메뉴 건너뛰기




Volumn 17, Issue 2, 2015, Pages 918-927

Intermediates caught in the act: Tracing insulin amyloid fibril formation in time by combined optical spectroscopy, light scattering, mass spectrometry and microscopy

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; INSULIN; PROTEIN AGGREGATE;

EID: 84916618826     PISSN: 14639076     EISSN: None     Source Type: Journal    
DOI: 10.1039/c4cp03072a     Document Type: Article
Times cited : (22)

References (43)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • C. M. Dobson, Protein folding and misfolding, Nature, 2003, 426, 884.
    • (2003) Nature , vol.426 , pp. 884
    • Dobson, C.M.1
  • 2
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • S. B. Prusiner, Novel proteinaceous infectious particles cause scrapie, Science, 1982, 216, 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 3
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • J. W. Kelly, Mechanisms of amyloidogenesis, Nat. Struct. Biol., 2000, 7, 824-826.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 5
    • 0035902492 scopus 로고    scopus 로고
    • Probing the mechanism of insulin fibril formation with insulin mutants
    • L. Nielsen, S. Frokjaer, J. Brange, V. N. Uversky and A. L. Fink, Probing the mechanism of insulin fibril formation with insulin mutants, Biochemistry, 2001, 40, 8397-8409.
    • (2001) Biochemistry , vol.40 , pp. 8397-8409
    • Nielsen, L.1    Frokjaer, S.2    Brange, J.3    Uversky, V.N.4    Fink, A.L.5
  • 9
    • 2442715309 scopus 로고    scopus 로고
    • Mechanismof insulin fibrillation
    • Q.-X. Hua and M. A. Weiss, Mechanismof insulin fibrillation, J. Biol. Chem., 2004, 279, 21449-21460.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21449-21460
    • Hua, Q.-X.1    Weiss, M.A.2
  • 10
    • 0000088925 scopus 로고
    • Pressure-soluble and pressure-displaceable components of monolayers of native and denatured proteins
    • I. Langmuir and D. F. Waugh, Pressure-soluble and pressure-displaceable components of monolayers of native and denatured proteins, J. Am. Chem. Soc., 1940, 62, 2771-2793.
    • (1940) J. Am. Chem. Soc. , vol.62 , pp. 2771-2793
    • Langmuir, I.1    Waugh, D.F.2
  • 11
    • 0000335935 scopus 로고
    • A fibrous modification of insilin. I. The heat precipitate of insulin
    • D. F. Waugh, A fibrous modification of insilin. I. The heat precipitate of insulin, J. Am. Chem. Soc., 1946, 68, 247-250.
    • (1946) J. Am. Chem. Soc. , vol.68 , pp. 247-250
    • Waugh, D.F.1
  • 12
    • 0008465437 scopus 로고
    • A mechanism for the formation of fibrils from protein molecules
    • D. F. Waugh, A mechanism for the formation of fibrils from protein molecules, J. Cell. Physiol., 1957, 49, 145-164.
    • (1957) J. Cell. Physiol. , vol.49 , pp. 145-164
    • Waugh, D.F.1
  • 13
    • 70349505749 scopus 로고    scopus 로고
    • Formation mechsnism of insulin fibrils and structural aspects of the insulin fibrillation process
    • M. Groenning, S. Frokjaer and B. Vestergaard, Formation mechsnism of insulin fibrils and structural aspects of the insulin fibrillation process, Curr. Protein Pept. Sci., 2009, 10, 509-528.
    • (2009) Curr. Protein Pept. Sci. , vol.10 , pp. 509-528
    • Groenning, M.1    Frokjaer, S.2    Vestergaard, B.3
  • 14
    • 0023948509 scopus 로고
    • Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient
    • F. E. Dische, C. Wernstedt, G. T. Westermark, P. Westermark, M. B. Pepys and J. A. Rennie, Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient, Diabetologia, 1988, 31, 158-161.
    • (1988) Diabetologia , vol.31 , pp. 158-161
    • Dische, F.E.1    Wernstedt, C.2    Westermark, G.T.3    Westermark, P.4    Pepys, M.B.5    Rennie, J.A.6
  • 15
    • 0030612301 scopus 로고    scopus 로고
    • Solution structures of the R6 human insulin hexamer
    • X. Chang, A. M. Jorgensen, P. Bardrum and J. J. Led, Solution structures of the R6 human insulin hexamer, Biochemistry, 1997, 36, 9409-9422.
    • (1997) Biochemistry , vol.36 , pp. 9409-9422
    • Chang, X.1    Jorgensen, A.M.2    Bardrum, P.3    Led, J.J.4
  • 16
    • 0026004620 scopus 로고
    • Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces
    • V. Sluzky, J. A. Tamada, A. M. Llibanov and R. Langer, Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces, Proc. Natl. Acad. Sci. U. S. A., 1991, 88, 9377-9381.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 9377-9381
    • Sluzky, V.1    Tamada, J.A.2    Llibanov, A.M.3    Langer, R.4
  • 17
    • 17144426174 scopus 로고    scopus 로고
    • Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy
    • R. Jansen, W. Dzwolak and R. Winter, Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy, Biophys. J., 2005, 88, 1344-1353.
    • (2005) Biophys. J. , vol.88 , pp. 1344-1353
    • Jansen, R.1    Dzwolak, W.2    Winter, R.3
  • 18
    • 1642417648 scopus 로고    scopus 로고
    • Amyloid fibrils fromthe viewpoint of protein folding
    • S. Ohnishi and K. Takano, Amyloid fibrils fromthe viewpoint of protein folding, Cell. Mol. Life Sci., 2004, 61, 511-524.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 511-524
    • Ohnishi, S.1    Takano, K.2
  • 19
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • T. R. Serio, A. G. Cashikar, A. S. Kowal, G. J. Sawicki, J. J. Moslehi and L. Serpell, Nucleated conformational conversion and the replication of conformational information by a prion determinant, Science, 2000, 289, 1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6
  • 22
    • 34248547813 scopus 로고    scopus 로고
    • Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases
    • S. T. Ferreira, M. N. Vieira and F. G. De Felice, Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases, IUBMB Life, 2007, 59, 332-345.
    • (2007) IUBMB Life , vol.59 , pp. 332-345
    • Ferreira, S.T.1    Vieira, M.N.2    De Felice, F.G.3
  • 23
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid formation by mass spectrometry
    • E. J. Nettleton, P. Tito, M. Sunde, M. Bouchard, C. M. Dobson and C. V. Robinson, Characterization of the oligomeric states of insulin in self-assembly and amyloid formation by mass spectrometry, Biophys. J., 2000, 79, 1053-1065.
    • (2000) Biophys. J. , vol.79 , pp. 1053-1065
    • Nettleton, E.J.1    Tito, P.2    Sunde, M.3    Bouchard, M.4    Dobson, C.M.5    Robinson, C.V.6
  • 24
    • 78650208860 scopus 로고    scopus 로고
    • Probing the nucleus model for oligomer formation during insulin amyloid fibrillogenesis
    • L. F. Pease, M. Sorci, S. Guha, D. H. Tsai, M. R. Zachariah and M. J. Tarlov, Probing the nucleus model for oligomer formation during insulin amyloid fibrillogenesis, Biophys. J., 2010, 99, 3979-3985.
    • (2010) Biophys. J. , vol.99 , pp. 3979-3985
    • Pease, L.F.1    Sorci, M.2    Guha, S.3    Tsai, D.H.4    Zachariah, M.R.5    Tarlov, M.J.6
  • 25
    • 2442715309 scopus 로고    scopus 로고
    • Mechanisms of insulin fibrillation: The structure of insilin under amyloidogenic conditions resembles a protein-folding intermediate
    • Q. X. Hua and M. A. Weiss, Mechanisms of insulin fibrillation: the structure of insilin under amyloidogenic conditions resembles a protein-folding intermediate, J. Biol. Chem., 2004, 279, 21449-21460.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21449-21460
    • Hua, Q.X.1    Weiss, M.A.2
  • 26
    • 78650990606 scopus 로고    scopus 로고
    • Paradoxical acceleration of dithiothreitol-induced aggregation of insulin in the presence of a chaperone
    • Z. Bumagina, B. Gurvits, N. Artemova, K. Muranov and B. Kurganov, Paradoxical acceleration of dithiothreitol-induced aggregation of insulin in the presence of a chaperone, Int. J. Mol. Sci., 2010, 11, 4556-4579.
    • (2010) Int. J. Mol. Sci. , vol.11 , pp. 4556-4579
    • Bumagina, Z.1    Gurvits, B.2    Artemova, N.3    Muranov, K.4    Kurganov, B.5
  • 28
    • 59849109485 scopus 로고    scopus 로고
    • A universal pathway for amyloid nucleus and precursor formation for insulin
    • A. Nayak, M. Sorci, S. Krueger and G. Belfort, A universal pathway for amyloid nucleus and precursor formation for insulin, Proteins, 2009, 74, 556-565.
    • (2009) Proteins , vol.74 , pp. 556-565
    • Nayak, A.1    Sorci, M.2    Krueger, S.3    Belfort, G.4
  • 30
    • 70349318348 scopus 로고    scopus 로고
    • Time-dependent insulin oligomer reaction pathway prior to fibril formation:Cooling and seeding
    • M. Sorci, R. A. Grassucci, I. Hahn, J. Frank and G. Belfort, Time-dependent insulin oligomer reaction pathway prior to fibril formation:cooling and seeding, Proteins, 2009, 77, 62-73.
    • (2009) Proteins , vol.77 , pp. 62-73
    • Sorci, M.1    Grassucci, R.A.2    Hahn, I.3    Frank, J.4    Belfort, G.5
  • 31
    • 33646199155 scopus 로고    scopus 로고
    • Early events in insulin fibrilisation studied by time-lapse atomic force microscopy
    • A. Podestra, G. Tiana, P. Milani and M. Manno, Early events in insulin fibrilisation studied by time-lapse atomic force microscopy, Biophys. J., 2006, 90, 589-597.
    • (2006) Biophys. J. , vol.90 , pp. 589-597
    • Podestra, A.1    Tiana, G.2    Milani, P.3    Manno, M.4
  • 33
    • 54749122331 scopus 로고    scopus 로고
    • Exploiting cross-amyloid interactions to inhibit protein aggregation but not function: Nanomolar affinity inhibition of insulin aggregation by an IAPP mimic
    • A. Veltova, M. Tatarek-Nossol, E. Andreetto and A. Kapurniotu, Exploiting cross-amyloid interactions to inhibit protein aggregation but not function: Nanomolar affinity inhibition of insulin aggregation by an IAPP mimic, Angew. Chem., Int. Ed., 2008, 47, 7114-7118.
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 7114-7118
    • Veltova, A.1    Tatarek-Nossol, M.2    Andreetto, E.3    Kapurniotu, A.4
  • 35
    • 0036770753 scopus 로고    scopus 로고
    • Analytical laser induced liquid beam desorption mass spectrometry of protonated amio acids and their non-covalently bound aggregates
    • A. Charvat, E. Lugovoj, M. Faubel and B. Abel, Analytical laser induced liquid beam desorption mass spectrometry of protonated amio acids and their non-covalently bound aggregates, Eur. Phys. J. D, 2002, 20, 573.
    • (2002) Eur. Phys. J. D , vol.20 , pp. 573
    • Charvat, A.1    Lugovoj, E.2    Faubel, M.3    Abel, B.4
  • 36
    • 3042682569 scopus 로고    scopus 로고
    • New design for a time-of-flight mass spectrometer
    • A. Charvat, E. Lugovoj, M. Faubel and B. Abel, New design for a time-of-flight mass spectrometer, Rev. Sci. Instrum., 2004, 75, 1209-1218.
    • (2004) Rev. Sci. Instrum. , vol.75 , pp. 1209-1218
    • Charvat, A.1    Lugovoj, E.2    Faubel, M.3    Abel, B.4
  • 37
    • 0038007461 scopus 로고    scopus 로고
    • Advanced Series in Physical Chemistry
    • ed. C. Y. Ng, World Scientific, New York
    • M. Faubel, Advanced Series in Physical Chemistry, in Photoelectron spectroscopy at liquid surfaces, ed. C. Y. Ng, World Scientific, New York, 2000, vol. 10A.
    • (2000) Photoelectron Spectroscopy at Liquid Surfaces , vol.10 A
    • Faubel, M.1
  • 38
    • 33750100829 scopus 로고
    • Non-equilibrium molecular evaporation of carboxylic acid dimers
    • M. Faubel and T. Kisters, Non-equilibrium molecular evaporation of carboxylic acid dimers, Nature, 1989, 339, 527-529.
    • (1989) Nature , vol.339 , pp. 527-529
    • Faubel, M.1    Kisters, T.2
  • 40
    • 34848889264 scopus 로고    scopus 로고
    • How to make big molecules fly out of liquid water: Applications, features and physics of laser assisted liquid phase dispersion mass spectrometry
    • A. Charvat and B. Abel, How to make big molecules fly out of liquid water: applications, features and physics of laser assisted liquid phase dispersion mass spectrometry, Phys. Chem. Chem. Phys., 2007, 9, 3335-3360.
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 3335-3360
    • Charvat, A.1    Abel, B.2
  • 41
    • 0030579560 scopus 로고    scopus 로고
    • Prionics or the kinetic basis of prion diseases
    • M. Eigen, Prionics or the kinetic basis of prion diseases, Biophys. Chem., 1996, 63, A1-A18.
    • (1996) Biophys. Chem. , vol.63 , pp. A1-A18
    • Eigen, M.1
  • 42
    • 79960320827 scopus 로고    scopus 로고
    • Isolating toxic insulin amyloid reactive species that lack beta-sheetsand have a wide pH-Stability
    • C. L. Heldt, D. Kurouski, M. Sorci, E. Grafeld, I. K. Lednev and G. Belfort, Isolating toxic insulin amyloid reactive species that lack beta-sheetsand have a wide pH-Stability, Biophys. J., 2011, 100, 2792-2800.
    • (2011) Biophys. J. , vol.100 , pp. 2792-2800
    • Heldt, C.L.1    Kurouski, D.2    Sorci, M.3    Grafeld, E.4    Lednev, I.K.5    Belfort, G.6
  • 43
    • 43049164334 scopus 로고    scopus 로고
    • Secondary Nucleation and Accessible Surface in Insulin Amyloid Fibril Formation
    • V. Foderà, F. Librizzi, M. Groenning, M. van de Weert and M. Leone, Secondary Nucleation and Accessible Surface in Insulin Amyloid Fibril Formation, J. Phys. Chem. B, 2008, 112, 3853-3858.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 3853-3858
    • Foderà, V.1    Librizzi, F.2    Groenning, M.3    Van De Weert, M.4    Leone, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.