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Volumn 35, Issue 1, 2004, Pages 39-45

Optimized expression and refolding of human keratoepithelin in BL21 (DE3)

Author keywords

BIGH3; Keratoepithelin; Refolding

Indexed keywords

ESCHERICHIA COLI;

EID: 16544362414     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2003.12.020     Document Type: Article
Times cited : (11)

References (27)
  • 1
    • 0026783009 scopus 로고
    • cDNa cloning and sequence analysis of beta ig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-beta
    • J. Skonier, M. Neubauer, L. Madisen, K. Bennett, G.D. Plowman, A.F. Purchio, cDNA cloning and sequence analysis of beta ig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-beta, DNA Cell Biol. 11 (1992) 511-522.
    • (1992) DNA Cell Biol. , vol.11 , pp. 511-522
    • Skonier, J.1    Neubauer, M.2    Madisen, L.3    Bennett, K.4    Plowman, G.D.5    Purchio, A.F.6
  • 4
    • 0032506997 scopus 로고    scopus 로고
    • Structural and phylogenetic analyses of RGD-CAP/βig-h3, a fasciclin-like adhesion protein expressed in chick chondrocytes
    • T. Kawamoto, M. Noshiro, M. Shen, K. Nakamasu, K. Hashimoto, Y. Kawashima-Ohya, Y. Kateo, Structural and phylogenetic analyses of RGD-CAP/βig-h3, a fasciclin-like adhesion protein expressed in chick chondrocytes, Biochim. Biochem. Acta 1395 (1998) 288-292.
    • (1998) Biochim. Biochem. Acta , vol.1395 , pp. 288-292
    • Kawamoto, T.1    Noshiro, M.2    Shen, M.3    Nakamasu, K.4    Hashimoto, K.5    Kawashima-Ohya, Y.6    Kateo, Y.7
  • 5
    • 0030696781 scopus 로고    scopus 로고
    • Immunohistochemical and ultrastructural localization of MP78/70 (/βig-h3) in extracellular matrix of developing and mature bovine tissues
    • M.A. Gibson, J.S. Kumaratilake, E.G. Cleary, Immunohistochemical and ultrastructural localization of MP78/70 (/βig-h3) in extracellular matrix of developing and mature bovine tissues, J. Histochem. Cytochem. 45 (1997) 1683-1696.
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 1683-1696
    • Gibson, M.A.1    Kumaratilake, J.S.2    Cleary, E.G.3
  • 6
    • 0029762295 scopus 로고    scopus 로고
    • Beta ig-h3 is synthesized by corneal epithelium and perhaps endothelium in Fuchs' dystrophic corneas
    • K. Hirano, G.K. Klintworth, Q. Zhan, K. Bennett, C. Cintron, Beta ig-h3 is synthesized by corneal epithelium and perhaps endothelium in Fuchs' dystrophic corneas, Curr. Eye. Res. 15 (1996) 965-972.
    • (1996) Curr. Eye. Res. , vol.15 , pp. 965-972
    • Hirano, K.1    Klintworth, G.K.2    Zhan, Q.3    Bennett, K.4    Cintron, C.5
  • 8
    • 0034024615 scopus 로고    scopus 로고
    • A TGFβ-inducible cell adhesion molecule, βig-h3, is downregulated in melorheostosis and involved in osteogenesis
    • J.E. Kim, E.H. Kim, E.H. Han, R.W. Park, I.H. Park, S.H. Jun, J.C. Kim, M.F. Young, I.S. Kim, A TGFβ-inducible cell adhesion molecule, βig-h3, is downregulated in melorheostosis and involved in osteogenesis, J. Cell. Biochem. 77 (2000) 169-178.
    • (2000) J. Cell. Biochem. , vol.77 , pp. 169-178
    • Kim, J.E.1    Kim, E.H.2    Han, E.H.3    Park, R.W.4    Park, I.H.5    Jun, S.H.6    Kim, J.C.7    Young, M.F.8    Kim, I.S.9
  • 10
    • 0028989879 scopus 로고
    • βIG-H3, a novel secretory protein inducible by transforming growth factor-β, is present in normal skin and promotes the adhesion and spreading of dermal fibroblasts in vitro
    • R.G. LeBaron, K.I. Bezverkov, M.P. Zimber, R. Pavelec, J. Skonier, A.F. Purchio, βIG-H3, a novel secretory protein inducible by transforming growth factor-β, is present in normal skin and promotes the adhesion and spreading of dermal fibroblasts in vitro, J. Invest. Dermatol. 104 (1995) 844-849.
    • (1995) J. Invest. Dermatol. , vol.104 , pp. 844-849
    • LeBaron, R.G.1    Bezverkov, K.I.2    Zimber, M.P.3    Pavelec, R.4    Skonier, J.5    Purchio, A.F.6
  • 11
    • 0034613378 scopus 로고    scopus 로고
    • Identification of motifs for cell adhesion within the repeated domains of transforming growth factor-β-induced gene, βig-h3
    • J.E. Kim, S.J. Kim, B.H. Lee, R.W. Park, K.S. Kim, I.S. Kim, Identification of motifs for cell adhesion within the repeated domains of transforming growth factor-β-induced gene, βig-h3, J. Biol. Chem. 275 (2000) 30907-30915.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30907-30915
    • Kim, J.E.1    Kim, S.J.2    Lee, B.H.3    Park, R.W.4    Kim, K.S.5    Kim, I.S.6
  • 16
    • 0036998665 scopus 로고    scopus 로고
    • TGFBI gene transcript is transforming growth factor-beta1-responsive and cell density-dependent in a human corneal epithelial cell line
    • M. Wang, F. Munier, K. Araki-Saski, D. Schorderet, TGFBI gene transcript is transforming growth factor-beta1-responsive and cell density-dependent in a human corneal epithelial cell line, Ophthalmic Genet. 23 (2002) 237-245.
    • (2002) Ophthalmic Genet. , vol.23 , pp. 237-245
    • Wang, M.1    Munier, F.2    Araki-Saski, K.3    Schorderet, D.4
  • 17
    • 0028145930 scopus 로고
    • cDNA from human ocular ciliary epithelium homologous to beta ig-h3 is preferentially expressed as an extracellular protein in the corneal epithelium
    • J. Escribano, N. Hernando, S. Ghosh, J. Crabb, M. Coca-Prados, cDNA from human ocular ciliary epithelium homologous to beta ig-h3 is preferentially expressed as an extracellular protein in the corneal epithelium, J. Cell Physiol. 160 (1994) 511-521.
    • (1994) J. Cell Physiol. , vol.160 , pp. 511-521
    • Escribano, J.1    Hernando, N.2    Ghosh, S.3    Crabb, J.4    Coca-Prados, M.5
  • 19
    • 0033462204 scopus 로고    scopus 로고
    • Advances in the molecular genetics of corneal dystrophies
    • G.K. Klintworth, Advances in the molecular genetics of corneal dystrophies, Am. J. Ophthalmol. 128 (1999) 747-754.
    • (1999) Am. J. Ophthalmol. , vol.128 , pp. 747-754
    • Klintworth, G.K.1
  • 22
    • 0034646599 scopus 로고    scopus 로고
    • Amyloid and non-amyloid forms of 5q31-linked corneal dystrophy resulting from kerato-epithelin mutations at Arg-124 are associated with abnormal turnover of the protein
    • E. Korvatska, H. Henry, Y. Mashima, M. Yamada, C. Bachmann, F.L. Munier, D.F. Schoderet, Amyloid and non-amyloid forms of 5q31-linked corneal dystrophy resulting from kerato-epithelin mutations at Arg-124 are associated with abnormal turnover of the protein, J. Biol. Chem. 275 (2000) 11465-11469.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11465-11469
    • Korvatska, E.1    Henry, H.2    Mashima, Y.3    Yamada, M.4    Bachmann, C.5    Munier, F.L.6    Schoderet, D.F.7
  • 24
    • 0032888314 scopus 로고    scopus 로고
    • Influence of fetal calf serum, fibroblast growth factors, and hepatocyte growth factor on three-dimensional cultures of human keratocytes in collagen gel matrix
    • V.M. Borderie, N. Mourra, L. Laroche, Influence of fetal calf serum, fibroblast growth factors, and hepatocyte growth factor on three-dimensional cultures of human keratocytes in collagen gel matrix, Graefes Arch. Clin. Exp. Ophthalmol. 237 (1999) 861-869.
    • (1999) Graefes Arch. Clin. Exp. Ophthalmol. , vol.237 , pp. 861-869
    • Borderie, V.M.1    Mourra, N.2    Laroche, L.3
  • 25
    • 0030579519 scopus 로고    scopus 로고
    • Method for increasing the yield of properly folded recombinant y interferon from inclusion bodies
    • D. Arora, N. Khanna, Method for increasing the yield of properly folded recombinant y interferon from inclusion bodies, J. Biotechnol. 52 (1996) 127-133.
    • (1996) J. Biotechnol. , vol.52 , pp. 127-133
    • Arora, D.1    Khanna, N.2
  • 26
    • 0031688064 scopus 로고    scopus 로고
    • Renaturation of recombinant human neurotrophin-3 from inclusion bodies using a suppressor agent of aggregation
    • M. Suenaga, H. Ohmae, S. Tsuji, T. Itoh, O. Nishimura, Renaturation of recombinant human neurotrophin-3 from inclusion bodies using a suppressor agent of aggregation, Biotechnol. Appl. Biochem. 28 (1998) 119-124.
    • (1998) Biotechnol. Appl. Biochem. , vol.28 , pp. 119-124
    • Suenaga, M.1    Ohmae, H.2    Tsuji, S.3    Itoh, T.4    Nishimura, O.5
  • 27
    • 0345636051 scopus 로고    scopus 로고
    • Practical considerations in refolding proteins from inclusion bodies
    • K. Tsumoto, D. Ejima, I. Kumagai, T. Arakawa, Practical considerations in refolding proteins from inclusion bodies, Protein Expr. Purif. 28 (2003) 1-8.
    • (2003) Protein Expr. Purif. , vol.28 , pp. 1-8
    • Tsumoto, K.1    Ejima, D.2    Kumagai, I.3    Arakawa, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.