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Volumn 268, Issue 2, 1997, Pages 375-389

X-ray diffraction analysis of scrapie prion: Intermediate and folded structures in a peptide containing two putative α-helices

Author keywords

Amyloid; Prion diseases; Synthetic peptide; pleated sheet

Indexed keywords

POLYPEPTIDE; PRION PROTEIN;

EID: 0031547975     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.0949     Document Type: Article
Times cited : (42)

References (41)
  • 1
    • 0014714631 scopus 로고
    • Kinematical theory of diffraction by matter of any kind and the theory of liquids
    • Bagchi S. N. Kinematical theory of diffraction by matter of any kind and the theory of liquids. Advan. Phys. 19:1970;119-173.
    • (1970) Advan. Phys. , vol.19 , pp. 119-173
    • Bagchi, S.N.1
  • 3
    • 84978554455 scopus 로고
    • Lorentz and orientation factors in fiber X-ray diffraction analysis
    • Cella R. J., Lee B., Hughes R. E. Lorentz and orientation factors in fiber X-ray diffraction analysis. Acta Crystallog. sect. A. 26:1970;118-124.
    • (1970) Acta Crystallog. Sect. a , vol.26 , pp. 118-124
    • Cella, R.J.1    Lee, B.2    Hughes, R.E.3
  • 4
    • 0027918455 scopus 로고
    • New folds for all-β proteins
    • Chothia C., Murzin A. G. New folds for all-β proteins. Structure. 1:1993;217-222.
    • (1993) Structure , vol.1 , pp. 217-222
    • Chothia, C.1    Murzin, A.G.2
  • 5
    • 0019997016 scopus 로고
    • Analysis and prediction of the packing of α-helices against β-sheet in the tertiary structure of globular proteins
    • Cohen F. E., Sternberg M. J. E., Taylor W. R. Analysis and prediction of the packing of α-helices against β-sheet in the tertiary structure of globular proteins. J. Mol. Biol. 156:1982;821-861.
    • (1982) J. Mol. Biol. , vol.156 , pp. 821-861
    • Cohen, F.E.1    Sternberg, M.J.E.2    Taylor, W.R.3
  • 6
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases: Importance of seeding
    • Come J. H., Fraser P. E., Lansbury P. T. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc. Natl Acad. Sci. USA. 90:1993;5959-5963.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury, P.T.3
  • 7
    • 0016287131 scopus 로고
    • Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods
    • Cooper J. H. Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods. Lab. Invest. 31:1974;232-238.
    • (1974) Lab. Invest. , vol.31 , pp. 232-238
    • Cooper, J.H.1
  • 8
    • 0027374785 scopus 로고
    • Alzheimer's disease and Creutzfeldt-Jakob disease: Overlap of pathogenic mechanism
    • DeArmond S. J. Alzheimer's disease and Creutzfeldt-Jakob disease: overlap of pathogenic mechanism. Curr. Opin. Neurol. 6:1993;872-881.
    • (1993) Curr. Opin. Neurol. , vol.6 , pp. 872-881
    • Dearmond, S.J.1
  • 10
    • 0030069023 scopus 로고    scopus 로고
    • Insoluble wild-type and protease-resistant mutant prion protein in brains of patients with inherited prion disease
    • Gabizon R., Telling G., Meiner Z., Halimi M., Kahana I., Prusiner S. B. Insoluble wild-type and protease-resistant mutant prion protein in brains of patients with inherited prion disease. Nature Med. 2:1996;59-64.
    • (1996) Nature Med. , vol.2 , pp. 59-64
    • Gabizon, R.1    Telling, G.2    Meiner, Z.3    Halimi, M.4    Kahana, I.5    Prusiner, S.B.6
  • 11
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier J., Osguthorpe D. J., Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:1978;97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 12
    • 0027388993 scopus 로고
    • Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity
    • Gasset M., Baldwin M. A., Fletterick R. J., Prusiner S. B. Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc. Natl Acad. Sci. USA. 90:1993;1-5.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1-5
    • Gasset, M.1    Baldwin, M.A.2    Fletterick, R.J.3    Prusiner, S.B.4
  • 15
    • 0029656091 scopus 로고    scopus 로고
    • Structures of prion proteins and conformational models for prion diseases
    • Huang Z., Prusiner S. B., Cohen F. E. Structures of prion proteins and conformational models for prion diseases. Curr. Top. Microbiol. Immunol. 207:1996a;49-67.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.207 , pp. 49-67
    • Huang, Z.1    Prusiner, S.B.2    Cohen, F.E.3
  • 16
    • 0030342679 scopus 로고    scopus 로고
    • Scrapie prions: A three-dimensional mode of an infectious segment
    • Huang Z., Prusiner S. B., Cohen F. E. Scrapie prions: a three-dimensional mode of an infectious segment. Folding Design. 1:1996b;13-19.
    • (1996) Folding Design , vol.1 , pp. 13-19
    • Huang, Z.1    Prusiner, S.B.2    Cohen, F.E.3
  • 17
    • 0011183689 scopus 로고
    • X-ray diffraction analysis of the β-crystallite assembly of Alzheimer β amyloid protein analogue
    • Inouye H. X-ray diffraction analysis of the β-crystallite assembly of Alzheimer β amyloid protein analogue. J. Crystallog. Soc. Japan. 35:1993;347-351.
    • (1993) J. Crystallog. Soc. Japan , vol.35 , pp. 347-351
    • Inouye, H.1
  • 18
    • 84977296697 scopus 로고
    • X-ray scattering from a discrete helix with cumulative angular and translational disorders
    • Inouye H. X-ray scattering from a discrete helix with cumulative angular and translational disorders. Acta Crystallog. sect. A. 50:1994;644-646.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 644-646
    • Inouye, H.1
  • 19
    • 0026022127 scopus 로고
    • Folding and function of the myelin proteins from primary sequence data
    • Inouye H., Kirschner D. A. Folding and function of the myelin proteins from primary sequence data. J. Neurochem. Res. 28:1991;1-17.
    • (1991) J. Neurochem. Res. , vol.28 , pp. 1-17
    • Inouye, H.1    Kirschner, D.A.2
  • 20
    • 0011215376 scopus 로고    scopus 로고
    • Refined fibril structures: The hydrophobic core in Alzheimer's β-amyloid and prion as revealed by X-ray diffraction
    • Chichester, UK and New York: John Wiley & Sons
    • Inouye H., Kirschner D. A. Refined fibril structures: the hydrophobic core in Alzheimer's β-amyloid and prion as revealed by X-ray diffraction. The Nature and Origin of Amyloid Fibrils; Ciba Foundation Symposium no. 199. 1996;John Wiley & Sons, Chichester, UK and New York.
    • (1996) The Nature and Origin of Amyloid Fibrils; Ciba Foundation Symposium No. 199
    • Inouye, H.1    Kirschner, D.A.2
  • 21
    • 0024706402 scopus 로고
    • Membrane structure in isolated and intact myelins
    • Inouye H., Karthigasan J., Kirschner D. A. Membrane structure in isolated and intact myelins. Biophys. J. 56:1989;129-137.
    • (1989) Biophys. J. , vol.56 , pp. 129-137
    • Inouye, H.1    Karthigasan, J.2    Kirschner, D.A.3
  • 22
    • 0027411230 scopus 로고
    • Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogues: Analysis by X-ray diffraction
    • Inouye H., Fraser P. E., Kirschner D. A. Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogues: Analysis by X-ray diffraction. Biophys. J. 64:1993;502-519.
    • (1993) Biophys. J. , vol.64 , pp. 502-519
    • Inouye, H.1    Fraser, P.E.2    Kirschner, D.A.3
  • 24
    • 0018118306 scopus 로고
    • Structures of membrane proteins
    • Kennedy S. J. Structures of membrane proteins. J. Membr. Biol. 42:1978;265-279.
    • (1978) J. Membr. Biol. , vol.42 , pp. 265-279
    • Kennedy, S.J.1
  • 25
    • 0027236933 scopus 로고
    • An amber mutation of prion protein in Gerstmann-Straussler syndrome with mutant PrP plaques
    • Kitamoto T., Iizuka R., Tateishi J. An amber mutation of prion protein in Gerstmann-Straussler syndrome with mutant PrP plaques. Biochem. Biophys. Res. Commun. 192:1993;525-531.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 525-531
    • Kitamoto, T.1    Iizuka, R.2    Tateishi, J.3
  • 26
    • 84959655043 scopus 로고
    • Computer building of β-helical polypeptide models
    • Koeppe R. E., Kimura M. Computer building of β-helical polypeptide models. Biopolymers. 23:1984;23-38.
    • (1984) Biopolymers , vol.23 , pp. 23-38
    • Koeppe, R.E.1    Kimura, M.2
  • 28
    • 0002705842 scopus 로고
    • A visual protein crystallographic software system for X11/XView
    • McRee D. E. A visual protein crystallographic software system for X11/XView. J. Mol. Graph. 10:1992;44-46.
    • (1992) J. Mol. Graph. , vol.10 , pp. 44-46
    • McRee, D.E.1
  • 29
    • 0028925377 scopus 로고
    • Prion protein peptides induce α-helix to β-sheet conformational transitions
    • Nguyen J., Baldwin M. A., Cohen F. E., Prusiner S. B. Prion protein peptides induce α-helix to β-sheet conformational transitions. Biochemistry. 34:1995a;4186-4192.
    • (1995) Biochemistry , vol.34 , pp. 4186-4192
    • Nguyen, J.1    Baldwin, M.A.2    Cohen, F.E.3    Prusiner, S.B.4
  • 33
    • 0027182522 scopus 로고
    • Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein
    • Safar J., Roller P. P., Gajdusek D. C., Gibbs C. J. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268:1993;20276-20284.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20276-20284
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs, C.J.4
  • 34
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McPC603: An X-ray diffraction study at 2.7 Å
    • Satow Y., Cohen G. H., Padlan E. A., Davis D. R. Phosphocholine binding immunoglobulin Fab McPC603: An X-ray diffraction study at 2.7 Å J. Mol. Biol. 190:1986;593-604.
    • (1986) J. Mol. Biol. , vol.190 , pp. 593-604
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davis, D.R.4
  • 35
    • 0022429703 scopus 로고
    • Formation of an infinite β-sheet arrangement dominates the crystallization behavior of λ-type antibody light chains
    • Schiffer M., Chang C.-H., Stevens F. J. Formation of an infinite β-sheet arrangement dominates the crystallization behavior of λ-type antibody light chains. J. Mol. Biol. 186:1985;475-478.
    • (1985) J. Mol. Biol. , vol.186 , pp. 475-478
    • Schiffer, M.1    Chang, C.-H.2    Stevens, F.J.3
  • 36
    • 0027229676 scopus 로고
    • Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes
    • Scott M., Groth D., Foster D., Torchia M., Yang S.-L., DeArmond S. J., Prusiner S. B. Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell. 73:1993;979-988.
    • (1993) Cell , vol.73 , pp. 979-988
    • Scott, M.1    Groth, D.2    Foster, D.3    Torchia, M.4    Yang, S.-L.5    Dearmond, S.J.6    Prusiner, S.B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.