메뉴 건너뛰기




Volumn 95, Issue 6, 2008, Pages 2909-2915

Nanomechanical properties of human prion protein amyloid as probed by force spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; PEPTIDE; PEPTIDE FRAGMENT; PEPTIDE HYDROLASE; PRION PROTEIN (90 231); PRION PROTEIN (90-231);

EID: 55549146133     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.133108     Document Type: Article
Times cited : (19)

References (48)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B. 1982. Novel proteinaceous infectious particles cause scrapie. Science. 1982:136-144.
    • (1982) Science , vol.1982 , pp. 136-144
    • Prusiner, S.B.1
  • 3
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey, B., and G. S. Baron. 2006. Prions and their partners in crime. Nature. 443:803-810.
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 4
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge, J. 2001. Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24:519-550.
    • (2001) Annu. Rev. Neurosci , vol.24 , pp. 519-550
    • Collinge, J.1
  • 5
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology: One century of evolving concepts
    • Agguzi, A., and M. Polymenidou. 2004. Mammalian prion biology: one century of evolving concepts. Cell. 116:313-327.
    • (2004) Cell , vol.116 , pp. 313-327
    • Agguzi, A.1    Polymenidou, M.2
  • 6
    • 9444267651 scopus 로고    scopus 로고
    • The state of the prion
    • Weissmann, C. 2004. The state of the prion. Nat. Rev. Microbiol. 2:861-871.
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 861-871
    • Weissmann, C.1
  • 7
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. 2003. Protein folding and misfolding. Nature. 426:884-889.
    • (2003) Nature , vol.426 , pp. 884-889
    • Dobson, C.M.1
  • 8
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B., and P. T. Lansbury. 2003. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26:267-298.
    • (2003) Annu. Rev. Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 10
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla, J., P. Saá, C. Hetz, and C. Soto. 2005. In vitro generation of infectious scrapie prions. Cell. 121:195-206.
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saá, P.2    Hetz, C.3    Soto, C.4
  • 15
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey, B. W., A. Dong, K. S. Bhat, D. Ernst, S. F. Hayes, and W. S. Caughey. 1991. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry. 30:7672-7680.
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 17
    • 33846811599 scopus 로고    scopus 로고
    • β-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange
    • Lu, X., P. L. Wintrode, and W. K. Surewicz. 2007. β-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc. Natl. Acad. Sci. USA. 104:1510-1515.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1510-1515
    • Lu, X.1    Wintrode, P.L.2    Surewicz, W.K.3
  • 18
    • 37649000487 scopus 로고    scopus 로고
    • Molecular architecture of human prion protein amyloid: A parallel, in-register beta-structure
    • Cobb, N. J., F. D. Sönnichsen, H. McHaourab, and W. K. Surewicz. 2007. Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure. Proc. Natl. Acad. Sci. USA. 104:18946-18951.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18946-18951
    • Cobb, N.J.1    Sönnichsen, F.D.2    McHaourab, H.3    Surewicz, W.K.4
  • 19
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer, P., and Y. Dufrêne. 2006. Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods. 3:347-355.
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrêne, Y.2
  • 20
    • 28544443624 scopus 로고    scopus 로고
    • Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231
    • Apetri, A. C., D. L. Vanik, and W. K. Surewicz. 2005. Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231. Biochemistry. 44:15880-15888.
    • (2005) Biochemistry , vol.44 , pp. 15880-15888
    • Apetri, A.C.1    Vanik, D.L.2    Surewicz, W.K.3
  • 21
    • 0028071373 scopus 로고
    • Entropic elasticity of lambda-phage DNA
    • Bustamante, C., J. F. Marko, E. D. Siggia, and S. Smith. 1994. Entropic elasticity of lambda-phage DNA. Science. 265:1599-1600.
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Siggia, E.D.3    Smith, S.4
  • 23
    • 31944436148 scopus 로고    scopus 로고
    • Protein structure by mechanical triangulation
    • Dietz, H., and M. Rief. 2006. Protein structure by mechanical triangulation. Proc. Natl. Acad. Sci. USA. 103:1244-1247.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1244-1247
    • Dietz, H.1    Rief, M.2
  • 24
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 27
    • 0030031382 scopus 로고    scopus 로고
    • Van der Waals interactions involving proteins.
    • Roth, C. M., B. L. Neal, and A. M. Lenhoff. 1996. Van der Waals interactions involving proteins. Biophys. J. 70:977-987.
    • (1996) Biophys. J , vol.70 , pp. 977-987
    • Roth, C.M.1    Neal, B.L.2    Lenhoff, A.M.3
  • 28
    • 3042748444 scopus 로고    scopus 로고
    • Nanomedicine
    • Landes Bioscience, Austin, TX
    • Freitas, R. A. 1999. Nanomedicine, Vol. 1. Basic Capabilities. Landes Bioscience, Austin, TX.
    • (1999) Basic Capabilities , vol.1
    • Freitas, R.A.1
  • 30
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel, R., P. Nassoy, A. Leung, K. Ritchie, and E. Evans. 1999. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature. 397:50-53.
    • (1999) Nature , vol.397 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 34
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E., and K. Ritchie. 1997. Dynamic strength of molecular adhesion bonds. Biophys. J. 72:1541-1555.
    • (1997) Biophys. J , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 35
    • 0031767965 scopus 로고    scopus 로고
    • The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy
    • Rief, M., M. Gautel, A. Schemmel, and H. E. Gaub. 1998. The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy. Biophys. J. 75:3008-3014.
    • (1998) Biophys. J , vol.75 , pp. 3008-3014
    • Rief, M.1    Gautel, M.2    Schemmel, A.3    Gaub, H.E.4
  • 36
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser, A. F., P. E. Marszalek, H. P. Erickson, and J. M. Fernandez. 1998. The molecular elasticity of the extracellular matrix protein tenascin. Nature. 393:181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 37
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief, M., J. Pascual, M. Saraste, and H. E. Gaub. 1999. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286:553-561.
    • (1999) J. Mol. Biol , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 40
    • 0033064934 scopus 로고    scopus 로고
    • Unraveling proteins: A molecular mechanics study
    • Rohs, R., C. Etchebest, and R. Lavery. 1999. Unraveling proteins: a molecular mechanics study. Biophys. J. 76:2760-2768.
    • (1999) Biophys. J , vol.76 , pp. 2760-2768
    • Rohs, R.1    Etchebest, C.2    Lavery, R.3
  • 42
    • 33748046806 scopus 로고    scopus 로고
    • Anisotropic deformation response of single protein molecules
    • Dietz, H., F. Berkemeier, M. Bertz, and M. Rief. 2006. Anisotropic deformation response of single protein molecules. Proc. Natl. Acad. Sci. USA. 103:12724-12728.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12724-12728
    • Dietz, H.1    Berkemeier, F.2    Bertz, M.3    Rief, M.4
  • 43
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed β-helices into trimers
    • Govaerts, C., H. Wille, S. B. Prusiner, and F. E. Cohen. 2004. Evidence for assembly of prions with left-handed β-helices into trimers. Proc. Natl. Acad. Sci. USA. 101:8342-8347.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 44
    • 1442330474 scopus 로고    scopus 로고
    • From conversion to aggregation: Protofibril formation of the prion protein
    • DeMarco, M. L., and V. Daggett. 2004. From conversion to aggregation: protofibril formation of the prion protein. Proc. Natl. Acad. Sci. USA. 101:2293-2298.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2293-2298
    • DeMarco, M.L.1    Daggett, V.2
  • 48
    • 17044381327 scopus 로고    scopus 로고
    • Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids
    • Jones, E. M., and W. K. Surewicz. 2005. Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell. 121:63-72.
    • (2005) Cell , vol.121 , pp. 63-72
    • Jones, E.M.1    Surewicz, W.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.