메뉴 건너뛰기




Volumn 589, Issue 15, 2015, Pages 1897-1903

Prefibrillar huntingtin oligomers isolated from HD brain potently seed amyloid formation

Author keywords

Amyloid; Huntington's disease; Neurodegeneration; Oligomer; Polyglutamine; Protein misfolding

Indexed keywords

AMYLOID; HUNTINGTIN; OLIGOMER; POLYGLUTAMINE; BIOPOLYMER; HTT PROTEIN, HUMAN; NERVE PROTEIN;

EID: 84934442982     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.05.041     Document Type: Article
Times cited : (15)

References (46)
  • 1
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group, Cell (1993) 72, 971-83.
    • (1993) Cell , vol.72 , pp. 971-983
  • 2
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • M. DiFiglia, E. Sapp, K.O. Chase, S.W. Davies, G.P. Bates, J.P. Vonsattel, and N. Aronin Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain Science 277 1997 1990 1993
    • (1997) Science , vol.277 , 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
  • 3
    • 79551655290 scopus 로고    scopus 로고
    • Huntington's disease: can mice lead the way to treatment?
    • Z.R. Crook, and D. Housman Huntington's disease: can mice lead the way to treatment? Neuron 69 2011 423 435
    • (2011) Neuron , vol.69 , pp. 423-435
    • Crook, Z.R.1    Housman, D.2
  • 7
    • 84884687047 scopus 로고    scopus 로고
    • Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model
    • M. Cushman-Nick, N.M. Bonini, and J. Shorter Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model PLoS Genet. 9 2013 e1003781
    • (2013) PLoS Genet. , vol.9
    • Cushman-Nick, M.1    Bonini, N.M.2    Shorter, J.3
  • 8
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • M. Arrasate, S. Mitra, E.S. Schweitzer, M.R. Segal, and S. Finkbeiner Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death Nature 431 2004 805 810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 10
    • 84856226648 scopus 로고    scopus 로고
    • Slow amyloid nucleation via alpha-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments
    • M. Jayaraman, R. Kodali, B. Sahoo, A.K. Thakur, A. Mayasundari, R. Mishra, C.B. Peterson, and R. Wetzel Slow amyloid nucleation via alpha-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments J. Mol. Biol. 415 2012 881 899
    • (2012) J. Mol. Biol. , vol.415 , pp. 881-899
    • Jayaraman, M.1    Kodali, R.2    Sahoo, B.3    Thakur, A.K.4    Mayasundari, A.5    Mishra, R.6    Peterson, C.B.7    Wetzel, R.8
  • 11
    • 25644434918 scopus 로고    scopus 로고
    • Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N-terminal fragments of expanded huntingtin and insoluble polymers
    • G. Hoffner, M.L. Island, and P. Djian Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N-terminal fragments of expanded huntingtin and insoluble polymers J. Neurochem. 95 2005 125 136
    • (2005) J. Neurochem. , vol.95 , pp. 125-136
    • Hoffner, G.1    Island, M.L.2    Djian, P.3
  • 13
    • 56249092747 scopus 로고    scopus 로고
    • Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells
    • A. Zameer, S. Kasturirangan, S. Emadi, S.V. Nimmagadda, and M.R. Sierks Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells J. Mol. Biol. 384 2008 917 928
    • (2008) J. Mol. Biol. , vol.384 , pp. 917-928
    • Zameer, A.1    Kasturirangan, S.2    Emadi, S.3    Nimmagadda, S.V.4    Sierks, M.R.5
  • 15
    • 77954379810 scopus 로고    scopus 로고
    • Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool
    • M.A. Olshina, L.M. Angley, Y.M. Ramdzan, J. Tang, M.F. Bailey, A.F. Hill, and D.M. Hatters Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool J. Biol. Chem. 285 2010 21807 21816
    • (2010) J. Biol. Chem. , vol.285 , pp. 21807-21816
    • Olshina, M.A.1    Angley, L.M.2    Ramdzan, Y.M.3    Tang, J.4    Bailey, M.F.5    Hill, A.F.6    Hatters, D.M.7
  • 16
  • 18
    • 77949905345 scopus 로고    scopus 로고
    • Fibrillar oligomers nucleate the oligomerization of monomeric amyloid beta but do not seed fibril formation
    • J.W. Wu, L. Breydo, J.M. Isas, J. Lee, Y.G. Kuznetsov, R. Langen, and C. Glabe Fibrillar oligomers nucleate the oligomerization of monomeric amyloid beta but do not seed fibril formation J. Biol. Chem. 285 2010 6071 6079
    • (2010) J. Biol. Chem. , vol.285 , pp. 6071-6079
    • Wu, J.W.1    Breydo, L.2    Isas, J.M.3    Lee, J.4    Kuznetsov, Y.G.5    Langen, R.6    Glabe, C.7
  • 19
    • 84898026266 scopus 로고    scopus 로고
    • Detection of misfolded Abeta oligomers for sensitive biochemical diagnosis of Alzheimer's disease
    • N. Salvadores, M. Shahnawaz, E. Scarpini, F. Tagliavini, and C. Soto Detection of misfolded Abeta oligomers for sensitive biochemical diagnosis of Alzheimer's disease Cell Rep. 7 2014 261 268
    • (2014) Cell Rep. , vol.7 , pp. 261-268
    • Salvadores, N.1    Shahnawaz, M.2    Scarpini, E.3    Tagliavini, F.4    Soto, C.5
  • 20
    • 84858964576 scopus 로고    scopus 로고
    • Protein misfolding detected early in pathogenesis of transgenic mouse model of Huntington disease using amyloid seeding assay
    • S. Gupta, S. Jie, and D.W. Colby Protein misfolding detected early in pathogenesis of transgenic mouse model of Huntington disease using amyloid seeding assay J. Biol. Chem. 287 2012 9982 9989
    • (2012) J. Biol. Chem. , vol.287 , pp. 9982-9989
    • Gupta, S.1    Jie, S.2    Colby, D.W.3
  • 23
    • 0034077939 scopus 로고    scopus 로고
    • Multiple epitope tagging of expressed proteins for enhanced detection
    • R. Hernan, K. Heuermann, and B. Brizzard Multiple epitope tagging of expressed proteins for enhanced detection Biotechniques 28 2000 789 793
    • (2000) Biotechniques , vol.28 , pp. 789-793
    • Hernan, R.1    Heuermann, K.2    Brizzard, B.3
  • 24
    • 79952371319 scopus 로고    scopus 로고
    • A kinetic aggregation assay allowing selective and sensitive amyloid-beta quantification in cells and tissues
    • D. Du, A.N. Murray, E. Cohen, H.E. Kim, R. Simkovsky, A. Dillin, and J.W. Kelly A kinetic aggregation assay allowing selective and sensitive amyloid-beta quantification in cells and tissues Biochemistry 50 2011 1607 1617
    • (2011) Biochemistry , vol.50 , pp. 1607-1617
    • Du, D.1    Murray, A.N.2    Cohen, E.3    Kim, H.E.4    Simkovsky, R.5    Dillin, A.6    Kelly, J.W.7
  • 26
    • 0035502934 scopus 로고    scopus 로고
    • New anti-huntingtin monoclonal antibodies: implications for huntingtin conformation and its binding proteins
    • J. Ko, S. Ou, and P.H. Patterson New anti-huntingtin monoclonal antibodies: implications for huntingtin conformation and its binding proteins Brain Res. Bull. 56 2001 319 329
    • (2001) Brain Res. Bull. , vol.56 , pp. 319-329
    • Ko, J.1    Ou, S.2    Patterson, P.H.3
  • 27
    • 0345701297 scopus 로고    scopus 로고
    • Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine
    • S. Iuchi, G. Hoffner, P. Verbeke, P. Djian, and H. Green Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine Proc. Natl. Acad. Sci. U.S.A. 100 2003 2409 2414
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 2409-2414
    • Iuchi, S.1    Hoffner, G.2    Verbeke, P.3    Djian, P.4    Green, H.5
  • 29
    • 62349111690 scopus 로고    scopus 로고
    • Aggregation of expanded huntingtin in the brains of patients with Huntington disease
    • G. Hoffner, S. Soues, and P. Djian Aggregation of expanded huntingtin in the brains of patients with Huntington disease Prion 1 2007 26 31
    • (2007) Prion , vol.1 , pp. 26-31
    • Hoffner, G.1    Soues, S.2    Djian, P.3
  • 33
    • 79952360891 scopus 로고    scopus 로고
    • Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent
    • K. Kar, M. Jayaraman, B. Sahoo, R. Kodali, and R. Wetzel Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent Nat. Struct. Mol. Biol. 18 2011 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
  • 35
    • 0030844513 scopus 로고    scopus 로고
    • Construction of multiple-epitope tag sequence by PCR for sensitive Western blot analysis
    • K. Nakajima, and Y. Yaoita Construction of multiple-epitope tag sequence by PCR for sensitive Western blot analysis Nucleic Acids Res. 25 1997 2231 2232
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2231-2232
    • Nakajima, K.1    Yaoita, Y.2
  • 38
    • 77956184558 scopus 로고    scopus 로고
    • Neurotoxic protein oligomerisation associated with polyglutamine diseases
    • S.L. Hands, and A. Wyttenbach Neurotoxic protein oligomerisation associated with polyglutamine diseases Acta Neuropathol. 120 2010 419 437
    • (2010) Acta Neuropathol. , vol.120 , pp. 419-437
    • Hands, S.L.1    Wyttenbach, A.2
  • 41
    • 0035084096 scopus 로고    scopus 로고
    • Solubilization and disaggregation of polyglutamine peptides
    • S. Chen, and R. Wetzel Solubilization and disaggregation of polyglutamine peptides Protein Sci. 10 2001 887 891
    • (2001) Protein Sci. , vol.10 , pp. 887-891
    • Chen, S.1    Wetzel, R.2
  • 42
    • 0034703634 scopus 로고    scopus 로고
    • Formic acid dissolves aggregates of an N-terminal huntingtin fragment containing an expanded polyglutamine tract: applying to quantification of protein components of the aggregates
    • N. Hazeki, T. Tukamoto, J. Goto, and I. Kanazawa Formic acid dissolves aggregates of an N-terminal huntingtin fragment containing an expanded polyglutamine tract: applying to quantification of protein components of the aggregates Biochem. Biophys. Res. Commun. 277 2000 386 393
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , pp. 386-393
    • Hazeki, N.1    Tukamoto, T.2    Goto, J.3    Kanazawa, I.4
  • 44
    • 44649113841 scopus 로고    scopus 로고
    • Suppression of neuropil aggregates and neurological symptoms by an intracellular antibody implicates the cytoplasmic toxicity of mutant huntingtin
    • C.E. Wang, H. Zhou, J.R. McGuire, V. Cerullo, B. Lee, S.H. Li, and X.J. Li Suppression of neuropil aggregates and neurological symptoms by an intracellular antibody implicates the cytoplasmic toxicity of mutant huntingtin J. Cell Biol. 181 2008 803 816
    • (2008) J. Cell Biol. , vol.181 , pp. 803-816
    • Wang, C.E.1    Zhou, H.2    McGuire, J.R.3    Cerullo, V.4    Lee, B.5    Li, S.H.6    Li, X.J.7
  • 46
    • 84892178364 scopus 로고    scopus 로고
    • Quantification of the concentration of Abeta42 propagons during the lag phase by an amyloid chain reaction assay
    • P. Arosio, R. Cukalevski, B. Frohm, T.P. Knowles, and S. Linse Quantification of the concentration of Abeta42 propagons during the lag phase by an amyloid chain reaction assay J. Am. Chem. Soc. 136 2014 219 225
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 219-225
    • Arosio, P.1    Cukalevski, R.2    Frohm, B.3    Knowles, T.P.4    Linse, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.