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Volumn 8, Issue 6, 1999, Pages 1350-1357

Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB

Author keywords

Acetonitrile; Aggregation; Amyloid; Circular dichroism; Electron microscopy; Misfolding; NMR spectroscopy; sheet

Indexed keywords

AMYLOID; BACTERIAL PROTEIN; COLD SHOCK PROTEIN;

EID: 0005431368     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.6.1350     Document Type: Article
Times cited : (66)

References (44)
  • 1
    • 0027480757 scopus 로고
    • The structure and mechanism of formation of human calcitonin fibrils
    • Arvinte T, Cudd A, Drake AF. 1993. The structure and mechanism of formation of human calcitonin fibrils. J Biol Chem 265:6415-6422.
    • (1993) J Biol Chem , vol.265 , pp. 6415-6422
    • Arvinte, T.1    Cudd, A.2    Drake, A.F.3
  • 2
    • 0030711713 scopus 로고    scopus 로고
    • Alzheimer's disease: The ins and outs of amyloid-β
    • Beyreuther K, Masters CL. 1997. Alzheimer's disease: The ins and outs of amyloid-β. Nature 389:677-678.
    • (1997) Nature , vol.389 , pp. 677-678
    • Beyreuther, K.1    Masters, C.L.2
  • 3
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • Blake C, Serpell L. 1996. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure 4:989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 5
    • 0031471204 scopus 로고    scopus 로고
    • The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold
    • Bycroft M, Hubbard TJP, Proctor M, Freund SMV, Murzin AG. 1997. The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold. Cell 88:235-242.
    • (1997) Cell , vol.88 , pp. 235-242
    • Bycroft, M.1    Hubbard, T.J.P.2    Proctor, M.3    Freund, S.M.V.4    Murzin, A.G.5
  • 6
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen Y-H, Yang JT, Chau KH. 1974. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 13:3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 8
    • 0016287131 scopus 로고
    • Selective amyloid staining as a function of amyloid composition and structure
    • Cooper JH. 1974. Selective amyloid staining as a function of amyloid composition and structure. Lab Invest 31:232-238.
    • (1974) Lab Invest , vol.31 , pp. 232-238
    • Cooper, J.H.1
  • 9
    • 0001040367 scopus 로고
    • An algorithm for protein secondary structure prediction based on class prediction
    • Deleage G, Roux B. 1987. An algorithm for protein secondary structure prediction based on class prediction. Protein Eng 1:289-294.
    • (1987) Protein Eng , vol.1 , pp. 289-294
    • Deleage, G.1    Roux, B.2
  • 10
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink AL. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Folding Design 3:R9-R23.
    • (1998) Folding Design , vol.3
    • Fink, A.L.1
  • 11
    • 0029595442 scopus 로고
    • Significant improvements in protein secondary structure prediction by prediction from multiple alignments
    • Geourjon C, Deleage G. 1995. Significant improvements in protein secondary structure prediction by prediction from multiple alignments. Comput Appl Biosci 11:681-684.
    • (1995) Comput Appl Biosci , vol.11 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 12
    • 0023555768 scopus 로고
    • Further developments of protein secondary structure prediction using information-theory - New parameters and consideration of residue pairs
    • Gibrat JF, Garnier J, Robson B. 1987. Further developments of protein secondary structure prediction using information-theory - New parameters and consideration of residue pairs. J Mol Biol 198:425-443.
    • (1987) J Mol Biol , vol.198 , pp. 425-443
    • Gibrat, J.F.1    Garnier, J.2    Robson, B.3
  • 13
    • 0030988929 scopus 로고    scopus 로고
    • Effects of heterologous expression of CspB, the major cold shock protein of Bacillus subtilis, on protein synthesis in Escherichia coll
    • Graumann P, Marahiel MA. 1997. Effects of heterologous expression of CspB, the major cold shock protein of Bacillus subtilis, on protein synthesis in Escherichia coll. Mol Gen Genet 253:745-752.
    • (1997) Mol Gen Genet , vol.253 , pp. 745-752
    • Graumann, P.1    Marahiel, M.A.2
  • 14
    • 0031658803 scopus 로고    scopus 로고
    • A superfamily of proteins that contain the cold-shock domain
    • Graumann PL, Marahiel MA. 1998. A superfamily of proteins that contain the cold-shock domain. Trends Biochem Sci 23:286-290.
    • (1998) Trends Biochem Sci , vol.23 , pp. 286-290
    • Graumann, P.L.1    Marahiel, M.A.2
  • 15
    • 0030605814 scopus 로고    scopus 로고
    • Linguistic analysis of protein folding
    • Groß M. 1996. Linguistic analysis of protein folding. FEBS Lett 390:249-252.
    • (1996) FEBS Lett , vol.390 , pp. 249-252
    • Groß, M.1
  • 16
    • 85069274870 scopus 로고    scopus 로고
    • Folding of nascent protein chains
    • Groß M, Dobson CM. 1997. Folding of nascent protein chains. Chimia 51:443.
    • (1997) Chimia , vol.51 , pp. 443
    • Groß, M.1    Dobson, C.M.2
  • 18
    • 0029257497 scopus 로고
    • The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by β-amyloid: Is NAC a common trigger of target in neurodegenerative disease?
    • Han H, Weinreb PH, Lansbury PT. 1995. The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by β-amyloid: Is NAC a common trigger of target in neurodegenerative disease? Chem Biol 2:163-169.
    • (1995) Chem Biol , vol.2 , pp. 163-169
    • Han, H.1    Weinreb, P.H.2    Lansbury, P.T.3
  • 21
    • 0000857723 scopus 로고    scopus 로고
    • Characterization of protein unfolding by NMR diffusion measurements
    • Jones JA, Wilkins DK, Smith LJ, Dobson CM. 1997. Characterization of protein unfolding by NMR diffusion measurements. J Biomol NMR 10:199-203.
    • (1997) J Biomol NMR , vol.10 , pp. 199-203
    • Jones, J.A.1    Wilkins, D.K.2    Smith, L.J.3    Dobson, C.M.4
  • 22
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases
    • Kelly JW. 1997. Amyloid fibril formation and protein misassembly: A structural quest for insights into amyloid and prion diseases. Structure 5:595-600.
    • (1997) Structure , vol.5 , pp. 595-600
    • Kelly, J.W.1
  • 23
    • 0032496368 scopus 로고    scopus 로고
    • Amyloidogenic determinant as a substrate recognition motif of insulin-degrading enzyme
    • Kurochkin IV. 1998. Amyloidogenic determinant as a substrate recognition motif of insulin-degrading enzyme. FEBS Lett 427:153-156.
    • (1998) FEBS Lett , vol.427 , pp. 153-156
    • Kurochkin, I.V.1
  • 24
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from β-helical protofibrils
    • Lazo ND, Downing DT. 1998. Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry 37:1731-1735.
    • (1998) Biochemistry , vol.37 , pp. 1731-1735
    • Lazo, N.D.1    Downing, D.T.2
  • 25
    • 0023050277 scopus 로고
    • An algorithm for secondary structure determination in proteins based on sequence similarity
    • Levin JM, Robson B, Garnier J. 1986. An algorithm for secondary structure determination in proteins based on sequence similarity. FEBS Lett 205:303-308.
    • (1986) FEBS Lett , vol.205 , pp. 303-308
    • Levin, J.M.1    Robson, B.2    Garnier, J.3
  • 26
    • 0032503933 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module
    • Litvinovich SV, Brew SA, Aota S, Akiyama SK, Haudenschild C, Ingham KC. 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
    • 0021114895 scopus 로고
    • Application of phase-sensitive two-dimensional correlated spectroscopy (COSY) for measurements of H1-H1 spin-spin coupling constants in proteins
    • Marion D, Wüthrich K. 1983. Application of phase-sensitive two-dimensional correlated spectroscopy (COSY) for measurements of H1-H1 spin-spin coupling constants in proteins. Biochem Biophys Res Comm 113:967-974.
    • (1983) Biochem Biophys Res Comm , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 31
    • 0001078545 scopus 로고    scopus 로고
    • The effects of guanidine hydrochloride on the random coil conformations and NMR chemical shifts of the peptide series GGXGG
    • Plaxco KW, Morton CJ, Grimshaw SB, Jones JA, Pitkeathly MC, Campbell ID, Dobson CM. 1997. The effects of guanidine hydrochloride on the random coil conformations and NMR chemical shifts of the peptide series GGXGG. J Biomol NMR 10:221-230.
    • (1997) J Biomol NMR , vol.10 , pp. 221-230
    • Plaxco, K.W.1    Morton, C.J.2    Grimshaw, S.B.3    Jones, J.A.4    Pitkeathly, M.C.5    Campbell, I.D.6    Dobson, C.M.7
  • 32
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco KW, Simons KT, Baker D. 1998. Contact order, transition state placement and the refolding rates of single domain proteins. J Mol Biol 277:985-994.
    • (1998) J Mol Biol , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 33
    • 0027296211 scopus 로고
    • Universal nucleic acid binding domain revealed by crystal structure of the Bacillus subtilis major cold-shock protein
    • Schindelin H, Marahiel MA, Heinemann U. 1993. Universal nucleic acid binding domain revealed by crystal structure of the Bacillus subtilis major cold-shock protein. Nature 364:164-168.
    • (1993) Nature , vol.364 , pp. 164-168
    • Schindelin, H.1    Marahiel, M.A.2    Heinemann, U.3
  • 35
    • 0030450051 scopus 로고    scopus 로고
    • Thermodynamic properties of an extremely rapid protein folding reaction
    • Schindler T, Schmid FX. 1996. Thermodynamic properties of an extremely rapid protein folding reaction. Biochemistry 35:16833-16842.
    • (1996) Biochemistry , vol.35 , pp. 16833-16842
    • Schindler, T.1    Schmid, F.X.2
  • 39
    • 0028790273 scopus 로고
    • Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation
    • Serrano L. 1995. Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation. J Mol Biol 254:322-333.
    • (1995) J Mol Biol , vol.254 , pp. 322-333
    • Serrano, L.1
  • 40
    • 0030320442 scopus 로고    scopus 로고
    • The concept of a random coil: Residual structure in peptides and denatured proteins
    • Smith LJ, Fiebig KM, Schwalbe H, Dobson CM. 1996. The concept of a random coil: Residual structure in peptides and denatured proteins. Folding Design 1:R95-R106.
    • (1996) Folding Design , 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, Blake C. 1997. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv Prot Chem 50:123-159.
    • (1997) Adv Prot Chem , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 42
    • 0023192941 scopus 로고
    • Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells
    • Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, Johnson KH. 1987. Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc Natl Acad Sci USA 84:3881-3885.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3881-3885
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Hayden, D.W.4    O'Brien, T.D.5    Johnson, K.H.6
  • 43
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J Biomol NMR 5:67-81.
    • (1995) J Biomol NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 44
    • 0028343072 scopus 로고
    • Far-UV circular dichroism reveals a conformational switch in a peptide fragment from the β sheet of hen lysozyme
    • Yang JJ, Pitkeathly M, Radford SE. 1994. Far-UV circular dichroism reveals a conformational switch in a peptide fragment from the β sheet of hen lysozyme. Biochemistry 33:7345-7353.
    • (1994) Biochemistry , vol.33 , pp. 7345-7353
    • Yang, J.J.1    Pitkeathly, M.2    Radford, S.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.