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Volumn 329, Issue 4, 2005, Pages 1200-1207

Single particle analysis of manganese-induced prion protein aggregates

Author keywords

Amyloid; Copper; Dementia; Fluorescence correlation spectroscopy; Manganese; Neurodegeneration; Prion; SIFT

Indexed keywords

COPPER ION; DODECYL SULFATE SODIUM; EDETIC ACID; HISTIDINE; MANGANESE; OLIGOMER; PRION PROTEIN;

EID: 17644380969     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.02.094     Document Type: Article
Times cited : (44)

References (34)
  • 2
    • 0035013510 scopus 로고    scopus 로고
    • Prion-induced neuronal damage-the mechanisms of neuronal destruction in the subacute spongiform encephalopathies
    • A. Giese, and H.A. Kretzschmar Prion-induced neuronal damage-the mechanisms of neuronal destruction in the subacute spongiform encephalopathies Curr. Top. Microbiol. Immunol. 253 2001 203 217
    • (2001) Curr. Top. Microbiol. Immunol. , vol.253 , pp. 203-217
    • Giese, A.1    Kretzschmar, H.A.2
  • 7
    • 0028844207 scopus 로고
    • Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: Structural studies using synthetic peptides
    • M.P. Hornshaw, J.R. McDermott, J.M. Candy, and J.H. Lakey Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides Biochem. Biophys. Res. Commun. 214 1995 993 999
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 993-999
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3    Lakey, J.H.4
  • 8
    • 0028883341 scopus 로고
    • Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
    • M.P. Hornshaw, J.R. McDermott, and J.M. Candy Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein Biochem. Biophys. Res. Commun. 207 1995 621 629
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 621-629
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3
  • 11
    • 0037083888 scopus 로고    scopus 로고
    • Metal imbalance and compromised antioxidant function are early changes in prion disease
    • A.M. Thackray, R. Knight, S.J. Haswell, R. Bujdoso, and D.R. Brown Metal imbalance and compromised antioxidant function are early changes in prion disease Biochem. J. 362 2002 253 258
    • (2002) Biochem. J. , vol.362 , pp. 253-258
    • Thackray, A.M.1    Knight, R.2    Haswell, S.J.3    Bujdoso, R.4    Brown, D.R.5
  • 13
    • 0035656122 scopus 로고    scopus 로고
    • A Yin-Yang role for metals in prion disease
    • B.S. Wong, D.R. Brown, and M.S. Sy A Yin-Yang role for metals in prion disease Panminerva Med. 43 2001 283 287
    • (2001) Panminerva Med. , vol.43 , pp. 283-287
    • Wong, B.S.1    Brown, D.R.2    Sy, M.S.3
  • 14
  • 16
    • 0034654304 scopus 로고    scopus 로고
    • Consequences of manganese replacement of copper for prion protein function and proteinase resistance
    • D.R. Brown, F. Hafiz, L.L. Glasssmith, B.S. Wong, I.M. Jones, C. Clive, and S.J. Haswell Consequences of manganese replacement of copper for prion protein function and proteinase resistance EMBO J. 19 2000 1180 1186
    • (2000) EMBO J. , vol.19 , pp. 1180-1186
    • Brown, D.R.1    Hafiz, F.2    Glasssmith, L.L.3    Wong, B.S.4    Jones, I.M.5    Clive, C.6    Haswell, S.J.7
  • 18
    • 17344375337 scopus 로고    scopus 로고
    • Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form
    • K. Jansen, O. Schafer, E. Birkmann, K. Post, H. Serban, S.B. Prusiner, and D. Riesner Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form Biol. Chem. 382 2001 683 691
    • (2001) Biol. Chem. , vol.382 , pp. 683-691
    • Jansen, K.1    Schafer, O.2    Birkmann, E.3    Post, K.4    Serban, H.5    Prusiner, S.B.6    Riesner, D.7
  • 20
    • 0037470178 scopus 로고    scopus 로고
    • Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: Insights from circular dichroism
    • A.P. Garnett, and J.H. Viles Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism J. Biol. Chem. 278 2003 6795 6802
    • (2003) J. Biol. Chem. , vol.278 , pp. 6795-6802
    • Garnett, A.P.1    Viles, J.H.2
  • 21
    • 0030878056 scopus 로고    scopus 로고
    • Recombinant full-length murine prion protein, mPrP(23-231): Purification and spectroscopic characterization
    • S. Hornemann, C. Korth, B. Oesch, R. Riek, G. Wider, K. Wuthrich, and R. Glockshuber Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization FEBS Lett. 413 1997 277 281
    • (1997) FEBS Lett. , vol.413 , pp. 277-281
    • Hornemann, S.1    Korth, C.2    Oesch, B.3    Riek, R.4    Wider, G.5    Wuthrich, K.6    Glockshuber, R.7
  • 23
    • 0034625009 scopus 로고    scopus 로고
    • Ultrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targets
    • J. Bieschke, A. Giese, W. Schulz-Schaeffer, I. Zerr, S. Poser, M. Eigen, and H. Kretzschmar Ultrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targets Proc. Natl. Acad. Sci. USA 97 2000 5468 5473
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5468-5473
    • Bieschke, J.1    Giese, A.2    Schulz-Schaeffer, W.3    Zerr, I.4    Poser, S.5    Eigen, M.6    Kretzschmar, H.7
  • 24
    • 28444454589 scopus 로고    scopus 로고
    • Putting prions into focus: Application of single molecule detection to the diagnosis of prion diseases
    • A. Giese, J. Bieschke, M. Eigen, and H.A. Kretzschmar Putting prions into focus: application of single molecule detection to the diagnosis of prion diseases Arch. Virol. Suppl. 2000 161 171
    • (2000) Arch. Virol. Suppl. , pp. 161-171
    • Giese, A.1    Bieschke, J.2    Eigen, M.3    Kretzschmar, H.A.4
  • 25
    • 0031871740 scopus 로고    scopus 로고
    • Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy
    • M. Pitschke, R. Prior, M. Haupt, and D. Riesner Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy Nat. Med. 4 1998 832 834
    • (1998) Nat. Med. , vol.4 , pp. 832-834
    • Pitschke, M.1    Prior, R.2    Haupt, M.3    Riesner, D.4
  • 26
    • 0030763365 scopus 로고    scopus 로고
    • Kinetic investigations by fluorescence correlation spectroscopy: The analytical and diagnostic potential of diffusion studies
    • P. Schwille, J. Bieschke, and F. Oehlenschlager Kinetic investigations by fluorescence correlation spectroscopy: the analytical and diagnostic potential of diffusion studies Biophys. Chem. 66 1997 211 228
    • (1997) Biophys. Chem. , vol.66 , pp. 211-228
    • Schwille, P.1    Bieschke, J.2    Oehlenschlager, F.3
  • 27
    • 0033598837 scopus 로고    scopus 로고
    • Fluorescence-intensity distribution analysis and its application in biomolecular detection technology
    • P. Kask, K. Palo, D. Ullmann, and K. Gall Fluorescence-intensity distribution analysis and its application in biomolecular detection technology Proc. Natl. Acad. Sci. USA 96 1999 13756 13761
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13756-13761
    • Kask, P.1    Palo, K.2    Ullmann, D.3    Gall, K.4
  • 29
    • 0030895059 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution
    • P. Schwille, F.J. Meyer-Almes, and R. Rigler Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution Biophys. J. 72 1997 1878 1886
    • (1997) Biophys. J. , vol.72 , pp. 1878-1886
    • Schwille, P.1    Meyer-Almes, F.J.2    Rigler, R.3
  • 30
    • 0037127206 scopus 로고    scopus 로고
    • Mapping Cu(II) binding sites in prion proteins by diethyl pyrocarbonate modification and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric footprinting
    • K. Qin, Y. Yang, P. Mastrangelo, and D. Westaway Mapping Cu(II) binding sites in prion proteins by diethyl pyrocarbonate modification and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric footprinting J. Biol. Chem. 277 2002 1981 1990
    • (2002) J. Biol. Chem. , vol.277 , pp. 1981-1990
    • Qin, K.1    Yang, Y.2    Mastrangelo, P.3    Westaway, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.