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Volumn 53, Issue 1, 2007, Pages 232-237

Overexpression and purification of single zinc finger peptides of human zinc finger protein ZNF191

Author keywords

Cyanogen bromide cleavage; Ketosteroid isomerase; Zinc finger protein

Indexed keywords

BUFFER; CYANOGEN BROMIDE; FORMIC ACID; FORMIC ACID DERIVATIVE; HISTIDINE; HYBRID PROTEIN; KRUPPEL LIKE FACTOR; PEPTIDE FRAGMENT; UNCLASSIFIED DRUG; ZINC; ZINC FINGER PROTEIN; ZNF24 PROTEIN, HUMAN;

EID: 33847156758     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.12.009     Document Type: Article
Times cited : (11)

References (21)
  • 1
    • 0033544943 scopus 로고    scopus 로고
    • Molecular cloning of six novel Krüppel-like zinc finger genes from hematopoietic cells and identification of a novel transregulatory domain KRNB
    • Han Z.G., Zhang Q.H., Ye M., Kan L.X., Gu B.W., He K.L., Shi S.L., Zhou J., Fu G., Mao M., Chen S.J., Yu L., and Chen Z. Molecular cloning of six novel Krüppel-like zinc finger genes from hematopoietic cells and identification of a novel transregulatory domain KRNB. J. Biol. Chem. 274 (1999) 35741-35748
    • (1999) J. Biol. Chem. , vol.274 , pp. 35741-35748
    • Han, Z.G.1    Zhang, Q.H.2    Ye, M.3    Kan, L.X.4    Gu, B.W.5    He, K.L.6    Shi, S.L.7    Zhou, J.8    Fu, G.9    Mao, M.10    Chen, S.J.11    Yu, L.12    Chen, Z.13
  • 2
    • 0035880416 scopus 로고    scopus 로고
    • Quantitative effects on gene silencing by allelic variation at a tetranucleotide microsatellite
    • Albanèse V., Biguet N.F., Kiefer H., Bayard E., Mallet J., and Meloni R. Quantitative effects on gene silencing by allelic variation at a tetranucleotide microsatellite. Human Mol. Genetics 10 (2001) 1785-1792
    • (2001) Human Mol. Genetics , vol.10 , pp. 1785-1792
    • Albanèse, V.1    Biguet, N.F.2    Kiefer, H.3    Bayard, E.4    Mallet, J.5    Meloni, R.6
  • 3
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Å
    • Pavletich N.P., and Pabo C.O. Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Å. Science 252 (1991) 809-817
    • (1991) Science , vol.252 , pp. 809-817
    • Pavletich, N.P.1    Pabo, C.O.2
  • 4
    • 13844297911 scopus 로고    scopus 로고
    • Zinc finger proteins: getting a grip on RNA
    • Brown R.S. Zinc finger proteins: getting a grip on RNA. Curr. Opin. Struct. Biol. 15 (2005) 94-98
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 94-98
    • Brown, R.S.1
  • 5
    • 0032560018 scopus 로고    scopus 로고
    • Helios, a novel dimerization partner of Ikaros expressed in the earliest hematopoietic progenitors
    • Kelley C.M., Ikeda T., Koipally J., Avitahl N., Wu L., Georgopoulos K., and Morgan B.A. Helios, a novel dimerization partner of Ikaros expressed in the earliest hematopoietic progenitors. Curr. Biol. 8 (1998) 508-515
    • (1998) Curr. Biol. , vol.8 , pp. 508-515
    • Kelley, C.M.1    Ikeda, T.2    Koipally, J.3    Avitahl, N.4    Wu, L.5    Georgopoulos, K.6    Morgan, B.A.7
  • 6
    • 0035960880 scopus 로고    scopus 로고
    • Structural analysis of regulatory protein domains using GST-fusion proteins
    • Zhan Y., Song X., and Zhou G.W. Structural analysis of regulatory protein domains using GST-fusion proteins. Gene 281 (2001) 1-9
    • (2001) Gene , vol.281 , pp. 1-9
    • Zhan, Y.1    Song, X.2    Zhou, G.W.3
  • 7
    • 33646596978 scopus 로고    scopus 로고
    • Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization
    • Bao W.J., Gao Y.G., Chang Y.G., Zhang T.Y., Lin X.J., Yan X.Z., and Hu H.Y. Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization. Protein Expres. Purif. 47 (2006) 599-606
    • (2006) Protein Expres. Purif. , vol.47 , pp. 599-606
    • Bao, W.J.1    Gao, Y.G.2    Chang, Y.G.3    Zhang, T.Y.4    Lin, X.J.5    Yan, X.Z.6    Hu, H.Y.7
  • 8
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion-body formation in the E. coli cytoplasm
    • LaVallie E.R., DiBlasio E.A., Kovacic S., Grant K.L., Schendel P.F., and McCoy J.M. A thioredoxin gene fusion expression system that circumvents inclusion-body formation in the E. coli cytoplasm. Biotecnology 11 (1993) 187-193
    • (1993) Biotecnology , vol.11 , pp. 187-193
    • LaVallie, E.R.1    DiBlasio, E.A.2    Kovacic, S.3    Grant, K.L.4    Schendel, P.F.5    McCoy, J.M.6
  • 10
    • 0141539503 scopus 로고    scopus 로고
    • Purification of recombinant plasminogen activator inhibitor-1 in the active conformation by refolding from inclusion bodies
    • Lee H.J., and Im H. Purification of recombinant plasminogen activator inhibitor-1 in the active conformation by refolding from inclusion bodies. Protein Expres. Purif. 31 (2003) 99-107
    • (2003) Protein Expres. Purif. , vol.31 , pp. 99-107
    • Lee, H.J.1    Im, H.2
  • 12
    • 20444372360 scopus 로고    scopus 로고
    • Expression and purification of a recombinant peptide from the Alzheimer's beta-amyloid protein for solid-state NMR
    • Sharpe S., Yau W.M., and Tycko R. Expression and purification of a recombinant peptide from the Alzheimer's beta-amyloid protein for solid-state NMR. Protein Expres. Purif. 42 (2005) 200-210
    • (2005) Protein Expres. Purif. , vol.42 , pp. 200-210
    • Sharpe, S.1    Yau, W.M.2    Tycko, R.3
  • 13
    • 0001067208 scopus 로고
    • Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromide
    • Gross E., and Witkop B. Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromide. J. Am. Chem. Soc. 83 (1961) 1510-1511
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 1510-1511
    • Gross, E.1    Witkop, B.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0034663605 scopus 로고    scopus 로고
    • Proteomics of Mycoplasma genitalium: identification and characterization of unannotated and atypical proteins in a small model genome
    • Balasubramanian S., Schneider T., Gerstein M., and Regan L. Proteomics of Mycoplasma genitalium: identification and characterization of unannotated and atypical proteins in a small model genome. Nucleic Acids Res. 28 (2000) 3075-3082
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3075-3082
    • Balasubramanian, S.1    Schneider, T.2    Gerstein, M.3    Regan, L.4
  • 16
    • 0034135428 scopus 로고    scopus 로고
    • Secretory production of human leptin in Escherichia coli
    • Jeong K.J., and Lee S.Y. Secretory production of human leptin in Escherichia coli. Biotechnol. Bioengin. 67 (2000) 398-407
    • (2000) Biotechnol. Bioengin. , vol.67 , pp. 398-407
    • Jeong, K.J.1    Lee, S.Y.2
  • 17
    • 0033010785 scopus 로고    scopus 로고
    • Lower molecular mass protein patterns in mycobacterial culture filtrates and purified protein derivatives
    • Rowland S.S., Ruckert J.L., and Cummings P.J. Lower molecular mass protein patterns in mycobacterial culture filtrates and purified protein derivatives. FEMS Immunol. Med. Microbiol. 23 (1999) 21-25
    • (1999) FEMS Immunol. Med. Microbiol. , vol.23 , pp. 21-25
    • Rowland, S.S.1    Ruckert, J.L.2    Cummings, P.J.3
  • 18
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
    • Zheng R.L., Jenkins T.M., and Craigie R. Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proc. Natl. Acad. Sci. USA 93 (1996) 13659-13664
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13659-13664
    • Zheng, R.L.1    Jenkins, T.M.2    Craigie, R.3
  • 19
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: fully automated sequence selection
    • Dahiyat B.I., and Mayo S.L. De novo protein design: fully automated sequence selection. Science 278 (1997) 82-87
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 20
    • 0037098864 scopus 로고    scopus 로고
    • Contribution of individual zinc ligands to metal binding and peptide folding of zinc finger peptides
    • Nomura A., and Sugiura Y. Contribution of individual zinc ligands to metal binding and peptide folding of zinc finger peptides. Inorg. Chem. 41 (2002) 3693-3698
    • (2002) Inorg. Chem. , vol.41 , pp. 3693-3698
    • Nomura, A.1    Sugiura, Y.2
  • 21
    • 33847171170 scopus 로고    scopus 로고
    • Construction and examination of the conformation of ZNF191 zinc-finger motifs using homology-based modeling
    • Bi A.D., Wang S.D., Wang X.K., Yu L., Shi S.L., Zhang Q., and Zhao S.Y. Construction and examination of the conformation of ZNF191 zinc-finger motifs using homology-based modeling. J. Fudan. Univ. 37 (1998) 123-128
    • (1998) J. Fudan. Univ. , vol.37 , pp. 123-128
    • Bi, A.D.1    Wang, S.D.2    Wang, X.K.3    Yu, L.4    Shi, S.L.5    Zhang, Q.6    Zhao, S.Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.