메뉴 건너뛰기




Volumn 18, Issue 3, 2011, Pages 328-336

Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent

Author keywords

[No Author keywords available]

Indexed keywords

POLYGLUTAMINE;

EID: 79952360891     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1992     Document Type: Article
Times cited : (175)

References (54)
  • 1
    • 3242692878 scopus 로고    scopus 로고
    • The polyglutamine diseases
    • (eds. Bates, G.P., Harper, P.S. & Jones, L.) Oxford University Press, Oxford, UK
    • Bates, G.P. & Benn, C. The polyglutamine diseases. in Huntington's Disease (eds. Bates, G.P., Harper, P.S. & Jones, L.) 429-472 (Oxford University Press, Oxford, UK, 2002).
    • (2002) Huntington's Disease , pp. 429-472
    • Bates, G.P.1    Benn, C.2
  • 2
    • 27644596641 scopus 로고    scopus 로고
    • What is the role of protein aggregation in neurodegeneration?
    • DOI 10.1038/nrm1742, PII N1742
    • Ross, C.A. & Poirier, M.A. Opinion: What is the role of protein aggregation in neurodegeneration? Nat. Rev. Mol. Cell Biol. 6, 891-898 (2005). (Pubitemid 41568738)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.11 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 4
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • DOI 10.1006/jmbi.2001.4850
    • Chen, S., Berthelier, V., Yang, W. & Wetzel, R. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. J. Mol. Biol. 311, 173-182 (2001). (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
  • 9
    • 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. 11, 1215-1222 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 10
    • 64049119303 scopus 로고    scopus 로고
    • Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
    • Thakur, A.K. et al. Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. Nat. Struct. Mol. Biol. 16, 380-389 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 380-389
    • Thakur, A.K.1
  • 11
    • 35648992125 scopus 로고    scopus 로고
    • The interplay between PolyQ and protein context delays aggregation by forming a reservoir of protofbrils
    • Bulone, D., Masino, L., Thomas, D.J., San Biagio, P.L. & Pastore, A. The interplay between PolyQ and protein context delays aggregation by forming a reservoir of protofbrils. PLoS One 1, e111 (2006).
    • (2006) PLoS One , vol.1
    • Bulone, D.1    Masino, L.2    Thomas, D.J.3    San Biagio, P.L.4    Pastore, A.5
  • 12
    • 37549011420 scopus 로고    scopus 로고
    • In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the fanking sequence
    • Ignatova, Z., Thakur, A.K., Wetzel, R. & Gierasch, L.M. In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the fanking sequence. J. Biol. Chem. 282, 36736-36743 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 36736-36743
    • Ignatova, Z.1    Thakur, A.K.2    Wetzel, R.3    Gierasch, L.M.4
  • 13
    • 28444444502 scopus 로고    scopus 로고
    • Polyglutamine is not all: The functional role of the AXH domain in the ataxin-1 protein
    • DOI 10.1016/j.jmb.2005.09.083, PII S0022283605011629
    • de Chiara, C., Menon, R.P., Dal Piaz, F., Calder, L. & Pastore, A. Polyglutamine is not all: the functional role of the AXH domain in the ataxin-1 protein. J. Mol. Biol. 354, 883-893 (2005). (Pubitemid 41735509)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.4 , pp. 883-893
    • De Chiara, C.1    Menon, R.P.2    Dal Piaz, F.3    Calder, L.4    Pastore, A.5
  • 14
    • 33745195252 scopus 로고    scopus 로고
    • The two-stage pathway of ataxin-3 fbrillogenesis involves a polyglutamine-independent step
    • Ellisdon, A.M., Thomas, B. & Bottomley, S.P. The two-stage pathway of ataxin-3 fbrillogenesis involves a polyglutamine-independent step. J. Biol. Chem. 281, 16888-16896 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 16888-16896
    • Ellisdon, A.M.1    Thomas, B.2    Bottomley, S.P.3
  • 16
    • 72149107077 scopus 로고    scopus 로고
    • Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice
    • Gu, X. et al. Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice. Neuron 64, 828-840 (2009).
    • (2009) Neuron , vol.64 , pp. 828-840
    • Gu, X.1
  • 17
    • 22744437069 scopus 로고    scopus 로고
    • Natively disordered proteins: Functions and predictions
    • DOI 10.2165/00822942-200403020-00005
    • Romero, P., Obradovic, Z. & Dunker, A.K. Natively disordered proteins: functions and predictions. Appl. Bioinformatics 3, 105-113 (2004). (Pubitemid 41032063)
    • (2004) Applied Bioinformatics , vol.3 , Issue.2-3 , pp. 105-113
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 19
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • DOI 10.1016/S0076-6879(99)09019-9
    • Ferrone, F. Analysis of protein aggregation kinetics. Methods Enzymol. 309, 256-274 (1999). (Pubitemid 29446454)
    • (1999) Methods in Enzymology , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 22
    • 70349194529 scopus 로고    scopus 로고
    • The impact of ataxin-1-like histidine insertions on polyglutamine aggregation
    • Jayaraman, M., Kodali, R. & Wetzel, R. The impact of ataxin-1-like histidine insertions on polyglutamine aggregation. Protein Eng. Des. Sel. 22, 469-478 (2009).
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 469-478
    • Jayaraman, M.1    Kodali, R.2    Wetzel, R.3
  • 23
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • DOI 10.1016/S1097-2765(04)00151-0, PII S1097276504001510
    • Venkatraman, P., Wetzel, R., Tanaka, M., Nukina, N. & Goldberg, A.L. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them intact during degradation of polyglutamine-containing proteins. Mol. Cell 14, 95-104 (2004). (Pubitemid 38469912)
    • (2004) Molecular Cell , vol.14 , Issue.1 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 24
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis
    • DOI 10.1006/jmbi.2001.4970
    • Kirkitadze, M.D., Condron, M.M. & Teplow, D.B. Identifcation and characterization of key kinetic intermediates in amyloid beta-protein fbrillogenesis. J. Mol. Biol. 312, 1103-1119 (2001). (Pubitemid 32980329)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.5 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 25
    • 35848945494 scopus 로고    scopus 로고
    • Reconsidering the mechanism of polyglutamine peptide aggregation
    • DOI 10.1021/bi700806c
    • Lee, C.C., Walters, R.H. & Murphy, R.M. Reconsidering the mechanism of polyglutamine peptide aggregation. Biochemistry 46, 12810-12820 (2007). (Pubitemid 350060102)
    • (2007) Biochemistry , vol.46 , Issue.44 , pp. 12810-12820
    • Lee, C.C.1    Walters, R.H.2    Murphy, R.M.3
  • 26
    • 0035084096 scopus 로고    scopus 로고
    • And disaggregation of polyglutamine peptides
    • Chen, S. & Wetzel, R. Solubilization and disaggregation of polyglutamine peptides. Protein Sci. 10, 887-891 (2001).
    • (2001) Protein Sci. , vol.10 , pp. 887-891
    • Chen, S.1    Solubilization, W.R.2
  • 27
    • 27344445112 scopus 로고    scopus 로고
    • Protein folding and aggregation in the expanded polyglutamine repeat diseases
    • (eds Buchner, J. & Kiefhaber, T.) Part II Wiley-VCH, Weinheim
    • Wetzel, R. Protein folding and aggregation in the expanded polyglutamine repeat diseases. in The Protein Folding Handbook (eds Buchner, J. & Kiefhaber, T.) Part II, 1170-1214 (Wiley-VCH, Weinheim, 2005).
    • (2005) The Protein Folding Handbook , pp. 1170-1214
    • Wetzel, R.1
  • 28
    • 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
    • O'Nuallain, B. et al. Kinetics and thermodynamics of amyloid assembly using a high-performance liquid chromatography-based sedimentation assay. Methods Enzymol. 413, 34-74 (2006). (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
  • 29
    • 77951988103 scopus 로고    scopus 로고
    • Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo
    • Legleiter, J. et al. Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo. J. Biol. Chem. 285, 14777-14790 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 14777-14790
    • Legleiter, J.1
  • 31
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • DOI 10.1021/bi011772q
    • Chen, S., Berthelier, V., Hamilton, J.B., O'Nuallain, B. & Wetzel, R. Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochemistry 41, 7391-7399 (2002). (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
  • 32
    • 79952189175 scopus 로고    scopus 로고
    • Assays for studying nucleated aggregation of polyglutamine proteins
    • published online doi:10.1016/j.ymeth.2011.01.001 (11 January 2011)
    • Jayaraman, M., Thakur, A.K., Kar, K., Kodali, R. & Wetzel, R. Assays for studying nucleated aggregation of polyglutamine proteins. Methods published online, doi:10.1016/j.ymeth.2011.01.001 (11 January 2011).
    • Methods
    • Jayaraman, M.1    Thakur, A.K.2    Kar, K.3    Kodali, R.4    Wetzel, R.5
  • 33
    • 35648945914 scopus 로고    scopus 로고
    • Protein aggregation processes: In search of the mechanism
    • DOI 10.1110/ps.073164107
    • Frieden, C. Protein aggregation processes: in search of the mechanism. Protein Sci. 16, 2334-2344 (2007). (Pubitemid 350036740)
    • (2007) Protein Science , vol.16 , Issue.11 , pp. 2334-2344
    • Frieden, C.1
  • 34
    • 25444522601 scopus 로고    scopus 로고
    • Thermodynamics of Aβ(1-40) amyloid fibril elongation
    • DOI 10.1021/bi050927h
    • O'Nuallain, B., Shivaprasad, S., Kheterpal, I. & Wetzel, R. Thermodynamics of Aβ(1-40) amyloid fbril elongation. Biochemistry 44, 12709-12718 (2005). (Pubitemid 41377310)
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12709-12718
    • O'Nuallain, B.1    Shivaprasad, S.2    Kheterpal, I.3    Wetzel, R.4
  • 35
    • 1842686289 scopus 로고    scopus 로고
    • Kinetic analysis of beta-amyloid fibril elongation
    • DOI 10.1016/j.ab.2004.01.014, PII S0003269704000922
    • Cannon, M.J., Williams, A.D., Wetzel, R. & Myszka, D.G. Kinetic analysis of β-amyloid fbril elongation. Anal. Biochem. 328, 67-75 (2004). (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
  • 36
    • 33749597429 scopus 로고    scopus 로고
    • Nucleation: The Connections Between Equilibrium and Kinetic Behavior
    • DOI 10.1016/S0076-6879(06)12017-0, PII S0076687906120170
    • Ferrone, F.A. Nucleation: the connections between equilibrium and kinetic behavior. Methods Enzymol. 412, 285-299 (2006). (Pubitemid 44548586)
    • (2006) Methods in Enzymology , vol.412 , pp. 285-299
    • Ferrone, F.A.1
  • 37
    • 71449084004 scopus 로고    scopus 로고
    • The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation
    • Tam, S. et al. The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Nat. Struct. Mol. Biol. 16, 1279-1285 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1279-1285
    • Tam, S.1
  • 39
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • Collins, S.R., Douglass, A., Vale, R.D. & Weissman, J.S. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2, e321 (2004).
    • (2004) PLoS Biol. , vol.2
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 40
    • 23644449548 scopus 로고    scopus 로고
    • Influence of the N-terminal domain on the aggregation properties of the prion protein
    • DOI 10.1110/ps.051434005
    • Frankenfeld, K.N., Powers, E.T. & Kelly, J.W. Infuence of the N-terminal domain on the aggregation properties of the prion protein. Protein Sci. 14, 2154-2166 (2005). (Pubitemid 41132380)
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2154-2166
    • Frankenfield, K.N.1    Powers, E.T.2    Kelly, J.W.3
  • 41
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • Xue, W.F., Homans, S.W. & Radford, S.E. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc. Natl. Acad. Sci. USA 105, 8926-8931 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8926-8931
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 42
    • 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. 393, 978-992 (2009).
    • (2009) J. Mol. Biol. , vol.393 , pp. 978-992
    • Walters, R.H.1    Murphy, R.M.2
  • 43
    • 55449095000 scopus 로고    scopus 로고
    • Molecular origin of polyglutamine aggregation in neurodegenerative diseases
    • Khare, S.D., Ding, F., Gwanmesia, K.N. & Dokholyan, N.V. Molecular origin of polyglutamine aggregation in neurodegenerative diseases. PLOS Comput. Biol. 1, 230-235 (2005).
    • (2005) PLOS Comput. Biol. , vol.1 , pp. 230-235
    • Khare, S.D.1    Ding, F.2    Gwanmesia, K.N.3    Dokholyan, N.V.4
  • 44
    • 33845652619 scopus 로고    scopus 로고
    • Effects of chain length on the aggregation of model polyglutamine peptides: Molecular dynamics simulations
    • DOI 10.1002/prot.21132
    • Marchut, A.J. & Hall, C.K. Effects of chain length on the aggregation of model polyglutamine peptides: molecular dynamics simulations. Proteins 66, 96-109 (2007). (Pubitemid 44955982)
    • (2007) Proteins: Structure, Function and Genetics , vol.66 , Issue.1 , pp. 96-109
    • Marchut, A.J.1    Hall, C.K.2
  • 45
    • 77953518502 scopus 로고    scopus 로고
    • Polyglutamine fbrils are formed using a simple designed beta-hairpin model
    • Smith, M.H. et al. Polyglutamine fbrils are formed using a simple designed beta-hairpin model. Proteins 78, 1971-1979 (2010).
    • (2010) Proteins , vol.78 , pp. 1971-1979
    • Smith, M.H.1
  • 47
    • 14044278010 scopus 로고    scopus 로고
    • New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils
    • DOI 10.1021/bm0494388
    • Sikorski, P. & Atkins, E. New model for crystalline polyglutamine assemblies and their connection with amyloid fbrils. Biomacromolecules 6, 425-432 (2005). (Pubitemid 40277042)
    • (2005) Biomacromolecules , vol.6 , Issue.1 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 50
    • 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 63, 297-311 (2006).
    • (2006) Proteins , vol.63 , pp. 297-311
    • Wang, X.1    Vitalis, A.2    Wyczalkowski, M.A.3    Pappu, R.V.4
  • 51
    • 0033450855 scopus 로고    scopus 로고
    • Folding of oligoglutamines: A theoretical approach based upon thermodynamics and molecular mechanics
    • Starikov, E.B., Lehrach, H. & Wanker, E.E. Folding of oligoglutamines: a theoretical approach based upon thermodynamics and molecular mechanics. J. Biomol. Struct. Dyn. 17, 409-427 (1999). (Pubitemid 30036652)
    • (1999) Journal of Biomolecular Structure and Dynamics , vol.17 , Issue.3 , pp. 409-427
    • Starikov, E.B.1    Lehrach, H.2    Wanker, E.E.3
  • 52
    • 43849090507 scopus 로고    scopus 로고
    • Insights into structure, stability, and toxicity of monomeric and aggregated polyglutamine models from molecular dynamics simulations
    • Esposito, L., Paladino, A., Pedone, C. & Vitagliano, L. Insights into structure, stability, and toxicity of monomeric and aggregated polyglutamine models from molecular dynamics simulations. Biophys. J. 94, 4031-4040 (2008).
    • (2008) Biophys. J. , vol.94 , pp. 4031-4040
    • Esposito, L.1    Paladino, A.2    Pedone, C.3    Vitagliano, L.4
  • 53
    • 77954616668 scopus 로고    scopus 로고
    • Polyglutamine induced misfolding of huntingtin exon1 is modulated by the fanking sequences
    • Lakhani, V.V., Ding, F. & Dokholyan, N.V. Polyglutamine induced misfolding of huntingtin exon1 is modulated by the fanking sequences. PLOS Comput. Biol. 6, e1000772 (2010).
    • (2010) PLOS Comput. Biol. , vol.6
    • Lakhani, V.V.1    Ding, F.2    Dokholyan, N.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.