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Volumn 582, Issue 11, 2008, Pages 1587-1592

Monitoring fibril formation of the N-terminal domain of PABPN1 carrying an alanine repeat by tryptophan fluorescence and real-time NMR

Author keywords

Fibril formation; PABPN1; Poly alanine; Real time NMR; Trinucleotide expansion; Tryptophan fluorescence

Indexed keywords

ACRYLAMIDE; ALANINE; BINDING PROTEIN; PROTEIN PABPN1; TRYPTOPHAN DERIVATIVE;

EID: 43049167415     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.04.002     Document Type: Article
Times cited : (8)

References (21)
  • 1
    • 0008146244 scopus 로고    scopus 로고
    • 3′-End processing of pre-mRNA in eukaryotes
    • Wahle E., and Ruegsegger U. 3′-End processing of pre-mRNA in eukaryotes. FEMS Microbiol. Rev. 23 (1999) 277-295
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 277-295
    • Wahle, E.1    Ruegsegger, U.2
  • 2
    • 0025817865 scopus 로고
    • A novel poly(A)-binding protein acts as a specificity factor in the second phase of messenger RNA polyadenylation
    • Wahle E. A novel poly(A)-binding protein acts as a specificity factor in the second phase of messenger RNA polyadenylation. Cell 66 (1991) 759-768
    • (1991) Cell , vol.66 , pp. 759-768
    • Wahle, E.1
  • 3
    • 0030813827 scopus 로고    scopus 로고
    • Morphological changes in muscle fibers in oculopharyngeal muscular dystrophy
    • Tome F.M., Chateau D., Helbling-Leclerc A., and Fardeau M. Morphological changes in muscle fibers in oculopharyngeal muscular dystrophy. Neuromuscul. Disord. 7 Suppl. 1 (1997) S63-S69
    • (1997) Neuromuscul. Disord. , vol.7 , Issue.SUPPL. 1
    • Tome, F.M.1    Chateau, D.2    Helbling-Leclerc, A.3    Fardeau, M.4
  • 4
    • 0018865908 scopus 로고
    • Nuclear inclusions in oculopharyngeal dystrophy
    • Tome F.M., and Fardeau M. Nuclear inclusions in oculopharyngeal dystrophy. Acta Neuropathol. (Berl.) 49 (1980) 85-87
    • (1980) Acta Neuropathol. (Berl.) , vol.49 , pp. 85-87
    • Tome, F.M.1    Fardeau, M.2
  • 5
    • 0034703413 scopus 로고    scopus 로고
    • Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA
    • Calado A., Tome F.M., Brais B., Rouleau G.A., Kuhn U., Wahle E., and Carmo-Fonseca M. Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA. Hum. Mol. Genet. 9 (2000) 2321-2328
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2321-2328
    • Calado, A.1    Tome, F.M.2    Brais, B.3    Rouleau, G.A.4    Kuhn, U.5    Wahle, E.6    Carmo-Fonseca, M.7
  • 7
    • 17344371397 scopus 로고    scopus 로고
    • Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy
    • Brais B., et al. Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. Nat. Genet. 18 (1998) 164-167
    • (1998) Nat. Genet. , vol.18 , pp. 164-167
    • Brais, B.1
  • 8
    • 0344845146 scopus 로고    scopus 로고
    • Trinucleotide expansions leading to an extended poly-l-alanine segment in the poly (A) binding protein PABPN1 cause fibril formation
    • Scheuermann T., Schulz B., Blume A., Wahle E., Rudolph R., and Schwarz E. Trinucleotide expansions leading to an extended poly-l-alanine segment in the poly (A) binding protein PABPN1 cause fibril formation. Protein Sci. 12 (2003) 2685-2692
    • (2003) Protein Sci. , vol.12 , pp. 2685-2692
    • Scheuermann, T.1    Schulz, B.2    Blume, A.3    Wahle, E.4    Rudolph, R.5    Schwarz, E.6
  • 9
    • 33845999251 scopus 로고    scopus 로고
    • Effect of oculopharyngeal muscular dystrophy-associated extension of seven alanines on the fibrillation properties of the N-terminal domain of PABPN1
    • Lodderstedt G., Hess S., Hause G., Scheuermann T., Scheibel T., and Schwarz E. Effect of oculopharyngeal muscular dystrophy-associated extension of seven alanines on the fibrillation properties of the N-terminal domain of PABPN1. FEBS J. 274 (2007) 346-355
    • (2007) FEBS J. , vol.274 , pp. 346-355
    • Lodderstedt, G.1    Hess, S.2    Hause, G.3    Scheuermann, T.4    Scheibel, T.5    Schwarz, E.6
  • 10
    • 39649092945 scopus 로고    scopus 로고
    • Hofmeister salts and potential therapeutic compounds accelerate in vitro fibril formation of the N-terminal domain of PABPN1 containing a disease-causing alanine extension
    • Lodderstedt G., et al. Hofmeister salts and potential therapeutic compounds accelerate in vitro fibril formation of the N-terminal domain of PABPN1 containing a disease-causing alanine extension. Biochemistry 47 (2008) 2181-2189
    • (2008) Biochemistry , vol.47 , pp. 2181-2189
    • Lodderstedt, G.1
  • 11
    • 0034725656 scopus 로고    scopus 로고
    • A conformation change in the carboxyl terminus of Alzheimer's Abeta (1-40) accompanies the transition from dimer to fibril as revealed by fluorescence quenching analysis
    • Garzon-Rodriguez W., Vega A., Sepulveda-Becerra M., Milton S., Johnson D.A., Yatsimirsky A.K., and Glabe C.G. A conformation change in the carboxyl terminus of Alzheimer's Abeta (1-40) accompanies the transition from dimer to fibril as revealed by fluorescence quenching analysis. J. Biol. Chem. 275 (2000) 22645-22649
    • (2000) J. Biol. Chem. , vol.275 , pp. 22645-22649
    • Garzon-Rodriguez, W.1    Vega, A.2    Sepulveda-Becerra, M.3    Milton, S.4    Johnson, D.A.5    Yatsimirsky, A.K.6    Glabe, C.G.7
  • 12
    • 33644527256 scopus 로고    scopus 로고
    • Characterization of oligomers during alpha-synuclein aggregation using intrinsic tryptophan fluorescence
    • Dusa A., Kaylor J., Edridge S., Bodner N., Hong D.P., and Fink A.L. Characterization of oligomers during alpha-synuclein aggregation using intrinsic tryptophan fluorescence. Biochemistry 45 (2006) 2752-2760
    • (2006) Biochemistry , vol.45 , pp. 2752-2760
    • Dusa, A.1    Kaylor, J.2    Edridge, S.3    Bodner, N.4    Hong, D.P.5    Fink, A.L.6
  • 14
    • 0000722070 scopus 로고    scopus 로고
    • Spectral methods of characterizing protein conformation and conformational changes
    • Creighton T.E. (Ed), IRL-Press/Oxford University Press, Oxford/New York/Tokio
    • Schmid F.X. Spectral methods of characterizing protein conformation and conformational changes. In: Creighton T.E. (Ed). Protein Structure: A Practical Approach (1997), IRL-Press/Oxford University Press, Oxford/New York/Tokio 251-285
    • (1997) Protein Structure: A Practical Approach , pp. 251-285
    • Schmid, F.X.1
  • 16
    • 33644818046 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of Abeta(1-40) amyloid fibril stability
    • Williams A.D., Shivaprasad S., and Wetzel R. Alanine scanning mutagenesis of Abeta(1-40) amyloid fibril stability. J. Mol. Biol. 357 (2006) 1283-1294
    • (2006) J. Mol. Biol. , vol.357 , pp. 1283-1294
    • Williams, A.D.1    Shivaprasad, S.2    Wetzel, R.3
  • 17
    • 34249782573 scopus 로고    scopus 로고
    • Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides
    • Meinhardt J., et al. Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides. Protein Sci. 16 (2007) 1214-1222
    • (2007) Protein Sci. , vol.16 , pp. 1214-1222
    • Meinhardt, J.1
  • 18
    • 37349004102 scopus 로고    scopus 로고
    • Parkinson's disease
    • Thomas B., and Beal M.F. Parkinson's disease. Hum. Mol. Genet. 16 Spec. No. 2 (2007) R183-R194
    • (2007) Hum. Mol. Genet. , vol.16 , Issue.Spec. 2
    • Thomas, B.1    Beal, M.F.2
  • 20
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • Chou P.Y., and Fasman G.D. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry 13 (1974) 211-222
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 21
    • 0034609561 scopus 로고    scopus 로고
    • Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein
    • Rochet J.C., Conway K.A., and Lansbury Jr. P.T. Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein. Biochemistry 39 (2000) 10619-10626
    • (2000) Biochemistry , vol.39 , pp. 10619-10626
    • Rochet, J.C.1    Conway, K.A.2    Lansbury Jr., P.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.