메뉴 건너뛰기




Volumn 342, Issue 1, 2004, Pages 321-331

Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin

Author keywords

aggregation intermediates; amyloid formation; protein misfolding; serine proteases; TFE induced protein denaturation; chymotrypsin

Indexed keywords

AMYLOID; CHYMOTRYPSIN; SULFONIC ACID DERIVATIVE; TRIFLUOROETHANOL;

EID: 4143097041     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.06.089     Document Type: Article
Times cited : (229)

References (45)
  • 2
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • C.M. Dobson The structural basis of protein folding and its links with human disease Phil. Trans. R. Soc. ser. B 356 2001 133 145
    • (2001) Phil. Trans. R. Soc. Ser. B , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 3
    • 0037041441 scopus 로고    scopus 로고
    • Medicine: Danger-misfolding proteins
    • R.J. Ellis, and T.J. Pinheiro Medicine: danger-misfolding proteins Nature 416 2002 483 484
    • (2002) Nature , vol.416 , pp. 483-484
    • Ellis1    Pinheiro, T.J.R.J.2
  • 4
    • 0036411969 scopus 로고    scopus 로고
    • Insights into the origin of the tendency of the PI3-SH3 domain to form amyloidfibrils
    • S. Ventura, E. Lacroix, and L. Serrano Insights into the origin of the tendency of the PI3-SH3 domain to form amyloidfibrils J. Mol. Biol. 322 2002 1147 1158
    • (2002) J. Mol. Biol. , vol.322 , pp. 1147-1158
    • Ventura, S.1    Lacroix2    Serrano, L.E.3
  • 6
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • M. Fandrich, M.A. Fletcher, and C.M. Dobson Amyloid fibrils from muscle myoglobin Nature 410 2001 165 166
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher2    Dobson, C.M.M.A.3
  • 7
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • M. Bucciantini, E. Giannoni, F. Chiti, F. Baroni, L. Formgli, and J. Zurdo Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 416 2002 507 511
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formgli5    Zurdo, J.L.6
  • 9
    • 0032503933 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module
    • S.V. Litvinovich, S.A. Brew, S. Aota, S.K. Akiyama, C. Haudenschild, and K.C. Ingham Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module J. Mol. Biol. 280 1998 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    Haudenschild5    Ingham, K.C.C.6
  • 11
    • 0032477873 scopus 로고    scopus 로고
    • The environmental dependency of protein folding best explains prion and amyloid diseases
    • J.W. Kelly The environmental dependency of protein folding best explains prion and amyloid diseases Proc. Natl Acad. Sci. USA 95 1998 930 932
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 930-932
    • Kelly, J.W.1
  • 12
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Z. Lai, W. Colon, and J.W. Kelly The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid Biochemistry 35 1996 6470 6482
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon2    Kelly, J.W.W.3
  • 13
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • D.R. Booth, M. Sunde, V. Belloti, C.V. Robinson, W.L. Hutchinson, and P.E. Fraser Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis Nature 385 1997 787 793
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1    Sunde, M.2    Belloti, V.3    Robinson, C.V.4    Hutchinson5    Fraser, P.E.W.L.6
  • 14
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in α-synuclein fibril formation
    • V.N. Uversky, J. Li, and A.L. Fink Evidence for a partially folded intermediate in α-synuclein fibril formation J. Biol. Chem. 276 2001 10737 10744
    • (2001) J. Biol. Chem. , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li2    Fink, A.L.J.3
  • 15
  • 16
  • 17
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • J.D. Harper, and P.T. Lansbury Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 66 1997 355 407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 355-407
    • Harper1    Lansbury, P.T.J.D.2
  • 18
    • 0015859701 scopus 로고
    • Comparison of the crystal structures of chymotrypsinogen-A and alpha-chymotrypsin
    • H.T. Wright Comparison of the crystal structures of chymotrypsinogen-A and alpha-chymotrypsin J. Mol. Biol. 79 1973 1 11
    • (1973) J. Mol. Biol. , vol.79 , pp. 1-11
    • Wright, H.T.1
  • 19
    • 0038043276 scopus 로고    scopus 로고
    • Amyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation
    • S. Srisailam, T.K. Kumar, D. Rajalingam, K.M. Kathir, H.S. Sheu, and F.J. Jan Amyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation J. Biol. Chem. 278 2003 17701 17709
    • (2003) J. Biol. Chem. , vol.278 , pp. 17701-17709
    • Srisailam, S.1    Kumar, T.K.2    Rajalingam, D.3    Kathir, K.M.4    Sheu5    Jan, F.J.H.S.6
  • 20
    • 0034599720 scopus 로고    scopus 로고
    • Mutational analysis of the propensity for amyloid formation by a globular protein
    • F. Chiti, N. Taddei, M. Bucciantini, P. White, G. Ramponi, and C.M. Dobson Mutational analysis of the propensity for amyloid formation by a globular protein EMBO J. 19 2000 1441 1449
    • (2000) EMBO J. , vol.19 , pp. 1441-1449
    • Chiti, F.1    Taddei, N.2    Bucciantini, M.3    White, P.4    Ramponi5    Dobson, C.M.G.6
  • 21
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease betaamyloid peptides: Detection of amyloid aggregation in solution
    • H. Le Vine 3rd Thioflavine T interaction with synthetic Alzheimer's disease betaamyloid peptides: detection of amyloid aggregation in solution Protein Sci. 2 1993 404 410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Le Vine III, H.1
  • 22
    • 0031570763 scopus 로고    scopus 로고
    • Stopped-flow kinetics reveal multiple phases of thioflavin T binding to Alzheimer beta (1-40) amyloid fibrils
    • H. Le Vine 3rd Stopped-flow kinetics reveal multiple phases of thioflavin T binding to Alzheimer beta (1-40) amyloid fibrils Arch. Biochem. Biophys. 342 1997 306 316
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 306-316
    • Le Vine III, H.1
  • 23
    • 0034938980 scopus 로고    scopus 로고
    • Why Congo red binding is specific for amyloid proteins - Model studies and a computer analysis approach
    • I. Roterman, M. Krül, M. Nowak, L. Konieczny, J. Rybarska, and B. Stopa Why Congo red binding is specific for amyloid proteins - model studies and a computer analysis approach Med. Sci. Monit. 7 2001 771 784
    • (2001) Med. Sci. Monit. , vol.7 , pp. 771-784
    • Roterman, I.1    Krül, M.2    Nowak, M.3    Konieczny, L.4    Rybarska5    Stopa, B.J.6
  • 25
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by Congo red spectral shift assay
    • W.E. Klunk, R.F. Jacob, and R.P. Mason Quantifying amyloid by Congo red spectral shift assay Methods Enzymol. 309 1999 285 305
    • (1999) Methods Enzymol. , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob2    Mason, R.P.R.F.3
  • 26
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • M. Sunde, and C. Blake The structure of amyloid fibrils by electron microscopy and X-ray diffraction Advan. Protein Chem. 50 1997 123 159
    • (1997) Advan. Protein Chem. , vol.50 , pp. 123-159
    • Sunde1    Blake, C.M.2
  • 27
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis
    • E.T. Jaikaran, C.E. Higham, L.C. Serpell, J. Zurdo, M. Gross, A. Clark, and P.E. Fraser Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis J. Mol. Biol. 308 2001 515 525
    • (2001) J. Mol. Biol. , vol.308 , pp. 515-525
    • Jaikaran, E.T.1    Higham, C.E.2    Serpell, L.C.3    Zurdo, J.4    Gross, M.5    Clark6    Fraser, P.E.A.7
  • 28
    • 0035839035 scopus 로고    scopus 로고
    • Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain
    • J. Zurdo, J.I. Guijarro, J.L. Jiménez, H.R. Saibil, and C.M. Dobson Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain J. Mol. Biol. 311 2001 325 340
    • (2001) J. Mol. Biol. , vol.311 , pp. 325-340
    • Zurdo, J.1    Guijarro, J.I.2    Jiménez, J.L.3    Saibil4    Dobson, C.M.H.R.5
  • 29
    • 0034722985 scopus 로고    scopus 로고
    • Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin
    • C.E. MacPhee, and C.M. Dobson Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin J. Am. Chem. Soc. 122 2000 12707 12713
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12707-12713
    • MacPhee1    Dobson, C.M.C.E.2
  • 31
    • 0018868515 scopus 로고
    • Amyloid deposits and amyloidosis: The beta-fibrilloses (second of two parts)
    • G.G. Glenner Amyloid deposits and amyloidosis: the beta-fibrilloses (second of two parts) N. Engl. J. Med. 302 1980 1333 1343
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1333-1343
    • Glenner, G.G.1
  • 32
    • 0028561835 scopus 로고
    • Development of non-polar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding
    • B.E. Jones, P.A. Jennings, R.A. Pierre, and C. Matthews Development of non-polar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding Biochemistry 33 1994 15250 15258
    • (1994) Biochemistry , vol.33 , pp. 15250-15258
    • Jones, B.E.1    Jennings, P.A.2    Pierre3    Matthews, C.R.A.4
  • 33
    • 0028120343 scopus 로고
    • Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate
    • J. Safar, P.P. Roller, D.C. Gajdusek, and C.J. Gibbs Jr Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate Biochemistry 33 1994 8375 8383
    • (1994) Biochemistry , vol.33 , pp. 8375-8383
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 34
    • 0030729481 scopus 로고    scopus 로고
    • Evolutionary divergente of substrate specificity within the chymotrypsin-like serine fold
    • J.J. Perona, and C.S. Craik Evolutionary divergente of substrate specificity within the chymotrypsin-like serine fold J. Biol. Chem. 272 1997 29987 29990
    • (1997) J. Biol. Chem. , vol.272 , pp. 29987-29990
    • Perona1    Craik, C.S.J.J.2
  • 35
    • 0037166276 scopus 로고    scopus 로고
    • Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s)
    • S. Srisailam, H.M. Wang, T.K. Kumar, D. Rajalingam, V. Sivaraja, and H.S. Sheu Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s) J. Biol. Chem. 277 2002 19027 19036
    • (2002) J. Biol. Chem. , vol.277 , pp. 19027-19036
    • Srisailam, S.1    Wang, H.M.2    Kumar, T.K.3    Rajalingam, D.4    Sivaraja5    Sheu, H.S.V.6
  • 36
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • C.M. Dobson Protein misfolding, evolution and disease Trends Biochem. Sci. 24 1999 329 332
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 38
    • 0033773935 scopus 로고    scopus 로고
    • Conformational disease
    • R.R. Kopito, and D. Ron Conformational disease Nature Cell Biol. 2 2000 207 209
    • (2000) Nature Cell Biol. , vol.2 , pp. 207-209
    • Kopito1    Ron, D.R.R.2
  • 39
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • A.L. Fink Protein aggregation: folding aggregates, inclusion bodies and amyloid Fold. Des. 3 1998 9 23
    • (1998) Fold. Des. , vol.3 , pp. 9-23
    • Fink, A.L.1
  • 40
    • 0033055898 scopus 로고    scopus 로고
    • Trifluoroethanol-induced conformational transitions of proteins: Insights gained from the differences between alpha-lactalbumin and ribonuclease a
    • K. Gast, D. Zirwer, M. Muller-Frohne, and G. Damaschun Trifluoroethanol-induced conformational transitions of proteins: insights gained from the differences between alpha-lactalbumin and ribonuclease A Protein Sci. 8 1999 625 634
    • (1999) Protein Sci. , vol.8 , pp. 625-634
    • Gast, K.1    Zirwer, D.2    Muller-Frohne3    Damaschun, G.M.4
  • 41
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • J.W. Kelly The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways Curr. Opin. Struct. Biol. 8 1998 101 106
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 44
    • 0035964955 scopus 로고    scopus 로고
    • Trans-suppression of misfolding in an amyloid disease
    • P. Hammarstrom, F. Schneider, and J.W. Kelly Trans-suppression of misfolding in an amyloid disease Science 293 2001 2459 2462
    • (2001) Science , vol.293 , pp. 2459-2462
    • Hammarstrom, P.1    Schneider2    Kelly, J.W.F.3
  • 45
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin amyloid disease by changing protein misfolding energetics
    • P. Hammarstrom, R.L. Wiseman, E.T. Powers, and J.W. Kelly Prevention of transthyretin amyloid disease by changing protein misfolding energetics Science 299 2003 713 716
    • (2003) Science , vol.299 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers3    Kelly, J.W.E.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.