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Volumn 49, Issue , 2016, Pages

Delayed emergence of subdiffraction-sized mutant huntingtin fibrils following inclusion body formation

Author keywords

amyloid; huntingtin; Huntington's Disease; protein aggregation; single molecule imaging; super resolution

Indexed keywords


EID: 84956819046     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583515000219     Document Type: Article
Times cited : (34)

References (39)
  • 1
    • 60049098657 scopus 로고
    • Beiträge zur Theorie des Mikroskops und der mikroskopischen Wahrnehmung
    • ABBE, E. (1873). Beiträge zur Theorie des Mikroskops und der mikroskopischen Wahrnehmung. Archiv für Mikroskopische Anatomie 9, 413-468.
    • (1873) Archiv für Mikroskopische Anatomie , vol.9 , pp. 413-468
    • Abbe, E.1
  • 2
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • ARRASATE, M., MITRA, S., SCHWEITZER, E. S., SEGAL, M.R. & FINKBEINER, S. (2004). Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431(7010), 805-810.
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 6
    • 38149030094 scopus 로고    scopus 로고
    • Determination of particle number and brightness using a laser scanning confocal microscope operating in the analog mode
    • DALAL, R. B., DIGMAN, M. A., HORWITZ, A. F., VETRI, V. & GRATTON, E. (2008). Determination of particle number and brightness using a laser scanning confocal microscope operating in the analog mode. Microscopy Research and Technique 71(1), 69-81.
    • (2008) Microscopy Research and Technique , vol.71 , Issue.1 , pp. 69-81
    • Dalal, R.B.1    Digman, M.A.2    Horwitz, A.F.3    Vetri, V.4    Gratton, E.5
  • 7
    • 0030832226 scopus 로고    scopus 로고
    • On/off blinking and switching behaviour of single molecules of green fluorescent protein
    • DICKSON, R. M., CUBITT, A. B., TSIEN, R.Y. & MOERNER, W. E. (1997). On/off blinking and switching behaviour of single molecules of green fluorescent protein. Nature 388(6640), 355-358.
    • (1997) Nature , vol.388 , Issue.6640 , pp. 355-358
    • Dickson, R.M.1    Cubitt, A.B.2    Tsien, R.Y.3    Moerner, W.E.4
  • 8
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DIFIGLIA, M., SAPP, E., CHASE, K. O., DAVIES, S.W., BATES, G.P., VONSATTEL, J.P. & ARONIN, N. (1997). Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277(5334), 1990-1993.
    • (1997) Science , vol.277 , Issue.5334 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 9
    • 44049105523 scopus 로고    scopus 로고
    • Mapping the number of molecules and brightness in the laser scanning microscope
    • DIGMAN, M. A., DALAL, R., HORWITZ, A.F. & GRATTON, E. (2008). Mapping the number of molecules and brightness in the laser scanning microscope. Biophysical Journal 94(6), 2320-2332.
    • (2008) Biophysical Journal , vol.94 , Issue.6 , pp. 2320-2332
    • Digman, M.A.1    Dalal, R.2    Horwitz, A.F.3    Gratton, E.4
  • 10
    • 80052501613 scopus 로고    scopus 로고
    • Subdiffraction imaging of huntingtin protein aggregates by fluorescence blink-microscopy and atomic force microscopy
    • DUIM, W. C., CHEN, B., FRYDMAN, J. & MOERNER, W. E. (2011). Subdiffraction imaging of huntingtin protein aggregates by fluorescence blink-microscopy and atomic force microscopy. ChemPhysChem 12(13), 2387-2390.
    • (2011) ChemPhysChem , vol.12 , Issue.13 , pp. 2387-2390
    • Duim, W.C.1    Chen, B.2    Frydman, J.3    Moerner, W.E.4
  • 11
    • 84919702871 scopus 로고    scopus 로고
    • Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregates
    • DUIM, W. C., JIANG, Y., SHEN, K., FRYDMAN, J. & MOERNER, W.E. (2014). Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregates. ACS Chemical Biology 9(12), 2767-2778.
    • (2014) ACS Chemical Biology , vol.9 , Issue.12 , pp. 2767-2778
    • Duim, W.C.1    Jiang, Y.2    Shen, K.3    Frydman, J.4    Moerner, W.E.5
  • 12
    • 0028460042 scopus 로고
    • Breaking the diffraction resolution limit by stimulated-emission - stimulated-emissiondepletion fluorescence microscopy
    • HELL, S.W. & WICHMANN, J. (1994). Breaking the diffraction resolution limit by stimulated-emission - stimulated-emissiondepletion fluorescence microscopy. Optics Letters 19(11), 780-782.
    • (1994) Optics Letters , vol.19 , Issue.11 , pp. 780-782
    • Hell, S.W.1    Wichmann, J.2
  • 13
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • HUNTINGTON'S DISEASE COLLABORATIVE RESEARCH GROUP. (1993). A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72(6), 971-983.
    • (1993) Cell , vol.72 , Issue.6 , pp. 971-983
  • 15
    • 0032607671 scopus 로고    scopus 로고
    • Subdiffraction resolution in farfield fluorescence microscopy
    • KLAR, T.A. & HELL, S.W. (1999). Subdiffraction resolution in farfield fluorescence microscopy. Optics Letters 24(14), 954-956.
    • (1999) Optics Letters , vol.24 , Issue.14 , pp. 954-956
    • Klar, T.A.1    Hell, S.W.2
  • 16
    • 84898623416 scopus 로고    scopus 로고
    • Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formation
    • LANDRUM, E. & WETZEL, R. (2014). Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formation. Journal of Biological Chemistry 289(15), 10254-10260.
    • (2014) Journal of Biological Chemistry , vol.289 , Issue.15 , pp. 10254-10260
    • Landrum, E.1    Wetzel, R.2
  • 18
    • 0001195918 scopus 로고
    • On the theory of optical images, with special reference to the microscope
    • LORD RAYLEIGH. (1896). On the theory of optical images, with special reference to the microscope. Philosophical Magazine 5(42), 167-195.
    • (1896) Philosophical Magazine , vol.5 , Issue.42 , pp. 167-195
  • 19
    • 0030866150 scopus 로고    scopus 로고
    • Those blinking molecules
    • MOERNER, W. E. (1997). Those blinking molecules. Science 277(5329), 1059-1060.
    • (1997) Science , vol.277 , Issue.5329 , pp. 1059-1060
    • Moerner, W.E.1
  • 20
    • 34547878369 scopus 로고    scopus 로고
    • New directions in single-molecule imaging and analysis
    • MOERNER, W. E. (2007). New directions in single-molecule imaging and analysis. Proceedings of the National Academy of Sciences 104(31), 12596-12602.
    • (2007) Proceedings of the National Academy of Sciences , vol.104 , Issue.31 , pp. 12596-12602
    • Moerner, W.E.1
  • 22
    • 77953567262 scopus 로고    scopus 로고
    • A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis
    • OSSATO, G., DIGMAN, M. A., AIKEN, C., LUKACSOVICH, T., MARSH, J.L. & GRATTON, E. (2010). A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis. Biophysical Journal 98(12), 3078-3085.
    • (2010) Biophysical Journal , vol.98 , Issue.12 , pp. 3078-3085
    • Ossato, G.1    Digman, M.A.2    Aiken, C.3    Lukacsovich, T.4    Marsh, J.L.5    Gratton, E.6
  • 23
    • 84862701723 scopus 로고    scopus 로고
    • Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells
    • PIERI, L., MADIONA, K., BOUSSET, L. & MELKI, R. (2012). Fibrillar α-synuclein and huntingtin Exon 1 assemblies are toxic to the cells. Biophysical Journal 102(12), 2894-2905.
    • (2012) Biophysical Journal , vol.102 , Issue.12 , pp. 2894-2905
    • Pieri, L.1    Madiona, K.2    Bousset, L.3    Melki, R.4
  • 24
    • 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. & ROSS, C.A. (2002). Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. Journal of Biological Chemistry 277(43), 41032-41037.
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    MacOsko, J.3    Cai, S.4    Amzel, M.5    Ross, C.A.6
  • 26
    • 78650031174 scopus 로고    scopus 로고
    • Huntington's disease: From molecular pathogenesis to clinical treatment
    • ROSS, C.A. & TABRIZI, S. J. (2011). Huntington's disease: from molecular pathogenesis to clinical treatment. Lancet Neurology 10(1), 83-98.
    • (2011) Lancet Neurology , vol.10 , Issue.1 , pp. 83-98
    • Ross, C.A.1    Tabrizi, S.J.2
  • 28
    • 84885862934 scopus 로고    scopus 로고
    • Super-resolution fluorescence imaging with single molecules
    • SAHL, S. J. & MOERNER, W. E. (2013). Super-resolution fluorescence imaging with single molecules. Current Opinion in Structural Biology 23(5), 778-787.
    • (2013) Current Opinion in Structural Biology , vol.23 , Issue.5 , pp. 778-787
    • Sahl, S.J.1    Moerner, W.E.2
  • 29
    • 84870839496 scopus 로고    scopus 로고
    • Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species
    • SAHL, S. J., WEISS, L.E., DUIM, W.C., FRYDMAN, J. & MOERNER, W.E. (2012). Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species. Scientific Reports 2, 895.
    • (2012) Scientific Reports , vol.2 , pp. 895
    • Sahl, S.J.1    Weiss, L.E.2    Duim, W.C.3    Frydman, J.4    Moerner, W.E.5
  • 30
    • 84903214409 scopus 로고    scopus 로고
    • Aggregation behavior of chemically synthesized, full-length huntingtin exon1
    • SAHOO, B., SINGER, D., KODALI, R., ZUCHNER, T. & WETZEL, R. (2014). Aggregation behavior of chemically synthesized, full-length huntingtin Exon1. Biochemistry 53(24), 3897-3907.
    • (2014) Biochemistry , vol.53 , Issue.24 , pp. 3897-3907
    • Sahoo, B.1    Singer, D.2    Kodali, R.3    Zuchner, T.4    Wetzel, R.5
  • 35
    • 84906255971 scopus 로고    scopus 로고
    • Spontaneous selfassembly of pathogenic huntingtin exon 1 protein into amyloid structures
    • TREPTE, P., STREMPEL, N. & WANKER, E. E. (2014). Spontaneous selfassembly of pathogenic huntingtin exon 1 protein into amyloid structures. Essays in Biochemistry 56(167-180).
    • (2014) Essays in Biochemistry , vol.56 , Issue.167-180
    • Trepte, P.1    Strempel, N.2    Wanker, E.E.3
  • 36
  • 37
    • 84893675019 scopus 로고    scopus 로고
    • Structural biology: Order, disorder, and conformational flux
    • (ed. G. P. BATES, TABRIZI, S.J. & JONES, L.), New York: Oxford University Press
    • WETZEL, R. & MISHRA, R. (2014). Structural Biology: Order, disorder, and conformational flux. In Huntington's Disease (ed. G. P. BATES, TABRIZI, S.J. & JONES, L.), pp. 274-322. New York: Oxford University Press.
    • (2014) Huntington's Disease , pp. 274-322
    • Wetzel, R.1    Mishra, R.2
  • 38
    • 35748933204 scopus 로고    scopus 로고
    • STED microscopy with continuous wave beams
    • WILLIG, K. I., HARKE, B., MEDDA, R. & HELL, S.W. (2007). STED microscopy with continuous wave beams. Nature Methods 4(11), 915-918.
    • (2007) Nature Methods , vol.4 , Issue.11 , pp. 915-918
    • Willig, K.I.1    Harke, B.2    Medda, R.3    Hell, S.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.