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Volumn 53, Issue 14, 2014, Pages 2366-2370

Fiber diffraction of the prion-forming domain HET-s(218-289) shows dehydration-induced deformation of a complex amyloid structure

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL SYSTEMS; DEHYDRATION; GLYCOPROTEINS; MOLECULAR STRUCTURE; PROTEINS;

EID: 84898898317     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5002807     Document Type: Article
Times cited : (8)

References (29)
  • 1
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes, E. D. and Glenner, G. G. (1968) X-ray diffraction studies on amyloid filaments J. Histochem. Cytochem. 16, 673-677
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 2
    • 0001419932 scopus 로고
    • The X-ray interpretation of denaturation and the structure of the seed globulins
    • Astbury, W. T., Dickinson, S., and Bailey, K. (1935) The X-ray interpretation of denaturation and the structure of the seed globulins Biochem. J. 29, 2351-2360
    • (1935) Biochem. J. , vol.29 , pp. 2351-2360
    • Astbury, W.T.1    Dickinson, S.2    Bailey, K.3
  • 3
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75, 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 7
    • 35748946237 scopus 로고    scopus 로고
    • Prions
    • in (Knipe, D. and Howley, P. M. Eds) 5 th ed. pp, Lippincott Williams & Wilkins, Philadelphia, PA.
    • Prusiner, S. B. (2007) Prions, in Fields Virology (Knipe, D. and Howley, P. M., Eds) 5 th ed., pp 3059-3091, Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields Virology , pp. 3059-3091
    • Prusiner, S.B.1
  • 8
    • 80053569870 scopus 로고    scopus 로고
    • The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility
    • Saupe, S. J. (2011) The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility Semin. Cell Dev. Biol. 22, 460-468
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 460-468
    • Saupe, S.J.1
  • 9
    • 33748481341 scopus 로고    scopus 로고
    • X-ray scattering study of the effect of hydration on the cross-β structure of amyloid fibrils
    • Squires, A. M., Devlin, G. L., Gras, S. L., Tickler, A. K., MacPhee, C. E., and Dobson, C. M. (2006) X-ray scattering study of the effect of hydration on the cross-β structure of amyloid fibrils J. Am. Chem. Soc. 128, 11738-11739
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11738-11739
    • Squires, A.M.1    Devlin, G.L.2    Gras, S.L.3    Tickler, A.K.4    MacPhee, C.E.5    Dobson, C.M.6
  • 10
    • 70349682422 scopus 로고    scopus 로고
    • Dehydration stability of amyloid fibrils studied by AFM
    • Maurstad, G., Prass, M., Serpell, L. C., and Sikorski, P. (2009) Dehydration stability of amyloid fibrils studied by AFM Eur. Biophys. J. 38, 1135-1140
    • (2009) Eur. Biophys. J. , vol.38 , pp. 1135-1140
    • Maurstad, G.1    Prass, M.2    Serpell, L.C.3    Sikorski, P.4
  • 12
    • 0347284249 scopus 로고    scopus 로고
    • Structural characterisation of islet amyloid polypeptide fibrils
    • Makin, O. S. and Serpell, L. C. (2004) Structural characterisation of islet amyloid polypeptide fibrils J. Mol. Biol. 335, 1279-1288
    • (2004) J. Mol. Biol. , vol.335 , pp. 1279-1288
    • Makin, O.S.1    Serpell, L.C.2
  • 13
    • 67049087912 scopus 로고    scopus 로고
    • Two prion variants of Sup35p have in-register parallel β-sheet structures, independent of hydration
    • Shewmaker, F., Kryndushkin, D., Chen, B., Tycko, R., and Wickner, R. B. (2009) Two prion variants of Sup35p have in-register parallel β-sheet structures, independent of hydration Biochemistry 48, 5074-5082
    • (2009) Biochemistry , vol.48 , pp. 5074-5082
    • Shewmaker, F.1    Kryndushkin, D.2    Chen, B.3    Tycko, R.4    Wickner, R.B.5
  • 16
    • 84867039782 scopus 로고    scopus 로고
    • Fiber diffraction data indicate a hollow core for the Alzheimer's Aβ 3-fold symmetric fibril
    • McDonald, M., Box, H., Bian, W., Kendall, A., Tycko, R., and Stubbs, G. (2012) Fiber diffraction data indicate a hollow core for the Alzheimer's Aβ 3-fold symmetric fibril J. Mol. Biol. 423, 454-461
    • (2012) J. Mol. Biol. , vol.423 , pp. 454-461
    • McDonald, M.1    Box, H.2    Bian, W.3    Kendall, A.4    Tycko, R.5    Stubbs, G.6
  • 17
    • 84884217594 scopus 로고    scopus 로고
    • Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue
    • Lu, J.-X., Qiang, W., Yau, W.-M., Schwieters, C. D., Meredith, S. C., and Tycko, R. (2013) Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue Cell 154, 1257-1268
    • (2013) Cell , vol.154 , pp. 1257-1268
    • Lu, J.-X.1    Qiang, W.2    Yau, W.-M.3    Schwieters, C.D.4    Meredith, S.C.5    Tycko, R.6
  • 18
    • 77957324146 scopus 로고    scopus 로고
    • Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy
    • Van Melckebeke, H., Wasmer, C., Lange, A., AB, E., Loquet, A., Böckmann, A., and Meier, B. H. (2010) Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy J. Am. Chem. Soc. 132, 13765-13775
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13765-13775
    • Van Melckebeke, H.1    Wasmer, C.2    Lange, A.3    Ab, E.4    Loquet, A.5    Böckmann, A.6    Meier, B.H.7
  • 20
    • 36048969163 scopus 로고    scopus 로고
    • Characterization of β-sheet structure in Ure2p1-89 yeast prion fibrils by solid-state nuclear magnetic resonance
    • Baxa, U., Wickner, R. B., Steven, A. C., Anderson, D. E., Marekov, L. N., Yau, W.-M., and Tycko, R. (2007) Characterization of β-sheet structure in Ure2p1-89 yeast prion fibrils by solid-state nuclear magnetic resonance Biochemistry 46, 13149-13162
    • (2007) Biochemistry , vol.46 , pp. 13149-13162
    • Baxa, U.1    Wickner, R.B.2    Steven, A.C.3    Anderson, D.E.4    Marekov, L.N.5    Yau, W.-M.6    Tycko, R.7
  • 21
    • 84861135685 scopus 로고    scopus 로고
    • Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid fold
    • Wan, W., Wille, H., Stöhr, J., Baxa, U., Prusiner, S. B., and Stubbs, G. (2012) Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid fold Biophys. J. 102, 2339-2344
    • (2012) Biophys. J. , vol.102 , pp. 2339-2344
    • Wan, W.1    Wille, H.2    Stöhr, J.3    Baxa, U.4    Prusiner, S.B.5    Stubbs, G.6
  • 22
    • 85025333148 scopus 로고
    • Methods of preparing orientated tobacco mosaic virus sols for X-ray diffraction
    • Gregory, J. and Holmes, K. C. (1965) Methods of preparing orientated tobacco mosaic virus sols for X-ray diffraction J. Mol. Biol. 13, 796-801
    • (1965) J. Mol. Biol. , vol.13 , pp. 796-801
    • Gregory, J.1    Holmes, K.C.2
  • 23
    • 38349164999 scopus 로고    scopus 로고
    • Enclosed chambers for humidity control and sample containment in fiber diffraction
    • McDonald, M., Kendall, A., Tanaka, M., Weissman, J. S., and Stubbs, G. (2008) Enclosed chambers for humidity control and sample containment in fiber diffraction J. Appl. Crystallogr. 41, 206-209
    • (2008) J. Appl. Crystallogr. , vol.41 , pp. 206-209
    • McDonald, M.1    Kendall, A.2    Tanaka, M.3    Weissman, J.S.4    Stubbs, G.5
  • 25
    • 33748762238 scopus 로고    scopus 로고
    • WCEN: A computer program for initial processing of fiber diffraction patterns
    • Bian, W., Wang, H., McCullough, I., and Stubbs, G. (2006) WCEN: a computer program for initial processing of fiber diffraction patterns J. Appl. Crystallogr. 39, 752-756
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 752-756
    • Bian, W.1    Wang, H.2    McCullough, I.3    Stubbs, G.4
  • 26
    • 84885650263 scopus 로고    scopus 로고
    • Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289)
    • Wan, W., Bian, W., McDonald, M., Kijac, A., Wemmer, D. E., and Stubbs, G. (2013) Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218-289) J. Biol. Chem. 288, 29604-29612
    • (2013) J. Biol. Chem. , vol.288 , pp. 29604-29612
    • Wan, W.1    Bian, W.2    McDonald, M.3    Kijac, A.4    Wemmer, D.E.5    Stubbs, G.6
  • 28
    • 0000568172 scopus 로고
    • Pf1 filamentous bacteriophage: Refinement of a molecular model by simulated annealing using 3.3 Å resolution X-ray fibre diffraction data
    • Gonzalez, A., Nave, C., and Marvin, D. A. (1995) Pf1 filamentous bacteriophage: refinement of a molecular model by simulated annealing using 3.3 Å resolution X-ray fibre diffraction data Acta Crystallogr., Sect. D 51, 792-804
    • (1995) Acta Crystallogr., Sect. D , vol.51 , pp. 792-804
    • Gonzalez, A.1    Nave, C.2    Marvin, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.