메뉴 건너뛰기




Volumn 379, Issue 11, 1998, Pages 1307-1317

Rapid acquisition of β-sheet structure in the prion protein prior to multimer formation

Author keywords

Fluorescence correlation spectroscopy; Kinetics; Multimerization; Prion protein

Indexed keywords

DODECYL SULFATE SODIUM; POLYMER; PRION PROTEIN; RECOMBINANT PROTEIN;

EID: 0031789527     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1998.379.11.1307     Document Type: Article
Times cited : (88)

References (50)
  • 1
    • 0027480757 scopus 로고
    • The structure and mechanism of formation human calcitonin fibrils
    • Arvinte, T., Cudd, A., and Drake, A.F. (1993). The structure and mechanism of formation human calcitonin fibrils. J. Biol. Chem. 268, 6415-6422.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6415-6422
    • Arvinte, T.1    Cudd, A.2    Drake, A.F.3
  • 3
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases: Importance of seeding
    • Come, J.H., Fraser, P.E., and Lansbury, P.T. (1993). A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc. Natl. Acad. Sci. USA 90, 5959-5963.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury, P.T.3
  • 5
    • 0030579560 scopus 로고    scopus 로고
    • Prionics or the kinetic basis of prion diseases
    • Eigen, M. (1996). Prionics or the kinetic basis of prion diseases. Biophysical Chemistry 63, A1-A18.
    • (1996) Biophysical Chemistry , vol.63
    • Eigen, M.1
  • 6
    • 0028229903 scopus 로고
    • Sorting molecules: Application to diagnostics and evolutionary biotechnology
    • Eigen, M., and Rigler, R. (1994). Sorting molecules: application to diagnostics and evolutionary biotechnology. Proc. Natl. Acad. Sci. USA 91, 5740-5747.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5740-5747
    • Eigen, M.1    Rigler, R.2
  • 7
    • 0017643758 scopus 로고
    • Unconventional viruses and the origin and disappearance of kuru
    • Gajdusek, D.C. (1977). Unconventional viruses and the origin and disappearance of kuru. Science 197, 943-960.
    • (1977) Science , vol.197 , pp. 943-960
    • Gajdusek, D.C.1
  • 8
    • 0027388993 scopus 로고
    • Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity
    • Gasset, M., Baldwin, M.A., Fletterick, R.J., and Prusiner, S.B. (1993). Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc. Natl. Acad. Sci. USA 90, 1-5.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1-5
    • Gasset, M.1    Baldwin, M.A.2    Fletterick, R.J.3    Prusiner, S.B.4
  • 9
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • Hennessey, J.P. Jr., and Johnson, W.C. Jr. (1981). Information content in the circular dichroism of proteins. Biochemistry 20, 1085-1094.
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey Jr., J.P.1    Johnson Jr., W.C.2
  • 10
    • 0030572627 scopus 로고    scopus 로고
    • Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein
    • Hornemann, S., and Glockshuber, R. (1996). Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein. J. Mol. Blol. 262, 614-619.
    • (1996) J. Mol. Blol. , vol.262 , pp. 614-619
    • Hornemann, S.1    Glockshuber, R.2
  • 11
    • 0030878056 scopus 로고    scopus 로고
    • Recombinant full-length murine prion protein, mPrP(23-231): Purification and spectroscopic characterization
    • Hornemann, S., Korth, C., Oesch, B., Riek, R., Wider, G., Wüthrich, K., and Glockshuber, R. (1997). Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization. FEBS-Letters 413, 227-281.
    • (1997) FEBS-Letters , vol.413 , pp. 227-281
    • Hornemann, S.1    Korth, C.2    Oesch, B.3    Riek, R.4    Wider, G.5    Wüthrich, K.6    Glockshuber, R.7
  • 13
    • 0025876740 scopus 로고
    • Protein folding: Local structures, domains, subunits, and assemblies
    • Jaenicke, R. (1991). Protein folding: Local structures, domains, subunits, and assemblies. Biochemistry 30, 3147-3161.
    • (1991) Biochemistry , vol.30 , pp. 3147-3161
    • Jaenicke, R.1
  • 15
    • 0002393234 scopus 로고
    • Amino acid analysis by o-Phthaldialdehyde precolumn derivatization and reverse phase HPLC
    • Jones, B.N. (1986). Amino acid analysis by o-Phthaldialdehyde precolumn derivatization and reverse phase HPLC. Methods in Protein Microcharacterisation, 121-151.
    • (1986) Methods in Protein Microcharacterisation , pp. 121-151
    • Jones, B.N.1
  • 16
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 18
    • 0030964917 scopus 로고    scopus 로고
    • COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform
    • Kaneko, K., Vey, M., Scott, M., Pilkuhn, S., Cohen, F.E., and Prusiner, S.B. (1997a).COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc. Natl. Acad. Sci. USA 94, 2333-2338.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2333-2338
    • Kaneko, K.1    Vey, M.2    Scott, M.3    Pilkuhn, S.4    Cohen, F.E.5    Prusiner, S.B.6
  • 21
    • 0026604959 scopus 로고
    • Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel elec- Trophoresis (RRGE)
    • Kellings, K., Meyer, N., Mirenda, C., Prusiner, S.B., and Riesner, D. (1992). Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel elec- trophoresis (RRGE). J. Gen. Virol. 73, 1025-1029.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1025-1029
    • Kellings, K.1    Meyer, N.2    Mirenda, C.3    Prusiner, S.B.4    Riesner, D.5
  • 22
    • 0031843985 scopus 로고    scopus 로고
    • Prion rods contain small amounts of the two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry
    • Klein, T.R., Kirsch, D., Kaufmann, R., and Riesner, D. (1998). Prion rods contain small amounts of the two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry. Biol. Chem. 379, 655-666.
    • (1998) Biol. Chem. , vol.379 , pp. 655-666
    • Klein, T.R.1    Kirsch, D.2    Kaufmann, R.3    Riesner, D.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriaphage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriaphage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0017701604 scopus 로고
    • Automatic Identification of Secondary Structure in Globular Proteins
    • Levitt, M., and Greer, J. (1977). Automatic Identification of Secondary Structure in Globular Proteins. J. Mol. Biol. 114, 181-293.
    • (1977) J. Mol. Biol. , vol.114 , pp. 181-293
    • Levitt, M.1    Greer, J.2
  • 27
    • 0030796231 scopus 로고    scopus 로고
    • The complete mature bovine prion protein highly expressed in Escherichla coli: Biochemical and structural studies
    • Negro, A., De Filippis, V., Skaper, S.D., James, P., and Sorgato, M.C. (1997). The complete mature bovine prion protein highly expressed in Escherichla coli: biochemical and structural studies. FEBS 412, 359-364.
    • (1997) FEBS , vol.412 , pp. 359-364
    • Negro, A.1    De Filippis, V.2    Skaper, S.D.3    James, P.4    Sorgato, M.C.5
  • 29
    • 0011089246 scopus 로고    scopus 로고
    • Analytical ultracentrifugation with fluorescence detection and biosafety containment and its application to the prion protein
    • Pitschke, M., Post, K., and Riesner, D. (1997). Analytical ultracentrifugation with fluorescence detection and biosafety containment and its application to the prion protein. Colloid Polym. Sci. 107, 72-76.
    • (1997) Colloid Polym. Sci. , vol.107 , pp. 72-76
    • Pitschke, M.1    Post, K.2    Riesner, D.3
  • 30
    • 0031871740 scopus 로고    scopus 로고
    • Detection of single amyloid β-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy
    • Pitschke, M., Prior, R., Haupt, M., and Riesner, D. (1998). Detection of single amyloid β-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy. Nat. Med. 4, 832-834.
    • (1998) Nat. Med. , vol.4 , pp. 832-834
    • Pitschke, M.1    Prior, R.2    Haupt, M.3    Riesner, D.4
  • 34
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S.B. (1991). Molecular biology of prion diseases. Science 252, 1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 35
    • 0025911762 scopus 로고
    • How does protein synthesis give rise to the 3D-structure?
    • Ptitsyn, O.B. (1991). How does protein synthesis give rise to the 3D-structure? FEBS Letters 285, 176-181.
    • (1991) FEBS Letters , vol.285 , pp. 176-181
    • Ptitsyn, O.B.1
  • 36
    • 0026702071 scopus 로고
    • Attempts to convert the cellular prion protein into the scrapie isoform in cell-free systems
    • Raeber, A.J., Borchelt, D.R., Scott, M., and Prusiner, S.B. (1992). Attempts to convert the cellular prion protein into the scrapie isoform in cell-free systems. J. Virol. 66, 6155-6163.
    • (1992) J. Virol. , vol.66 , pp. 6155-6163
    • Raeber, A.J.1    Borchelt, D.R.2    Scott, M.3    Prusiner, S.B.4
  • 38
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • Riek, R., Hornemann, S., Wider, G., Glockshuber, R., and, Wüth-rich, K. (1997). NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS-Lett. 413, 282-288.
    • (1997) FEBS-Lett. , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wüth-rich, K.5
  • 39
    • 0030026759 scopus 로고    scopus 로고
    • Disruption of prion rods genrates 10-nm spherical particles having high α-heli;cal content and lacking scrapie infectivity
    • Riesner, D., Kellings, K., Post, K., Wille, H., Serban, H. Groth, D., Baldwin, M.B., and Prusiner, S.B. (1996). Disruption of prion rods genrates 10-nm spherical particles having high α-heli;cal content and lacking scrapie infectivity. J. Virol. 70, 1714-1722.
    • (1996) J. Virol. , vol.70 , pp. 1714-1722
    • Riesner, D.1    Kellings, K.2    Post, K.3    Wille, H.4    Serban, H.5    Groth, D.6    Baldwin, M.B.7    Prusiner, S.B.8
  • 40
    • 0027182522 scopus 로고
    • Conformatlonal transitions, dissosiation and unfolding of scrapie amyloid (prion) protein
    • Safar, J., Roller, P.P., Gaydusek, D.C., and Gibbs, C.J. Jr. (1993a). Conformatlonal transitions, dissosiation and unfolding of scrapie amyloid (prion) protein. J. Blol. Chem. 268, 20276-20284.
    • (1993) J. Blol. Chem. , vol.268 , pp. 20276-20284
    • Safar, J.1    Roller, P.P.2    Gaydusek, D.C.3    Gibbs Jr., C.J.4
  • 41
    • 0027363495 scopus 로고
    • Thermal-stability and conformational transition of scrapie amyloid (prion) protein correlate with infectivity
    • Safar, J., Roller, P.P., Gaydusek, D.C., and Gibbs, C.J.Jr. (1993) Thermal-stability and conformational transition of scrapie amyloid (prion) protein correlate with infectivity. Protein Sci. 2, 2206-2216.
    • (1993) Protein Sci. , vol.2 , pp. 2206-2216
    • Safar, J.1    Roller, P.P.2    Gaydusek, D.C.3    Gibbs, C.J.J.4
  • 42
    • 0025245195 scopus 로고
    • A fluorescence detection system for the analytical ultracentrifuge and its application to proteins, nucleic acids and viruses
    • Schmidt B., Rappold, W., Rosenbaum, V., Fischer, R., and Riesner, D. (1990). A fluorescence detection system for the analytical ultracentrifuge and its application to proteins, nucleic acids and viruses. Colloid Polym. Sci. 268, 45-54.
    • (1990) Colloid Polym. Sci. , vol.268 , pp. 45-54
    • Schmidt, B.1    Rappold, W.2    Rosenbaum, V.3    Fischer, R.4    Riesner, D.5
  • 44
    • 0026811273 scopus 로고
    • Peptide sequencing by matrix-assisted laser-desorption mass spectrometry
    • Spengler, B., Kirsch, D., Kaufmann, R., and Jaeger, S. (1992). peptide sequencing by matrix-assisted laser-desorption mass spectrometry. Rapid Commun. Mass Spectrom. 6, 105-108.
    • (1992) Rapid Commun. Mass Spectrom. , vol.6 , pp. 105-108
    • Spengler, B.1    Kirsch, D.2    Kaufmann, R.3    Jaeger, S.4
  • 45
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama, N., and Woody, R.W. (1993). A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209, 32-44.
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 46
    • 0027534612 scopus 로고
    • Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl, N., Baldwin, M.A., Teplow, D.B., Hood, L., Gibson, B.W., Burlingame, A.L., and Prusiner, S.B. (1993). Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32, 1991-2002.
    • (1993) Biochemistry , vol.32 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.A.2    Teplow, D.B.3    Hood, L.4    Gibson, B.W.5    Burlingame, A.L.6    Prusiner, S.B.7
  • 47
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling, G.C., Gott, M., Mastrianni, J., Gabizon, R., Torchia, M., Cohen, F.E., DeArmond, S.J., and Prusiner, S.B. (1995). Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83, 79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Gott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    DeArmond, S.J.7    Prusiner, S.B.8
  • 48
    • 0028982292 scopus 로고
    • Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes
    • Terzi, E., Hölzemann, G., and Seelig, J. (1995). Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes. J. Molec. Biol. 252, 633-642.
    • (1995) J. Molec. Biol. , vol.252 , pp. 633-642
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 49
    • 0030600139 scopus 로고    scopus 로고
    • Molecular biology of prion diseases
    • Weissmann, C. (1996). Molecular biology of prion diseases. FEBS Letters 389, 3-11.
    • (1996) FEBS Letters , vol.389 , pp. 3-11
    • Weissmann, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.