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Volumn 106, Issue 7, 2014, Pages 1433-1435

Amyloid fibrils: The eighth wonder of the world in protein folding and aggregation

Author keywords

[No Author keywords available]

Indexed keywords

AMYLIN; AMYLOID; HISTIDINE; TYROSINE;

EID: 84897436519     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.02.007     Document Type: Short Survey
Times cited : (23)

References (10)
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    • Dobson, C.M.1
  • 2
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    • F. Chiti, and M. Stefani C.M. Dobson Rationalization of the effects of mutations on peptide and protein aggregation rates Nature 424 2003 805 808 (Pubitemid 37021713)
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  • 4
    • 84897414719 scopus 로고    scopus 로고
    • Mutational analysis of pre-amyloid intermediates: The role of His-Tyr interactions in islet amyloid formation
    • L.-H. Tu, and A.L. Serrano D.P. Raleigh Mutational analysis of pre-amyloid intermediates: the role of His-Tyr interactions in islet amyloid formation Biophys. J. 106 2014 1520 1527
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    • Tu, L.-H.1    Serrano, A.L.2    Raleigh, D.P.3
  • 5
    • 84861730624 scopus 로고    scopus 로고
    • Disulfide bridges remain intact while native insulin converts into amyloid fibrils
    • D. Kurouski, and J. Washington I.K. Lednev Disulfide bridges remain intact while native insulin converts into amyloid fibrils PLoS ONE 7 2012 e36989
    • (2012) PLoS ONE , vol.7 , pp. 36989
    • Kurouski, D.1    Washington, J.2    Lednev, I.K.3
  • 6
    • 84863834613 scopus 로고    scopus 로고
    • Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy
    • V. Shashilov, and M. Xu I.K. Lednev Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy J. Phys. Chem. B 116 2012 7926 7930
    • (2012) J. Phys. Chem. B , vol.116 , pp. 7926-7930
    • Shashilov, V.1    Xu, M.2    Lednev, I.K.3
  • 7
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    • Normal and reversed supramolecular chirality of insulin fibrils probed by vibrational circular dichroism at the protofilament level of fibril structure
    • D. Kurouski, and R.K. Dukor I.K. Lednev Normal and reversed supramolecular chirality of insulin fibrils probed by vibrational circular dichroism at the protofilament level of fibril structure Biophys. J. 103 2012 522 531
    • (2012) Biophys. J. , vol.103 , pp. 522-531
    • Kurouski, D.1    Dukor, R.K.2    Lednev, I.K.3
  • 8
    • 84891854485 scopus 로고    scopus 로고
    • Surface characterization of insulin protofilaments and fibril polymorphs using tip-enhanced Raman spectroscopy (TERS)
    • D. Kurouski, and T. Deckert-Gaudig I.K. Lednev Surface characterization of insulin protofilaments and fibril polymorphs using tip-enhanced Raman spectroscopy (TERS) Biophys. J. 106 2014 263 271
    • (2014) Biophys. J. , vol.106 , pp. 263-271
    • Kurouski, D.1    Deckert-Gaudig, T.2    Lednev, I.K.3
  • 9
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    • Amyloid fibrils are "alive": Spontaneous refolding from one polymorph to another
    • D. Kurouski, W. Lauro, and I.K. Lednev Amyloid fibrils are "alive": spontaneous refolding from one polymorph to another Chem. Commun. (Camb.) 46 2010 4249 4251
    • (2010) Chem. Commun. (Camb.) , vol.46 , pp. 4249-4251
    • Kurouski, D.1    Lauro, W.2    Lednev, I.K.3
  • 10
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    • Spontaneous inter-conversion of insulin fibril chirality
    • D. Kurouski, and R.K. Dukor I.K. Lednev Spontaneous inter-conversion of insulin fibril chirality Chem. Commun. (Camb.) 48 2012 2837 2839
    • (2012) Chem. Commun. (Camb.) , vol.48 , pp. 2837-2839
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.