메뉴 건너뛰기




Volumn 362, Issue 1-2, 2010, Pages 161-167

New ELISA approach based on coiled-coil interactions

Author keywords

E K coiled coil interactions; EGF; ELISA test

Indexed keywords

EPIDERMAL GROWTH FACTOR; POLYHISTIDINE TAG; PROTEIN ANTIBODY; RECOMBINANT PROTEIN;

EID: 77958498880     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jim.2010.09.027     Document Type: Article
Times cited : (15)

References (19)
  • 1
    • 56549095636 scopus 로고    scopus 로고
    • The bioactivity and receptor affinity of recombinant tagged EGF designed for tissue engineering applications is defined by the nature and position of the tags
    • Boucher C., St-Laurent G., Loignon M., Jolicoeur M., De Crescenzo G., Durocher Y. The bioactivity and receptor affinity of recombinant tagged EGF designed for tissue engineering applications is defined by the nature and position of the tags. Tissue Eng. A 2008, 14:2069.
    • (2008) Tissue Eng. A , vol.14 , pp. 2069
    • Boucher, C.1    St-Laurent, G.2    Loignon, M.3    Jolicoeur, M.4    De Crescenzo, G.5    Durocher, Y.6
  • 2
    • 70349102959 scopus 로고    scopus 로고
    • Epidermal growth factor tethered through coiled-coil interactions induces cell surface receptor phosphorylation
    • Boucher C., Liberelle B., Jolicoeur M., Durocher Y., De Crescenzo G. Epidermal growth factor tethered through coiled-coil interactions induces cell surface receptor phosphorylation. Bioconjugate Chem. 2009, 20:1569.
    • (2009) Bioconjugate Chem. , vol.20 , pp. 1569
    • Boucher, C.1    Liberelle, B.2    Jolicoeur, M.3    Durocher, Y.4    De Crescenzo, G.5
  • 6
    • 0000920828 scopus 로고
    • The packing of alpha-helices: simple coiled coils
    • Crick F.H.C. The packing of alpha-helices: simple coiled coils. Acta Crystallogr. 1953, 6:689.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689
    • Crick, F.H.C.1
  • 7
    • 12244313435 scopus 로고    scopus 로고
    • Real-time monitoring of the interactions of two-stranded de novo designed coiled-coils: Effect of chain length on the kinetic and thermodynamic constants of binding
    • De Crescenzo G., Litowski J.R., Hodges R.S., O'Connor-McCourt M.D. Real-time monitoring of the interactions of two-stranded de novo designed coiled-coils: Effect of chain length on the kinetic and thermodynamic constants of binding. Biochemistry (Mosc). 2003, 42:1754.
    • (2003) Biochemistry (Mosc). , vol.42 , pp. 1754
    • De Crescenzo, G.1    Litowski, J.R.2    Hodges, R.S.3    O'Connor-McCourt, M.D.4
  • 8
    • 0242684423 scopus 로고    scopus 로고
    • Transforming growth factor-beta (TGF-beta) binding to the extracellular domain of the type II TGF-beta receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding
    • De Crescenzo G., Pham P.L., Durocher Y., O'Connor-McCourt M.D. Transforming growth factor-beta (TGF-beta) binding to the extracellular domain of the type II TGF-beta receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding. J. Mol. Biol. 2003, 328:1173.
    • (2003) J. Mol. Biol. , vol.328 , pp. 1173
    • De Crescenzo, G.1    Pham, P.L.2    Durocher, Y.3    O'Connor-McCourt, M.D.4
  • 9
    • 2942733360 scopus 로고    scopus 로고
    • Enhancement of the antagonistic potency of transforming growth factor-beta receptor extracellular domains by coiled coil-induced homo- and heterodimerization
    • De Crescenzo G., Pham P.L., Durocher Y., Chao H., O'Connor-McCourt M.D. Enhancement of the antagonistic potency of transforming growth factor-beta receptor extracellular domains by coiled coil-induced homo- and heterodimerization. J. Biol. Chem. 2004, 279:26013.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26013
    • De Crescenzo, G.1    Pham, P.L.2    Durocher, Y.3    Chao, H.4    O'Connor-McCourt, M.D.5
  • 10
    • 58749095819 scopus 로고    scopus 로고
    • Escherichia coli expression and refolding of E/K-coil-tagged EGF generates fully bioactive EGF for diverse applications
    • Le P.U., Lenferink A.E., Pinard M., Baardsnes J., Massie B., O'Connor-McCourt M.D. Escherichia coli expression and refolding of E/K-coil-tagged EGF generates fully bioactive EGF for diverse applications. Protein Expr. Purif. 2009, 64:108.
    • (2009) Protein Expr. Purif. , vol.64 , pp. 108
    • Le, P.U.1    Lenferink, A.E.2    Pinard, M.3    Baardsnes, J.4    Massie, B.5    O'Connor-McCourt, M.D.6
  • 11
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: new structures and new functions
    • Lupas A. Coiled coils: new structures and new functions. Trends Biochem. Sci. 1996, 21:375.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375
    • Lupas, A.1
  • 13
    • 61849152831 scopus 로고    scopus 로고
    • Surface-Anchoring of Spontaneously Dimerized Epidermal Growth Factor for Highly Selective Expansion of Neural Stem Cells
    • Nakaji-Hirabayashi T., Kato K., Iwata H. Surface-Anchoring of Spontaneously Dimerized Epidermal Growth Factor for Highly Selective Expansion of Neural Stem Cells. Bioconjugate Chem. 2009, 20:102.
    • (2009) Bioconjugate Chem. , vol.20 , pp. 102
    • Nakaji-Hirabayashi, T.1    Kato, K.2    Iwata, H.3
  • 14
    • 13144257721 scopus 로고    scopus 로고
    • In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae
    • Noirclerc-Savoye M., Le Gouellec A., Morlot C., Dideberg O., Vernet T., Zapun A. In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae. Mol. Microbiol. 2005, 55:413.
    • (2005) Mol. Microbiol. , vol.55 , pp. 413
    • Noirclerc-Savoye, M.1    Le Gouellec, A.2    Morlot, C.3    Dideberg, O.4    Vernet, T.5    Zapun, A.6
  • 15
    • 51349107479 scopus 로고    scopus 로고
    • Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure
    • Parry D.A., Fraser R.D., Squire J.M. Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure. J. Struct. Biol. 2008, 163:258.
    • (2008) J. Struct. Biol. , vol.163 , pp. 258
    • Parry, D.A.1    Fraser, R.D.2    Squire, J.M.3
  • 17
    • 0029850976 scopus 로고    scopus 로고
    • Engineering a de novo-designed coiled-coil heterodimerization domain off the rapid detection, purification and characterization of recombinantly expressed peptides and proteins
    • Tripet B., Yu L., Bautista D.L., Wong W.Y., Irvin R.T., Hodges R.S. Engineering a de novo-designed coiled-coil heterodimerization domain off the rapid detection, purification and characterization of recombinantly expressed peptides and proteins. Protein Eng. 1996, 9:1029.
    • (1996) Protein Eng. , vol.9 , pp. 1029
    • Tripet, B.1    Yu, L.2    Bautista, D.L.3    Wong, W.Y.4    Irvin, R.T.5    Hodges, R.S.6
  • 18
    • 12244269333 scopus 로고    scopus 로고
    • Kinetic analysis of the interactions between troponin C (TnC) and troponin I (TnI) binding peptides: evidence for separate binding sites for the "structural" N-terminus and the "regulatory" C-terminus of TnI on TnC
    • Tripet B., De Crescenzo G., Grothe S., O'Connor-McCourt M., Hodges R.S. Kinetic analysis of the interactions between troponin C (TnC) and troponin I (TnI) binding peptides: evidence for separate binding sites for the "structural" N-terminus and the "regulatory" C-terminus of TnI on TnC. J. Mol. Recognit. 2003, 16:37.
    • (2003) J. Mol. Recognit. , vol.16 , pp. 37
    • Tripet, B.1    De Crescenzo, G.2    Grothe, S.3    O'Connor-McCourt, M.4    Hodges, R.S.5
  • 19
    • 0035853291 scopus 로고    scopus 로고
    • Socket: a program for identifying and analysing coiled-coil motifs within protein structures
    • Walshaw J., Woolfson D.N. Socket: a program for identifying and analysing coiled-coil motifs within protein structures. J. Mol. Biol. 2001, 307:1427.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1427
    • Walshaw, J.1    Woolfson, D.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.