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Volumn 48, Issue 1, 2006, Pages 90-97

Cloning, high yield over-expression, purification, and characterization of CG18594, a new PEBP/RKIP family member from Drosophila melanogaster

Author keywords

CG10298; CG17917; CG17919; CG18594; CG6180; CG7054; Drosophila; Isotope labeling; NMR; Phosphatidylethanolamine binding protein; Purification; RKIP

Indexed keywords

CG18594 PROTEIN, DROSOPHILA; DROSOPHILA PROTEIN; PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN; RECOMBINANT PROTEIN;

EID: 33646885002     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.01.020     Document Type: Article
Times cited : (9)

References (33)
  • 1
    • 0026689451 scopus 로고
    • Main structural and functional features of the basic cytosolic bovine 21 kDa protein delineated through hydrophobic cluster analysis and molecular modelling
    • Schoentgen F., Seddiqi N., Bucquoy S., Jolles P., Lemesle-Varloot L., Provost K., and Mornon J.P. Main structural and functional features of the basic cytosolic bovine 21 kDa protein delineated through hydrophobic cluster analysis and molecular modelling. Protein Eng. 5 4 (1992) 295-303
    • (1992) Protein Eng. , vol.5 , Issue.4 , pp. 295-303
    • Schoentgen, F.1    Seddiqi, N.2    Bucquoy, S.3    Jolles, P.4    Lemesle-Varloot, L.5    Provost, K.6    Mornon, J.P.7
  • 2
    • 0028104165 scopus 로고
    • Relationships between molecular interactions (nucleotides, lipids and proteins) and structural features of the bovine brain 21-kDa protein
    • Bucquoy S., Jolles P., and Schoentgen F. Relationships between molecular interactions (nucleotides, lipids and proteins) and structural features of the bovine brain 21-kDa protein. Eur. J. Biochem. 225 3 (1994) 1203-1210
    • (1994) Eur. J. Biochem. , vol.225 , Issue.3 , pp. 1203-1210
    • Bucquoy, S.1    Jolles, P.2    Schoentgen, F.3
  • 5
    • 0035955736 scopus 로고    scopus 로고
    • Human phosphatidylethanolamine-binding protein facilitates heterotrimeric G protein-dependent signaling
    • Kroslak T., Koch T., Kahl E., and Hollt V. Human phosphatidylethanolamine-binding protein facilitates heterotrimeric G protein-dependent signaling. J. Biol. Chem. 276 43 (2001) 39772-39778
    • (2001) J. Biol. Chem. , vol.276 , Issue.43 , pp. 39772-39778
    • Kroslak, T.1    Koch, T.2    Kahl, E.3    Hollt, V.4
  • 6
    • 0035808362 scopus 로고    scopus 로고
    • The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors
    • Hengst U., Albrecht H., Hess D., and Monard D. The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors. J. Biol. Chem. 276 1 (2001) 535-540
    • (2001) J. Biol. Chem. , vol.276 , Issue.1 , pp. 535-540
    • Hengst, U.1    Albrecht, H.2    Hess, D.3    Monard, D.4
  • 7
    • 0038275924 scopus 로고    scopus 로고
    • Effects of raf kinase inhibitor protein expression on suppression of prostate cancer metastasis
    • Fu Z., Smith P.C., Zhang L., Rubin M.A., Dunn R.L., Yao Z., and Keller E.T. Effects of raf kinase inhibitor protein expression on suppression of prostate cancer metastasis. J. Natl. Cancer Inst. 95 12 (2003) 878-889
    • (2003) J. Natl. Cancer Inst. , vol.95 , Issue.12 , pp. 878-889
    • Fu, Z.1    Smith, P.C.2    Zhang, L.3    Rubin, M.A.4    Dunn, R.L.5    Yao, Z.6    Keller, E.T.7
  • 8
    • 4143151672 scopus 로고    scopus 로고
    • Metastasis suppressor genes: a role for raf kinase inhibitor protein (RKIP)
    • Keller E.T. Metastasis suppressor genes: a role for raf kinase inhibitor protein (RKIP). Anticancer Drugs 15 7 (2004) 663-669
    • (2004) Anticancer Drugs , vol.15 , Issue.7 , pp. 663-669
    • Keller, E.T.1
  • 9
    • 33646868702 scopus 로고    scopus 로고
    • A.J. George, R.M. Holsinger, C.A. McLean, S.S. Tan, H.S. Scott, T. Cardamone, R. Cappai, C.L. Masters, Q.X. Li, Decreased phosphatidylethanolamine binding protein expression correlates with Abeta accumulation in the Tg2576 mouse model of Alzheimer's disease, Neurobiol. Aging, 2005, in press.
  • 12
    • 4143071652 scopus 로고    scopus 로고
    • The role of Raf kinase inhibitor protein (RKIP) in health and disease
    • Keller E.T., Fu Z., and Brennan M. The role of Raf kinase inhibitor protein (RKIP) in health and disease. Biochem. Pharmacol. 68 6 (2004) 1049-1053
    • (2004) Biochem. Pharmacol. , vol.68 , Issue.6 , pp. 1049-1053
    • Keller, E.T.1    Fu, Z.2    Brennan, M.3
  • 13
    • 0032532458 scopus 로고    scopus 로고
    • Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction
    • Banfield M.J., Barker J.J., Perry A.C., and Brady R.L. Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure 6 10 (1998) 1245-1254
    • (1998) Structure , vol.6 , Issue.10 , pp. 1245-1254
    • Banfield, M.J.1    Barker, J.J.2    Perry, A.C.3    Brady, R.L.4
  • 14
    • 0032532743 scopus 로고    scopus 로고
    • Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: a novel structural class of phospholipid-binding proteins
    • Serre L., Vallee B., Bureaud N., Schoentgen F., and Zelwer C. Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: a novel structural class of phospholipid-binding proteins. Structure 6 10 (1998) 1255-1265
    • (1998) Structure , vol.6 , Issue.10 , pp. 1255-1265
    • Serre, L.1    Vallee, B.2    Bureaud, N.3    Schoentgen, F.4    Zelwer, C.5
  • 15
    • 0036077621 scopus 로고    scopus 로고
    • P.C. Simister, M.J. Banfield, R.L. Brady, The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family, Acta Crystallogr. D, Biol. Crystallogr. 58 (Pt 6 Pt 2) (2002) 1077-1080.
  • 16
    • 13844281614 scopus 로고    scopus 로고
    • Structure of the carboxypeptidase Y inhibitor IC in complex with the cognate proteinase reveals a novel mode of the proteinase-protein inhibitor interaction
    • Mima J., Hayashida M., Fujii T., Narita Y., Hayashi R., Ueda M., and Hata Y. Structure of the carboxypeptidase Y inhibitor IC in complex with the cognate proteinase reveals a novel mode of the proteinase-protein inhibitor interaction. J. Mol. Biol. 346 5 (2005) 1323-1334
    • (2005) J. Mol. Biol. , vol.346 , Issue.5 , pp. 1323-1334
    • Mima, J.1    Hayashida, M.2    Fujii, T.3    Narita, Y.4    Hayashi, R.5    Ueda, M.6    Hata, Y.7
  • 17
    • 0034646560 scopus 로고    scopus 로고
    • The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator
    • Banfield M.J., and Brady R.L. The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator. J. Mol. Biol. 297 5 (2000) 1159-1170
    • (2000) J. Mol. Biol. , vol.297 , Issue.5 , pp. 1159-1170
    • Banfield, M.J.1    Brady, R.L.2
  • 19
    • 0035854480 scopus 로고    scopus 로고
    • Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein
    • Serre L., Pereira de Jesus K., Zelwer C., Bureaud N., Schoentgen F., and Benedetti H. Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein. J. Mol. Biol. 310 3 (2001) 617-634
    • (2001) J. Mol. Biol. , vol.310 , Issue.3 , pp. 617-634
    • Serre, L.1    Pereira de Jesus, K.2    Zelwer, C.3    Bureaud, N.4    Schoentgen, F.5    Benedetti, H.6
  • 20
    • 0030034502 scopus 로고    scopus 로고
    • Distribution of hippocampal cholinergic neurostimulating peptide (HCNP) immunoreactivity in the central nervous system of the rat
    • Mitake S., Ojika K., Katada E., Otsuka Y., Matsukawa N., and Fujimori O. Distribution of hippocampal cholinergic neurostimulating peptide (HCNP) immunoreactivity in the central nervous system of the rat. Brain Res. 706 1 (1996) 57-70
    • (1996) Brain Res. , vol.706 , Issue.1 , pp. 57-70
    • Mitake, S.1    Ojika, K.2    Katada, E.3    Otsuka, Y.4    Matsukawa, N.5    Fujimori, O.6
  • 21
    • 0037311241 scopus 로고    scopus 로고
    • Peptides corresponding to the N- and C-terminal parts of PEBP are well-structured in solution: new insights into their possible interaction with partners in vivo
    • Vallee B.S., Coadou G., Labbe H., Sy D., Vovelle F., and Schoentgen F. Peptides corresponding to the N- and C-terminal parts of PEBP are well-structured in solution: new insights into their possible interaction with partners in vivo. J. Pept. Res. 61 2 (2003) 47-57
    • (2003) J. Pept. Res. , vol.61 , Issue.2 , pp. 47-57
    • Vallee, B.S.1    Coadou, G.2    Labbe, H.3    Sy, D.4    Vovelle, F.5    Schoentgen, F.6
  • 26
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley J., Lu M., and Bracken C. A method for efficient isotopic labeling of recombinant proteins. J. Biomol. NMR 20 1 (2001) 71-75
    • (2001) J. Biomol. NMR , vol.20 , Issue.1 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 27
    • 0029181728 scopus 로고
    • 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • Wishart D.S., Bigam C.G., Holm A., Hodges R.S., and Sykes B.D. 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5 1 (1995) 67-81
    • (1995) J. Biomol. NMR , vol.5 , Issue.1 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 28
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., and Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 3 (1995) 277-293
    • (1995) J. Biomol. NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 29
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson B.A. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278 (2004) 313-352
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 30
    • 0023655581 scopus 로고
    • Complete amino acid sequence of a basic 21-kDa protein from bovine brain cytosol
    • Schoentgen F., Saccoccio F., Jolles J., Bernier I., and Jolles P. Complete amino acid sequence of a basic 21-kDa protein from bovine brain cytosol. Eur. J. Biochem. 166 2 (1987) 333-338
    • (1987) Eur. J. Biochem. , vol.166 , Issue.2 , pp. 333-338
    • Schoentgen, F.1    Saccoccio, F.2    Jolles, J.3    Bernier, I.4    Jolles, P.5
  • 31
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis
    • Sreerama N., Venyaminov S.Y., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 287 2 (2000) 243-251
    • (2000) Anal. Biochem. , vol.287 , Issue.2 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 32
    • 0033571741 scopus 로고    scopus 로고
    • Stability and physicochemical properties of the bovine brain phosphatidylethanolamine-binding protein
    • Vallee B., Teyssier C., Maget-Dana R., Ramstein J., Bureaud N., and Schoentgen F. Stability and physicochemical properties of the bovine brain phosphatidylethanolamine-binding protein. Eur. J. Biochem. 266 1 (1999) 40-52
    • (1999) Eur. J. Biochem. , vol.266 , Issue.1 , pp. 40-52
    • Vallee, B.1    Teyssier, C.2    Maget-Dana, R.3    Ramstein, J.4    Bureaud, N.5    Schoentgen, F.6
  • 33
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 4 (2000) 404-405
    • (2000) Bioinformatics , vol.16 , Issue.4 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.