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Volumn 426, Issue 4, 2014, Pages 816-829

D-polyglutamine amyloid recruits l-polyglutamine monomers and kills cells

Author keywords

chiral cross seeding; Huntington's disease; recruitment; rippled sheet; toxicity

Indexed keywords

AMYLOID; MONOMER; POLYGLUTAMINE; SYNTHETIC PEPTIDE; DEXTRO POLYGLUTAMINE AMYLOID; GLUTAMINE; LEVO POLYGLUTAMINE MONOMER; UNCLASSIFIED DRUG;

EID: 84893649786     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.11.019     Document Type: Article
Times cited : (35)

References (74)
  • 1
    • 3242692878 scopus 로고    scopus 로고
    • The polyglutamine diseases
    • G.P. Bates, P.S. Harper, L. Jones, 3rd ed. Oxford University Press Oxford, UK
    • G.P. Bates, and C. Benn The polyglutamine diseases G.P. Bates, P.S. Harper, L. Jones, Huntington's Disease 3rd ed. 2002 Oxford University Press Oxford, UK 429 472
    • (2002) Huntington's Disease , pp. 429-472
    • Bates, G.P.1    Benn, C.2
  • 2
    • 77955643169 scopus 로고    scopus 로고
    • Molecular mechanisms and potential therapeutical targets in Huntington's disease
    • C. Zuccato, M. Valenza, and E. Cattaneo Molecular mechanisms and potential therapeutical targets in Huntington's disease Physiol Rev 90 2010 905 981
    • (2010) Physiol Rev , vol.90 , pp. 905-981
    • Zuccato, C.1    Valenza, M.2    Cattaneo, E.3
  • 3
    • 78650031174 scopus 로고    scopus 로고
    • Huntington's disease: From molecular pathogenesis to clinical treatment
    • C.A. Ross, and S.J. Tabrizi Huntington's disease: from molecular pathogenesis to clinical treatment Lancet Neurol 10 2011 83 98
    • (2011) Lancet Neurol , vol.10 , pp. 83-98
    • Ross, C.A.1    Tabrizi, S.J.2
  • 5
    • 33745616511 scopus 로고    scopus 로고
    • If it's not one thing, it's another
    • DOI 10.1038/ng0706-743, PII N0706743
    • H.L. Paulson If it's not one thing, it's another Nat Genet 38 2006 743 744 (Pubitemid 43982547)
    • (2006) Nature Genetics , vol.38 , Issue.7 , pp. 743-744
    • Paulson, H.L.1
  • 6
    • 79955660764 scopus 로고    scopus 로고
    • An antisense CAG repeat transcript at JPH3 locus mediates expanded polyglutamine protein toxicity in Huntington's disease-like 2 mice
    • B. Wilburn, D.D. Rudnicki, J. Zhao, T.M. Weitz, Y. Cheng, and X.F. Gu et al. An antisense CAG repeat transcript at JPH3 locus mediates expanded polyglutamine protein toxicity in Huntington's disease-like 2 mice Neuron 70 2011 427 440
    • (2011) Neuron , vol.70 , pp. 427-440
    • Wilburn, B.1    Rudnicki, D.D.2    Zhao, J.3    Weitz, T.M.4    Cheng, Y.5    Gu, X.F.6
  • 7
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DOI 10.1126/science.277.5334.1990
    • M. DiFiglia, E. Sapp, K.O. Chase, S.W. Davies, G.P. Bates, and J.P. Vonsattel et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain Science 277 1997 1990 1993 (Pubitemid 27449140)
    • (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
    • 77649297870 scopus 로고    scopus 로고
    • Identical oligomeric and fibrillar structures captured from the brains of R6/2 and knock-in mouse models of Huntington's disease
    • K. Sathasivam, A. Lane, J. Legleiter, A. Warley, B. Woodman, and S. Finkbeiner et al. Identical oligomeric and fibrillar structures captured from the brains of R6/2 and knock-in mouse models of Huntington's disease Hum Mol Genet 19 2010 65 78
    • (2010) Hum Mol Genet , vol.19 , pp. 65-78
    • Sathasivam, K.1    Lane, A.2    Legleiter, J.3    Warley, A.4    Woodman, B.5    Finkbeiner, S.6
  • 11
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • DOI 10.1006/jmbi.2001.4850
    • S. Chen, V. Berthelier, W. Yang, and R. Wetzel Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity J Mol Biol 311 2001 173 182 (Pubitemid 32735322)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.1 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3    Wetzel, R.4
  • 12
    • 84863990252 scopus 로고    scopus 로고
    • Physical chemistry of polyglutamine: Intriguing tales of a monotonous sequence
    • R. Wetzel Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence J Mol Biol 421 2012 466 490
    • (2012) J Mol Biol , vol.421 , pp. 466-490
    • Wetzel, R.1
  • 13
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • J.F. Morley, H.R. Brignull, J.J. Weyers, and R.I. Morimoto The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans Proc Natl Acad Sci U S A 99 2002 10417 10422
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 14
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • DOI 10.1038/nature02998
    • 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 (Pubitemid 39434070)
    • (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
  • 15
    • 84870839496 scopus 로고    scopus 로고
    • Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species
    • S.J. Sahl, L.E. Weiss, W.C. Duim, J. Frydman, and W.E. Moerner Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species Sci Rep 2 2012 895
    • (2012) Sci Rep , vol.2 , pp. 895
    • Sahl, S.J.1    Weiss, L.E.2    Duim, W.C.3    Frydman, J.4    Moerner, W.E.5
  • 16
    • 84893675019 scopus 로고    scopus 로고
    • Structural biology: Order, disorder, and conformational flux
    • G.P. Bates, S.J. Tabrizi, L. Jones, 4th ed. Oxford University Press Oxford, UK [in press]
    • R. Wetzel Structural biology: order, disorder, and conformational flux G.P. Bates, S.J. Tabrizi, L. Jones, Huntington's Disease 4th ed. 2014 Oxford University Press Oxford, UK [in press]
    • (2014) Huntington's Disease
    • Wetzel, R.1
  • 17
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
    • W. Yang, J.R. Dunlap, R.B. Andrews, and R. Wetzel Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells Hum Mol Genet 11 2002 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
  • 18
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • Y. Nekooki-Machida, M. Kurosawa, N. Nukina, K. Ito, T. Oda, and M. Tanaka Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity Proc Natl Acad Sci U S A 106 2009 9679 9684
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 19
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine- mediated aggregation
    • DOI 10.1083/jcb.143.6.1457
    • M.K. Perez, H.L. Paulson, S.J. Pendse, S.J. Saionz, N.M. Bonini, and R.N. Pittman Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation J Cell Biol 143 1998 1457 1470 (Pubitemid 29006496)
    • (1998) Journal of Cell Biology , vol.143 , Issue.6 , pp. 1457-1470
    • Perez, M.K.1    Paulson, H.L.2    Pendse, S.J.3    Saionz, S.J.4    Bonini, N.M.5    Pittman, R.N.6
  • 21
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • DOI 10.1126/science.1105850
    • A.T. Petkova, R.D. Leapman, Z. Guo, W.M. Yau, M.P. Mattson, and R. Tycko Self-propagating, molecular-level polymorphism in Alzheimer's b-amyloid fibrils Science 307 2005 262 265 (Pubitemid 40116242)
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 22
    • 2342444028 scopus 로고    scopus 로고
    • Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils
    • DOI 10.1074/jbc.M311300200
    • B. O'Nuallain, A.D. Williams, P. Westermark, and R. Wetzel Seeding specificity in amyloid growth induced by heterologous fibrils J Biol Chem 279 2004 17490 17499 (Pubitemid 38560512)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17490-17499
    • O'Nuallain, B.1    Williams, A.D.2    Westermark, P.3    Wetzel, R.4
  • 23
    • 3042675121 scopus 로고    scopus 로고
    • Observation of sequence specificity in the seeding of protein amyloid fibrils
    • DOI 10.1110/ps.04707004
    • M.R. Krebs, L.A. Morozova-Roche, K. Daniel, C.V. Robinson, and C.M. Dobson Observation of sequence specificity in the seeding of protein amyloid fibrils Protein Sci 13 2004 1933 1938 (Pubitemid 38822133)
    • (2004) Protein Science , vol.13 , Issue.7 , pp. 1933-1938
    • Krebs, M.R.H.1    Morozova-Roche, L.A.2    Daniel, K.3    Robinson, C.V.4    Dobson, C.M.5
  • 26
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • P.H. Ren, J.E. Lauckner, I. Kachirskaia, J.E. Heuser, R. Melki, and R.R. Kopito Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates Nat Cell Biol 11 2009 219 U232
    • (2009) Nat Cell Biol , vol.11
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 27
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • DOI 10.1021/bi011772q
    • S. Chen, V. Berthelier, J.B. Hamilton, B. O'Nuallain, and R. Wetzel Amyloid-like features of polyglutamine aggregates and their assembly kinetics Biochemistry 41 2002 7391 7399 (Pubitemid 34602457)
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7391-7399
    • Chen, S.1    Berthelier, V.2    Hamilton, J.B.3    O'Nuallain, B.4    Wetzel, R.5
  • 29
    • 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, and R. Mishra et al. 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
  • 30
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
    • DOI 10.1016/0003-2697(89)90046-8
    • H. Naiki, K. Higuchi, M. Hosokawa, and T. Takeda Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T Anal Biochem 177 1989 244 249 (Pubitemid 19088253)
    • (1989) Analytical Biochemistry , vol.177 , Issue.2 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 31
    • 0026686436 scopus 로고
    • Total chemical synthesis of a d-enzyme: The enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected]
    • R.C. Milton, S.C. Milton, and S.B. Kent Total chemical synthesis of a d-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected] Science 256 1992 1445 1448
    • (1992) Science , vol.256 , pp. 1445-1448
    • Milton, R.C.1    Milton, S.C.2    Kent, S.B.3
  • 32
    • 3242723420 scopus 로고    scopus 로고
    • A cell-based screen for drugs to treat Huntington's disease
    • DOI 10.1016/j.nbd.2004.04.001, PII S0969996104000828
    • C.T. Aiken, A.J. Tobin, and E.S. Schweitzer A cell-based screen for drugs to treat Huntington's disease Neurobiol Dis 16 2004 546 555 (Pubitemid 38942987)
    • (2004) Neurobiology of Disease , vol.16 , Issue.3 , pp. 546-555
    • Aiken, C.T.1    Tobin, A.J.2    Schweitzer, E.S.3
  • 33
    • 0035502934 scopus 로고    scopus 로고
    • New anti-huntingtin monoclonal antibodies: Implications for huntingtin conformation and its binding proteins
    • DOI 10.1016/S0361-9230(01)00599-8, PII S0361923001005998
    • 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 (Pubitemid 33062356)
    • (2001) Brain Research Bulletin , vol.56 , Issue.3-4 , pp. 319-329
    • Ko, J.1    Ou, S.2    Patterson, P.H.3
  • 35
    • 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
  • 38
    • 67651098677 scopus 로고    scopus 로고
    • Aggregation of amyloidogenic peptides near hydrophobic and hydrophilic surfaces
    • I. Brovchenko, G. Singh, and R. Winter Aggregation of amyloidogenic peptides near hydrophobic and hydrophilic surfaces Langmuir 25 2009 8111 8116
    • (2009) Langmuir , vol.25 , pp. 8111-8116
    • Brovchenko, I.1    Singh, G.2    Winter, R.3
  • 40
    • 1842686289 scopus 로고    scopus 로고
    • Kinetic analysis of beta-amyloid fibril elongation
    • DOI 10.1016/j.ab.2004.01.014, PII S0003269704000922
    • M.J. Cannon, A.D. Williams, R. Wetzel, and D.G. Myszka Kinetic analysis of beta-amyloid fibril elongation Anal Biochem 328 2004 67 75 (Pubitemid 38479619)
    • (2004) Analytical Biochemistry , vol.328 , Issue.1 , pp. 67-75
    • Cannon, M.J.1    Williams, A.D.2    Wetzel, R.3    Myszka, D.G.4
  • 42
    • 14044278010 scopus 로고    scopus 로고
    • New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils
    • DOI 10.1021/bm0494388
    • P. Sikorski, and E. Atkins New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils Biomacromolecules 6 2005 425 432 (Pubitemid 40277042)
    • (2005) Biomacromolecules , vol.6 , Issue.1 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 43
    • 0001402095 scopus 로고
    • Two rippled-sheet configurations of polypeptide chains, and a note about the pleated sheets
    • L. Pauling, and R.B. Corey Two rippled-sheet configurations of polypeptide chains, and a note about the pleated sheets Proc Natl Acad Sci U S A 39 1953 253 256
    • (1953) Proc Natl Acad Sci U S A , vol.39 , pp. 253-256
    • Pauling, L.1    Corey, R.B.2
  • 44
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • J.S. Griffith Self-replication and scrapie Nature 215 1967 1043 1044
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 45
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • J.T. Jarrett, and P.J. Lansbury Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? [Review] Cell 73 1993 1055 1058 (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 46
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • DOI 10.1038/35081095
    • G.P. Saborio, B. Permanne, and C. Soto Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding Nature 411 2001 810 813 (Pubitemid 32588105)
    • (2001) Nature , vol.411 , Issue.6839 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 47
    • 0042358923 scopus 로고    scopus 로고
    • Generation of prion transmission barriers by mutational control of amyloid conformations
    • DOI 10.1038/nature01894
    • P. Chien, A.H. DePace, S.R. Collins, and J.S. Weissman Generation of prion transmission barriers by mutational control of amyloid conformations Nature 424 2003 948 951 (Pubitemid 37051686)
    • (2003) Nature , vol.424 , Issue.6951 , pp. 948-951
    • Chien, P.1    DePace, A.H.2    Collins, S.R.3    Weissman, J.S.4
  • 48
    • 67649286622 scopus 로고    scopus 로고
    • Cell biology: Beyond the prion principle
    • A. Aguzzi Cell biology: beyond the prion principle Nature 459 2009 924 925
    • (2009) Nature , vol.459 , pp. 924-925
    • Aguzzi, A.1
  • 49
    • 1642388486 scopus 로고    scopus 로고
    • Enantioselective molecular recognition between beta-sheets
    • D.M. Chung, and J.S. Nowick Enantioselective molecular recognition between beta-sheets J Am Chem Soc 126 2004 3062 3063
    • (2004) J Am Chem Soc , vol.126 , pp. 3062-3063
    • Chung, D.M.1    Nowick, J.S.2
  • 50
    • 1642299396 scopus 로고    scopus 로고
    • The Diastereomeric Assembly of Polylysine is the Low-Volume Pathway for Preferential Formation of β-Sheet Aggregates
    • DOI 10.1021/ja039138i
    • W. Dzwolak, R. Ravindra, C. Nicolini, R. Jansen, and R. Winter The diastereomeric assembly of polylysine is the low-volume pathway for preferential formation of beta-sheet aggregates J Am Chem Soc 126 2004 3762 3768 (Pubitemid 38391869)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.12 , pp. 3762-3768
    • Dzwolak, W.1    Ravindra, R.2    Nicolini, C.3    Jansen, R.4    Winter, R.5
  • 51
    • 84859125703 scopus 로고    scopus 로고
    • Coassembly of enantiomeric amphipathic peptides into amyloid-inspired rippled β-sheet fibrils
    • R.J. Swanekamp, J.T. Dimaio, C.J. Bowerman, and B.L. Nilsson Coassembly of enantiomeric amphipathic peptides into amyloid-inspired rippled β-sheet fibrils J Am Chem Soc 134 2012 5556 5559
    • (2012) J Am Chem Soc , vol.134 , pp. 5556-5559
    • Swanekamp, R.J.1    Dimaio, J.T.2    Bowerman, C.J.3    Nilsson, B.L.4
  • 52
    • 29344462783 scopus 로고    scopus 로고
    • Structural control of self-assembled nanofibers by artificial β-sheet peptides composed of D- or L-isomer
    • DOI 10.1021/ja0558387
    • T. Koga, M. Matsuoka, and N. Higashi Structural control of self-assembled nanofibers by artificial beta-sheet peptides composed of d- or l-isomer J Am Chem Soc 127 2005 17596 17597 (Pubitemid 43003361)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.50 , pp. 17596-17597
    • Koga, T.1    Matsuoka, M.2    Higashi, N.3
  • 53
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • DOI 10.1038/nature04922, PII NATURE04922
    • M. Tanaka, S.R. Collins, B.H. Toyama, and J.S. Weissman The physical basis of how prion conformations determine strain phenotypes Nature 442 2006 585 589 (Pubitemid 44167919)
    • (2006) Nature , vol.442 , Issue.7102 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 54
    • 84883541737 scopus 로고    scopus 로고
    • PolyQ disease: Misfiring of a developmental cell death program?
    • E.S. Blum, A.R. Schwendeman, and S. Shaham PolyQ disease: misfiring of a developmental cell death program? Trends Cell Biol 23 2013 168 174
    • (2013) Trends Cell Biol , vol.23 , pp. 168-174
    • Blum, E.S.1    Schwendeman, A.R.2    Shaham, S.3
  • 56
    • 84870057666 scopus 로고    scopus 로고
    • Origins of Alzheimer's disease: Reconciling cerebrospinal fluid biomarker and neuropathology data regarding the temporal sequence of amyloid-beta and tau involvement
    • E.S. Musiek, and D.M. Holtzman Origins of Alzheimer's disease: reconciling cerebrospinal fluid biomarker and neuropathology data regarding the temporal sequence of amyloid-beta and tau involvement Curr Opin Neurol 25 2012 715 720
    • (2012) Curr Opin Neurol , vol.25 , pp. 715-720
    • Musiek, E.S.1    Holtzman, D.M.2
  • 58
    • 84869887960 scopus 로고    scopus 로고
    • Structural features and cytotoxicity of amyloid oligomers: Implications in Alzheimer's disease and other diseases with amyloid deposits
    • M. Stefani Structural features and cytotoxicity of amyloid oligomers: implications in Alzheimer's disease and other diseases with amyloid deposits Prog Neurobiol 99 2012 226 245
    • (2012) Prog Neurobiol , vol.99 , pp. 226-245
    • Stefani, M.1
  • 59
    • 84862501578 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Expanded glutamines enhance native functions
    • H.T. Orr Polyglutamine neurodegeneration: expanded glutamines enhance native functions Curr Opin Genet Dev 22 2012 251 255
    • (2012) Curr Opin Genet Dev , vol.22 , pp. 251-255
    • Orr, H.T.1
  • 60
    • 84865770337 scopus 로고    scopus 로고
    • An in vitro perspective on the molecular mechanisms underlying mutant huntingtin protein toxicity
    • G. Cisbani, and F. Cicchetti An in vitro perspective on the molecular mechanisms underlying mutant huntingtin protein toxicity Cell Death Dis 3 2012 e382
    • (2012) Cell Death Dis , vol.3 , pp. 382
    • Cisbani, G.1    Cicchetti, F.2
  • 61
    • 84875599536 scopus 로고    scopus 로고
    • Mitochondria-associated ER membranes in Alzheimer disease
    • E.A. Schon, and E. Area-Gomez Mitochondria-associated ER membranes in Alzheimer disease Mol Cell Neurosci 55 2013 26 36
    • (2013) Mol Cell Neurosci , vol.55 , pp. 26-36
    • Schon, E.A.1    Area-Gomez, E.2
  • 63
    • 79959778716 scopus 로고    scopus 로고
    • Huntingtin affinity for partners is not changed by polyglutamine length: Aggregation itself triggers aberrant interactions
    • A. Davranche, H. Aviolat, G. Zeder-Lutz, D. Busso, D. Altschuh, and Y. Trottier et al. Huntingtin affinity for partners is not changed by polyglutamine length: aggregation itself triggers aberrant interactions Hum Mol Genet 20 2011 2795 2806
    • (2011) Hum Mol Genet , vol.20 , pp. 2795-2806
    • Davranche, A.1    Aviolat, H.2    Zeder-Lutz, G.3    Busso, D.4    Altschuh, D.5    Trottier, Y.6
  • 65
    • 84862680862 scopus 로고    scopus 로고
    • Proteomic analysis of wild-type and mutant huntingtin-associated proteins in mouse brains identifies unique interactions and involvement in protein synthesis
    • B.P. Culver, J.N. Savas, S.K. Park, J.H. Choi, S. Zheng, and S.O. Zeitlin et al. Proteomic analysis of wild-type and mutant huntingtin-associated proteins in mouse brains identifies unique interactions and involvement in protein synthesis J Biol Chem 287 2012 21599 21614
    • (2012) J Biol Chem , vol.287 , pp. 21599-21614
    • Culver, B.P.1    Savas, J.N.2    Park, S.K.3    Choi, J.H.4    Zheng, S.5    Zeitlin, S.O.6
  • 66
    • 84893674793 scopus 로고    scopus 로고
    • PhD Dissertation, The University of Tennessee, ProQuest, UMI Dissertations Publishing, document number 3151870
    • Yang, W (2003). The role of polyglutamine aggregate cytotoxicity in Huntington's disease. PhD Dissertation, The University of Tennessee, ProQuest, UMI Dissertations Publishing, document number 3151870
    • (2003) The Role of Polyglutamine Aggregate Cytotoxicity in Huntington's Disease
    • Yang, W.1
  • 70
    • 0035031779 scopus 로고    scopus 로고
    • Polyglutamine and CBP: Fatal attraction?
    • DOI 10.1038/87842
    • A. McCampbell, and K.H. Fischbeck Polyglutamine and CBP: fatal attraction? Nat Med 7 2001 528 530 (Pubitemid 32448308)
    • (2001) Nature Medicine , vol.7 , Issue.5 , pp. 528-530
    • McCampbell, A.1    Fischbeck, K.H.2
  • 71
    • 23444458415 scopus 로고
    • Transcriptional activation modulated by homopolymeric glutamine and proline stretches
    • H.P. Gerber, K. Seipel, O. Georgiev, M. Hofferer, M. Hug, and S. Rusconi et al. Transcriptional activation modulated by homopolymeric glutamine and proline stretches Science 263 1994 808 811 (Pubitemid 24093208)
    • (1994) Science , vol.263 , Issue.5148 , pp. 808-811
    • Gerber, H.-P.1    Seipel, K.2    Georgiev, O.3    Hofferer, M.4    Hug, M.5    Rusconi, S.6    Schaffner, W.7
  • 72
    • 4644334088 scopus 로고    scopus 로고
    • Inhibition of polyglutamine aggregate cytotoxicity by a structure-based elongation inhibitor
    • A.K. Thakur, W. Yang, and R. Wetzel Inhibition of polyglutamine aggregate cytotoxicity by a structure-based elongation inhibitor FASEB J 18 2004 923 925
    • (2004) FASEB J , vol.18 , pp. 923-925
    • Thakur, A.K.1    Yang, W.2    Wetzel, R.3
  • 73
    • 33749251222 scopus 로고    scopus 로고
    • Kinetics and Thermodynamics of Amyloid Assembly Using a High-Performance Liquid Chromatography-Based Sedimentation Assay
    • DOI 10.1016/S0076-6879(06)13003-7, PII S0076687906130037, Amyloid, Prions, and Other Protein Aggregates, Part C
    • B. O'Nuallain, A.K. Thakur, A.D. Williams, A.M. Bhattacharyya, S. Chen, and G. Thiagarajan et al. Kinetics and thermodynamics of amyloid assembly using a high-performance liquid chromatography-based sedimentation assay Methods Enzymol 413 2006 34 74 (Pubitemid 44528684)
    • (2006) Methods in Enzymology , vol.413 , pp. 34-74
    • O'Nuallain, B.1    Thakur, A.K.2    Williams, A.D.3    Bhattacharyya, A.M.4    Chen, S.5    Thiagarajan, G.6    Wetzel, R.7
  • 74
    • 0025296985 scopus 로고
    • Localization of human growth hormone to a sub-set of cytoplasmic vesicles in transfected PC12 cells
    • E.S. Schweitzer, and S. Paddock Localization of human growth hormone to a sub-set of cytoplasmic vesicles in transfected PC12 cells J Cell Sci 96 1990 375 381
    • (1990) J Cell Sci , vol.96 , pp. 375-381
    • Schweitzer, E.S.1    Paddock, S.2


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