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Volumn 12, Issue 8, 2003, Pages 1675-1685

Amyloid-forming peptides selected proteolytically from phage display library

Author keywords

Amyloid; FSD 1; Phage display; Proteolytic selection; Zif268; Zinc finger

Indexed keywords

AMYLOID; CHYMOTRYPSIN INHIBITOR; COAT PROTEIN; CONGO RED; DNA BINDING PROTEIN; M PROTEIN; METAL ION; PEPTIDE; PEPTIDE LIBRARY; PROTEIN FSD1; PROTEINASE; PROTEINASE K; THIOFLAVINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ZIF268; TRYPSIN; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN;

EID: 0041341887     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0236103     Document Type: Article
Times cited : (13)

References (33)
  • 1
    • 0028823758 scopus 로고
    • Synthetic human antibodies: Selecting and evolving functional proteins
    • Barbas III, C.F. and Wagner, J. 1995. Synthetic human antibodies: Selecting and evolving functional proteins. Methods Enzymol. 8: 94-103.
    • (1995) Methods Enzymol. , vol.8 , pp. 94-103
    • Barbas C.F. III1    Wagner, J.2
  • 2
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease: Analysis of circular dichroism spectra
    • Barrow, C.J., Yasuda, A., Kenny, P.T., and Zagorski, M.G. 1992. Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease: Analysis of circular dichroism spectra. J. Mol. Biol. 225: 1075-1093.
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.3    Zagorski, M.G.4
  • 3
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • Blake, C. and Serpell, L. 1996. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure 4: 989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 4
    • 0036130801 scopus 로고    scopus 로고
    • Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI)
    • Buczek, O., Krowarsch, D., and Otlewski, J. 2002. Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI). Protein Sci. 806: 924-932.
    • (2002) Protein Sci. , vol.806 , pp. 924-932
    • Buczek, O.1    Krowarsch, D.2    Otlewski, J.3
  • 5
    • 0034599720 scopus 로고    scopus 로고
    • Mutational analysis of the propensity for amyloid formation by a globular protein
    • Chiti, F., Taddei, N., Bucciantini, M., White, P., Ramponi, G., and Dobson, C.M. 2000. Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 19: 1441-1449.
    • (2000) EMBO J. , vol.19 , pp. 1441-1449
    • Chiti, F.1    Taddei, N.2    Bucciantini, M.3    White, P.4    Ramponi, G.5    Dobson, C.M.6
  • 6
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P.Y. and Fasman, G.D. 1978. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol. 47: 45-148.
    • (1978) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 7
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat, B.I. and Mayo, S.L. 1997. De novo protein design: Fully automated sequence selection. Science 278: 82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 8
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding: Evolution and disease
    • Dobson, C.M. 1999. Protein misfolding: Evolution and disease. Trends Biochem. Sci. 24: 329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 9
    • 0030587774 scopus 로고    scopus 로고
    • Zif268 protein-DNA complex refined at 1.6 Å: A model system for understanding zinc finger-DNA interactions
    • Elrod-Erickson, M., Rould, M.A., Nekludova, L., and Pabo, C.O. 1996. Zif268 protein-DNA complex refined at 1.6 A: A model system for understanding zinc finger-DNA interactions. Structure 4: 1171-1180.
    • (1996) Structure , vol.4 , pp. 1171-1180
    • Elrod-Erickson, M.1    Rould, M.A.2    Nekludova, L.3    Pabo, C.O.4
  • 11
    • 0033533387 scopus 로고    scopus 로고
    • Core-directed protein design, II: Rescue of a multiply mutated and destabilized variant of ubiquitin
    • Finucane, M.D. and Woolfson, D.N. 1999. Core-directed protein design, II: Rescue of a multiply mutated and destabilized variant of ubiquitin. Biochemistry 38: 11613-11623.
    • (1999) Biochemistry , vol.38 , pp. 11613-11623
    • Finucane, M.D.1    Woolfson, D.N.2
  • 12
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana, A., Fassina, G., Vita, C., Dalzoppo, D., Zamai, M., and Zambonin, M. 1986. Correlation between sites of limited proteolysis and segmental mobility in thermolysin. Biochemistry 25: 1847-1851.
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 14
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light-chain amyloidosis
    • Hurle, M.R., Helms, L.R., Li, L., Chan, W., and Wetzel, R. 1994. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc. Natl. Acad. Sci. 91: 5446-5450.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Chan, W.4    Wetzel, R.5
  • 15
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • Kelly, J.W. 1996. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6: 11-17.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 16
    • 0035905430 scopus 로고    scopus 로고
    • Selection of potent chymotrypsin and elastase inhibitors from M13 phage library of basic pancreatic trypsin inhibitor (BPTI)
    • Kiczak, L., Kasztura, M., Koscielska-Kasprzak, K., Dadlez, M., and Otlewski, J. 2001. Selection of potent chymotrypsin and elastase inhibitors from M13 phage library of basic pancreatic trypsin inhibitor (BPTI). Biochim. Biophys. Acta 1550: 153-163.
    • (2001) Biochim. Biophys. Acta , vol.1550 , pp. 153-163
    • Kiczak, L.1    Kasztura, M.2    Koscielska-Kasprzak, K.3    Dadlez, M.4    Otlewski, J.5
  • 17
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by congo red spectral shift assay
    • Klunk, W.E., Jacob, R.F., and Mason, R.P. 1999. Quantifying amyloid by congo red spectral shift assay. Methods Enzymol. 309: 285-305.
    • (1999) Methods Enzymol. , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 18
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics 14: 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 19
    • 0031759422 scopus 로고    scopus 로고
    • Proteolytic selection for protein folding using filamentous bacteriophages
    • Kristensen, P. and Winter, G. 1998. Proteolytic selection for protein folding using filamentous bacteriophages. Fold. Des. 3: 321-328.
    • (1998) Fold. Des. , vol.3 , pp. 321-328
    • Kristensen, P.1    Winter, G.2
  • 20
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R.F. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157: 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 21
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin T
    • LeVine III, H. 1999. Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309: 274-284.
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • LeVine H. III1
  • 22
    • 0031911439 scopus 로고    scopus 로고
    • The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p
    • Lubkowski, J., Hennecke, F., Pluckthun, A., and Wlodawer, A. 1998. The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p. Nat. Struct. Biol. 5: 140-147.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 140-147
    • Lubkowski, J.1    Hennecke, F.2    Pluckthun, A.3    Wlodawer, A.4
  • 23
    • 0035827175 scopus 로고    scopus 로고
    • In-vitro selection of highly stabilized protein variants with optimized surface
    • Martin, A., Sieber, V., and Schmid, F.X. 2001. In-vitro selection of highly stabilized protein variants with optimized surface. J. Mol. Biol. 309: 717-726.
    • (2001) J. Mol. Biol. , vol.309 , pp. 717-726
    • Martin, A.1    Sieber, V.2    Schmid, F.X.3
  • 24
    • 0027363264 scopus 로고
    • Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity
    • McCutchen, S.L., Colon, W., and Kelly, J.W. 1993. Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry 32: 12119-12127.
    • (1993) Biochemistry , vol.32 , pp. 12119-12127
    • McCutchen, S.L.1    Colon, W.2    Kelly, J.W.3
  • 25
    • 0034255027 scopus 로고    scopus 로고
    • A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
    • Ramirez-Alvarado, M., Merkel, J.S., and Regan, L. 2000. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. 97: 8979-8984.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 26
    • 0034730144 scopus 로고    scopus 로고
    • Novel folded protein domains generated by combinatorial shuffling of polypeptide segments
    • Riechmann, L. and Winter, G. 2000. Novel folded protein domains generated by combinatorial shuffling of polypeptide segments. Proc. Natl. Acad. Sci. 97: 10068-10073.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 10068-10073
    • Riechmann, L.1    Winter, G.2
  • 27
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. and von Jagow, G. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 39: 368-379.
    • (1987) Anal. Biochem. , vol.39 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 28
    • 0031729179 scopus 로고    scopus 로고
    • Selecting proteins with improved stability by a phage-based method
    • Sieber, V., Pluckthun, A., and Schmid, F.X. 1998. Selecting proteins with improved stability by a phage-based method. Nat. Biotechnol. 16: 955-960.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 955-960
    • Sieber, V.1    Pluckthun, A.2    Schmid, F.X.3
  • 32
    • 0034112069 scopus 로고    scopus 로고
    • Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B
    • Wilkins, D.K., Dobson, C.M., and Groß, M. 2000. Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B. Eur. J. Biochem. 267: 2609-2616.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2609-2616
    • Wilkins, D.K.1    Dobson, C.M.2    Groß, M.3
  • 33
    • 0030864811 scopus 로고    scopus 로고
    • Combinatorial protein design: Strategies for screening protein libraries
    • Zhao, H. and Arnold, F.H. 1997. Combinatorial protein design: Strategies for screening protein libraries. Curr. Opin. Struct. Biol. 7: 480-485.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 480-485
    • Zhao, H.1    Arnold, F.H.2


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