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Volumn 347, Issue 5, 2005, Pages 903-909

High hydrostatic pressure dissociates early aggregates of TTR 105-115, but not the mature amyloid fibrils

Author keywords

Amyloid; Atomic force microscopy; Fourier transform infrared spectroscopy; Hydrogen bonds; Transthyretin

Indexed keywords

AMYLOID; PEPTIDE DERIVATIVE; PREALBUMIN; WATER;

EID: 15244356060     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.073     Document Type: Article
Times cited : (99)

References (41)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 3
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • M. Fändrich, and C.M. Dobson The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation EMBO J. 21 2002 5682 5690
    • (2002) EMBO J. , vol.21 , pp. 5682-5690
    • Fändrich, M.1    Dobson, C.M.2
  • 4
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • D. Shortle The denatured state (the other half of the folding equation) and its role in protein stability FASEB J. 10 1996 27 34
    • (1996) FASEB J. , vol.10 , pp. 27-34
    • Shortle, D.1
  • 5
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • J.L. Silva, D. Foguel, and C. Royer Pressure provides new insights into protein folding, dynamics and structure Trends Biochem. Sci. 26 2001 612 618
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.3
  • 6
    • 0037171122 scopus 로고    scopus 로고
    • High pressure effects on biological macromolecules: From structural changes to alteration of cellular processes
    • C. Balny, P. Masson, and K. Heremans High pressure effects on biological macromolecules: from structural changes to alteration of cellular processes Biochim. Biophys. Acta 1595 2002 3 10
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 3-10
    • Balny, C.1    Masson, P.2    Heremans, K.3
  • 7
    • 0034612254 scopus 로고    scopus 로고
    • The preaggregated state of an amyloidogenic protein: Hydrostatic pressure converts native transthyretin into the amyloidogenic state
    • A.D. Ferrão-Gonzales, S.O. Souto, J.L. Silva, and D. Foguel The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state Proc. Natl Acad. Sci. USA 97 2000 6645 6650
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6645-6650
    • Ferrão-Gonzales, A.D.1    Souto, S.O.2    Silva, J.L.3    Foguel, D.4
  • 8
    • 0043194011 scopus 로고    scopus 로고
    • Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities
    • D. Foguel, M.C. Suarez, A.D. Ferrão-Gonzales, T.C.R. Porto, L. Palmieri, and C.M. Einsiedler Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities Proc. Natl Acad. Sci. USA 100 2003 9831 9836
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9831-9836
    • Foguel, D.1    Suarez, M.C.2    Ferrão-Gonzales, A.D.3    Porto, T.C.R.4    Palmieri, L.5    Einsiedler, C.M.6
  • 9
    • 0025801516 scopus 로고
    • Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro
    • A. Gustavsson, U. Engström, and P. Westermark Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro Biochem. Biophys. Res. Commun. 175 1991 1159 1164
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 1159-1164
    • Gustavsson, A.1    Engström, U.2    Westermark, P.3
  • 10
    • 1642575162 scopus 로고    scopus 로고
    • Neurodegeneration in familial amyloid polyneuropathy: From pathology to molecular signaling
    • M.M. Sousa, and M.J. Saraiva Neurodegeneration in familial amyloid polyneuropathy: from pathology to molecular signaling Prog. Neurobiol. 71 2003 385 400
    • (2003) Prog. Neurobiol. , vol.71 , pp. 385-400
    • Sousa, M.M.1    Saraiva, M.J.2
  • 11
    • 0033857583 scopus 로고    scopus 로고
    • TTR amyloidosis-structural features leading to protein aggregation and their implications on therapeutic strategies
    • A.M. Damas, and M.J. Saraiva TTR amyloidosis-structural features leading to protein aggregation and their implications on therapeutic strategies J. Struct. Biol. 130 2000 290 299
    • (2000) J. Struct. Biol. , vol.130 , pp. 290-299
    • Damas, A.M.1    Saraiva, M.J.2
  • 13
    • 1642433249 scopus 로고    scopus 로고
    • High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
    • C.P. Jaroniec, C.E. MacPhee, V.S. Bajaj, M.T. McMahon, C.M. Dobson, and R.G. Griffin High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy Proc. Natl Acad. Sci. USA 101 2004 711 716
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 711-716
    • Jaroniec, C.P.1    MacPhee, C.E.2    Bajaj, V.S.3    McMahon, M.T.4    Dobson, C.M.5    Griffin, R.G.6
  • 14
    • 2942707921 scopus 로고    scopus 로고
    • Molecular dynamics studies of the process of amyloid aggregation of peptide fragments of transthyretin
    • E. Paci, J. Gspöner, X. Salvatella, and M. Vendruscolo Molecular dynamics studies of the process of amyloid aggregation of peptide fragments of transthyretin J. Mol. Biol. 340 2004 555 569
    • (2004) J. Mol. Biol. , vol.340 , pp. 555-569
    • Paci, E.1    Gspöner, J.2    Salvatella, X.3    Vendruscolo, M.4
  • 15
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • M. Jackson, and H.H. Mantsch The use and misuse of FTIR spectroscopy in the determination of protein structure Crit. Rev. Biochem. Mol. Biol. 30 1995 95 120
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 16
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • D.M. Byler, and H. Susi Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymers 25 1986 469 487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 17
    • 0035158241 scopus 로고    scopus 로고
    • Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy
    • L. Nielsen, S. Frokjaer, J.F. Carpenter, and J. Brange Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy J. Pharm. Sci. 90 2001 29 37
    • (2001) J. Pharm. Sci. , vol.90 , pp. 29-37
    • Nielsen, L.1    Frokjaer, S.2    Carpenter, J.F.3    Brange, J.4
  • 18
    • 0037432332 scopus 로고    scopus 로고
    • Conformational behavior and aggregation of α-synuclein in organic solvents: Modelling the effects of membranes
    • L.A. Munishkina, C. Phelan, V.N. Uversky, and A.L. Fink Conformational behavior and aggregation of α-synuclein in organic solvents: modelling the effects of membranes Biochemistry 42 2003 2720 2730
    • (2003) Biochemistry , vol.42 , pp. 2720-2730
    • Munishkina, L.A.1    Phelan, C.2    Uversky, V.N.3    Fink, A.L.4
  • 19
    • 0034834580 scopus 로고    scopus 로고
    • Preparation and characterization of purified amyloid fibrils
    • J. Zurdo, J.I. Guijarro, and C.M. Dobson Preparation and characterization of purified amyloid fibrils J. Am. Chem. Soc. 123 2001 8141 8142
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8141-8142
    • Zurdo, J.1    Guijarro, J.I.2    Dobson, C.M.3
  • 20
    • 0031170886 scopus 로고    scopus 로고
    • The toxicity of the Alzheimer's beta-amyloid peptide correlates with a distinct fiber morphology
    • B. Seilheimer, B. Bohrmann, L. Bondolfi, F. Muller, D. Stuber, and H. Dobeli The toxicity of the Alzheimer's beta-amyloid peptide correlates with a distinct fiber morphology J. Struct. Biol. 119 1997 59 71
    • (1997) J. Struct. Biol. , vol.119 , pp. 59-71
    • Seilheimer, B.1    Bohrmann, B.2    Bondolfi, L.3    Muller, F.4    Stuber, D.5    Dobeli, H.6
  • 21
    • 0034951056 scopus 로고    scopus 로고
    • The assembly of amyloidogenic yeast sup35 as assessed by scanning (atomic) force microscopy: An analogy to linear colloidal aggregation?
    • S. Xu, B. Bevis, and M.F. Arnsdorf The assembly of amyloidogenic yeast sup35 as assessed by scanning (atomic) force microscopy: an analogy to linear colloidal aggregation? Biophys. J. 81 2001 446 454
    • (2001) Biophys. J. , vol.81 , pp. 446-454
    • Xu, S.1    Bevis, B.2    Arnsdorf, M.F.3
  • 22
    • 9444299029 scopus 로고    scopus 로고
    • Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure
    • F.G. De Felice, M.N.N. Vieira, M.N.L. Meirelles, L.A. Morozova-Roche, C.M. Dobson, and S.T. Ferreira Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure FASEB J. 18 2004 1099 1101
    • (2004) FASEB J. , vol.18 , pp. 1099-1101
    • De Felice, F.G.1    Vieira, M.N.N.2    Meirelles, M.N.L.3    Morozova-Roche, L.A.4    Dobson, C.M.5    Ferreira, S.T.6
  • 24
    • 0346110652 scopus 로고    scopus 로고
    • Unfolding and fibrillogenesis of insulin: Temperature, pressure and chemistry
    • C. Dirix, F. Meersman, L. Smeller, and K. Heremans Unfolding and fibrillogenesis of insulin: temperature, pressure and chemistry High Pressure Res. 22 2002 733 736
    • (2002) High Pressure Res. , vol.22 , pp. 733-736
    • Dirix, C.1    Meersman, F.2    Smeller, L.3    Heremans, K.4
  • 25
    • 1842786897 scopus 로고    scopus 로고
    • Core and heterogeneity of beta(2)-microglobulin amyloid fibrils as revealed by H/D exchange
    • K.I. Yamaguchi, H. Katou, M. Hoshino, K. Hasegawa, H. Naiki, and Y. Goto Core and heterogeneity of beta(2)-microglobulin amyloid fibrils as revealed by H/D exchange J. Mol. Biol. 338 2004 559 571
    • (2004) J. Mol. Biol. , vol.338 , pp. 559-571
    • Yamaguchi, K.I.1    Katou, H.2    Hoshino, M.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 26
    • 2342468009 scopus 로고    scopus 로고
    • The N-terminal prion domain of Ure2p converts from an unfolded to a thermally resistant conformation upon filament formation
    • U. Baxa, P.D. Ross, R.B. Wickner, and A.C. Steven The N-terminal prion domain of Ure2p converts from an unfolded to a thermally resistant conformation upon filament formation J. Mol. Biol. 339 2004 259 264
    • (2004) J. Mol. Biol. , vol.339 , pp. 259-264
    • Baxa, U.1    Ross, P.D.2    Wickner, R.B.3    Steven, A.C.4
  • 28
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • K. Heremans, and L. Smeller Protein structure and dynamics at high pressure Biochim. Biophys. Acta 1386 1998 353 370
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 353-370
    • Heremans, K.1    Smeller, L.2
  • 29
    • 0031789585 scopus 로고    scopus 로고
    • Probing the contribution of internal cavities to the volume change of protein unfolding under pressure
    • K.J. Frye, and C.A. Royer Probing the contribution of internal cavities to the volume change of protein unfolding under pressure Protein Sci. 7 1998 2217 2222
    • (1998) Protein Sci. , vol.7 , pp. 2217-2222
    • Frye, K.J.1    Royer, C.A.2
  • 30
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid
    • M. Balbirnie, R. Grothe, and D.S. Eisenberg An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid Proc. Natl Acad. Sci. USA 98 2001 2375 2380
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 32
    • 0034610180 scopus 로고    scopus 로고
    • Beta amyloid fibrils possess a core structure highly resistant to hydrogen exchange
    • I. Kheterpal, S. Zhou, K.D. Cook, and R. Wetzel Beta amyloid fibrils possess a core structure highly resistant to hydrogen exchange Proc. Natl Acad. Sci. USA 97 2000 13597 13601
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13597-13601
    • Kheterpal, I.1    Zhou, S.2    Cook, K.D.3    Wetzel, R.4
  • 33
    • 2542542833 scopus 로고    scopus 로고
    • A model for Ure2p prion filaments and other amyloids: The parallel superpleated β-structure
    • A.V. Kajava, U. Baxa, R.B. Wickner, and A.C. Steven A model for Ure2p prion filaments and other amyloids: the parallel superpleated β-structure Proc. Natl Acad. Sci. USA 101 2004 7885 7890
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7885-7890
    • Kajava, A.V.1    Baxa, U.2    Wickner, R.B.3    Steven, A.C.4
  • 34
    • 0037171151 scopus 로고    scopus 로고
    • Pressure effects on intra- and intermolecular interactions within proteins
    • B.B. Boonyaratanakornkit, C. Beum Park, and D.S. Clark Pressure effects on intra- and intermolecular interactions within proteins Biochim. Biophys. Acta 1595 2002 235 249
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 235-249
    • Boonyaratanakornkit, B.B.1    Beum Park, C.2    Clark, D.S.3
  • 35
    • 1642488929 scopus 로고    scopus 로고
    • Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils
    • T.N. Niraula, T. Konno, H. Li, H. Yamada, K. Akasaka, and H. Tachibana Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils Proc. Natl Acad. Sci. USA 101 2004 4089 4093
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4089-4093
    • Niraula, T.N.1    Konno, T.2    Li, H.3    Yamada, H.4    Akasaka, K.5    Tachibana, H.6
  • 36
    • 0033596963 scopus 로고    scopus 로고
    • Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin
    • L. Smeller, P. Rubens, and K. Heremans Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin Biochemistry 38 1999 3816 3820
    • (1999) Biochemistry , vol.38 , pp. 3816-3820
    • Smeller, L.1    Rubens, P.2    Heremans, K.3
  • 37
    • 3543030409 scopus 로고    scopus 로고
    • Hydration and packing effects on prion folding and beta-sheet conversion: High-pressure spectroscopy and pressure perturbation calorimetry studies
    • Y. Cordeiro, J. Kraineva, R. Ravindra, M.L.T.R. Lima, M.P.B. Gomes, and D. Foguel Hydration and packing effects on prion folding and beta-sheet conversion: high-pressure spectroscopy and pressure perturbation calorimetry studies J. Biol. Chem. 279 2004 32354 32359
    • (2004) J. Biol. Chem. , vol.279 , pp. 32354-32359
    • Cordeiro, Y.1    Kraineva, J.2    Ravindra, R.3    Lima, M.L.T.R.4    Gomes, M.P.B.5    Foguel, D.6
  • 39
    • 0036971123 scopus 로고    scopus 로고
    • Dynamics of hydrogen bond desolvation in protein folding
    • A. Fernández, T.R. Sosnick, and A. Colubri Dynamics of hydrogen bond desolvation in protein folding J. Mol. Biol. 321 2002 569 675
    • (2002) J. Mol. Biol. , vol.321 , pp. 569-675
    • Fernández, A.1    Sosnick, T.R.2    Colubri, A.3
  • 40
    • 0037154268 scopus 로고    scopus 로고
    • Protein folding mediated by solvation: Water expulsion and formation of the hydrophobic core occur after the structural collapse
    • M.S. Cheung, A.E. Garcia, and J.N. Onuchic Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse Proc. Natl Acad. Sci. USA 99 2002 685 690
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 685-690
    • Cheung, M.S.1    Garcia, A.E.2    Onuchic, J.N.3
  • 41
    • 0038692903 scopus 로고    scopus 로고
    • High pressure induces the formation of aggregation-prone states of proteins under reducing conditions
    • F. Meersman, and K. Heremans High pressure induces the formation of aggregation-prone states of proteins under reducing conditions Biophys. Chem. 104 2003 297 304
    • (2003) Biophys. Chem. , vol.104 , pp. 297-304
    • Meersman, F.1    Heremans, K.2


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