메뉴 건너뛰기




Volumn 89, Issue 6, 2005, Pages 4234-4244

Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACYLPHOSPHATASE; AMYLOID; CONGO RED; PROTEIN ACPDRO2; THIOFLAVINE; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

EID: 28444464509     PISSN: 00063495     EISSN: 00063495     Source Type: Journal    
DOI: 10.1529/biophysj.105.067538     Document Type: Article
Times cited : (63)

References (50)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. 2003. Protein folding and misfolding. Nature. 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M., and C. M. Dobson. 2003. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81:678-699.
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 3
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky, V. N., and A. L. Fink. 2004. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta. 1698:131-153.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 4
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • Walsh, D. M., and D. J. Selkoe. 2004. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept. Lett. 11:213-228.
    • (2004) Protein Pept. Lett. , vol.11 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 5
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and x-ray diffraction
    • Sunde, M., and C. Blake. 1997. The structure of amyloid fibrils by electron microscopy and x-ray diffraction. Adv. Protein Chem. 50:123-159.
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 7
    • 0037465708 scopus 로고    scopus 로고
    • Insights into the amyloid folding problem from solid-state NMR
    • Tycko, R. 2003. Insights into the amyloid folding problem from solid-state NMR. Biochemistry. 42:3151-3159.
    • (2003) Biochemistry , vol.42 , pp. 3151-3159
    • Tycko, R.1
  • 8
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by Congo red spectral shift assay
    • Klunk, W. E., R. F. Jacob, and R. P. Mason. 1999. Quantifying amyloid by Congo red spectral shift assay. Methods Enzymol. 309:285-305.
    • (1999) Methods Enzymol. , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 9
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • LeVine 3rd, H. 1999. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309:274-284.
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • Levine III, H.1
  • 10
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: Localisation and implications
    • Krebs, M. R., E. H. Bromley, and A. M. Donald. 2005. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 149:30-37.
    • (2005) J. Struct. Biol. , vol.149 , pp. 30-37
    • Krebs, M.R.1    Bromley, E.H.2    Donald, A.M.3
  • 12
    • 2142762962 scopus 로고    scopus 로고
    • Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p
    • Bousset, L., V. Redeker, P. Decottignies, S. Dubois, P. Le Marechal, and R. Melki. 2004. Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p. Biochemistry. 43:5022-5032.
    • (2004) Biochemistry , vol.43 , pp. 5022-5032
    • Bousset, L.1    Redeker, V.2    Decottignies, P.3    Dubois, S.4    Le Marechal, P.5    Melki, R.6
  • 13
    • 0345118103 scopus 로고    scopus 로고
    • Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: A model for misfolding in polyglutamine disease
    • Chow, M. K., H. L. Paulson, and S. P. Bottomley. 2004. Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: a model for misfolding in polyglutamine disease. J. Mol. Biol. 335:333-341.
    • (2004) J. Mol. Biol. , vol.335 , pp. 333-341
    • Chow, M.K.1    Paulson, H.L.2    Bottomley, S.P.3
  • 14
    • 0037168643 scopus 로고    scopus 로고
    • Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state
    • Lindberg, M. J., L. Tibell, and M. Oliveberg. 2002. Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state. Proc. Natl. Acad. Sci. USA. 99:16607-16612.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16607-16612
    • Lindberg, M.J.1    Tibell, L.2    Oliveberg, M.3
  • 16
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J. W. 1998. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8:101-106.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 18
    • 9144264986 scopus 로고    scopus 로고
    • Polyglutamine expansion in Ataxin-3 does not affect protein stability: Implications for misfolding and disease
    • Chow, M. K., A. M. Ellisdon, L. D. Cabrita, and S. P. Bottomley. 2005. Polyglutamine expansion in Ataxin-3 does not affect protein stability: implications for misfolding and disease. J. Biol. Chem. 279:47643-47651.
    • (2005) J. Biol. Chem. , vol.279 , pp. 47643-47651
    • Chow, M.K.1    Ellisdon, A.M.2    Cabrita, L.D.3    Bottomley, S.P.4
  • 19
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • Bouchard, M., J. Zurdo, E. J. Nettleton, C. M. Dobson, and C. V. Robinson. 2000. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9:960-967.
    • (2000) Protein Sci. , vol.9 , pp. 960-967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 20
    • 3342902033 scopus 로고    scopus 로고
    • Modulation of S6 fibrillation by unfolding rates and gatekeeper residues
    • Pedersen, J. S., G. Christensen, and D. E. Otzen. 2004. Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. J. Mol. Biol. 341:575-588.
    • (2004) J. Mol. Biol. , vol.341 , pp. 575-588
    • Pedersen, J.S.1    Christensen, G.2    Otzen, D.E.3
  • 21
    • 1842790837 scopus 로고    scopus 로고
    • Aggregation of the acylphosphatase from Sulfolobus solfataricus: The folded and partially unfolded states can both be precursors for amyloid formation
    • Plakoutsi, G., N. Taddei, M. Stefani, and F. Chiti. 2004. Aggregation of the acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation. J. Biol. Chem. 279:14111-14119.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14111-14119
    • Plakoutsi, G.1    Taddei, N.2    Stefani, M.3    Chiti, F.4
  • 24
    • 0017123760 scopus 로고
    • A new synthesis of benzoyl phosphate: A substrate for acyl phosphatase assay
    • Camici, G., G. Manao, G. Cappugi, and G. Ramponi. 1976. A new synthesis of benzoyl phosphate: a substrate for acyl phosphatase assay. Experientia. 32:535-536.
    • (1976) Experientia , vol.32 , pp. 535-536
    • Camici, G.1    Manao, G.2    Cappugi, G.3    Ramponi, G.4
  • 25
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C., Jr. 1990. Protein secondary structure and circular dichroism: a practical guide. Proteins. 7:205-214.
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 26
    • 0013923439 scopus 로고
    • Aromatic acyl phosphates as substrates of acyl phosphatase
    • Ramponi, G., C. Treves, and A. A. Guerritore. 1966. Aromatic acyl phosphates as substrates of acyl phosphatase. Arch. Biochem. Biophys. 115:129-135.
    • (1966) Arch. Biochem. Biophys. , vol.115 , pp. 129-135
    • Ramponi, G.1    Treves, C.2    Guerritore, A.A.3
  • 27
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenyl-methanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro, M. M., and D. W. Bolen. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenyl-methanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry. 27:8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 28
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson, S. E., and A. R. Fersht. 1991. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry. 30:10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 29
    • 0028063528 scopus 로고
    • Determination of protein tertiary structure class from circular dichroism spectra
    • Venyaminov, S. Yu., and K. S. Vassilenko. 1994. Determination of protein tertiary structure class from circular dichroism spectra. Anal. Biochem. 222:176-184.
    • (1994) Anal. Biochem. , vol.222 , pp. 176-184
    • Yu, V.S.1    Vassilenko, K.S.2
  • 31
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Stryer, L. 1965. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13:482-495.
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 32
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O. B. 1995. Molten globule and protein folding. Adv. Protein Chem. 47:83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 33
    • 0031972919 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation
    • Matulis, D., and R. Lovrien. 1998. 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys. J. 74:422-429.
    • (1998) Biophys. J. , vol.74 , pp. 422-429
    • Matulis, D.1    Lovrien, R.2
  • 34
    • 0030814166 scopus 로고    scopus 로고
    • Insights into acylphosphatase structure and catalytic mechanism
    • Stefani, M., N. Taddei, and G. Ramponi. 1997. Insights into acylphosphatase structure and catalytic mechanism. Cell. Mol. Life Sci. 53:141-151.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 141-151
    • Stefani, M.1    Taddei, N.2    Ramponi, G.3
  • 35
    • 0033988167 scopus 로고    scopus 로고
    • Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol
    • Hamada, D., F. Chili, J. I. Guijarro, M. Kataoka, N. Taddei, and C. M. Dobson. 2000. Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol. Nat. Struct. Biol. 7:58-61.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 58-61
    • Hamada, D.1    Chili, F.2    Guijarro, J.I.3    Kataoka, M.4    Taddei, N.5    Dobson, C.M.6
  • 36
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek, A., J. T. Kellis, Jr., L. Serrano, M. Bycroft, and A. R. Fersht. 1990. Transient folding intermediates characterized by protein engineering. Nature. 346:440-445.
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 38
    • 3242785264 scopus 로고    scopus 로고
    • Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
    • DuBay, K. F., A. P. Pawar, F. Chiti, J. Zurdo, C. M. Dobson, and M. Vendruscolo. 2004. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J. Mol. Biol. 341:1317-1326.
    • (2004) J. Mol. Biol. , vol.341 , pp. 1317-1326
    • Dubay, K.F.1    Pawar, A.P.2    Chiti, F.3    Zurdo, J.4    Dobson, C.M.5    Vendruscolo, M.6
  • 39
    • 0037059069 scopus 로고    scopus 로고
    • Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
    • Chiti, F., M. Calamai, N. Taddei, M. Stefani, G. Ramponi, and C. M. Dobson. 2002. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl. Acad. Sci. USA. 99:16419-16426.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16419-16426
    • Chiti, F.1    Calamai, M.2    Taddei, N.3    Stefani, M.4    Ramponi, G.5    Dobson, C.M.6
  • 40
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 42
    • 0034612254 scopus 로고    scopus 로고
    • The preaggregated state of an amyloidogenic protein: Hydrostatic pressure converts native transthyretin into the amyloidogenic state
    • Ferrao-Gonzales, A. D., S. O. Souto, J. L. Silva, and D. Foguel. 2000. The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state. Proc. Natl. Acad. Sci. USA. 97:6445-6450.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6445-6450
    • Ferrao-Gonzales, A.D.1    Souto, S.O.2    Silva, J.L.3    Foguel, D.4
  • 44
    • 0034599720 scopus 로고    scopus 로고
    • Mutational analysis of the propensity for amyloid formation by a globular protein
    • Chiti, R, N. Taddei, M. Bucciantini, P. White, G. Ramponi, and C. M. Dobson. 2000. Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 19:1441-1449.
    • (2000) EMBO J. , vol.19 , pp. 1441-1449
    • Chiti, R.1    Taddei, N.2    Bucciantini, M.3    White, P.4    Ramponi, G.5    Dobson, C.M.6
  • 46
    • 0037058942 scopus 로고    scopus 로고
    • Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity
    • Hammarstrom, P., X. Jiang, A. R. Hurshman, E. T. Powers, and J. W. Kelly. 2002. Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity. Proc. Natl. Acad. Sci. USA. 99:16427-16432.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16427-16432
    • Hammarstrom, P.1    Jiang, X.2    Hurshman, A.R.3    Powers, E.T.4    Kelly, J.W.5
  • 47
    • 0034255027 scopus 로고    scopus 로고
    • A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
    • Ramirez-Alvarado, M., J. S. Merkel, and L. Regan. 2000. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. USA. 97:8979-8984.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 48
    • 15444373859 scopus 로고    scopus 로고
    • Investigating the effects of mutations on protein aggregation in the cell
    • Calloni, G., S. Zoffoli, M. Stefani, C. M. Dobson, and F. Chiti. 2005. Investigating the effects of mutations on protein aggregation in the cell. J. Biol. Chem. 280:10607-10613.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10607-10613
    • Calloni, G.1    Zoffoli, S.2    Stefani, M.3    Dobson, C.M.4    Chiti, F.5
  • 49
    • 0346500469 scopus 로고    scopus 로고
    • The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process
    • Monti, M., B. L. Garolla di Bard, G. Calloni, F. Chiti, A. Amoresano, G. Ramponi, and P. Pucci. 2004. The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. J. Mol. Biol. 336:253-262.
    • (2004) J. Mol. Biol. , vol.336 , pp. 253-262
    • Monti, M.1    Garolla Di Bard, B.L.2    Calloni, G.3    Chiti, F.4    Amoresano, A.5    Ramponi, G.6    Pucci, P.7
  • 50
    • 0037022563 scopus 로고    scopus 로고
    • Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson, J. S., and D. C. Richardson. 2002. Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. USA. 99:2754-2759.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.