메뉴 건너뛰기




Volumn 19, Issue 7, 2000, Pages 1441-1449

Mutational analysis of the propensity for amyloid formation by a globular protein

Author keywords

Acylphosphatase; Amyloid fibrils; Conformational stability; Protein engineering; Protein misfolding

Indexed keywords

ACYLPHOSPHATASE; AMYLOID; GLOBULAR PROTEIN; MUTANT PROTEIN; TRIFLUOROETHANOL;

EID: 0034599720     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.7.1441     Document Type: Article
Times cited : (219)

References (46)
  • 1
    • 0028800177 scopus 로고
    • Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin
    • Bauer, H.H., Aebi, U., Haner, M., Hermann, R., Muller, M., Arvinte, T. and Merkle, H.P. (1995) Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. J. Struct. Biol., 115, 1-15.
    • (1995) J. Struct. Biol. , vol.115 , pp. 1-15
    • Bauer, H.H.1    Aebi, U.2    Haner, M.3    Hermann, R.4    Muller, M.5    Arvinte, T.6    Merkle, H.P.7
  • 2
    • 0032970177 scopus 로고    scopus 로고
    • Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug flufenamic acid
    • Baures, P.W., Oza, V.B., Peterson, S.A. and Kelly, J.W. (1999) Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug flufenamic acid. Bioorg. Med. Chem., 7, 1339-1347.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 1339-1347
    • Baures, P.W.1    Oza, V.B.2    Peterson, S.A.3    Kelly, J.W.4
  • 3
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth, D.R. et al. (1997) Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature, 385, 787-793.
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1
  • 6
    • 0032477888 scopus 로고    scopus 로고
    • Conformational stability of muscle acylphosphatase. The role of temperature, denaturant concentration and pH
    • Chiti, F., van Nuland, N.A.J., Taddei, N., Magherini, F., Stefani, M., Ramponi, G. and Dobson, C.M. (1998b) Conformational stability of muscle acylphosphatase. The role of temperature, denaturant concentration and pH. Biochemistry, 37, 1447-1455.
    • (1998) Biochemistry , vol.37 , pp. 1447-1455
    • Chiti, F.1    Van Nuland, N.A.J.2    Taddei, N.3    Magherini, F.4    Stefani, M.5    Ramponi, G.6    Dobson, C.M.7
  • 10
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease
    • Conway, K.A., Harper, J.D. and Lansbury, P.T. (1998) Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease. Nature Med., 11, 1318-1320.
    • (1998) Nature Med. , vol.11 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 11
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C.M. (1999) Protein misfolding, evolution and disease. Trends Biochem. Sci., 9, 329-332.
    • (1999) Trends Biochem. Sci. , vol.9 , pp. 329-332
    • Dobson, C.M.1
  • 12
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink, A.L. (1998) Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold Des., 3, R9-R23.
    • (1998) Fold Des. , vol.3
    • Fink, A.L.1
  • 13
    • 0030474922 scopus 로고    scopus 로고
    • The structure, stability and folding process of amyloidogenic mutant human lysozyme
    • Funahashi, J., Takano, K., Ogasahara, K., Yamagata, Y. and Yutani, K. (1996) The structure, stability and folding process of amyloidogenic mutant human lysozyme. J. Biochem., 120, 1216-1223.
    • (1996) J. Biochem. , vol.120 , pp. 1216-1223
    • Funahashi, J.1    Takano, K.2    Ogasahara, K.3    Yamagata, Y.4    Yutani, K.5
  • 14
    • 0015150725 scopus 로고
    • Creation of 'amyloid' fibrils from Bence Jones proteins in vitro
    • Glenner, G.G., Ein, D., Eanes, E.D., Bladen, H.A., Terry, W. and Page, D.L. (1971) Creation of 'amyloid' fibrils from Bence Jones proteins in vitro. Science, 174, 712-714.
    • (1971) Science , vol.174 , pp. 712-714
    • Glenner, G.G.1    Ein, D.2    Eanes, E.D.3    Bladen, H.A.4    Terry, W.5    Page, D.L.6
  • 15
    • 0031170857 scopus 로고    scopus 로고
    • Polymorphic fibrillar assembly of human amylin
    • Goldsbury, C.S. et al. (1997) Polymorphic fibrillar assembly of human amylin. J. Struct. Biol., 119, 17-27.
    • (1997) J. Struct. Biol. , vol.119 , pp. 17-27
    • Goldsbury, C.S.1
  • 16
  • 18
    • 0031444010 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper, J.D., Lieber, C.M. and Lansbury, P.T. (1997) Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol., 4, 951-959.
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 19
    • 0028305304 scopus 로고
    • A role for destabilising amino acid replacements in light chain amyloidosis
    • Hurle, M.R., Helms, L.R., Li, L., Chan, W. and Wetzel, R. (1994) A role for destabilising amino acid replacements in light chain amyloidosis. Proc. Natl Acad Sci. USA, 91, 5446-5450.
    • (1994) Proc. Natl Acad Sci. USA , vol.91 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Chan, W.4    Wetzel, R.5
  • 20
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez, J.L., Guijarro, J.L., Orlova, E., Zurdo, J., Dobson, C.M., Sunde, M. and Saibil, H.R. (1999) Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J., 18, 815-821.
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.L.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 21
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • Kelly, J.W. (1996) Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol., 6, 11-17.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 22
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Lai, Z., Colon, W. and Kelly, J.W. (1996) The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry, 35, 6470-6482.
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 23
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
    • Lansbury, P.T. (1999) Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl Acad. Sci. USA, 96, 3342-3344.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3342-3344
    • Lansbury, P.T.1
  • 24
    • 0001733723 scopus 로고
    • Thioflavine T interaction with amyloid β-sheet structures
    • LeVine III, H. (1995) Thioflavine T interaction with amyloid β-sheet structures. Amyloid: Int. J. Exp. Clin. Invest., 2, 1-6.
    • (1995) Amyloid: Int. J. Exp. Clin. Invest. , vol.2 , pp. 1-6
    • LeVine H. III1
  • 25
    • 0033574161 scopus 로고    scopus 로고
    • Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
    • Liemann, S. and Glockshuber, R. (1999) Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry, 38, 3258-3267.
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 26
    • 0032503933 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module
    • Litvinovich, S.V., Brew, S.A., Aota, S., Akiyama, S.K., Haudenschild, C. and Ingham, K.C. (1998) Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. J. Mol. Biol., 280, 245-258.
    • (1998) J. Mol. Biol. , vol.280 , pp. 245-258
    • Litvinovich, S.V.1    Brew, S.A.2    Aota, S.3    Akiyama, S.K.4    Haudenschild, C.5    Ingham, K.C.6
  • 27
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal transthyrethin variants and their relationship to amyloid disease
    • McCutchen, S.L., Lai, Z.H., Miroy, G.J., Kelly, J.W. and Colon, W. (1995) Comparison of lethal and nonlethal transthyrethin variants and their relationship to amyloid disease. Biochemistry, 34, 13527-13536.
    • (1995) Biochemistry , vol.34 , pp. 13527-13536
    • McCutchen, S.L.1    Lai, Z.H.2    Miroy, G.J.3    Kelly, J.W.4    Colon, W.5
  • 31
    • 0026522991 scopus 로고
    • Three-dimensional structure of acylphosphatase. Refinement and structure analysis
    • Pastore, A., Saudek, V., Ramponi, G. and Williams, R.J.P. (1992) Three-dimensional structure of acylphosphatase. Refinement and structure analysis. J. Mol. Biol., 224, 427-440.
    • (1992) J. Mol. Biol. , vol.224 , pp. 427-440
    • Pastore, A.1    Saudek, V.2    Ramponi, G.3    Williams, R.J.P.4
  • 32
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • Perutz, M.F. (1999) Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci., 24, 58-63.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 33
    • 0023697408 scopus 로고
    • Unfolding free-energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M.M. and Bolen, D.W. (1988) Unfolding free-energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry, 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 35
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid β-protein and the genetics of Alzheimer's disease
    • Selkoe, D.J. (1996) Amyloid β-protein and the genetics of Alzheimer's disease. J. Biol. Chem., 271, 18295-18298.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 36
    • 0028845988 scopus 로고
    • Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs
    • Serpell, L.C., Sunde, M., Fraser, P.E., Luther, P.K., Morris, E.P., Sangren, O., Lundgren, E. and Blake, C.C.F. (1995) Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs. J. Mol. Biol., 254, 113-118.
    • (1995) J. Mol. Biol. , vol.254 , pp. 113-118
    • Serpell, L.C.1    Sunde, M.2    Fraser, P.E.3    Luther, P.K.4    Morris, E.P.5    Sangren, O.6    Lundgren, E.7    Blake, C.C.F.8
  • 37
    • 0014098295 scopus 로고
    • High resolution electron microscopic analysis of the amyloid fibril
    • Shirahama, T. and Cohen, A.S. (1967) High resolution electron microscopic analysis of the amyloid fibril. J. Cell Biol., 33, 679-706.
    • (1967) J. Cell Biol. , vol.33 , pp. 679-706
    • Shirahama, T.1    Cohen, A.S.2
  • 38
    • 0015549030 scopus 로고
    • Fibrillar assemblage of variable segments of immunoglobulin light chains: An electron microscopy study
    • Shirahama, T., Benson, M.D., Cohen, A.S. and Tanaka, A. (1973) Fibrillar assemblage of variable segments of immunoglobulin light chains: an electron microscopy study. J. Immunol., 110, 21-30.
    • (1973) J. Immunol. , vol.110 , pp. 21-30
    • Shirahama, T.1    Benson, M.D.2    Cohen, A.S.3    Tanaka, A.4
  • 39
    • 0017226393 scopus 로고
    • Characterisation of amyloid fibril proteins from medullary carcinoma of the thyroid
    • Sletten, K., Westermark, P. and Natvig, J.B. (1976) Characterisation of amyloid fibril proteins from medullary carcinoma of the thyroid. J. Exp. Med., 143, 993-998.
    • (1976) J. Exp. Med. , vol.143 , pp. 993-998
    • Sletten, K.1    Westermark, P.2    Natvig, J.B.3
  • 40
    • 0030320442 scopus 로고    scopus 로고
    • The concept of a random coil - Residual structure in peptides and denatured proteins
    • Smith, L.J., Fiebig, K.M., Schwalbe, H. and Dobson, C.M. (1996) The concept of a random coil - Residual structure in peptides and denatured proteins. Fold. Des., 1, R95-R106.
    • (1996) Fold. Des. , vol.1
    • Smith, L.J.1    Fiebig, K.M.2    Schwalbe, H.3    Dobson, C.M.4
  • 41
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde, M. and Blake, C. (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
  • 42
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki, W., Petersen, R.B., Gambetti, P. and Surewicz, W.K. (1998) Familial mutations and the thermodynamic stability of the recombinant human prion protein. J. Biol. Chem., 273, 31048-31052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3    Surewicz, W.K.4
  • 43
    • 0029953734 scopus 로고    scopus 로고
    • Looking for residues involved in muscle acylphosphatase catalytic mechanism and structural stabilization: The role of Asn41, Thr42 and Thr46
    • Taddei, N., Stefani, M., Magherini, F., Chitli, F., Modesti, A., Raugei, G. and Ramponi, G. (1996) Looking for residues involved in muscle acylphosphatase catalytic mechanism and structural stabilization: the role of Asn41, Thr42 and Thr46. Biochemistry, 35, 7077-7083.
    • (1996) Biochemistry , vol.35 , pp. 7077-7083
    • Taddei, N.1    Stefani, M.2    Magherini, F.3    Chitli, F.4    Modesti, A.5    Raugei, G.6    Ramponi, G.7
  • 46
    • 26344441261 scopus 로고    scopus 로고
    • Inhibition of amyloid assembly
    • Wetzel, R. (1997) Inhibition of amyloid assembly. J. Neurochem., 69, S104.
    • (1997) J. Neurochem. , vol.69
    • Wetzel, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.