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Volumn 66, Issue 1, 2009, Pages 107-112

Expression and purification of amyloid-β peptides from Escherichia coli

Author keywords

Amyloid ; Expression; Fatty acid binding protein; Fusion protein

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA-PROTEIN (1-42); FATTY ACID BINDING PROTEIN; HYBRID PROTEIN; PEPTIDE FRAGMENT;

EID: 63649096009     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.02.009     Document Type: Article
Times cited : (32)

References (27)
  • 1
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D.J. The molecular pathology of Alzheimer's disease. Neuron 6 (1991) 487-498
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 2
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81 (2001) 741-766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 3
    • 0032084472 scopus 로고    scopus 로고
    • Structural and kinetic features of amyloid beta-protein fibrillogenesis
    • Teplow D.B. Structural and kinetic features of amyloid beta-protein fibrillogenesis. Amyloid 5 (1998) 121-142
    • (1998) Amyloid , vol.5 , pp. 121-142
    • Teplow, D.B.1
  • 4
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo Red
    • Lorenzo A., and Yankner B.A. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo Red. Proc. Natl. Acad. Sci. USA 91 (1994) 12243-12247
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 6
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum
    • Klein W.L., Krafft G.A., and Finch C.E. Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum. Trends Neurosci. 24 (2001) 219-224
    • (2001) Trends Neurosci. , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 7
  • 8
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3beta
    • Hoshi M., Sato M., Matsumoto S., Noguchi A., Yasutake K., Yoshida N., and Sato K. Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3beta. Proc. Natl. Acad. Sci. USA 100 (2003) 6370-6375
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6370-6375
    • Hoshi, M.1    Sato, M.2    Matsumoto, S.3    Noguchi, A.4    Yasutake, K.5    Yoshida, N.6    Sato, K.7
  • 9
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley D.M., Walsh D.M., Ye C.P., Diehl T., Vasquez S., Vassilev P.M., Teplow D.B., and Selkoe D.J. Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19 (1999) 8876-8884
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 11
    • 4143138471 scopus 로고    scopus 로고
    • In vivo effects of ApoE and clusterin on amyloid-beta metabolism and neuropathology
    • Holtzman D.M. In vivo effects of ApoE and clusterin on amyloid-beta metabolism and neuropathology. J. Mol. Neurosci. 23 (2004) 247-254
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 247-254
    • Holtzman, D.M.1
  • 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 Expr. Purif. 42 (2005) 200-210
    • (2005) Protein Expr. Purif. , vol.42 , pp. 200-210
    • Sharpe, S.1    Yau, W.M.2    Tycko, R.3
  • 13
    • 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. Biotechnology (N.Y.) 11 (1993) 187-193
    • (1993) Biotechnology (N.Y.) , 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
  • 14
    • 0033166082 scopus 로고    scopus 로고
    • Functional characterization of apolipoprotein E isoforms overexpressed in Escherichia coli
    • Morrow J.A., Arnold K.S., and Weisgraber K.H. Functional characterization of apolipoprotein E isoforms overexpressed in Escherichia coli. Protein Expr. Purif. 16 (1999) 224-230
    • (1999) Protein Expr. Purif. , vol.16 , pp. 224-230
    • Morrow, J.A.1    Arnold, K.S.2    Weisgraber, K.H.3
  • 15
    • 84934437421 scopus 로고    scopus 로고
    • Hexahistidine-tagged maltose-binding protein as a fusion partner for the production of soluble recombinant proteins in Escherichia coli
    • Austin B.P., Nallamsetty S., and Waugh D.S. Hexahistidine-tagged maltose-binding protein as a fusion partner for the production of soluble recombinant proteins in Escherichia coli. Methods Mol. Biol. 498 (2009) 157-172
    • (2009) Methods Mol. Biol. , vol.498 , pp. 157-172
    • Austin, B.P.1    Nallamsetty, S.2    Waugh, D.S.3
  • 17
    • 22244439242 scopus 로고    scopus 로고
    • The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation
    • Hortschansky P., Schroeckh V., Christopeit T., Zandomeneghi G., and Fandrich M. The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation. Prot. Sci. 14 (2005) 1753-1759
    • (2005) Prot. Sci. , vol.14 , pp. 1753-1759
    • Hortschansky, P.1    Schroeckh, V.2    Christopeit, T.3    Zandomeneghi, G.4    Fandrich, M.5
  • 18
    • 13844256497 scopus 로고    scopus 로고
    • Production of recombinant amyloid-beta peptide 42 as an ubiquitin extension
    • Lee E.K., Hwang J.H., Shin D.Y., Kim D.I., and Yoo Y.J. Production of recombinant amyloid-beta peptide 42 as an ubiquitin extension. Protein Expr. Purif. 40 (2005) 183-189
    • (2005) Protein Expr. Purif. , vol.40 , pp. 183-189
    • Lee, E.K.1    Hwang, J.H.2    Shin, D.Y.3    Kim, D.I.4    Yoo, Y.J.5
  • 19
    • 34548686320 scopus 로고    scopus 로고
    • Expression and purification of uniformly (15)N-labeled amyloid beta peptide 1-40 in Escherichia coli
    • Nagata-Uchiyama M., Yaguchi M., Hirano Y., and Ueda T. Expression and purification of uniformly (15)N-labeled amyloid beta peptide 1-40 in Escherichia coli. Protein Pept. Lett. 14 (2007) 788-792
    • (2007) Protein Pept. Lett. , vol.14 , pp. 788-792
    • Nagata-Uchiyama, M.1    Yaguchi, M.2    Hirano, Y.3    Ueda, T.4
  • 20
    • 57649105330 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant human beta-amyloid42 peptide in Escherichia coli
    • Zhang L., Yu H., Song C., Lin X., Chen B., Tan C., Cao G., and Wang Z. Expression, purification, and characterization of recombinant human beta-amyloid42 peptide in Escherichia coli. Protein Expr. Purif. 64 (2009) 55-62
    • (2009) Protein Expr. Purif. , vol.64 , pp. 55-62
    • Zhang, L.1    Yu, H.2    Song, C.3    Lin, X.4    Chen, B.5    Tan, C.6    Cao, G.7    Wang, Z.8
  • 21
    • 0025150465 scopus 로고
    • Expression of rat intestinal fatty acid binding protein in E. coli and its subsequent structural analysis: a model system for studying the molecular details of fatty acid-protein interaction
    • Sacchettini J.C., Banaszak L.J., and Gordon J.I. Expression of rat intestinal fatty acid binding protein in E. coli and its subsequent structural analysis: a model system for studying the molecular details of fatty acid-protein interaction. Mol. Cell. Biochem. 98 (1990) 81-93
    • (1990) Mol. Cell. Biochem. , vol.98 , pp. 81-93
    • Sacchettini, J.C.1    Banaszak, L.J.2    Gordon, J.I.3
  • 22
    • 0029367113 scopus 로고
    • 15N assignments and chemical shift-derived secondary structure of intestinal fatty acid-binding protein
    • 15N assignments and chemical shift-derived secondary structure of intestinal fatty acid-binding protein. J. Biomol. NMR 6 (1995) 198-210
    • (1995) J. Biomol. NMR , vol.6 , pp. 198-210
    • Hodsdon, M.E.1    Toner, J.J.2    Cistola, D.P.3
  • 23
    • 0027371147 scopus 로고
    • Intestinal fatty acid binding protein: characterization of mutant proteins containing inserted cysteine residues
    • Jiang N., and Frieden C. Intestinal fatty acid binding protein: characterization of mutant proteins containing inserted cysteine residues. Biochemistry 32 (1993) 11015-11021
    • (1993) Biochemistry , vol.32 , pp. 11015-11021
    • Jiang, N.1    Frieden, C.2
  • 24
    • 0032469297 scopus 로고    scopus 로고
    • Turn scanning by site-directed mutagenesis: application to the protein folding problem using the intestinal fatty acid binding protein
    • Kim K., and Frieden C. Turn scanning by site-directed mutagenesis: application to the protein folding problem using the intestinal fatty acid binding protein. Prot. Sci. 7 (1998) 1821-1828
    • (1998) Prot. Sci. , vol.7 , pp. 1821-1828
    • Kim, K.1    Frieden, C.2
  • 25
    • 0037177227 scopus 로고    scopus 로고
    • The intestinal fatty acid binding protein: the role of turns in fast and slow folding processes
    • Chattopadhyay K., Zhong S., Yeh S.R., Rousseau D.L., and Frieden C. The intestinal fatty acid binding protein: the role of turns in fast and slow folding processes. Biochemistry 41 (2002) 4040-4047
    • (2002) Biochemistry , vol.41 , pp. 4040-4047
    • Chattopadhyay, K.1    Zhong, S.2    Yeh, S.R.3    Rousseau, D.L.4    Frieden, C.5
  • 27
    • 58049164489 scopus 로고    scopus 로고
    • Recombinant amyloid beta-peptide production by coexpression with an antibody ligand BMC
    • Macao B., Hoyer W., Sandberg A., Brorsson A.C., Dobson C.M., and Hard T. Recombinant amyloid beta-peptide production by coexpression with an antibody ligand BMC. Biotechnology 8 (2008) 82
    • (2008) Biotechnology , vol.8 , pp. 82
    • Macao, B.1    Hoyer, W.2    Sandberg, A.3    Brorsson, A.C.4    Dobson, C.M.5    Hard, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.