메뉴 건너뛰기




Volumn 9, Issue 5, 2015, Pages 333-338

Truncated forms of the prion protein PrP demonstrate the need for complexity in prion structure

Author keywords

amyloid; fiber diffraction; peptide models; prion structure; protein aggregation; self propagation

Indexed keywords

AMYLOID; PRION PROTEIN; PRION;

EID: 84961254491     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.1080/19336896.2015.1084464     Document Type: Note
Times cited : (2)

References (32)
  • 1
    • 0001419932 scopus 로고
    • The X-ray interpretation of denaturation and the structure of the seed globulins
    • 16745914
    • W.T.Astbury, S.Dickinson, K.Bailey. The X-ray interpretation of denaturation and the structure of the seed globulins. Biochem J 1935; 29:2351-60; PMID:16745914; http://dx.doi.org/10.1042/bj0292351
    • (1935) Biochem J , vol.29 , pp. 2351-2360
    • Astbury, W.T.1    Dickinson, S.2    Bailey, K.3
  • 6
    • 77957324146 scopus 로고    scopus 로고
    • Atomic-resolution three-dimensional structure of HET-s(218−289) amyloid fibrils by solid-state NMR spectroscopy
    • 20828131
    • H.Van Melckebeke, C.Wasmer, A.Lange, E.Ab, A.Loquet, A.Böckmann, B.H.Meier. Atomic-resolution three-dimensional structure of HET-s(218−289) amyloid fibrils by solid-state NMR spectroscopy. J Am Chem Soc 2010; 132:13765-75; PMID:20828131; http://dx.doi.org/10.1021/ja104213j
    • (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
  • 7
    • 84861135685 scopus 로고    scopus 로고
    • Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid fold
    • 22677387
    • W.Wan, H.Wille, J.Stöhr, U.Baxa, S.B.Prusiner, G.Stubbs. Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid fold. Biophys J 2012; 102:2339-44; PMID:22677387; http://dx.doi.org/10.1016/j.bpj.2012.04.011
    • (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
  • 8
    • 84867039782 scopus 로고    scopus 로고
    • Fiber diffraction data indicate a hollow core for the Alzheimer's Aβ 3-fold symmetric fibril
    • 22903058
    • M.McDonald, H.Box, W.Bian, A.Kendall, R.Tycko, G.Stubbs. Fiber diffraction data indicate a hollow core for the Alzheimer's Aβ 3-fold symmetric fibril. J Mol Biol 2012; 423:454-61; PMID:22903058; http://dx.doi.org/10.1016/j.jmb.2012.08.004
    • (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
  • 9
    • 84884217594 scopus 로고    scopus 로고
    • Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue
    • 24034249
    • J.Lu, W.Qiang, W.Yau, C.D.Schwieters, S.C.Meredith, R.Tycko. Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue. Cell 2013; 154:1257-68; PMID:24034249; http://dx.doi.org/10.1016/j.cell.2013.08.035
    • (2013) Cell , vol.154 , pp. 1257-1268
    • Lu, J.1    Qiang, W.2    Yau, W.3    Schwieters, C.D.4    Meredith, S.C.5    Tycko, R.6
  • 11
    • 61449258353 scopus 로고    scopus 로고
    • Core structure of amyloid fibrils formed by residues 106–126 of the human prion protein
    • 19278656
    • P.Walsh, K.Simonetti, S.Sharpe. Core structure of amyloid fibrils formed by residues 106–126 of the human prion protein. Structure 2009; 17:417-26; PMID:19278656; http://dx.doi.org/10.1016/j.str.2008.12.018
    • (2009) Structure , vol.17 , pp. 417-426
    • Walsh, P.1    Simonetti, K.2    Sharpe, S.3
  • 15
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • 1704926
    • M.P.McKinley, R.K.Meyer, L.Kenaga, F.Rahbar, R.Cotter, A.Serban, S.B.Prusiner. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J Virol 1991; 65:1340-51; PMID:1704926
    • (1991) J Virol , vol.65 , pp. 1340-1351
    • McKinley, M.P.1    Meyer, R.K.2    Kenaga, L.3    Rahbar, F.4    Cotter, R.5    Serban, A.6    Prusiner, S.B.7
  • 17
    • 84865740820 scopus 로고    scopus 로고
    • Stabilization of a prion strain of synthetic origin requires multiple serial passages
    • 22807452
    • N.Makarava, G.G.Kovacs, R.Savtchenko, I.Alexeeva, H.Budka, R.G.Rohwer, I.V.Baskakov. Stabilization of a prion strain of synthetic origin requires multiple serial passages. J Biol Chem 2012; 287:30205-14; PMID:22807452; http://dx.doi.org/10.1074/jbc.M112.392985
    • (2012) J Biol Chem , vol.287 , pp. 30205-30214
    • Makarava, N.1    Kovacs, G.G.2    Savtchenko, R.3    Alexeeva, I.4    Budka, H.5    Rohwer, R.G.6    Baskakov, I.V.7
  • 19
    • 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)
    • 23986444
    • W.Wan, W.Bian, M.McDonald, A.Kijac, D.E.Wemmer, G.Stubbs. Heterogeneous seeding of a prion structure by a generic amyloid form of the fungal prion-forming domain HET-s(218–289). J Biol Chem 2013; 288:29604-12; PMID:23986444; http://dx.doi.org/10.1074/jbc.M113.505511
    • (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
  • 20
    • 84898047961 scopus 로고    scopus 로고
    • Fungal prion HET-s as a model for structural complexity and self-propagation in prions
    • 24706820
    • W.Wan, G.Stubbs. Fungal prion HET-s as a model for structural complexity and self-propagation in prions. Proc Natl Acad Sci USA 2014; 111:5201-6; PMID: 24706820; http://dx.doi.org/10.1073/pnas.1322933111
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 5201-5206
    • Wan, W.1    Stubbs, G.2
  • 22
    • 84898898317 scopus 로고    scopus 로고
    • Fiber diffraction of the prion-forming domain HET-s(218–289) shows dehydration-induced deformation of a complex amyloid structure
    • 24670041
    • W.Wan, G.Stubbs. Fiber diffraction of the prion-forming domain HET-s(218–289) shows dehydration-induced deformation of a complex amyloid structure. Biochemistry 2014; 53:2366-70; PMID:24670041; http://dx.doi.org/10.1021/bi5002807
    • (2014) Biochemistry , vol.53 , pp. 2366-2370
    • Wan, W.1    Stubbs, G.2
  • 23
    • 38349164999 scopus 로고    scopus 로고
    • Enclosed chambers for humidity control and sample containment in fiber diffraction
    • M.McDonald, A.Kendall, M.Tanaka, J.S.Weissman, G.Stubbs. Enclosed chambers for humidity control and sample containment in fiber diffraction. J Appl Cryst 2008; 41:206-9; http://dx.doi.org/10.1107/S0021889807060803
    • (2008) J Appl Cryst , vol.41 , pp. 206-209
    • McDonald, M.1    Kendall, A.2    Tanaka, M.3    Weissman, J.S.4    Stubbs, G.5
  • 26
  • 27
    • 84992188723 scopus 로고    scopus 로고
    • Alternative salt bridge formation in Aβ - a hallmark of early-onset Alzheimer disease?
    • 25988181
    • M.Schledorn, B.Meier, A.Böckmann. Alternative salt bridge formation in Aβ - a hallmark of early-onset Alzheimer disease? Front Mol Biosci 2015; 2:14; PMID:25988181
    • (2015) Front Mol Biosci , vol.2 , pp. 14
    • Schledorn, M.1    Meier, B.2    Böckmann, A.3
  • 28
    • 84907508821 scopus 로고    scopus 로고
    • Heterogeneous seeding of HET-s(218-289) and the mutability of prion structures
    • 25077317
    • W.Wan, G.Stubbs. Heterogeneous seeding of HET-s(218-289) and the mutability of prion structures. Prion 2014; 8:1-5; PMID:25077317; http://dx.doi.org/10.4161/pri.28126
    • (2014) Prion , vol.8 , pp. 1-5
    • Wan, W.1    Stubbs, G.2
  • 29
    • 35748946237 scopus 로고    scopus 로고
    • Prions
    • Knipe D.M., Howley P.M., Griffin D.E., (eds), Philadelphia, PA: Lippincott: Williams & Wilkins
    • S.B.Prusiner. Prions. In: D.M.Knipe, P.M.Howley, D.E.Griffin, eds., Fields Virology. Philadelphia, PA: Lippincott Williams & Wilkins; 2007; 3059-92.
    • (2007) Fields Virology , pp. 3059-3092
    • Prusiner, S.B.1
  • 32
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed β-helices into trimers
    • 15155909
    • C.Govaerts, H.Wille, S.B.Prusiner, F.E.Cohen. Evidence for assembly of prions with left-handed β-helices into trimers. Proc Natl Acad Sci USA 2004; 101:8342-7; PMID:15155909; http://dx.doi.org/10.1073/pnas.0402254101
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.