메뉴 건너뛰기




Volumn 12, Issue 22, 2012, Pages 2611-2622

Putting huntingtin "aggregation" in view with windows into the cellular milieu

Author keywords

Aggregation; Huntingtin; Huntington's disease (HD); Misfolding; Polyglutamine (polyQ)

Indexed keywords

CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; HEAT SHOCK PROTEIN 70; HUNTINGTIN; POLYGLUTAMINE;

EID: 84874872486     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026611212220013     Document Type: Review
Times cited : (16)

References (154)
  • 2
    • 0034847765 scopus 로고    scopus 로고
    • Juvenile onset Huntington's disease-clinical and research perspectives
    • Nance, M. A.; Myers, R. H., Juvenile onset Huntington's disease-clinical and research perspectives. Ment. Retard. Dev. Disabil. Res. Rev., 2001, 7 (3), 153-157.
    • (2001) Ment. Retard. Dev. Disabil. Res. Rev , vol.7 , Issue.3 , pp. 153-157
    • Nance, M.A.1    Myers, R.H.2
  • 4
    • 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., Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain. Science, 1997, 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
  • 6
    • 77950547661 scopus 로고    scopus 로고
    • Formation of polyglutamine inclusions in a wide range of non-CNS tissues in the HdhQ150 knock-in mouse model of Huntington's disease
    • Moffitt, H.; McPhail, G. D.; Woodman, B.; Hobbs, C; Bates, G. P., Formation of polyglutamine inclusions in a wide range of non-CNS tissues in the HdhQ150 knock-in mouse model of Huntington's disease. PLoS ONE, 2009, 4 (11), e8025.
    • (2009) PLoS ONE , vol.4 , Issue.11
    • Moffitt, H.1    McPhail, G.D.2    Woodman, B.3    Hobbs, C.4    Bates, G.P.5
  • 7
    • 14044278010 scopus 로고    scopus 로고
    • New Model for Crystalline Polyglutamine Assemblies and Their Connection with Amyloid Fibrils
    • Sikorski, P.; Atkins, E., New Model for Crystalline Polyglutamine Assemblies and Their Connection with Amyloid Fibrils. Biomacromolecules, 2004, 6 (1), 425-432.
    • (2004) Biomacromolecules , vol.6 , Issue.1 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 8
    • 26444575834 scopus 로고    scopus 로고
    • Polyglutamine homopolymers having 8-45 residues form slablike p-crystallite assemblies
    • Sharma, D.; Shinchuk, L. M.; Inouye, H.; Wetzel, R.; Kirschner, D. A., Polyglutamine homopolymers having 8-45 residues form slablike p-crystallite assemblies. Proteins, 2005, 61 (2), 398-411.
    • (2005) Proteins , vol.61 , Issue.2 , pp. 398-411
    • Sharma, D.1    Shinchuk, L.M.2    Inouye, H.3    Wetzel, R.4    Kirschner, D.A.5
  • 9
    • 77955647254 scopus 로고    scopus 로고
    • Towards the treatment of polyglutamine diseases: The modulatory role of protein context
    • Robertson, A. L.; Bottomley, S. P., Towards the treatment of polyglutamine diseases: the modulatory role of protein context. Curr. Med. Chem., 2010, 17 (27), 3058-3068.
    • (2010) Curr. Med. Chem , vol.17 , Issue.27 , pp. 3058-3068
    • Robertson, A.L.1    Bottomley, S.P.2
  • 10
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, and Human Disease
    • Chiti, F.; Dobson, C. M., Protein Misfolding, Functional Amyloid, and Human Disease. Ann. Rev. Biochem., 2006, 75 (1), 333-366.
    • (2006) Ann. Rev. Biochem , vol.75 , Issue.1 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 13
    • 77953536158 scopus 로고    scopus 로고
    • Roles of trinucleotide-repeat RNA in neurological disease and degeneration
    • Li, L.-B.; Bonini, N. M., Roles of trinucleotide-repeat RNA in neurological disease and degeneration. Trends Neurosci., 2010, 33 (6), 292-298.
    • (2010) Trends Neurosci , vol.33 , Issue.6 , pp. 292-298
    • Li, L.-B.1    Bonini, N.M.2
  • 16
    • 78649315112 scopus 로고    scopus 로고
    • Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis
    • Sipe, J. D.; Benson, M. D.; Buxbaum, J. N.; Ikeda, S.-I.; Merlini, G.; Saraiva, M. J. M.; Westermark, P., Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis. Amyloid, 2010, 17 (3-4), 101-104.
    • (2010) Amyloid , vol.17 , Issue.3-4 , pp. 101-104
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.-I.4    Merlini, G.5    Saraiva, M.J.M.6    Westermark, P.7
  • 17
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J. W., The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol., 1998, 8 (1), 101-106.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , Issue.1 , pp. 101-106
    • Kelly, J.W.1
  • 18
    • 0347357617 scopus 로고    scopus 로고
    • Protein Folding and Misfolding
    • Dobson, C. M., Protein Folding and Misfolding. Nature, 2003, 426 (6968), 884-890.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 19
  • 20
    • 58149352666 scopus 로고    scopus 로고
    • Protein Misfolding Inside Cells: The Case of Huntingtin and Huntington's Disease
    • Hatters, D. M., Protein Misfolding Inside Cells: The Case of Huntingtin and Huntington's Disease. IUBMB life, 2008, 60 (11), 724-728.
    • (2008) IUBMB Life , vol.60 , Issue.11 , pp. 724-728
    • Hatters, D.M.1
  • 25
    • 84861206757 scopus 로고    scopus 로고
    • Toxic fibrillar oligomers of amyloid-p have cross-p structure
    • Stroud, J. C; Liu, C; Teng, P. K.; Eisenberg, D., Toxic fibrillar oligomers of amyloid-p have cross-p structure. Proc. Natl. Acad. Sci. USA, 2012, 109 (20), 7717-7722.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , Issue.20 , pp. 7717-7722
    • Stroud, J.C.1    Liu, C.2    Teng, P.K.3    Eisenberg, D.4
  • 27
    • 0033613212 scopus 로고    scopus 로고
    • Insoluble Detergent-resistant Aggregates Form Between Pathological and Nonpathological Lengths of Polyglutamine in Mammalian Cells
    • Kazantsev, A.; Preisinger, E.; Dranovsky, A.; Goldgaber, D.; Housman, D., Insoluble Detergent-resistant Aggregates Form Between Pathological and Nonpathological Lengths of Polyglutamine in Mammalian Cells. Proc. Natl. Acad. Sci. USA, 1999, 96 (20), 11404-11409.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.20 , pp. 11404-11409
    • Kazantsev, A.1    Preisinger, E.2    Dranovsky, A.3    Goldgaber, D.4    Housman, D.5
  • 30
    • 0037047123 scopus 로고    scopus 로고
    • Live-cell Imaging Reveals Divergent Intracellular Dynamics of Polyglutamine Disease Proteins and Supports a Sequestration Model of Pathogenesis
    • Chai, Y.; Shao, J.; Miller, V. M.; Williams, A.; Paulson, H. L., Live-cell Imaging Reveals Divergent Intracellular Dynamics of Polyglutamine Disease Proteins and Supports a Sequestration Model of Pathogenesis. Proc. Natl. Acad. Sci. USA, 2002, 99 (14), 9310-9315.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.14 , pp. 9310-9315
    • Chai, Y.1    Shao, J.2    Miller, V.M.3    Williams, A.4    Paulson, H.L.5
  • 31
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin Acts in the Nucleus to Induce Apoptosis but Death Does Not Correlate with the Formation of Intranuclear Inclusions
    • Saudou, F.; Finkbeiner, S.; Devys, D.; Greenberg, M. E., Huntingtin Acts in the Nucleus to Induce Apoptosis but Death Does Not Correlate with the Formation of Intranuclear Inclusions. Cell, 1998, 95 (1), 55-66.
    • (1998) Cell , vol.95 , Issue.1 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 32
    • 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., Inclusion Body Formation Reduces Levels of Mutant Huntingtin and the Risk of Neuronal Death. Nature, 2004, 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
  • 34
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J. A.; Ward, C. L.; Kopito, R. R., Aggresomes: a cellular response to misfolded proteins. J. Cell Biol., 1998, 143 (7), 1883-1898.
    • (1998) J. Cell Biol , vol.143 , Issue.7 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 35
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
    • Garcia-Mata, R.; Bebok, Z.; Sorscher, E. J.; Sztul, E. S., Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J. Cell Biol., 1999, 146 (6), 1239-1254.
    • (1999) J. Cell Biol , vol.146 , Issue.6 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 36
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, Inclusion Bodies and Protein Aggregation
    • Kopito, R. R., Aggresomes, Inclusion Bodies and Protein Aggregation. Trends Cell Biol., 2000, 10 (12), 524.
    • (2000) Trends Cell Biol , vol.10 , Issue.12 , pp. 524
    • Kopito, R.R.1
  • 37
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of Mutant Huntingtin Fragments in Aggresome-like Inclusion Bodies as a Result of Insufficient Protein Degradation
    • Waelter, S.; Boeddrich, A.; Lurz, R.; Scherzinger, E.; Lueder, G.; Lehrach, H.; Wanker, E. E., Accumulation of Mutant Huntingtin Fragments in Aggresome-like Inclusion Bodies as a Result of Insufficient Protein Degradation. Mol. Biol. Cell, 2001, 12 (5), 1393-1407.
    • (2001) Mol. Biol. Cell , vol.12 , Issue.5 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6    Wanker, E.E.7
  • 38
    • 0037154229 scopus 로고    scopus 로고
    • Requirement of an intact microtubule cytoskeleton for aggregation and inclusion body formation by a mutant huntingtin fragment
    • Muchowski, P. J.; Ning, K.; D'Souza-Schorey, C.; Fields, S., Requirement of an intact microtubule cytoskeleton for aggregation and inclusion body formation by a mutant huntingtin fragment. Proc. Natl. Acad. Sci. USA, 2002, 99 (2), 727-732.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.2 , pp. 727-732
    • Muchowski, P.J.1    Ning, K.2    D'souza-Schorey, C.3    Fields, S.4
  • 39
    • 59649096550 scopus 로고    scopus 로고
    • Abnormal Proteins can form Aggresome in Yeast: Aggresome-targeting Signals and Components of the Machinery
    • Wang, Y.; Meriin, A. B.; Zaarur, N.; Romanova, N. V.; Chernoff, Y. O.; Costello, C. E.; Sherman, M. Y., Abnormal Proteins can form Aggresome in Yeast: Aggresome-targeting Signals and Components of the Machinery. FASEB J., 2009, 23 (2), 451-463.
    • (2009) FASEB J , vol.23 , Issue.2 , pp. 451-463
    • Wang, Y.1    Meriin, A.B.2    Zaarur, N.3    Romanova, N.V.4    Chernoff, Y.O.5    Costello, C.E.6    Sherman, M.Y.7
  • 40
    • 0035818579 scopus 로고    scopus 로고
    • Specificity in intracellular protein aggregation and inclusion body formation
    • Rajan, R. S.; Illing, M. E.; Bence, N. F.; Kopito, R. R., Specificity in intracellular protein aggregation and inclusion body formation. Proc. Natl. Acad. Sci. USA, 2001, 98 (23), 13060-13065.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.23 , pp. 13060-13065
    • Rajan, R.S.1    Illing, M.E.2    Bence, N.F.3    Kopito, R.R.4
  • 41
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded Proteins Partition Between Two Distinct Quality Control Compartments
    • Kaganovich, D.; Kopito, R.; Frydman, J., Misfolded Proteins Partition Between Two Distinct Quality Control Compartments. Nature, 2008, 454 (7208), 1088-1095.
    • (2008) Nature , vol.454 , Issue.7208 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 42
    • 33645214602 scopus 로고    scopus 로고
    • Huntingtin and Mutant SOD1 Form Aggregate Structures with Distinct Molecular Properties in Human Cells
    • Matsumoto, G.; Kim, S.; Morimoto, R. I., Huntingtin and Mutant SOD1 Form Aggregate Structures with Distinct Molecular Properties in Human Cells. J. Biol. Chem., 2006, 281 (7), 4477-4485.
    • (2006) J. Biol. Chem , vol.281 , Issue.7 , pp. 4477-4485
    • Matsumoto, G.1    Kim, S.2    Morimoto, R.I.3
  • 44
    • 5044239107 scopus 로고    scopus 로고
    • Pathways of Chaperone-Mediated Protein Folding in the Cytosol
    • Young, J. C.; Agashe, V. R.; Siegers, K.; Hartl, F. U., Pathways of Chaperone-Mediated Protein Folding in the Cytosol. Nat. Rev. Mol. Cell. Biol., 2004, 5 (10), 781-791.
    • (2004) Nat. Rev. Mol. Cell. Biol , vol.5 , Issue.10 , pp. 781-791
    • Young, J.C.1    Agashe, V.R.2    Siegers, K.3    Hartl, F.U.4
  • 45
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: A unique way to enter the lysosome world
    • Kaushik, S.; Cuervo, A. M., Chaperone-mediated autophagy: a unique way to enter the lysosome world. Trends Cell Biol., 2012, 22 (8), 407-417.
    • (2012) Trends Cell Biol , vol.22 , Issue.8 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 46
    • 23144443884 scopus 로고    scopus 로고
    • Protein quality control: Chaperones culling corrupt conformations
    • McClellan, A. J.; Tam, S.; Kaganovich, D.; Frydman, J., Protein quality control: chaperones culling corrupt conformations. Nature Cell Biol., 2005, 7 (8), 736-741.
    • (2005) Nature Cell Biol , vol.7 , Issue.8 , pp. 736-741
    • McClellan, A.J.1    Tam, S.2    Kaganovich, D.3    Frydman, J.4
  • 48
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 Attenuate Formation of Spherical and Annular Polyglutamine Oligomers by Partitioning Monomer
    • Wacker, J. L.; Zareie, M. H.; Fong, H.; Sarikaya, M.; Muchowski, P. J., Hsp70 and Hsp40 Attenuate Formation of Spherical and Annular Polyglutamine Oligomers by Partitioning Monomer. Nat. Struct. Mol. Biol., 2004, 11 (12), 1215-1222.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , Issue.12 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 49
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of Polyglutamine-mediated Neurodegeneration in Drosophila by the Molecular Chaperone HSP70
    • Warrick, J. M.; Chan, H. Y. E.; Gray-Board, G. L.; Chai, Y.; Paulson, H. L.; Bonini, N. M., Suppression of Polyglutamine-mediated Neurodegeneration in Drosophila by the Molecular Chaperone HSP70. Nat. Genet., 1999, 23 (4), 425.
    • (1999) Nat. Genet , vol.23 , Issue.4 , pp. 425
    • Warrick, J.M.1    Chan, H.Y.E.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 50
    • 78649685457 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle
    • Lotz, G. P.; Legleiter, J.; Aron, R.; Mitchell, E. J.; Huang, S. Y.; Ng, C.; Glabe, C.; Thompson, L. M.; Muchowski, P. J., Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle. J. Biol. Chem., 2010, 285 (49), 38183-38193.
    • (2010) J. Biol. Chem , vol.285 , Issue.49 , pp. 38183-38193
    • Lotz, G.P.1    Legleiter, J.2    Aron, R.3    Mitchell, E.J.4    Huang, S.Y.5    Ng, C.6    Glabe, C.7    Thompson, L.M.8    Muchowski, P.J.9
  • 51
    • 77954379810 scopus 로고    scopus 로고
    • Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool
    • Olshina, M. A.; Angley, L. M.; Ramdzan, Y. M.; Tang, J.; Bailey, M. F.; Hill, A. F.; Hatters, D. M., Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool. J. Biol. Chem., 2010, 285 (28), 21807-21816.
    • (2010) J. Biol. Chem , vol.285 , Issue.28 , 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
  • 53
    • 80052830376 scopus 로고    scopus 로고
    • Chaperone-mediated hierarchical control in targeting misfolded proteins to aggresomes
    • Zhang, X.; Qian, S.-B., Chaperone-mediated hierarchical control in targeting misfolded proteins to aggresomes. Mol. Biol. Cell, 2011, 22 (18), 3277-3288.
    • (2011) Mol. Biol. Cell , vol.22 , Issue.18 , pp. 3277-3288
    • Zhang, X.1    Qian, S.-B.2
  • 54
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine Length-dependent Interaction of Hsp40 and Hsp70 Family Chaperones with Truncated N-terminal Huntingtin: Their Role in Suppression of Aggregation and Cellular Toxicity
    • Jana, N. R.; Tanaka, M.; Wang, G.-H.; Nukina, N., Polyglutamine Length-dependent Interaction of Hsp40 and Hsp70 Family Chaperones with Truncated N-terminal Huntingtin: their Role in Suppression of Aggregation and Cellular Toxicity. Hum. Mol. Genet., 2000, 9 (13), 2009-2018.
    • (2000) Hum. Mol. Genet , vol.9 , Issue.13 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.-H.3    Nukina, N.4
  • 55
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone Suppression of Cellular Toxicity of Huntingtin Is Independent of Polyglutamine Aggregation
    • Zhou, H.; Li, S.-H.; Li, X.-J., Chaperone Suppression of Cellular Toxicity of Huntingtin Is Independent of Polyglutamine Aggregation. J. Biol. Chem., 2001, 276 (51), 48417-48424.
    • (2001) J. Biol. Chem , vol.276 , Issue.51 , pp. 48417-48424
    • Zhou, H.1    Li, S.-H.2    Li, X.-J.3
  • 56
    • 34548608465 scopus 로고    scopus 로고
    • Modulation of Polyglutamine Inclusion Formation by the Hsp70 Chaperone Machine
    • Rujano, M. A.; Kampinga, H. H.; Salomons, F. A., Modulation of Polyglutamine Inclusion Formation by the Hsp70 Chaperone Machine. Exp. Cell. Res., 2007, 313 (16), 3568-3578.
    • (2007) Exp. Cell. Res , vol.313 , Issue.16 , pp. 3568-3578
    • Rujano, M.A.1    Kampinga, H.H.2    Salomons, F.A.3
  • 58
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of Inducible HSP70 Chaperone Suppresses Neuropathology and Improves Motor Function in SCA1 Mice
    • Cummings, C. J.; Sun, Y.; Opal, P.; Antalffy, B.; Mestril, R.; Orr, H. T.; Dillmann, W. H.; Zoghbi, H. Y., Over-expression of Inducible HSP70 Chaperone Suppresses Neuropathology and Improves Motor Function in SCA1 Mice. Hum. Mol. Genet., 2001, 10 (14), 1511-1518.
    • (2001) Hum. Mol. Genet , vol.10 , Issue.14 , pp. 1511-1518
    • Cummings, C.J.1    Sun, Y.2    Opal, P.3    Antalffy, B.4    Mestril, R.5    Orr, H.T.6    Dillmann, W.H.7    Zoghbi, H.Y.8
  • 59
    • 0034608868 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 Chaperones Can Inhibit Self-assembly of Polyglutamine Proteins into Amyloid-like Fibrils
    • Muchowski, P. J.; Schaffar, G.; Sittler, A.; Wanker, E. E.; Hayer-Hartl, M. K.; Hartl, F. U., Hsp70 and Hsp40 Chaperones Can Inhibit Self-assembly of Polyglutamine Proteins into Amyloid-like Fibrils. Proc. Natl. Acad. Sci. USA, 2000, 97 (14), 7841-7846.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.14 , pp. 7841-7846
    • Muchowski, P.J.1    Schaffar, G.2    Sittler, A.3    Wanker, E.E.4    Hayer-Hartl, M.K.5    Hartl, F.U.6
  • 60
    • 84861369587 scopus 로고    scopus 로고
    • Impaired Heat Shock Response in Cells Expressing Full-Length Polyglutamine-Expanded Huntingtin
    • Chafekar, S. M.; Duennwald, M. L., Impaired Heat Shock Response in Cells Expressing Full-Length Polyglutamine-Expanded Huntingtin. PLoS ONE, 2012, 7 (5), e37929.
    • (2012) PLoS ONE , vol.7 , Issue.5
    • Chafekar, S.M.1    Duennwald, M.L.2
  • 61
    • 33644850056 scopus 로고    scopus 로고
    • Progressive Disruption of Cellular Protein Folding in Models of Polyglutamine Diseases
    • Gidalevitz, T.; Ben-Zvi, A.; Ho, K. H.; Brignull, H. R.; Morimoto, R. I., Progressive Disruption of Cellular Protein Folding in Models of Polyglutamine Diseases. Science, 2006, 311 (5766), 1471-1474.
    • (2006) Science , vol.311 , Issue.5766 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 62
    • 39349083915 scopus 로고    scopus 로고
    • Adapting Proteostasis for Disease Intervention
    • Balch, W. E.; Morimoto, R. I.; Dillin, A.; Kelly, J. W., Adapting Proteostasis for Disease Intervention. Science, 2008, 319 (5865), 916-919.
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 63
    • 0035502934 scopus 로고    scopus 로고
    • New Anti-huntingtin Monoclonal Antibodies: Implications for Huntingtin Conformation and its Binding Proteins
    • Ko, J.; Ou, S.; Patterson, P. H., New Anti-huntingtin Monoclonal Antibodies: Implications for Huntingtin Conformation and its Binding Proteins. Brain Res. Bull., 2001, 56 (3-4), 319-329.
    • (2001) Brain Res. Bull , vol.56 , Issue.3-4 , pp. 319-329
    • Ko, J.1    Ou, S.2    Patterson, P.H.3
  • 64
    • 84993924942 scopus 로고    scopus 로고
    • The structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice model
    • Li, P.; Huey-Tubman, K. E.; Gao, T.; Li, X.; West, A. P.; Bennett, M. J.; Bjorkman, P. J., The structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice model. Nat. Struct. Mol. Biol., 2007, 14 (5), 381-387.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , Issue.5 , pp. 381-387
    • Li, P.1    Huey-Tubman, K.E.2    Gao, T.3    Li, X.4    West, A.P.5    Bennett, M.J.6    Bjorkman, P.J.7
  • 66
    • 84863178573 scopus 로고    scopus 로고
    • TR-FRET-Based Duplex Immunoassay Reveals an Inverse Correlation of Soluble and Aggregated Mutant huntingtin in Huntington's Disease
    • Semmelroth, M.; Zivanovic, A.; Abramowski, D.; Smith, D.; Lotz, Gregor P.; Bates, Gillian P.; Weiss, A., TR-FRET-Based Duplex Immunoassay Reveals an Inverse Correlation of Soluble and Aggregated Mutant huntingtin in Huntington's Disease. Chem. Biol., 2012, 19 (2), 264-275.
    • (2012) Chem. Biol , vol.19 , Issue.2 , pp. 264-275
    • Semmelroth, M.1    Zivanovic, A.2    Abramowski, D.3    Smith, D.4    Lotz Gregor, P.5    Bates Gillian, P.6    Weiss, A.7
  • 69
    • 54049111928 scopus 로고    scopus 로고
    • Intrabodies Binding the Proline-Rich Domains of Mutant Huntingtin Increase Its Turnover and Reduce Neurotoxicity
    • Southwell, A. L.; Khoshnan, A.; Dunn, D. E.; Bugg, C. W.; Lo, D. C.; Patterson, P. H., Intrabodies Binding the Proline-Rich Domains of Mutant Huntingtin Increase Its Turnover and Reduce Neurotoxicity. J. Neurosci., 2008, 28 (36), 9013-9020.
    • (2008) J. Neurosci , vol.28 , Issue.36 , pp. 9013-9020
    • Southwell, A.L.1    Khoshnan, A.2    Dunn, D.E.3    Bugg, C.W.4    Lo, D.C.5    Patterson, P.H.6
  • 70
    • 44649113841 scopus 로고    scopus 로고
    • Suppression of neuropil aggregates and neurological symptoms by an intracellular antibody implicates the cytoplasmic toxicity of mutant huntingtin
    • Wang, C.-E.; Zhou, H.; McGuire, J. R.; Cerullo, V.; Lee, B.; Li, S.-H.; Li, X.-J., Suppression of neuropil aggregates and neurological symptoms by an intracellular antibody implicates the cytoplasmic toxicity of mutant huntingtin. J. Cell Biol., 2008, 181 (5), 803-816.
    • (2008) J. Cell Biol , vol.181 , Issue.5 , 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
  • 71
    • 70350543879 scopus 로고    scopus 로고
    • Intrabody Gene Therapy Ameliorates Motor, Cognitive, and Neuropathological Symptoms in Multiple Mouse Models of Huntington's Disease
    • Southwell, A. L.; Ko, J.; Patterson, P. H., Intrabody Gene Therapy Ameliorates Motor, Cognitive, and Neuropathological Symptoms in Multiple Mouse Models of Huntington's Disease. J. Neurosci., 2009, 29 (43), 13589-13602.
    • (2009) J. Neurosci , vol.29 , Issue.43 , pp. 13589-13602
    • Southwell, A.L.1    Ko, J.2    Patterson, P.H.3
  • 72
    • 77957930942 scopus 로고    scopus 로고
    • Early or late-stage anti-N-terminal Huntingtin intrabody gene therapy reduces pathological features in B6.HDR6/1 mice
    • Snyder-Keller, A.; McLear, J. A.; Hathorn, T.; Messer, A., Early or late-stage anti-N-terminal Huntingtin intrabody gene therapy reduces pathological features in B6.HDR6/1 mice. J. Neuropathol. Exp. Neurol., 2010, 69 (10), 1078-1085.
    • (2010) J. Neuropathol. Exp. Neurol , vol.69 , Issue.10 , pp. 1078-1085
    • Snyder-Keller, A.1    McLear, J.A.2    Hathorn, T.3    Messer, A.4
  • 73
    • 84055182535 scopus 로고    scopus 로고
    • Bifunctional Anti-Huntingtin Proteasome-Directed Intrabodies Mediate Efficient Degradation of Mutant Huntingtin Exon 1 Protein Fragments
    • Butler, D. C.; Messer, A., Bifunctional Anti-Huntingtin Proteasome-Directed Intrabodies Mediate Efficient Degradation of Mutant Huntingtin Exon 1 Protein Fragments. PLoS ONE, 2011, 6 (12), e29199.
    • (2011) PLoS ONE , vol.6 , Issue.12
    • Butler, D.C.1    Messer, A.2
  • 74
    • 66449106372 scopus 로고    scopus 로고
    • Conformational Targeting of Fibrillar Polyglutamine Proteins in Live Cells Escalates Aggregation and Cytotoxicity
    • Kvam, E.; Nannenga, B. L.; Wang, M. S.; Jia, Z.; Sierks, M. R.; Messer, A., Conformational Targeting of Fibrillar Polyglutamine Proteins in Live Cells Escalates Aggregation and Cytotoxicity. PLoS ONE, 2009, 4 (5), e5727.
    • (2009) PLoS ONE , vol.4 , Issue.5
    • Kvam, E.1    Nannenga, B.L.2    Wang, M.S.3    Jia, Z.4    Sierks, M.R.5    Messer, A.6
  • 75
    • 33750291199 scopus 로고    scopus 로고
    • Isolating recombinant antibodies against specific protein morphologies using atomic force microscopy and phage display technologies
    • Barkhordarian, H.; Emadi, S.; Schulz, P.; Sierks, M. R., Isolating recombinant antibodies against specific protein morphologies using atomic force microscopy and phage display technologies. Protein Eng. Des. Sel., 2006, 19 (11), 497-502.
    • (2006) Protein Eng. Des. Sel , vol.19 , Issue.11 , pp. 497-502
    • Barkhordarian, H.1    Emadi, S.2    Schulz, P.3    Sierks, M.R.4
  • 77
    • 77951988103 scopus 로고    scopus 로고
    • Mutant Huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo
    • Legleiter, J.; Mitchell, E.; Lotz, G. P.; Sapp, E.; Ng, C.; DiFiglia, M.; Thompson, L. M.; Muchowski, P. J., Mutant Huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo. J. Biol. Chem., 2010, 285 (19), 14777-14790.
    • (2010) J. Biol. Chem , vol.285 , Issue.19 , pp. 14777-14790
    • Legleiter, J.1    Mitchell, E.2    Lotz, G.P.3    Sapp, E.4    Ng, C.5    Difiglia, M.6    Thompson, L.M.7    Muchowski, P.J.8
  • 79
    • 38049139425 scopus 로고    scopus 로고
    • Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease
    • Andreas, W.; Corinna, K.; Ben, W.; Kirupa, S.; Miriam, B.; Etienne, R.; Gillian, P. B.; Paolo, P., Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease. J. Neurochem., 2008, 104 (3), 846-858.
    • (2008) J. Neurochem , vol.104 , Issue.3 , pp. 846-858
    • Andreas, W.1    Corinna, K.2    Ben, W.3    Kirupa, S.4    Miriam, B.5    Etienne, R.6    Gillian, P.B.7    Paolo, P.8
  • 81
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • Nekooki-Machida, Y.; Kurosawa, M.; Nukina, N.; Ito, K.; Oda, T.; Tanaka, M., Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc. Natl. Acad. Sci. U S A, 2009, 106 (24), 9679-9684.
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , Issue.24 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 82
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka, M.; Chien, P.; Naber, N.; Cooke, R.; Weissman, J. S., Conformational variations in an infectious protein determine prion strain differences. Nature, 2004, 428 (6980), 323-328.
    • (2004) Nature , vol.428 , Issue.6980 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 83
    • 12244249201 scopus 로고    scopus 로고
    • Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
    • Petkova, A. T.; Leapman, R. D.; Guo, Z.; Yau, W.-M.; Mattson, M. P.; Tycko, R., Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils. Science, 2005, 307 (5707), 262-265.
    • (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
  • 84
    • 36348996602 scopus 로고    scopus 로고
    • Phospholipid Interaction Induces Molecular-level Polymorphism in Apolipoprotein C-II Amyloid Fibrils via Alternative Assembly Pathways
    • Griffin, M. D. W.; Mok, M. L. Y.; Wilson, L. M.; Pham, C. L. L.; Waddington, L. J.; Perugini, M. A.; Howlett, G. J., Phospholipid Interaction Induces Molecular-level Polymorphism in Apolipoprotein C-II Amyloid Fibrils via Alternative Assembly Pathways. J. Mol. Biol, 2008, 375 (1), 240-256.
    • (2008) J. Mol. Biol , vol.375 , Issue.1 , pp. 240-256
    • Griffin, M.D.W.1    Mok, M.L.Y.2    Wilson, L.M.3    Pham, C.L.L.4    Waddington, L.J.5    Perugini, M.A.6    Howlett, G.J.7
  • 85
    • 23444445907 scopus 로고    scopus 로고
    • Competing pathways determine fibril morphology in the self-assembly of β2-microglobulin into amyloid
    • Gosal, W. S.; Morten, I. J.; Hewitt, E. W.; Smith, D. A.; Thomson, N. H.; Radford, S. E., Competing pathways determine fibril morphology in the self-assembly of β2-microglobulin into amyloid. J. Mol. Biol., 2005, 351 (4), 850-864.
    • (2005) J. Mol. Biol , vol.351 , Issue.4 , pp. 850-864
    • Gosal, W.S.1    Morten, I.J.2    Hewitt, E.W.3    Smith, D.A.4    Thomson, N.H.5    Radford, S.E.6
  • 89
    • 4444226434 scopus 로고    scopus 로고
    • Polymeric Ligands with Specificity for Aggregated Prion Proteins
    • Lane, A.; Stanley, C. J.; Dealler, S.; Wilson, S. M., Polymeric Ligands with Specificity for Aggregated Prion Proteins. Clin. Chem., 2003, 49 (10), 1774-1775.
    • (2003) Clin. Chem , vol.49 , Issue.10 , pp. 1774-1775
    • Lane, A.1    Stanley, C.J.2    Dealler, S.3    Wilson, S.M.4
  • 96
    • 79953123196 scopus 로고    scopus 로고
    • Premature death and neurologic abnormalities in transgenic mice expressing a mutant huntingtin exon-2 fragment
    • Tebbenkamp, A. T. N.; Swing, D.; Tessarollo, L.; Borchelt, D. R., Premature death and neurologic abnormalities in transgenic mice expressing a mutant huntingtin exon-2 fragment. Hum. Mol. Genet., 2011, 20 (8), 1633-1642.
    • (2011) Hum. Mol. Genet , vol.20 , Issue.8 , pp. 1633-1642
    • Tebbenkamp, A.T.N.1    Swing, D.2    Tessarollo, L.3    Borchelt, D.R.4
  • 98
    • 0036671821 scopus 로고    scopus 로고
    • Proteases Acting on Mutant Huntingtin Generate Cleaved Products that Differentially Build Up Cytoplasmic and Nuclear Inclusions
    • Lunkes, A.; Lindenberg, K. S.; Ben-Hai, L.; Weber, C.; Devys, D.; Landwehrmeyer, G. B.; Mandel, J.-L.; Trottier, Y., Proteases Acting on Mutant Huntingtin Generate Cleaved Products that Differentially Build Up Cytoplasmic and Nuclear Inclusions. Mol. Cell, 2002, 10 (2), 259-269.
    • (2002) Mol. Cell , vol.10 , Issue.2 , pp. 259-269
    • Lunkes, A.1    Lindenberg, K.S.2    Ben-Hai, L.3    Weber, C.4    Devys, D.5    Landwehrmeyer, G.B.6    Mandel, J.-L.7    Trottier, Y.8
  • 101
    • 79959802847 scopus 로고    scopus 로고
    • Transgenic mice expressing caspase-6-derived N-terminal fragments of mutant huntingtin develop neurologic abnormalities with predominant cytoplasmic inclusion pathology composed largely of a smaller proteolytic derivative
    • Tebbenkamp, A. T. N.; Green, C.; Xu, G.; Denovan-Wright, E. M.; Rising, A. C.; Fromholt, S. E.; Brown, H. H.; Swing, D.; Mandel, R. J.; Tessarollo, L.; Borchelt, D. R., Transgenic mice expressing caspase-6-derived N-terminal fragments of mutant huntingtin develop neurologic abnormalities with predominant cytoplasmic inclusion pathology composed largely of a smaller proteolytic derivative. Hum. Mol. Genet., 2011, 20 (14), 2770-2782.
    • (2011) Hum. Mol. Genet , vol.20 , Issue.14 , pp. 2770-2782
    • Tebbenkamp, A.T.N.1    Green, C.2    Xu, G.3    Denovan-Wright, E.M.4    Rising, A.C.5    Fromholt, S.E.6    Brown, H.H.7    Swing, D.8    Mandel, R.J.9    Tessarollo, L.10    Borchelt, D.R.11
  • 104
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction
    • Li, S. S., Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction. Biochem. J., 2005, 390 (Pt 3), 641-653.
    • (2005) Biochem. J , vol.390 , Issue.Pt 3 , pp. 641-653
    • Li, S.S.1
  • 106
    • 79959778716 scopus 로고    scopus 로고
    • Huntingtin affinity for partners is not changed by polyglutamine length: Aggregation itself triggers aberrant interactions
    • Davranche, A.; Aviolat, H.; Zeder-Lutz, G.; Busso, D.; Altschuh, D.; Trottier, Y.; Klein, F. A. C., Huntingtin affinity for partners is not changed by polyglutamine length: aggregation itself triggers aberrant interactions. Hum. Mol. Genet., 2011, 20 (14), 2795-2806.
    • (2011) Hum. Mol. Genet , vol.20 , Issue.14 , pp. 2795-2806
    • Davranche, A.1    Aviolat, H.2    Zeder-Lutz, G.3    Busso, D.4    Altschuh, D.5    Trottier, Y.6    Klein, F.A.C.7
  • 107
    • 0037154165 scopus 로고    scopus 로고
    • Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity
    • Khoshnan, A.; Ko, J.; Patterson, P. H., Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity. Proc. Natl. Acad. Sci. USA, 2002, 99 (2), 1002-1007.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.2 , pp. 1002-1007
    • Khoshnan, A.1    Ko, J.2    Patterson, P.H.3
  • 108
    • 23344440853 scopus 로고    scopus 로고
    • Formation of Morphologically Similar Globular Aggregates From Diverse Aggregation-prone Proteins in Mammalian Cells
    • Mukai, H.; Isagawa, T.; Goyama, E.; Tanaka, S.; Bence, N. F.; Tamura, A.; Ono, Y.; Kopito, R. R., Formation of Morphologically Similar Globular Aggregates From Diverse Aggregation-prone Proteins in Mammalian Cells. Proc. Natl. Acad. Sci. USA, 2005, 102 (31), 10887-10892.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.31 , pp. 10887-10892
    • Mukai, H.1    Isagawa, T.2    Goyama, E.3    Tanaka, S.4    Bence, N.F.5    Tamura, A.6    Ono, Y.7    Kopito, R.R.8
  • 109
    • 34548227453 scopus 로고    scopus 로고
    • Detection of Polyglutamine Protein Oligomers in Cells by Fluorescence Correlation Spectroscopy
    • Takahashi, Y.; Okamoto, Y.; Popiel, H. A.; Fujikake, N.; Toda, T.; Kinjo, M.; Nagai, Y., Detection of Polyglutamine Protein Oligomers in Cells by Fluorescence Correlation Spectroscopy. J. Biol. Chem., 2007, 282 (33), 24039-24048.
    • (2007) J. Biol. Chem , vol.282 , Issue.33 , pp. 24039-24048
    • Takahashi, Y.1    Okamoto, Y.2    Popiel, H.A.3    Fujikake, N.4    Toda, T.5    Kinjo, M.6    Nagai, Y.7
  • 110
    • 38349158062 scopus 로고    scopus 로고
    • Soluble Polyglutamine Oligomers Formed Prior to Inclusion Body Formation are Cytotoxic
    • Takahashi, T.; Kikuchi, S.; Katada, S.; Nagai, Y.; Nishizawa, M.; Onodera, O., Soluble Polyglutamine Oligomers Formed Prior to Inclusion Body Formation are Cytotoxic. Hum. Mol. Genet., 2007, 17 (3), 345-346.
    • (2007) Hum. Mol. Genet , vol.17 , Issue.3 , pp. 345-346
    • Takahashi, T.1    Kikuchi, S.2    Katada, S.3    Nagai, Y.4    Nishizawa, M.5    Onodera, O.6
  • 111
    • 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., A Two-Step Path to Inclusion Formation of Huntingtin Peptides Revealed by Number and Brightness Analysis. Biophys. J., 2010, 98 (12), 3078-3085.
    • (2010) Biophys. J , 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
  • 112
    • 78650811716 scopus 로고    scopus 로고
    • Formation and Toxicity of Soluble Polyglutamine Oligomers in Living Cells
    • Lajoie, P.; Snapp, E. L., Formation and Toxicity of Soluble Polyglutamine Oligomers in Living Cells. PLoS ONE, 2011, 5 (12), e15245.
    • (2011) PLoS ONE , vol.5 , Issue.12
    • Lajoie, P.1    Snapp, E.L.2
  • 113
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu, C.-D.; Kerppola, T. K., Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotech, 2003, 21 (5), 539-545.
    • (2003) Nat. Biotech , vol.21 , Issue.5 , pp. 539-545
    • Hu, C.-D.1    Kerppola, T.K.2
  • 115
    • 0032168160 scopus 로고    scopus 로고
    • Polyglutamine-Expanded Human Huntingtin Transgenes Induce Degeneration of Drosophila Photoreceptor Neurons
    • Jackson, G. R.; Salecker, I.; Dong, X.; Yao, X.; Arnheim, N.; Faber, P. W.; MacDonald, M. E.; Zipursky, S. L., Polyglutamine-Expanded Human Huntingtin Transgenes Induce Degeneration of Drosophila Photoreceptor Neurons. Neuron, 1998, 21 (3), 633-642.
    • (1998) Neuron , vol.21 , Issue.3 , pp. 633-642
    • Jackson, G.R.1    Salecker, I.2    Dong, X.3    Yao, X.4    Arnheim, N.5    Faber, P.W.6    Macdonald, M.E.7    Zipursky, S.L.8
  • 116
    • 33747053662 scopus 로고    scopus 로고
    • Polyglutamine Proteins at the Pathogenic Threshold Display Neuron-Specific Aggregation in a Pan-Neuronal Caenorhabditis elegans Model
    • Brignull, H. R.; Moore, F. E.; Tang, S. J.; Morimoto, R. I., Polyglutamine Proteins at the Pathogenic Threshold Display Neuron-Specific Aggregation in a Pan-Neuronal Caenorhabditis elegans Model. J. Neurosci., 2006, 26 (29), 7597-7606.
    • (2006) J. Neurosci , vol.26 , Issue.29 , pp. 7597-7606
    • Brignull, H.R.1    Moore, F.E.2    Tang, S.J.3    Morimoto, R.I.4
  • 117
    • 77950932967 scopus 로고    scopus 로고
    • Conformation sensors that distinguish monomeric proteins from oligomers in live cells
    • Ramdzan, Y. M.; Nisbet, R. M.; Miller, J.; Finkbeiner, S.; Hill, A. F.; Hatters, D. M., Conformation sensors that distinguish monomeric proteins from oligomers in live cells. Chem. Biol, 2010, 17 (4), 371-379.
    • (2010) Chem. Biol , vol.17 , Issue.4 , pp. 371-379
    • Ramdzan, Y.M.1    Nisbet, R.M.2    Miller, J.3    Finkbeiner, S.4    Hill, A.F.5    Hatters, D.M.6
  • 119
    • 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., Huntingtin Spheroids and Protofibrils as Precursors in Polyglutamine Fibrilization. J. Biol. Chem., 2002, 277 (43), 41032-41037.
    • (2002) J. Biol. Chem , 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
  • 120
    • 0037181179 scopus 로고    scopus 로고
    • Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins
    • Masino, L.; Kelly, G.; Leonard, K.; Trottier, Y.; Pastore, A., Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins. FEBS Lett., 2002, 513 (2-3), 267-272.
    • (2002) FEBS Lett , vol.513 , Issue.2-3 , pp. 267-272
    • Masino, L.1    Kelly, G.2    Leonard, K.3    Trottier, Y.4    Pastore, A.5
  • 121
    • 33750934185 scopus 로고    scopus 로고
    • Fluorescence Correlation Spectroscopy Shows That Monomeric Polyglutamine Molecules Form Collapsed Structures in Aqueous Solutions
    • Crick, S. L.; Jayaraman, M.; Frieden, C.; Wetzel, R.; Pappu, R. V., Fluorescence Correlation Spectroscopy Shows That Monomeric Polyglutamine Molecules Form Collapsed Structures in Aqueous Solutions. Proc. Natl. Acad. Sci. USA, 2006, 103 (45), 16764-16769.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.45 , pp. 16764-16769
    • Crick, S.L.1    Jayaraman, M.2    Frieden, C.3    Wetzel, R.4    Pappu, R.V.5
  • 122
    • 33645281939 scopus 로고    scopus 로고
    • Characterizing the conformational ensemble of monomeric polyglutamine
    • Wang, X.; Vitalis, A.; Wyczalkowski, M. A.; Pappu, R. V., Characterizing the conformational ensemble of monomeric polyglutamine. Proteins, 2006, 63 (2), 297-311.
    • (2006) Proteins , vol.63 , Issue.2 , pp. 297-311
    • Wang, X.1    Vitalis, A.2    Wyczalkowski, M.A.3    Pappu, R.V.4
  • 123
    • 55649096822 scopus 로고    scopus 로고
    • The Intrinsic Stiffness of Polyglutamine Peptides
    • Singh, V. R.; Lapidus, L. J., The Intrinsic Stiffness of Polyglutamine Peptides. J. Phys. Chem. B, 2008, 112 (42), 13172-13176.
    • (2008) J. Phys. Chem. B , vol.112 , Issue.42 , pp. 13172-13176
    • Singh, V.R.1    Lapidus, L.J.2
  • 124
    • 69149105917 scopus 로고    scopus 로고
    • Single Homopolypeptide Chains Collapse into Mechanically Rigid Conformations
    • Dougan, L.; Li, J.; Badilla, C. L.; Berne, B. J.; Fernandez, J. M., Single Homopolypeptide Chains Collapse into Mechanically Rigid Conformations. Proc. Natl. Acad. Sci. USA, 2009, 106 (31), 12605-12610.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , Issue.31 , pp. 12605-12610
    • Dougan, L.1    Li, J.2    Badilla, C.L.3    Berne, B.J.4    Fernandez, J.M.5
  • 125
    • 69849086690 scopus 로고    scopus 로고
    • Secondary Structure of Huntingtin Amino-Terminal Region
    • Kim, M. W.; Chelliah, Y.; Kim, S. W.; Otwinowski, Z.; Bezprozvanny, I., Secondary Structure of Huntingtin Amino-Terminal Region. Structure, 2009, 17 (9), 1205-1212.
    • (2009) Structure , vol.17 , Issue.9 , pp. 1205-1212
    • Kim, M.W.1    Chelliah, Y.2    Kim, S.W.3    Otwinowski, Z.4    Bezprozvanny, I.5
  • 126
    • 70349838220 scopus 로고    scopus 로고
    • Examining Polyglutamine Peptide Length: A Connection between Collapsed Conformations and Increased Aggregation
    • Walters, R. H.; Murphy, R. M., Examining Polyglutamine Peptide Length: A Connection between Collapsed Conformations and Increased Aggregation. J. Mol. Biol., 2009, 393 (4), 978-992.
    • (2009) J. Mol. Biol , vol.393 , Issue.4 , pp. 978-992
    • Walters, R.H.1    Murphy, R.M.2
  • 128
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman, P.; Wetzel, R.; Tanaka, M.; Nukina, N.; Goldberg, A. L., Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol. Cell, 2004, 14 (1), 95-104.
    • (2004) Mol. Cell , vol.14 , Issue.1 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 133
    • 0037168642 scopus 로고    scopus 로고
    • Mutational Analysis of the Structural Organization of Polyglutamine Aggregates
    • Thakur, A. K.; Wetzel, R., Mutational Analysis of the Structural Organization of Polyglutamine Aggregates. Proc. Natl. Acad. Sci. USA, 2002, 99 (26), 17014-17019.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.26 , pp. 17014-17019
    • Thakur, A.K.1    Wetzel, R.2
  • 134
    • 15544372340 scopus 로고    scopus 로고
    • A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: Evidence for a compact beta-sheet structure
    • Poirier, M. A.; Jiang, H.; Ross, C. A., A structure-based analysis of huntingtin mutant polyglutamine aggregation and toxicity: evidence for a compact beta-sheet structure. Hum. Mol. Genet, 2005, 14 (6), 765-774.
    • (2005) Hum. Mol. Genet , vol.14 , Issue.6 , pp. 765-774
    • Poirier, M.A.1    Jiang, H.2    Ross, C.A.3
  • 136
    • 35448994487 scopus 로고    scopus 로고
    • Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity
    • Atwal, R. S.; Xia, J.; Pinchev, D.; Taylor, J.; Epand, R. M.; Truant, R., Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum. Mol. Genet, 2007, 16 (21), 2600-2615.
    • (2007) Hum. Mol. Genet , vol.16 , Issue.21 , pp. 2600-2615
    • Atwal, R.S.1    Xia, J.2    Pinchev, D.3    Taylor, J.4    Epand, R.M.5    Truant, R.6
  • 139
    • 84856226648 scopus 로고    scopus 로고
    • Slow Amyloid Nucleation via a-Helix-Rich Oligomeric Intermediates in Short Polyglutamine-Containing Huntingtin Fragments
    • Jayaraman, M.; Kodali, R.; Sahoo, B.; Thakur, A. K.; Mayasundari, A.; Mishra, R.; Peterson, C. B.; Wetzel, R., Slow Amyloid Nucleation via a-Helix-Rich Oligomeric Intermediates in Short Polyglutamine-Containing Huntingtin Fragments. J. Mol. Biol, 2012, 415 (5), 881-899.
    • (2012) J. Mol. Biol , vol.415 , Issue.5 , 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
  • 140
    • 0036520326 scopus 로고    scopus 로고
    • The Structural Basis for Amyloid Formation by Plasma Apolipoproteins: A Review
    • Hatters, D. M.; Howlett, G. J., The Structural Basis for Amyloid Formation by Plasma Apolipoproteins: A Review. Eur. Biophys. J., 2002, 31, 2-8.
    • (2002) Eur. Biophys. J , vol.31 , pp. 2-8
    • Hatters, D.M.1    Howlett, G.J.2
  • 141
    • 33746932145 scopus 로고    scopus 로고
    • Amino-terminal Domain Stability Mediates Apolipoprotein E Aggregation into Neurotoxic Fibrils
    • Hatters, D. M.; Zhong, N.; Rutenber, E.; Weisgraber, K. H., Amino-terminal Domain Stability Mediates Apolipoprotein E Aggregation into Neurotoxic Fibrils. J. Mol. Biol, 2006, 361 (5), 932-944.
    • (2006) J. Mol. Biol , vol.361 , Issue.5 , pp. 932-944
    • Hatters, D.M.1    Zhong, N.2    Rutenber, E.3    Weisgraber, K.H.4
  • 144
    • 80053415277 scopus 로고    scopus 로고
    • Protein alpha-N-acetylation studied by N-terminomics
    • Van Damme, P.; Arnesen, T.; Gevaert, K., Protein alpha-N-acetylation studied by N-terminomics. FEBS J., 2011, 278 (20), 3822-3834.
    • (2011) FEBS J , vol.278 , Issue.20 , pp. 3822-3834
    • van Damme, P.1    Arnesen, T.2    Gevaert, K.3
  • 145
    • 84862555977 scopus 로고    scopus 로고
    • N-terminal acetylation of a-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer
    • Kang, L.; Moriarty, G. M.; Woods, L. A.; Ashcroft, A. E.; Radford, S. E.; Baum, J., N-terminal acetylation of a-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer. Protein Sci., 2012, 21 (7), 911-917.
    • (2012) Protein Sci , vol.21 , Issue.7 , pp. 911-917
    • Kang, L.1    Moriarty, G.M.2    Woods, L.A.3    Ashcroft, A.E.4    Radford, S.E.5    Baum, J.6
  • 147
    • 84874891098 scopus 로고    scopus 로고
    • Amyloid disease drug approved
    • Garber, K., Amyloid disease drug approved. Nat. Biotech, 2012, 30 (2), 121-121.
    • (2012) Nat. Biotech , vol.30 , Issue.2 , pp. 121
    • Garber, K.1
  • 149
    • 70349675573 scopus 로고    scopus 로고
    • RNAi screening in Drosophila cells identifies new modifiers of mutant huntingtin aggregation
    • Doumanis, J.; Wada, K.; Kino, Y.; Moore, A. W.; Nukina, N., RNAi screening in Drosophila cells identifies new modifiers of mutant huntingtin aggregation. PLoS ONE, 2009, 4 (9), e7275.
    • (2009) PLoS ONE , vol.4 , Issue.9
    • Doumanis, J.1    Wada, K.2    Kino, Y.3    Moore, A.W.4    Nukina, N.5
  • 150
    • 77955870526 scopus 로고    scopus 로고
    • A Genomewide RNA Interference Screen for Modifiers of Aggregates Formation by Mutant Huntingtin in Drosophila
    • Zhang, S.; Binari, R.; Zhou, R.; Perrimon, N., A Genomewide RNA Interference Screen for Modifiers of Aggregates Formation by Mutant Huntingtin in Drosophila. Genetics, 2010, 184 (4), 1165-1179.
    • (2010) Genetics , vol.184 , Issue.4 , pp. 1165-1179
    • Zhang, S.1    Binari, R.2    Zhou, R.3    Perrimon, N.4
  • 152
    • 84856103060 scopus 로고    scopus 로고
    • An aggregation sensing reporter identifies leflunomide and teriflunomide as polyglutamine aggregate inhibitors
    • Fuentealba, R. A.; Marasa, J.; Diamond, M. I.; Piwnica-Worms, D.; Weihl, C. C, An aggregation sensing reporter identifies leflunomide and teriflunomide as polyglutamine aggregate inhibitors. Hum. Mol. Genet, 2012, 21 (3), 664-680.
    • (2012) Hum. Mol. Genet , vol.21 , Issue.3 , pp. 664-680
    • Fuentealba, R.A.1    Marasa, J.2    Diamond, M.I.3    Piwnica-Worms, D.4    Weihl, C.C.5
  • 153
    • 0028972448 scopus 로고
    • Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias
    • Trottier, Y.; Lutz, Y.; Stevanin, G.; Imbert, G.; Devys, D.; Cancel, G.; Saudou, F.; Weber, C; David, G.; Tora, L.; et al., Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias. Nature, 1995, 378 (6555), 403-406.
    • (1995) Nature , vol.378 , Issue.6555 , pp. 403-406
    • Trottier, Y.1    Lutz, Y.2    Stevanin, G.3    Imbert, G.4    Devys, D.5    Cancel, G.6    Saudou, F.7    Weber, C.8    David, G.9    Tora, L.10
  • 154
    • 41549129945 scopus 로고    scopus 로고
    • Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice
    • Wang, J.; Wang, C. E.; Orr, A.; Tydlacka, S.; Li, S. H.; Li, X. J., Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice. J. Cell Biol, 2008, 180 (6), 1177-1189.
    • (2008) J. Cell Biol , vol.180 , Issue.6 , pp. 1177-1189
    • Wang, J.1    Wang, C.E.2    Orr, A.3    Tydlacka, S.4    Li, S.H.5    Li, X.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.