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Volumn 52, Issue 1, 2007, Pages 202-209

On-column refolding of recombinant chemokines for NMR studies and biological assays

Author keywords

Artificial chaperones; Metal affinity chromatography; Protein folding

Indexed keywords

CHEMOKINE; RECOMBINANT PROTEIN;

EID: 33845933655     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.09.009     Document Type: Article
Times cited : (31)

References (27)
  • 1
    • 0034144269 scopus 로고    scopus 로고
    • Chemokines: a new classification system and their role in immunity
    • Zlotnik A., and Yoshie O. Chemokines: a new classification system and their role in immunity. Immunity 12 (2000) 121-127
    • (2000) Immunity , vol.12 , pp. 121-127
    • Zlotnik, A.1    Yoshie, O.2
  • 2
    • 0034829818 scopus 로고    scopus 로고
    • Chemokines in pathology and medicine
    • Baggiolini M. Chemokines in pathology and medicine. J. Intern. Med. 250 (2001) 91-104
    • (2001) J. Intern. Med. , vol.250 , pp. 91-104
    • Baggiolini, M.1
  • 5
    • 0032507962 scopus 로고    scopus 로고
    • Function of the chemokine receptor CXCR4 in haematopoiesis and in cerebellar development
    • Zou Y.R., Kottmann A.H., Kuroda M., Taniuchi I., and Littman D.R. Function of the chemokine receptor CXCR4 in haematopoiesis and in cerebellar development. Nature 393 (1998) 595-599
    • (1998) Nature , vol.393 , pp. 595-599
    • Zou, Y.R.1    Kottmann, A.H.2    Kuroda, M.3    Taniuchi, I.4    Littman, D.R.5
  • 10
    • 15244345079 scopus 로고    scopus 로고
    • The monomer-dimer equilibrium of stromal cell-derived factor-1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin
    • Veldkamp C.T., Peterson F.C., Pelzek A.J., and Volkman B.F. The monomer-dimer equilibrium of stromal cell-derived factor-1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin. Protein Sci. 14 (2005) 1071-1081
    • (2005) Protein Sci. , vol.14 , pp. 1071-1081
    • Veldkamp, C.T.1    Peterson, F.C.2    Pelzek, A.J.3    Volkman, B.F.4
  • 11
    • 10044240717 scopus 로고    scopus 로고
    • Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1alpha
    • Gozansky E.K., Louis J.M., Caffrey M., and Clore G.M. Mapping the binding of the N-terminal extracellular tail of the CXCR4 receptor to stromal cell-derived factor-1alpha. J. Mol. Biol. 345 (2005) 651-658
    • (2005) J. Mol. Biol. , vol.345 , pp. 651-658
    • Gozansky, E.K.1    Louis, J.M.2    Caffrey, M.3    Clore, G.M.4
  • 12
    • 0029774156 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation
    • Rozema D., and Gellman S.H. Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation. Biochemistry 35 (1996) 15760-15771
    • (1996) Biochemistry , vol.35 , pp. 15760-15771
    • Rozema, D.1    Gellman, S.H.2
  • 13
    • 0030041098 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of carbonic anhydrase B
    • Rozema D., and Gellman S.H. Artificial chaperone-assisted refolding of carbonic anhydrase B. J. Biol. Chem. 271 (1996) 3478-3487
    • (1996) J. Biol. Chem. , vol.271 , pp. 3478-3487
    • Rozema, D.1    Gellman, S.H.2
  • 16
    • 1842477451 scopus 로고    scopus 로고
    • Identification and characterization of a glycosaminoglycan recognition element of the C chemokine lymphotactin
    • Peterson F.C., Elgin E.S., Nelson T.J., Zhang F., Hoeger T.J., Linhardt R.J., and Volkman B.F. Identification and characterization of a glycosaminoglycan recognition element of the C chemokine lymphotactin. J. Biol. Chem. 279 (2004) 12598-12604
    • (2004) J. Biol. Chem. , vol.279 , pp. 12598-12604
    • Peterson, F.C.1    Elgin, E.S.2    Nelson, T.J.3    Zhang, F.4    Hoeger, T.J.5    Linhardt, R.J.6    Volkman, B.F.7
  • 17
    • 0040560068 scopus 로고    scopus 로고
    • Solution structure and dynamics of the CX3C chemokine domain of fractalkine and its interaction with an N-terminal fragment of CX3CR1
    • Mizoue L.S., Bazan J.F., Johnson E.C., and Handel T.M. Solution structure and dynamics of the CX3C chemokine domain of fractalkine and its interaction with an N-terminal fragment of CX3CR1. Biochemistry 38 (1999) 1402-1414
    • (1999) Biochemistry , vol.38 , pp. 1402-1414
    • Mizoue, L.S.1    Bazan, J.F.2    Johnson, E.C.3    Handel, T.M.4
  • 19
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
    • Mori S., Abeygunawardana C., Johnson M.O., and van Zijl P.C.M. Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J. Magn. Reson. Ser. B 105 (1995) 94-98
    • (1995) J. Magn. Reson. Ser. B , vol.105 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    Johnson, M.O.3    van Zijl, P.C.M.4
  • 20
    • 0032499791 scopus 로고    scopus 로고
    • Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 "fusin" coreceptor
    • Dealwis C., Fernandez E.J., Thompson D.A., Simon R.J., Siani M.A., and Lolis E. Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 "fusin" coreceptor. Proc. Natl. Acad. Sci. USA 95 (1998) 6941-6946
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6941-6946
    • Dealwis, C.1    Fernandez, E.J.2    Thompson, D.A.3    Simon, R.J.4    Siani, M.A.5    Lolis, E.6
  • 21
    • 0033895828 scopus 로고    scopus 로고
    • Crystal structure of recombinant native SDF-1alpha with additional mutagenesis studies: an attempt at a more comprehensive interpretation of accumulated structure-activity relationship data
    • Ohnishi Y., Senda T., Nandhagopal N., Sugimoto K., Shioda T., Nagal Y., and Mitsui Y. Crystal structure of recombinant native SDF-1alpha with additional mutagenesis studies: an attempt at a more comprehensive interpretation of accumulated structure-activity relationship data. J. Interferon Cytokine Res. 20 (2000) 691-700
    • (2000) J. Interferon Cytokine Res. , vol.20 , pp. 691-700
    • Ohnishi, Y.1    Senda, T.2    Nandhagopal, N.3    Sugimoto, K.4    Shioda, T.5    Nagal, Y.6    Mitsui, Y.7
  • 23
    • 0037124112 scopus 로고    scopus 로고
    • Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions
    • Kuloglu E.S., McCaslin D.R., Markley J.L., and Volkman B.F. Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions. J. Biol. Chem. 277 (2002) 17863-17870
    • (2002) J. Biol. Chem. , vol.277 , pp. 17863-17870
    • Kuloglu, E.S.1    McCaslin, D.R.2    Markley, J.L.3    Volkman, B.F.4
  • 24
    • 0032575620 scopus 로고    scopus 로고
    • N-terminal peptides of stromal cell-derived factor-1 with CXC chemokine receptor 4 agonist and antagonist activities
    • Loetscher P., Gong J.H., Dewald B., Baggiolini M., and Clark-Lewis I. N-terminal peptides of stromal cell-derived factor-1 with CXC chemokine receptor 4 agonist and antagonist activities. J. Biol. Chem. 273 (1998) 22279-22283
    • (1998) J. Biol. Chem. , vol.273 , pp. 22279-22283
    • Loetscher, P.1    Gong, J.H.2    Dewald, B.3    Baggiolini, M.4    Clark-Lewis, I.5
  • 25
  • 26
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • Middelberg A.P. Preparative protein refolding. TRENDS Biotechnol. 20 (2002) 437-443
    • (2002) TRENDS Biotechnol. , vol.20 , pp. 437-443
    • Middelberg, A.P.1
  • 27
    • 0033654609 scopus 로고    scopus 로고
    • Purification of recombinant chemokines from E. coli
    • Proudfoot A.E., and Borlat F. Purification of recombinant chemokines from E. coli. Methods Mol. Biol. 138 (2000) 75-87
    • (2000) Methods Mol. Biol. , vol.138 , pp. 75-87
    • Proudfoot, A.E.1    Borlat, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.