메뉴 건너뛰기




Volumn 48, Issue 1, 2006, Pages 134-141

Histidine tag fusion increases expression levels of active recombinant amelogenin in Escherichia coli

Author keywords

Histidine; Human osteoblasts; Immobilised metal ion affinity chromatography; Murine amelogenin; Osteocalcin

Indexed keywords

AMELOGENIN; HISTIDINE; HYBRID PROTEIN; OSTEOCALCIN;

EID: 33646882130     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.01.005     Document Type: Article
Times cited : (45)

References (32)
  • 1
    • 0019205616 scopus 로고
    • Properties of dissociatively extracted fetal tooth matrix proteins. I. Principal molecular species in developing bovine enamel
    • Termine J.D., Belcourt A.B., Christner P.J., Conn K.M., and Nylen M.U. Properties of dissociatively extracted fetal tooth matrix proteins. I. Principal molecular species in developing bovine enamel. J. Biol. Chem. 255 (1980) 9760-9768
    • (1980) J. Biol. Chem. , vol.255 , pp. 9760-9768
    • Termine, J.D.1    Belcourt, A.B.2    Christner, P.J.3    Conn, K.M.4    Nylen, M.U.5
  • 2
    • 0033617953 scopus 로고    scopus 로고
    • The structural biology of the developing dental enamel matrix
    • Fincham A.G., Moradian-Oldak J., and Simmer J.P. The structural biology of the developing dental enamel matrix. J. Struct. Biol. 126 (1999) 270-299
    • (1999) J. Struct. Biol. , vol.126 , pp. 270-299
    • Fincham, A.G.1    Moradian-Oldak, J.2    Simmer, J.P.3
  • 3
    • 12844282379 scopus 로고    scopus 로고
    • The effect of recombinant mouse amelogenins on the formation and organization of hydroxyapatite crystals in vitro
    • Beniash E., Simmer J.P., and Margolis H.C. The effect of recombinant mouse amelogenins on the formation and organization of hydroxyapatite crystals in vitro. J. Struct. Biol. 149 (2005) 182-190
    • (2005) J. Struct. Biol. , vol.149 , pp. 182-190
    • Beniash, E.1    Simmer, J.P.2    Margolis, H.C.3
  • 4
    • 0032487612 scopus 로고    scopus 로고
    • Interaction of amelogenin with hydroxyapatite crystals: an adherence effect through amelogenin molecular self-association
    • Moradian-Oldak J., Tan J., and Fincham A.G. Interaction of amelogenin with hydroxyapatite crystals: an adherence effect through amelogenin molecular self-association. Biopolymers 46 (1998) 225-238
    • (1998) Biopolymers , vol.46 , pp. 225-238
    • Moradian-Oldak, J.1    Tan, J.2    Fincham, A.G.3
  • 7
    • 0029177801 scopus 로고
    • Alternative splicing of amelogenins
    • Simmer J.P. Alternative splicing of amelogenins. Connect. Tissue Res. 32 (1995) 131-136
    • (1995) Connect. Tissue Res. , vol.32 , pp. 131-136
    • Simmer, J.P.1
  • 10
    • 0028519190 scopus 로고
    • Detection of monodisperse aggregates of a recombinant amelogenin by dynamic light scattering
    • Moradian-Oldak J., Simmer J.P., Lau E.C., Sarte P.E., Slavkin H.C., and Fincham A.G. Detection of monodisperse aggregates of a recombinant amelogenin by dynamic light scattering. Biopolymers 34 (1994) 1339-1347
    • (1994) Biopolymers , vol.34 , pp. 1339-1347
    • Moradian-Oldak, J.1    Simmer, J.P.2    Lau, E.C.3    Sarte, P.E.4    Slavkin, H.C.5    Fincham, A.G.6
  • 12
    • 0033278065 scopus 로고    scopus 로고
    • Characterization of recombinant pig enamelysin activity and cleavage of recombinant pig and mouse amelogenins
    • Ryu O.H., Fincham A.G., Hu C.C., Zhang C., Qian Q., Bartlett J.D., and Simmer J.P. Characterization of recombinant pig enamelysin activity and cleavage of recombinant pig and mouse amelogenins. J. Dent. Res. 78 (1999) 743-750
    • (1999) J. Dent. Res. , vol.78 , pp. 743-750
    • Ryu, O.H.1    Fincham, A.G.2    Hu, C.C.3    Zhang, C.4    Qian, Q.5    Bartlett, J.D.6    Simmer, J.P.7
  • 14
    • 0037364601 scopus 로고    scopus 로고
    • X-linked amelogenesis imperfecta may result from decreased formation of tyrosine rich amelogenin peptide (TRAP)
    • Li W., Gao C., Yan Y., and DenBesten P. X-linked amelogenesis imperfecta may result from decreased formation of tyrosine rich amelogenin peptide (TRAP). Arch. Oral Biol. 48 (2003) 177-183
    • (2003) Arch. Oral Biol. , vol.48 , pp. 177-183
    • Li, W.1    Gao, C.2    Yan, Y.3    DenBesten, P.4
  • 15
    • 0031227926 scopus 로고    scopus 로고
    • Enamel matrix derivative (EMDOGAIN) in the treatment of intrabony periodontal defects
    • Heijl L., Heden G., Svardstrom G., and Ostgren A. Enamel matrix derivative (EMDOGAIN) in the treatment of intrabony periodontal defects. J. Clin. Periodontol. 24 (1997) 705-714
    • (1997) J. Clin. Periodontol. , vol.24 , pp. 705-714
    • Heijl, L.1    Heden, G.2    Svardstrom, G.3    Ostgren, A.4
  • 16
    • 0034852854 scopus 로고    scopus 로고
    • Is there more to enamel matrix proteins than biomineralization?
    • Zeichner-David M. Is there more to enamel matrix proteins than biomineralization?. Matrix Biol. 20 (2001) 307-316
    • (2001) Matrix Biol. , vol.20 , pp. 307-316
    • Zeichner-David, M.1
  • 17
    • 0037280016 scopus 로고    scopus 로고
    • Amelogenin gene splice products: potential signaling molecules
    • Veis A. Amelogenin gene splice products: potential signaling molecules. Cell. Mol. Life Sci. 60 (2003) 38-55
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 38-55
    • Veis, A.1
  • 19
    • 0031230219 scopus 로고    scopus 로고
    • Periodontal regeneration in a buccal dehiscence model in monkeys after application of enamel matrix proteins
    • Hammarstrom L., Heijl L., and Gestrelius S. Periodontal regeneration in a buccal dehiscence model in monkeys after application of enamel matrix proteins. J. Clin. Periodontol. 24 (1997) 669-677
    • (1997) J. Clin. Periodontol. , vol.24 , pp. 669-677
    • Hammarstrom, L.1    Heijl, L.2    Gestrelius, S.3
  • 20
    • 0035576368 scopus 로고    scopus 로고
    • Porcine enamel matrix derivative enhances trabecular bone regeneration during wound healing of injured rat femur
    • Kawana F., Sawae Y., Sahara T., Tanaka S., Debari K., Shimizu M., and Sasaki T. Porcine enamel matrix derivative enhances trabecular bone regeneration during wound healing of injured rat femur. Anat. Rec. 264 (2001) 438-446
    • (2001) Anat. Rec. , vol.264 , pp. 438-446
    • Kawana, F.1    Sawae, Y.2    Sahara, T.3    Tanaka, S.4    Debari, K.5    Shimizu, M.6    Sasaki, T.7
  • 22
    • 0042760453 scopus 로고    scopus 로고
    • The effects of enamel matrix derivative (EMD) on osteoblastic cells in culture and bone regeneration in a rat skull defect
    • Yoneda S., Itoh D., Kuroda S., Kondo H., Umezawa A., Ohya K., Ohyama T., and Kasugai S. The effects of enamel matrix derivative (EMD) on osteoblastic cells in culture and bone regeneration in a rat skull defect. J. Periodontal Res. 38 (2003) 333-342
    • (2003) J. Periodontal Res. , vol.38 , pp. 333-342
    • Yoneda, S.1    Itoh, D.2    Kuroda, S.3    Kondo, H.4    Umezawa, A.5    Ohya, K.6    Ohyama, T.7    Kasugai, S.8
  • 24
    • 0034243492 scopus 로고    scopus 로고
    • Porcine fetal enamel matrix derivative stimulates proliferation but not differentiation of pre-osteoblastic 2T9 cells, inhibits proliferation and stimulates differentiation of osteoblast-like MG63 cells, and increases proliferation and differentiation of normal human osteoblast NHOst cells
    • Schwartz Z., Carnes Jr. D.L., Pulliam R., Lohmann C.H., Sylvia V.L., Liu Y., Dean D.D., Cochran D.L., and Boyan B.D. Porcine fetal enamel matrix derivative stimulates proliferation but not differentiation of pre-osteoblastic 2T9 cells, inhibits proliferation and stimulates differentiation of osteoblast-like MG63 cells, and increases proliferation and differentiation of normal human osteoblast NHOst cells. J. Periodontol. 71 (2000) 1287-1296
    • (2000) J. Periodontol. , vol.71 , pp. 1287-1296
    • Schwartz, Z.1    Carnes Jr., D.L.2    Pulliam, R.3    Lohmann, C.H.4    Sylvia, V.L.5    Liu, Y.6    Dean, D.D.7    Cochran, D.L.8    Boyan, B.D.9
  • 25
    • 0034241456 scopus 로고    scopus 로고
    • In vitro wound healing responses to enamel matrix derivative
    • Hoang A.M., Oates T.W., and Cochran D.L. In vitro wound healing responses to enamel matrix derivative. J. Periodontol. 71 (2000) 1270-1277
    • (2000) J. Periodontol. , vol.71 , pp. 1270-1277
    • Hoang, A.M.1    Oates, T.W.2    Cochran, D.L.3
  • 26
    • 0041758588 scopus 로고    scopus 로고
    • Effect of Emdogain on human periodontal fibroblasts in an in vitro wound-healing model
    • Rincon J.C., Haase H.R., and Bartold P.M. Effect of Emdogain on human periodontal fibroblasts in an in vitro wound-healing model. J. Periodontal Res. 38 (2003) 290-295
    • (2003) J. Periodontal Res. , vol.38 , pp. 290-295
    • Rincon, J.C.1    Haase, H.R.2    Bartold, P.M.3
  • 28
    • 0033821661 scopus 로고    scopus 로고
    • Self-assembly properties of recombinant engineered amelogenin proteins analyzed by dynamic light scattering and atomic force microscopy
    • Moradian-Oldak J., Paine M.L., Lei Y.P., Fincham A.G., and Snead M.L. Self-assembly properties of recombinant engineered amelogenin proteins analyzed by dynamic light scattering and atomic force microscopy. J. Struct. Biol. 131 (2000) 27-37
    • (2000) J. Struct. Biol. , vol.131 , pp. 27-37
    • Moradian-Oldak, J.1    Paine, M.L.2    Lei, Y.P.3    Fincham, A.G.4    Snead, M.L.5
  • 30
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31 (2003) 3406-3415
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 31
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews D.H., Sabina J., Zuker M., and Turner D.H. Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J. Mol. Biol. 288 (1999) 911-940
    • (1999) J. Mol. Biol. , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 32
    • 0035007266 scopus 로고    scopus 로고
    • Controlled proteolysis of amelogenins reveals exposure of both carboxy- and amino-terminal regions
    • Moradian-Oldak J., Jimenez I., Maltby D., and Fincham A.G. Controlled proteolysis of amelogenins reveals exposure of both carboxy- and amino-terminal regions. Biopolymers 58 (2001) 606-616
    • (2001) Biopolymers , vol.58 , pp. 606-616
    • Moradian-Oldak, J.1    Jimenez, I.2    Maltby, D.3    Fincham, A.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.