, A. Brooks, and R.V. Lewis A protocol for the production of recombinant spider silk-like proteins for artificial fiber spinning Nat. Protoc. 4 3 2009 341 355
    • (2009) Nat. Protoc. , vol.4 , Issue.3 , pp. 341-355
    • Teulé, F.1    Cooper, A.R.2    Furin, W.A.3    Bittencourt, D.4    Rech, E.L.5    Brooks, A.6    Lewis, R.V.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.