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Volumn 103, Issue 3, 2012, Pages 522-531

Normal and reversed supramolecular chirality of insulin fibrils probed by vibrational circular dichroism at the protofilament level of fibril structure

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN;

EID: 84864686797     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.04.042     Document Type: Article
Times cited : (91)

References (32)
  • 1
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
    • C.M. Dobson Protein misfolding, evolution and disease Trends Biochem. Sci. 24 1999 329 332 (Pubitemid 29421804)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 3
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890 (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 6
    • 0023192941 scopus 로고
    • Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells
    • DOI 10.1073/pnas.84.11.3881
    • P. Westermark, and C. Wernstedt K.H. Johnson Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells Proc. Natl. Acad. Sci. USA 84 1987 3881 3885 (Pubitemid 17088383)
    • (1987) Proceedings of the National Academy of Sciences of the United States of America , vol.84 , Issue.11 , pp. 3881-3885
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3
  • 7
    • 0023948509 scopus 로고
    • Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient
    • F.E. Dische, and C. Wernstedt P.J. Watkins Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient Diabetologia 31 1988 158 161
    • (1988) Diabetologia , vol.31 , pp. 158-161
    • Dische, F.E.1    Wernstedt, C.2    Watkins, P.J.3
  • 8
    • 33646093028 scopus 로고    scopus 로고
    • Polymorphism and ultrastructural organization of prion protein amyloid fibrils: An insight from high resolution atomic force microscopy
    • M. Anderson, and O.V. Bocharova I.V. Baskakov Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy J. Mol. Biol. 358 2006 580 596
    • (2006) J. Mol. Biol. , vol.358 , pp. 580-596
    • Anderson, M.1    Bocharova, O.V.2    Baskakov, I.V.3
  • 10
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • DOI 10.1038/nature03679
    • R. Krishnan, and S.L. Lindquist Structural insights into a yeast prion illuminate nucleation and strain diversity Nature 435 2005 765 772 (Pubitemid 40839721)
    • (2005) Nature , vol.435 , Issue.7043 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 11
    • 33845637320 scopus 로고    scopus 로고
    • From the Polymorphism of Amyloid Fibrils to their Assembly Mechanism and Cytotoxicity
    • DOI 10.1016/S0065-3233(06)73007-8, PII S0065323306730078, Fibrous Proteins: Amyloids, Prions and Beta Proteins
    • L. Kreplak, and U. Aebi From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity Adv. Protein Chem. 73 2006 217 233 (Pubitemid 44960405)
    • (2006) Advances in Protein Chemistry , vol.73 , pp. 217-233
    • Kreplak, L.1    Aebi, U.2
  • 12
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • DOI 10.1126/science.1105850
    • A.T. Petkova, and R.D. Leapman R. Tycko Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils Science 307 2005 262 265 (Pubitemid 40116242)
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 14
    • 17144426174 scopus 로고    scopus 로고
    • Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy
    • DOI 10.1529/biophysj.104.048843
    • R. Jansen, W. Dzwolak, and R. Winter Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy Biophys. J. 88 2005 1344 1353 (Pubitemid 40975961)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 1344-1353
    • Jansen, R.1    Dzwolak, W.2    Winter, R.3
  • 15
    • 66149140617 scopus 로고    scopus 로고
    • Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure
    • A.K. Paravastu, and I. Qahwash R. Tycko Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure Proc. Natl. Acad. Sci. USA 106 2009 7443 7448
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7443-7448
    • Paravastu, A.K.1    Qahwash, I.2    Tycko, R.3
  • 16
    • 77950288850 scopus 로고    scopus 로고
    • Relation between serum amyloid A truncated peptides and their suprastructure chirality
    • N. Rubin, and E. Perugia L. Addadi Relation between serum amyloid A truncated peptides and their suprastructure chirality J. Am. Chem. Soc. 132 2010 4242 4248
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4242-4248
    • Rubin, N.1    Perugia, E.2    Addadi, L.3
  • 17
    • 77956812220 scopus 로고    scopus 로고
    • Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism
    • D. Kurouski, and R.A. Lombardi L.A. Nafie Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism Chem. Commun. (Camb.) 46 2010 7154 7156
    • (2010) Chem. Commun. (Camb.) , vol.46 , pp. 7154-7156
    • Kurouski, D.1    Lombardi, R.A.2    Nafie, L.A.3
  • 19
    • 79851507329 scopus 로고    scopus 로고
    • Vibrational circular dichroism as a probe of fibrillogenesis: The origin of the anomalous intensity enhancement of amyloid-like fibrils
    • T.J. Measey, and R. Schweitzer-Stenner Vibrational circular dichroism as a probe of fibrillogenesis: the origin of the anomalous intensity enhancement of amyloid-like fibrils J. Am. Chem. Soc. 133 2011 1066 1076
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 1066-1076
    • Measey, T.J.1    Schweitzer-Stenner, R.2
  • 20
    • 80052823373 scopus 로고    scopus 로고
    • Spiral superstructures of amyloid-like fibrils of polyglutamic acid: An infrared absorption and vibrational circular dichroism study
    • A. Fulara, and A. Lakhani W. Dzwolak Spiral superstructures of amyloid-like fibrils of polyglutamic acid: an infrared absorption and vibrational circular dichroism study J. Phys. Chem. B. 115 2011 11010 11016
    • (2011) J. Phys. Chem. B. , vol.115 , pp. 11010-11016
    • Fulara, A.1    Lakhani, A.2    Dzwolak, W.3
  • 23
    • 13844254633 scopus 로고    scopus 로고
    • Deep-UV Raman spectrometer tunable between 193 and 205 nm for structural characterization of proteins
    • DOI 10.1007/s00216-004-2991-5
    • I.K. Lednev, and V.V. Ermolenkov M. Xu Deep-UV Raman spectrometer tunable between 193 and 205 nm for structural characterization of proteins Anal. Bioanal. Chem. 381 2005 431 437 (Pubitemid 40249165)
    • (2005) Analytical and Bioanalytical Chemistry , vol.381 , Issue.2 , pp. 431-437
    • Lednev, I.K.1    Ermolenkov, V.V.2    He, W.3    Xu, M.4
  • 25
    • 27944455577 scopus 로고    scopus 로고
    • Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: An induced circular dichroism/DFT study
    • DOI 10.1016/j.febslet.2005.10.048, PII S0014579305013177
    • W. Dzwolak, and M. Pecul Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: an induced circular dichroism/DFT study FEBS Lett. 579 2005 6601 6603 (Pubitemid 41682446)
    • (2005) FEBS Letters , vol.579 , Issue.29 , pp. 6601-6603
    • Dzwolak, W.1    Pecul, M.2
  • 26
    • 42749089759 scopus 로고    scopus 로고
    • Chiral bifurcation in aggregating insulin: An induced circular dichroism study
    • A. Loksztejn, and W. Dzwolak Chiral bifurcation in aggregating insulin: an induced circular dichroism study J. Mol. Biol. 379 2008 9 16
    • (2008) J. Mol. Biol. , vol.379 , pp. 9-16
    • Loksztejn, A.1    Dzwolak, W.2
  • 27
    • 78349297127 scopus 로고    scopus 로고
    • Vortex-induced chiral bifurcation in aggregating insulin
    • W. Dzwolak Vortex-induced chiral bifurcation in aggregating insulin Chirality 22 Suppl 1 2010 E154 E160
    • (2010) Chirality , vol.22 , Issue.SUPPL. 1
    • Dzwolak, W.1
  • 29
    • 73249133310 scopus 로고    scopus 로고
    • Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal
    • T.J. Measey, and K.B. Smith R. Schweitzer-Stenner Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal J. Am. Chem. Soc. 131 2009 18218 18219
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 18218-18219
    • Measey, T.J.1    Smith, K.B.2    Schweitzer-Stenner, R.3
  • 30
    • 84857218620 scopus 로고    scopus 로고
    • 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
    • Kurouski, D.1    Dukor, R.K.2    Lednev, I.K.3
  • 31
    • 34247093347 scopus 로고    scopus 로고
    • Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked β-solenoid model of HET-s prion fibrils
    • DOI 10.1074/jbc.M611464200
    • A. Sen, and U. Baxa A.C. Steven Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked β-solenoid model of HET-s prion fibrils J. Biol. Chem. 282 2007 5545 5550 (Pubitemid 47093734)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5545-5550
    • Sen, A.1    Baxa, U.2    Simon, M.N.3    Wall, J.S.4    Sabate, R.5    Saupe, S.J.6    Steven, A.C.7
  • 32
    • 0036386364 scopus 로고    scopus 로고
    • Dependence of α-synuclein aggregate morphology on solution conditions
    • W. Hoyer, and T. Antony V. Subramaniam Dependence of α-synuclein aggregate morphology on solution conditions J. Mol. Biol. 322 2002 383 393
    • (2002) J. Mol. Biol. , vol.322 , pp. 383-393
    • Hoyer, W.1    Antony, T.2    Subramaniam, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.