메뉴 건너뛰기




Volumn 8, Issue 2, 2014, Pages 349-356

Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p

Author keywords

Assignments; Fibrils; Secondary structure; Solid state NMR; Sup35p

Indexed keywords

AMYLOID; SACCHAROMYCES CEREVISIAE PROTEIN; SUP35 PROTEIN, S CEREVISIAE; TRANSLATION TERMINATION FACTOR;

EID: 84908298458     PISSN: 18742718     EISSN: 1874270X     Source Type: Journal    
DOI: 10.1007/s12104-013-9515-1     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 77955623501 scopus 로고    scopus 로고
    • Prions: en route from structural models to structures
    • Böckmann A, Meier BH (2010) Prions: en route from structural models to structures. Prion 4(2):72–79
    • (2010) Prion , vol.4 , Issue.2 , pp. 72-79
    • Böckmann, A.1    Meier, B.H.2
  • 4
    • 84966138908 scopus 로고
    • PSI, a cytoplasmic suppressor of super-suppressor in yeast
    • Cox BS (1965) PSI, a cytoplasmic suppressor of super-suppressor in yeast. Heredity 20(4):505–521
    • (1965) Heredity , vol.20 , Issue.4 , pp. 505-521
    • Cox, B.S.1
  • 5
    • 77955045091 scopus 로고    scopus 로고
    • Magic angle spinning NMR analysis of beta(2)-microglobulin amyloid fibrils in two distinct morphologies
    • Debelouchina GT, Platt GW, Bayro MJ, Radford SE, Griffin RG (2010) Magic angle spinning NMR analysis of beta(2)-microglobulin amyloid fibrils in two distinct morphologies. J Am Chem Soc 132(30):10414–10423
    • (2010) J Am Chem Soc , vol.132 , Issue.30 , pp. 10414-10423
    • Debelouchina, G.T.1    Platt, G.W.2    Bayro, M.J.3    Radford, S.E.4    Griffin, R.G.5
  • 6
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion
    • DePace AH, Santoso A, Hillner P, Weissman JS (1998) A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell 93(7):1241–1252
    • (1998) Cell , vol.93 , Issue.7 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 11
    • 51749125627 scopus 로고    scopus 로고
    • Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein
    • Heise H, Celej MS, Becker S, Riede D, Pelah A, Kumar A, Jovin TM, Baldus M (2008) Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein. J Mol Biol 380(3):444–450
    • (2008) J Mol Biol , vol.380 , Issue.3 , pp. 444-450
    • Heise, H.1    Celej, M.S.2    Becker, S.3    Riede, D.4    Pelah, A.5    Kumar, A.6    Jovin, T.M.7    Baldus, M.8
  • 12
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • Krishnan R, Lindquist S (2005) Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435(7043):765–772
    • (2005) Nature , vol.435 , Issue.7043 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.2
  • 13
    • 33644555537 scopus 로고    scopus 로고
    • Molecular chaperones and the assembly of the prion Sup35p, an in vitro study
    • Krzewska J, Melki R (2006) Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J 25(4):822–833
    • (2006) EMBO J , vol.25 , Issue.4 , pp. 822-833
    • Krzewska, J.1    Melki, R.2
  • 14
    • 33847266871 scopus 로고    scopus 로고
    • Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain
    • Krzewska J, Tanaka M, Burston SG, Melki R (2007) Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain. J Biol Chem 282(3):1679–1686
    • (2007) J Biol Chem , vol.282 , Issue.3 , pp. 1679-1686
    • Krzewska, J.1    Tanaka, M.2    Burston, S.G.3    Melki, R.4
  • 17
    • 78049396749 scopus 로고    scopus 로고
    • Supramolecular interactions probed by 13C–13C solid-state NMR spectroscopy
    • Loquet A, Giller K, Becker S, Lange A (2010) Supramolecular interactions probed by 13C–13C solid-state NMR spectroscopy. J Am Chem Soc 132(43):15164–15166
    • (2010) J Am Chem Soc , vol.132 , Issue.43 , pp. 15164-15166
    • Loquet, A.1    Giller, K.2    Becker, S.3    Lange, A.4
  • 18
    • 84978096010 scopus 로고    scopus 로고
    • Luckgei N, Schütz AK, Bousset L, Habenstein B, Sourigues Y, Gardiennet C, Meier BH, Melki R, Böckmann A (2013a) The conformation of the prion domain of Sup35p in isolation and in the full-length protein is different (submitted)
  • 21
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer’s beta-amyloid fibrils
    • Paravastu AK, Leapman RD, Yau W-M, Tycko R (2008) Molecular structural basis for polymorphism in Alzheimer’s beta-amyloid fibrils. Proc Natl Acad Sci USA 105(47):18349–18354
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.47 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.-M.3    Tycko, R.4
  • 22
    • 43949153555 scopus 로고
    • Optimized spectral editing of 13C MAS NMR spectra of rigid solids using cross-polarization methods
    • Sangill R, Rastrupandersen N, Bildsoe H, Jakobsen HJ, Nielsen NC (1994) Optimized spectral editing of 13C MAS NMR spectra of rigid solids using cross-polarization methods. J Magn Reson A 107(1):67–78
    • (1994) J Magn Reson A , vol.107 , Issue.1 , pp. 67-78
    • Sangill, R.1    Rastrupandersen, N.2    Bildsoe, H.3    Jakobsen, H.J.4    Nielsen, N.C.5
  • 23
    • 77955123982 scopus 로고    scopus 로고
    • Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227)
    • Schuetz A, Wasmer C, Habenstein B, Verel R, Greenwald J, Riek R, Böckmann A, Meier BH (2010) Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227). Chembiochem 11(11):1543–1551
    • (2010) Chembiochem , vol.11 , Issue.11 , pp. 1543-1551
    • Schuetz, A.1    Wasmer, C.2    Habenstein, B.3    Verel, R.4    Greenwald, J.5    Riek, R.6    Böckmann, A.7    Meier, B.H.8
  • 24
    • 33845938549 scopus 로고    scopus 로고
    • Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure
    • Shewmaker F, Wickner RB, Tycko R (2006) Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. Proc Natl Acad Sci USA 103(52):19754–19759
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.52 , pp. 19754-19759
    • Shewmaker, F.1    Wickner, R.B.2    Tycko, R.3
  • 27
    • 34548615995 scopus 로고    scopus 로고
    • The structural basis of yeast prion strain variants
    • Toyama B, Kelly M, Gross J, Weissman J (2007) The structural basis of yeast prion strain variants. Nature 449(7159):233–237
    • (2007) Nature , vol.449 , Issue.7159 , pp. 233-237
    • Toyama, B.1    Kelly, M.2    Gross, J.3    Weissman, J.4
  • 28
    • 33645513429 scopus 로고    scopus 로고
    • Solid-state NMR as a probe of amyloid structure
    • Tycko R (2006) Solid-state NMR as a probe of amyloid structure. Protein Pept Lett 13:229–234
    • (2006) Protein Pept Lett , vol.13 , pp. 229-234
    • Tycko, R.1
  • 29
    • 33747799315 scopus 로고    scopus 로고
    • Dynamic nuclear polarization of amyloidogenic peptide nanocrystals: GNNQQNY, a core segment of the yeast prion protein Sup35p
    • van der Wel PC, Hu K, Lewandowski JR, Griffin RG (2006) Dynamic nuclear polarization of amyloidogenic peptide nanocrystals: GNNQQNY, a core segment of the yeast prion protein Sup35p. J Am Chem Soc 128(33):10840–10846
    • (2006) J Am Chem Soc , vol.128 , Issue.33 , pp. 10840-10846
    • van der Wel, P.C.1    Hu, K.2    Lewandowski, J.R.3    Griffin, R.G.4
  • 30
    • 34247504580 scopus 로고    scopus 로고
    • Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p
    • van der Wel PCA, Lewandowski JR, Griffin RG (2007) Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p. J Am Chem Soc 129(16):5117–5130
    • (2007) J Am Chem Soc , vol.129 , Issue.16 , pp. 5117-5130
    • van der Wel, P.C.A.1    Lewandowski, J.R.2    Griffin, R.G.3
  • 31
    • 78149340576 scopus 로고    scopus 로고
    • Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR
    • van der Wel PCA, Lewandowski JR, Griffin RG (2010) Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR. Biochemistry 49(44):9457–9469
    • (2010) Biochemistry , vol.49 , Issue.44 , pp. 9457-9469
    • van der Wel, P.C.A.1    Lewandowski, J.R.2    Griffin, R.G.3
  • 32
    • 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, Meier BH (2010) Atomic-resolution three-dimensional structure of HET-s(218–289) amyloid fibrils by solid-state NMR spectroscopy. J Am Chem Soc 132(39):13765–13775
    • (2010) J Am Chem Soc , vol.132 , Issue.39 , 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
  • 34
    • 0036129107 scopus 로고    scopus 로고
    • Probability-based protein secondary structure identification using combined NMR chemical-shift data
    • Wang Y, Jardetzky O (2002) Probability-based protein secondary structure identification using combined NMR chemical-shift data. Protein Sci 11(4):852–861
    • (2002) Protein Sci , vol.11 , Issue.4 , pp. 852-861
    • Wang, Y.1    Jardetzky, O.2
  • 35
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218–289) prion form a beta solenoid with a triangular hydrophobic core
    • Wasmer C, Lange A, van Melckebeke H, Siemer AB, Riek R, Meier BH (2008) Amyloid fibrils of the HET-s(218–289) prion form a beta solenoid with a triangular hydrophobic core. Science 319(5869):1523–1526
    • (2008) Science , vol.319 , Issue.5869 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 36
    • 0029584303 scopus 로고
    • [PSI] and [URE3] as yeast prions
    • Wickner RB, Masison DC, Edskes HK (1995) [PSI] and [URE3] as yeast prions. Yeast 11(16):1671–1685
    • (1995) Yeast , vol.11 , Issue.16 , pp. 1671-1685
    • Wickner, R.B.1    Masison, D.C.2    Edskes, H.K.3
  • 37
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4(2):171–180
    • (1994) J Biomol NMR , vol.4 , Issue.2 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 38
    • 0000563331 scopus 로고
    • Complete spectral editing in CPMAS NMR
    • Wu X, Zilm K (1993) Complete spectral editing in CPMAS NMR. J Magn Reson A 102(2):205–213
    • (1993) J Magn Reson A , vol.102 , Issue.2 , pp. 205-213
    • Wu, X.1    Zilm, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.