메뉴 건너뛰기




Volumn 289, Issue 39, 2014, Pages 26817-26828

Architecture of polyglutamine-containing fibrils from time-resolved fluorescence decay

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE; GLYCOPROTEINS; INTELLIGENT SYSTEMS; MONTE CARLO METHODS; PATHOLOGY;

EID: 84907587238     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.581991     Document Type: Article
Times cited : (9)

References (37)
  • 1
    • 84861398901 scopus 로고    scopus 로고
    • Explaining the length threshold of polyglutamine aggregation
    • De Los Rios, P., Hafner, M., and Pastore, A. (2012) Explaining the length threshold of polyglutamine aggregation. J. Phys. Condens. Matter. 24, 244105
    • (2012) J. Phys. Condens. Matter. , vol.24 , pp. 244105
    • De Los Rios, P.1    Hafner, M.2    Pastore, A.3
  • 2
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A., and Poirier, M. A. (2004) Protein aggregation and neurodegenerative disease. Nat. Med. 10, (suppl.) S10-S17
    • (2004) Nat. Med. , vol.10 , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 3
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr, H. T., and Zoghbi, H. Y. (2007) Trinucleotide repeat disorders. Annu. Rev. Neurosci. 30, 575-621
    • (2007) Annu. Rev. Neurosci. , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 5
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren, P. H., Lauckner, J. E., Kachirskaia, I., Heuser, J. E., Melki, R., and Kopito, R. R. (2009) Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat. Cell Biol. 11, 219-225
    • (2009) Nat. Cell Biol. , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 7
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
    • Yang, W., Dunlap, J. R., Andrews, R. B., and Wetzel, R. (2002) Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum. Mol. Genet. 11, 2905-2917
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2905-2917
    • Yang, W.1    Dunlap, J.R.2    Andrews, R.B.3    Wetzel, R.4
  • 8
    • 23044445857 scopus 로고    scopus 로고
    • A novel therapeutic strategy for polyglutamine diseases by stabilizing aggregation-prone proteins with small molecules
    • Tanaka, M., Machida, Y., and Nukina, N. (2005) A novel therapeutic strategy for polyglutamine diseases by stabilizing aggregation-prone proteins with small molecules. J. Mol. Med. (Berl) 83, 343-352
    • (2005) J. Mol. Med. (Berl , vol.83 , pp. 343-352
    • Tanaka, M.1    Machida, Y.2    Nukina, N.3
  • 10
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
    • Poirier, M. A., Li, H., Macosko, J., Cai, S., Amzel, M., and Ross, C. A. (2002) Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. J. Biol. Chem. 277, 41032-41037
    • (2002) J. Biol. Chem. , vol.277 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    Macosko, J.3    Cai, S.4    Amzel, M.5    Ross, C.A.6
  • 13
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fibril structure
    • Tycko, R. (2011) Solid-state NMR studies of amyloid fibril structure. Annu. Rev. Phys. Chem. 62, 279-299
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 279-299
    • Tycko, R.1
  • 15
    • 33645101164 scopus 로고    scopus 로고
    • Computational study of the fibril organization of polyglutamine repeats reveals a common motif identified in βhelices
    • Zanuy, D., Gunasekaran, K., Lesk, A. M., and Nussinov, R. (2006) Computational study of the fibril organization of polyglutamine repeats reveals a common motif identified in βhelices. J. Mol. Biol. 358, 330-345
    • (2006) J. Mol. Biol. , vol.358 , pp. 330-345
    • Zanuy, D.1    Gunasekaran, K.2    Lesk, A.M.3    Nussinov, R.4
  • 16
    • 14044278010 scopus 로고    scopus 로고
    • New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils
    • Sikorski, P., and Atkins, E. (2005) New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils. Biomacromolecules 6, 425-432
    • (2005) Biomacromolecules , vol.6 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 17
    • 84866419575 scopus 로고    scopus 로고
    • Structural features and domain organization of huntingtin fibrils
    • Bugg, C. W., Isas, J. M., Fischer, T., Patterson, P. H., and Langen, R. (2012) Structural features and domain organization of huntingtin fibrils. J. Biol. Chem. 287, 31739-31746
    • (2012) J. Biol. Chem. , vol.287 , pp. 31739-31746
    • Bugg, C.W.1    Isas, J.M.2    Fischer, T.3    Patterson, P.H.4    Langen, R.5
  • 22
    • 79952923961 scopus 로고    scopus 로고
    • Natural osmolytes remodel the aggregation pathway of mutant huntingtin exon 1
    • Borwankar, T., Röthlein, C., Zhang, G., Techen, A., Dosche, C., and Ignatova, Z. (2011) Natural osmolytes remodel the aggregation pathway of mutant huntingtin exon 1. Biochemistry 50, 2048-2060
    • (2011) Biochemistry , vol.50 , pp. 2048-2060
    • Borwankar, T.1    Röthlein, C.2    Zhang, G.3    Techen, A.4    Dosche, C.5    Ignatova, Z.6
  • 23
  • 24
    • 15544372340 scopus 로고    scopus 로고
    • A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: Evidence for a compact β-sheet structure
    • Poirier, M. A., Jiang, H., and Ross, C. A. (2005) A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: evidence for a compact β-sheet structure. Hum. Mol. Genet. 14, 765-774
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 765-774
    • Poirier, M.A.1    Jiang, H.2    Ross, C.A.3
  • 25
    • 0037168642 scopus 로고    scopus 로고
    • Mutational analysis of the structural organization of polyglutamine aggregates
    • Thakur, A. K., and Wetzel, R. (2002) Mutational analysis of the structural organization of polyglutamine aggregates. Proc. Natl. Acad. Sci. U.S.A. 99, 17014-17019
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 17014-17019
    • Thakur, A.K.1    Wetzel, R.2
  • 27
    • 71449084004 scopus 로고    scopus 로고
    • The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation
    • Tam, S., Spiess, C., Auyeung, W., Joachimiak, L., Chen, B., Poirier, M. A., and Frydman, J. (2009) The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Nat. Struct. Mol. Biol. 16, 1279-1285
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1279-1285
    • Tam, S.1    Spiess, C.2    Auyeung, W.3    Joachimiak, L.4    Chen, B.5    Poirier, M.A.6    Frydman, J.7
  • 29
    • 84856471945 scopus 로고    scopus 로고
    • Dynamic imaging of homo-FRET in live cells by fluorescence anisotropy microscopy
    • Ghosh, S., Saha, S., Goswami, D., Bilgrami, S., and Mayor, S. (2012) Dynamic imaging of homo-FRET in live cells by fluorescence anisotropy microscopy. Methods Enzymol. 505, 291-327
    • (2012) Methods Enzymol. , vol.505 , pp. 291-327
    • Ghosh, S.1    Saha, S.2    Goswami, D.3    Bilgrami, S.4    Mayor, S.5
  • 30
    • 78650441363 scopus 로고    scopus 로고
    • Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins
    • Fiumara, F., Fioriti, L., Kandel, E. R., and Hendrickson, W. A. (2010) Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins. Cell 143, 1121-1135
    • (2010) Cell , vol.143 , pp. 1121-1135
    • Fiumara, F.1    Fioriti, L.2    Kandel, E.R.3    Hendrickson, W.A.4
  • 31
    • 79952360891 scopus 로고    scopus 로고
    • Critical nucleus size for disease-related polyglutamine aggregation is repeatlength dependent
    • Kar, K., Jayaraman, M., Sahoo, B., Kodali, R., and Wetzel, R. (2011) Critical nucleus size for disease-related polyglutamine aggregation is repeatlength dependent. Nat. Struct. Mol. Biol. 18, 328-336
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 328-336
    • Kar, K.1    Jayaraman, M.2    Sahoo, B.3    Kodali, R.4    Wetzel, R.5
  • 32
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • Berney, C., and Danuser, G. (2003) FRET or no FRET: a quantitative comparison. Biophys. J. 84, 3992-4010
    • (2003) Biophys. J. , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 33
    • 28444437454 scopus 로고    scopus 로고
    • A flexible approach to the calculation of resonance energy transfer efficiency between multiple donors and acceptors in complex geometries
    • Corry, B., Jayatilaka, D., and Rigby, P. (2005) A flexible approach to the calculation of resonance energy transfer efficiency between multiple donors and acceptors in complex geometries. Biophys. J. 89, 3822-3836
    • (2005) Biophys. J. , vol.89 , pp. 3822-3836
    • Corry, B.1    Jayatilaka, D.2    Rigby, P.3
  • 34
    • 0037019478 scopus 로고    scopus 로고
    • Dynamic Monte Carlo simulations to model FRET and photobleaching in systems with multiple donor-acceptor interactions
    • Frederix, P. L., de Beer, E. L., Hamelink, W., and Gerritsen, H. C. (2002) Dynamic Monte Carlo simulations to model FRET and photobleaching in systems with multiple donor-acceptor interactions. J. Phys. Chem. B 106, 6793-6801
    • (2002) J. Phys. Chem. B , vol.106 , pp. 6793-6801
    • Frederix, P.L.1    De Beer, E.L.2    Hamelink, W.3    Gerritsen, H.C.4
  • 35
    • 84898623416 scopus 로고    scopus 로고
    • Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formation
    • Landrum, E., and Wetzel, R. (2014) Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formation. J. Biol. Chem. 289, 10254-10260
    • (2014) J. Biol. Chem. , vol.289 , pp. 10254-10260
    • Landrum, E.1    Wetzel, R.2
  • 36
    • 84865683315 scopus 로고    scopus 로고
    • Assessing polyglutamine conformation in the nucleating event by molecular dynamics simulations
    • Miettinen, M. S., Knecht, V., Monticelli, L., and Ignatova, Z. (2012) Assessing polyglutamine conformation in the nucleating event by molecular dynamics simulations. J. Phys. Chem. B 116, 10259-10265
    • (2012) J. Phys. Chem. B , vol.116 , pp. 10259-10265
    • Miettinen, M.S.1    Knecht, V.2    Monticelli, L.3    Ignatova, Z.4
  • 37
    • 84898867352 scopus 로고    scopus 로고
    • Stable polyglutamine dimers can contain β-hairpins with interdigitated side chains-but not α-helices, β-nanotubes, β-pseudohelices, or steric zippers
    • Miettinen, M. S., Monticelli, L., Nedumpully-Govindan, P., Knecht, V., and Ignatova, Z. (2014) Stable polyglutamine dimers can contain β-hairpins with interdigitated side chains-but not α-helices, β-nanotubes, β-pseudohelices, or steric zippers. Biophys. J. 106, 1721-1728
    • (2014) Biophys. J. , vol.106 , pp. 1721-1728
    • Miettinen, M.S.1    Monticelli, L.2    Nedumpully-Govindan, P.3    Knecht, V.4    Ignatova, Z.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.