메뉴 건너뛰기




Volumn 47, Issue 2, 2006, Pages 355-366

High-throughput identification of refolding conditions for LXRβ without a functional assay

Author keywords

Inclusion bodies; Liver X receptor ; Protein folding; Refolding screen

Indexed keywords

CELL RECEPTOR; COLLAGENASE; COLLAGENASE 3; DNA BINDING PROTEIN; INTERLEUKIN 13; LIVER X RECEPTOR; MMP13 PROTEIN, HUMAN; MMP13 PROTEIN, RAT; RECOMBINANT PROTEIN;

EID: 33646580434     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.11.010     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • Lilie H., Schwarz E., and Rudolph R. Advances in refolding of proteins produced in E. coli. Curr. Opin. Biotech. 9 (1998) 497-501
    • (1998) Curr. Opin. Biotech. , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 2
    • 0033386134 scopus 로고    scopus 로고
    • Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies
    • Misawa S., and Kumagai I. Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies. Biopolymers (Peptide Science) 51 (1999) 297-307
    • (1999) Biopolymers (Peptide Science) , vol.51 , pp. 297-307
    • Misawa, S.1    Kumagai, I.2
  • 3
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R., and Lilie H. In vitro folding of inclusion body proteins. FASEB J. 10 (1996) 49-56
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 5
    • 0028361018 scopus 로고
    • Refolding of recombinant proteins: process strategies and novel approaches
    • Chaudhuri J.B. Refolding of recombinant proteins: process strategies and novel approaches. Ann. N. Y. Acad. Sci. 721 (1994) 374-385
    • (1994) Ann. N. Y. Acad. Sci. , vol.721 , pp. 374-385
    • Chaudhuri, J.B.1
  • 6
    • 0348227649 scopus 로고    scopus 로고
    • In vitro protein refolding by chromatographic procedures
    • Li M., Su Z.-G., and Janson J.-C. In vitro protein refolding by chromatographic procedures. Protein Expr. Purif. 33 (2004) 1-10
    • (2004) Protein Expr. Purif. , vol.33 , pp. 1-10
    • Li, M.1    Su, Z.-G.2    Janson, J.-C.3
  • 7
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • Middelberg A. Preparative protein refolding. Trends Biotechnol. 20 (2002) 437-443
    • (2002) Trends Biotechnol. , vol.20 , pp. 437-443
    • Middelberg, A.1
  • 8
    • 0031471216 scopus 로고    scopus 로고
    • Overexpression of a Glutamate Receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen
    • Chen G., and Gouaux E. Overexpression of a Glutamate Receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen. Proc. Natl. Acad. Sci. USA 94 (1997) 13431-13436
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13431-13436
    • Chen, G.1    Gouaux, E.2
  • 9
    • 0032789940 scopus 로고    scopus 로고
    • A new protein folding screen: application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase
    • Armstrong N., De Lencastre A., and Gouaux E. A new protein folding screen: application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase. Protein Sci. 8 (1999) 1475-1483
    • (1999) Protein Sci. , vol.8 , pp. 1475-1483
    • Armstrong, N.1    De Lencastre, A.2    Gouaux, E.3
  • 11
    • 0034999062 scopus 로고    scopus 로고
    • Folding screening assayed by proteolysis: application to various cystine deletion mutants of vascular endothelial growth factor
    • Heiring C., and Muller Y.A. Folding screening assayed by proteolysis: application to various cystine deletion mutants of vascular endothelial growth factor. Protein Sci. 14 (2001) 183-188
    • (2001) Protein Sci. , vol.14 , pp. 183-188
    • Heiring, C.1    Muller, Y.A.2
  • 12
    • 1642493929 scopus 로고    scopus 로고
    • An automated in vitro protein folding screen applied to a human dynactin subunit
    • Scheich C., Niesen F.H., Seckler R., and Bussow K. An automated in vitro protein folding screen applied to a human dynactin subunit. Protein Sci. 13 (2004) 370-380
    • (2004) Protein Sci. , vol.13 , pp. 370-380
    • Scheich, C.1    Niesen, F.H.2    Seckler, R.3    Bussow, K.4
  • 14
    • 0035967912 scopus 로고    scopus 로고
    • Solution structure of interleukin-13 and insights into receptor engagement
    • Eisenmesser E.Z., Horita D.A., Altieri A.S., and Byrd R.A. Solution structure of interleukin-13 and insights into receptor engagement. J. Mol. Biol. 310 (2001) 231-241
    • (2001) J. Mol. Biol. , vol.310 , pp. 231-241
    • Eisenmesser, E.Z.1    Horita, D.A.2    Altieri, A.S.3    Byrd, R.A.4
  • 15
    • 0035967886 scopus 로고    scopus 로고
    • Solution structure of human IL-13 and implication for receptor binding
    • Moy F.J., Diblasio E., Wilhelm J., and Powers R. Solution structure of human IL-13 and implication for receptor binding. J. Mol. Biol. 310 (2001) 219-230
    • (2001) J. Mol. Biol. , vol.310 , pp. 219-230
    • Moy, F.J.1    Diblasio, E.2    Wilhelm, J.3    Powers, R.4
  • 16
    • 0031174862 scopus 로고    scopus 로고
    • Assignments, secondary structure and dynamics of the inhibitor-free catalytic fragment of human fibroblast collagenase
    • Moy F.J., Pisano M.R., Chanda P.K., Urbano C., Killar L.M., Sung M.L., and Powers R. Assignments, secondary structure and dynamics of the inhibitor-free catalytic fragment of human fibroblast collagenase. J. Biomol. NMR 10 (1997) 9-19
    • (1997) J. Biomol. NMR , vol.10 , pp. 9-19
    • Moy, F.J.1    Pisano, M.R.2    Chanda, P.K.3    Urbano, C.4    Killar, L.M.5    Sung, M.L.6    Powers, R.7
  • 21
    • 0142223221 scopus 로고    scopus 로고
    • The Three-dimensional structure of the liver X receptor {β} reveals a flexible ligand-binding pocket that can accommodate fundamentally different ligands
    • Farnegardh M., Bonn T., Sun S., Ljunggren J., Ahola H., Wilhelmsson A., Gustafsson J.-A., and Carlquist M. The Three-dimensional structure of the liver X receptor {β} reveals a flexible ligand-binding pocket that can accommodate fundamentally different ligands. J. Biol. Chem. 278 (2003) 38821-38828
    • (2003) J. Biol. Chem. , vol.278 , pp. 38821-38828
    • Farnegardh, M.1    Bonn, T.2    Sun, S.3    Ljunggren, J.4    Ahola, H.5    Wilhelmsson, A.6    Gustafsson, J.-A.7    Carlquist, M.8
  • 22
    • 0034703476 scopus 로고    scopus 로고
    • High-resolution solution structure of the catalytic fragment of human collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor
    • Moy F.J., Chanda P.K., Chen J.M., Cosmi S., Edris W., Levin J.I., and Powers R. High-resolution solution structure of the catalytic fragment of human collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor. J. Mol. Biol. 302 (2000) 671-689
    • (2000) J. Mol. Biol. , vol.302 , pp. 671-689
    • Moy, F.J.1    Chanda, P.K.2    Chen, J.M.3    Cosmi, S.4    Edris, W.5    Levin, J.I.6    Powers, R.7
  • 23
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of progesterone complexed with its receptor
    • Williams S.P., and Sigler P.B. Atomic structure of progesterone complexed with its receptor. Nature 393 (1998) 392-396
    • (1998) Nature , vol.393 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 25
    • 0002439879 scopus 로고
    • Circular dichroism of peptides
    • Neurath H. (Ed), Academic Press, New York
    • Woody R.W. Circular dichroism of peptides. In: Neurath H. (Ed). The peptides (1988), Academic Press, New York 15-114
    • (1988) The peptides , pp. 15-114
    • Woody, R.W.1
  • 26
    • 0018588511 scopus 로고
    • Stability of proteins: small globular proteins
    • Privalov P.L. Stability of proteins: small globular proteins. Adv. Protein Chem. 33 (1979) 167-241
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 27
    • 0000893108 scopus 로고
    • Studies on the reduction and re-formation of protein disulfide bonds
    • Anfinsen C.B., and Haber E. Studies on the reduction and re-formation of protein disulfide bonds. J. Biol. Chem. 236 (1961) 1361-1363
    • (1961) J. Biol. Chem. , vol.236 , pp. 1361-1363
    • Anfinsen, C.B.1    Haber, E.2
  • 28
    • 0015859467 scopus 로고
    • Principle that govern the folding of protein chains
    • Anfinsen C.B. Principle that govern the folding of protein chains. Science 181 (1973) 223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 30
    • 0034213831 scopus 로고    scopus 로고
    • Crystal structure of the human RXRa ligand-binding domain bound to its natural ligand: 9-cis retinoic acid
    • Egea P.F., Mitschler A., Rochel N., Ruff M., Chambon P., and Moras D. Crystal structure of the human RXRa ligand-binding domain bound to its natural ligand: 9-cis retinoic acid. EMBO J. 19 (2000) 2592-2601
    • (2000) EMBO J. , vol.19 , pp. 2592-2601
    • Egea, P.F.1    Mitschler, A.2    Rochel, N.3    Ruff, M.4    Chambon, P.5    Moras, D.6
  • 31
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    • Tanenbaum D.M., Wang Y., Williams S.P., and Sigler P.B. Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc. Natl. Acad. Sci. USA 95 (1998) 5998-6003
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5998-6003
    • Tanenbaum, D.M.1    Wang, Y.2    Williams, S.P.3    Sigler, P.B.4
  • 32
    • 0036076144 scopus 로고    scopus 로고
    • Folding and stability of the ligand-binding domain of the glucocorticoid receptor
    • McLaughlin S.H., and Jackson S.E. Folding and stability of the ligand-binding domain of the glucocorticoid receptor. Protein Sci. 11 (2002) 1926-1936
    • (2002) Protein Sci. , vol.11 , pp. 1926-1936
    • McLaughlin, S.H.1    Jackson, S.E.2
  • 33
    • 0034463399 scopus 로고    scopus 로고
    • Molecular chaperone interactions with steroid receptors: An update
    • Cheung J., and Smith D.F. Molecular chaperone interactions with steroid receptors: An update. Mol. Endocrinol. 14 (2000) 939-946
    • (2000) Mol. Endocrinol. , vol.14 , pp. 939-946
    • Cheung, J.1    Smith, D.F.2
  • 34
    • 0032731203 scopus 로고    scopus 로고
    • Refolding and recovery of recombinant human Matrix Metalloproteinase 7 (Matrilysin) from inclusion bodies Expressed by Escherichia coli
    • Oneda H., and Inouye K. Refolding and recovery of recombinant human Matrix Metalloproteinase 7 (Matrilysin) from inclusion bodies Expressed by Escherichia coli. J. Biochem. 126 (1999) 905-911
    • (1999) J. Biochem. , vol.126 , pp. 905-911
    • Oneda, H.1    Inouye, K.2
  • 36
    • 0024405681 scopus 로고
    • Structure and activity dependence of recombinant human insulin-like growth factor 2 on disulfide bond pairing
    • Smith M.C., Cook J.A., Furman T.C., and Occolowitz J.L. Structure and activity dependence of recombinant human insulin-like growth factor 2 on disulfide bond pairing. J. Biol. Chem. 264 (1989) 9314-9321
    • (1989) J. Biol. Chem. , vol.264 , pp. 9314-9321
    • Smith, M.C.1    Cook, J.A.2    Furman, T.C.3    Occolowitz, J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.