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Volumn 385, Issue 2, 2009, Pages 374-376

Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; FINANCE; NEURODEGENERATIVE DISEASES; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES;

EID: 58149376285     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.10.034     Document Type: Article
Times cited : (18)

References (17)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • Tycko R. Molecular structure of amyloid fibrils: Insights from solid-state NMR. Q. Rev. Biophys. 39 (2006) 1-55
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 1-55
    • Tycko, R.1
  • 3
    • 0035234662 scopus 로고    scopus 로고
    • An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A
    • Alexandrescu S.T. An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A. Pac. Symp. Biocomput. 6 (2001) 67-78
    • (2001) Pac. Symp. Biocomput. , vol.6 , pp. 67-78
    • Alexandrescu, S.T.1
  • 7
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M., and Blake C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50 (1997) 123-159
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 8
    • 28244484729 scopus 로고    scopus 로고
    • Structures for amyloid fibrils
    • Makin O.S., and Serpell L.C. Structures for amyloid fibrils. FEBS J. 272 (2005) 5950-5961
    • (2005) FEBS J. , vol.272 , pp. 5950-5961
    • Makin, O.S.1    Serpell, L.C.2
  • 9
    • 33749838193 scopus 로고    scopus 로고
    • Hydrogen/Deuterium exchange mass spectrometry: A window into amyloid structure
    • Kheterpal I., and Wetzel R. Hydrogen/Deuterium exchange mass spectrometry: A window into amyloid structure. Acc. Chem. Res. 39 (2006) 584-593
    • (2006) Acc. Chem. Res. , vol.39 , pp. 584-593
    • Kheterpal, I.1    Wetzel, R.2
  • 12
    • 1242316998 scopus 로고    scopus 로고
    • Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy
    • Olofsson A., Ippel J.H., Wijmenga S.S., Lundgren E., and Öhman A. Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy. J. Biol. Chem. 279 (2004) 5699-5707
    • (2004) J. Biol. Chem. , vol.279 , pp. 5699-5707
    • Olofsson, A.1    Ippel, J.H.2    Wijmenga, S.S.3    Lundgren, E.4    Öhman, A.5
  • 13
    • 33644851439 scopus 로고    scopus 로고
    • The solvent protection of Alzheimer amyloid-β(1-42) fibrils as determined by solution NMR spectroscopy
    • Olofsson A., Sauer-Eriksson A.E., and Öhman A. The solvent protection of Alzheimer amyloid-β(1-42) fibrils as determined by solution NMR spectroscopy. J. Biol. Chem. 281 (2006) 477-483
    • (2006) J. Biol. Chem. , vol.281 , pp. 477-483
    • Olofsson, A.1    Sauer-Eriksson, A.E.2    Öhman, A.3
  • 14
    • 34249051698 scopus 로고    scopus 로고
    • Amide solvent protection analysis demonstrates that amyloid-β(1-40) and amyloid-β(1-42) form different fibrillar structures under identical conditions
    • Olofsson A., Lindhagen-Persson M., Sauer-Eriksson A.E., and Öhman A. Amide solvent protection analysis demonstrates that amyloid-β(1-40) and amyloid-β(1-42) form different fibrillar structures under identical conditions. Biochem. J. 404 (2007) 63-70
    • (2007) Biochem. J. , vol.404 , pp. 63-70
    • Olofsson, A.1    Lindhagen-Persson, M.2    Sauer-Eriksson, A.E.3    Öhman, A.4
  • 15
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • Petkova A.T., Yau W.M., and Tycko R. Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils. Biochemistry 45 (2006) 498-512
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 16
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 17
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological, and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ
    • Wood S.J., Maleeff B., Hart T., and Wetzel R. Physical, morphological, and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ. J. Mol. Biol. 256 (1996) 870-877
    • (1996) J. Mol. Biol. , vol.256 , pp. 870-877
    • Wood, S.J.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.