메뉴 건너뛰기




Volumn 108, Issue 42, 2011, Pages 17308-17313

Cellular prion protein conformation and function

Author keywords

Prion disease; Protein dynamics; Protein structure; Transmissible spongiform encephalopathy

Indexed keywords

CELLULAR PRION PROTEIN; PRION PROTEIN; UNCLASSIFIED DRUG;

EID: 80054826268     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1106325108     Document Type: Article
Times cited : (55)

References (40)
  • 5
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • DOI 10.1016/S0014-5793(97)00920-4, PII S0014579397009204
    • Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett 413:282-288. (Pubitemid 27353285)
    • (1997) FEBS Letters , vol.413 , Issue.2 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wuthrich, K.5
  • 6
    • 12144271772 scopus 로고    scopus 로고
    • NMR structure of the bovine prion protein isolated from healthy calf brains
    • DOI 10.1038/sj.embor.7400297
    • Hornemann S, Schorn C, Wüthrich K (2004) NMR structure of the bovine prion protein isolated from healthy calf brains. EMBO Rep 5:1159-1164. (Pubitemid 40103610)
    • (2004) EMBO Reports , vol.5 , Issue.12 , pp. 1159-1164
    • Hornemann, S.1    Schorn, C.2    Wuthrich, K.3
  • 8
    • 0030967895 scopus 로고    scopus 로고
    • Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform
    • James TL, et al. (1997) Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc Natl Acad Sci USA 94:10086-10091.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10086-10091
    • James, T.L.1
  • 13
    • 52949137870 scopus 로고    scopus 로고
    • NMR structure of the bank vole prion protein at 20 °C contains a structured loop of residues 165-171
    • Christen B, Pérez DR, Hornemann S, Wüthrich K (2008) NMR structure of the bank vole prion protein at 20 °C contains a structured loop of residues 165-171. J Mol Biol 383:306-312.
    • (2008) J Mol Biol , vol.383 , pp. 306-312
    • Christen, B.1    Pérez, D.R.2    Hornemann, S.3    Wüthrich, K.4
  • 14
    • 67349152665 scopus 로고    scopus 로고
    • Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the β2-α2 loop is modulated by long-range sequence effects
    • Christen B, Hornemann S, Damberger FF, Wüthrich K (2009) Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the β2-α2 loop is modulated by long-range sequence effects. J Mol Biol 389:833-845.
    • (2009) J Mol Biol , vol.389 , pp. 833-845
    • Christen, B.1    Hornemann, S.2    Damberger, F.F.3    Wüthrich, K.4
  • 15
    • 77953808355 scopus 로고    scopus 로고
    • Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein
    • Pérez DR, Damberger FF, Wüthrich K (2010) Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein. J Mol Biol 400:121-128.
    • (2010) J Mol Biol , vol.400 , pp. 121-128
    • Pérez, D.R.1    Damberger, F.F.2    Wüthrich, K.3
  • 16
    • 77957793037 scopus 로고    scopus 로고
    • Unique structural characteristics of the rabbit prion protein
    • Wen Y, et al. (2010) Unique structural characteristics of the rabbit prion protein. J Biol Chem 285:31682-31693.
    • (2010) J Biol Chem , vol.285 , pp. 31682-31693
    • Wen, Y.1
  • 20
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax A, Grzesiek S (1993) Methodological advances in protein NMR. Acc Chem Res 26:131-138.
    • (1993) Acc Chem Res , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 21
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • DOI 10.1023/A:1021614115432
    • Herrmann T, Güntert P, Wüthrich K (2002) Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 24:171-189. (Pubitemid 36113646)
    • (2002) Journal of Biomolecular NMR , vol.24 , Issue.3 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 22
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • DOI 10.1016/S0022-2836(02)00241-3
    • Herrmann T, Güntert P, Wüthrich K (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319:209-227. (Pubitemid 34729497)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 23
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P, Mumenthaler C, Wüthrich K (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 273:283-298.
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 24
    • 0030236215 scopus 로고    scopus 로고
    • The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules
    • Luginbühl P, Güntert P, Billeter M, Wüthrich K (1996) The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules. J Biomol NMR 8:136-146.
    • (1996) J Biomol NMR , vol.8 , pp. 136-146
    • Luginbühl, P.1    Güntert, P.2    Billeter, M.3    Wüthrich, K.4
  • 25
    • 0034140558 scopus 로고    scopus 로고
    • Point-centered domain decomposition for parallel molecular dynamics simulation
    • DOI 10.1016/S0010-4655(99)00436-1
    • Koradi R, Billeter M, Güntert P (2000) Point-centered domain decomposition for parallel molecular dynamics simulation. Comput Phys Commun 124:139-147. (Pubitemid 30562273)
    • (2000) Computer Physics Communications , vol.124 , Issue.2-3 , pp. 139-147
    • Koradi, R.1    Billeter, M.2    Guntert, P.3
  • 26
    • 0024311951 scopus 로고
    • Comparison of the high-resolution structures of the alpha-amylase inhibitor Tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals
    • DOI 10.1016/0022-2836(89)90575-5
    • Billeter M, Kline AD, Braun W, Huber R, Wüthrich K (1989) Comparison of the high-resolution structures of the alpha-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals. J Mol Biol 206:677-687. (Pubitemid 19137422)
    • (1989) Journal of Molecular Biology , vol.206 , Issue.4 , pp. 677-687
    • Billeter, M.1    Kline, A.D.2    Braun, W.3    Huber, R.4    Wuthrich, K.5
  • 27
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson J (1981) The anatomy and taxonomy of protein structure. Adv Protein Chem 34:167-339.
    • (1981) Adv Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.1
  • 28
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson EG, Thornton JM (1994) A revised set of potentials for beta-turn formation in proteins. Protein Sci 3:2207-2216.
    • (1994) Protein Sci , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 29
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi R, Billeter M, Wüthrich K (1996) MOLMOL: A program for display and analysis of macromolecular structures. J Mol Graph 14:51-55. (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 33
    • 0030931519 scopus 로고    scopus 로고
    • Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
    • Kaneko K, et al. (1997) Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc Natl Acad Sci USA 94:10069-10074.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10069-10074
    • Kaneko, K.1
  • 34
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling GC, et al. (1995) Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83:79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1
  • 35
    • 0030810150 scopus 로고    scopus 로고
    • Human prion proteins expressed in Escherichia cell and purified by high-affinity column refolding
    • DOI 10.1016/S0014-5793(97)01330-6, PII S0014579397013306
    • Zahn R, von Schroetter C, Wüthrich K (1997) Human prion proteins expressed in Escherichia coliand purified by high-affinity column refolding. FEBS Lett 417:400-404. (Pubitemid 27511631)
    • (1997) FEBS Letters , vol.417 , Issue.3 , pp. 400-404
    • Zahn, R.1    Von Schroetter, C.2    Wuthrich, K.3
  • 36
    • 4043053590 scopus 로고    scopus 로고
    • Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy
    • DOI 10.1021/bi0494828
    • Lysek DA, Wüthrich K (2004) Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy. Biochemistry 43:10393-10399. (Pubitemid 39079313)
    • (2004) Biochemistry , vol.43 , Issue.32 , pp. 10393-10399
    • Lysek, D.A.1    Wuthrich, K.2
  • 38
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules
    • Cornell WD, et al. (1995) A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J Am Chem Soc 117:5179-5197.
    • (1995) J Am Chem Soc , vol.117 , pp. 5179-5197
    • Cornell, W.D.1
  • 39
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.