P.O. Bauer, and N. Nukina The pathogenic mechanisms of polyglutamine diseases and current therapeutic strategies J. Neurochem. 110 6 2009 1737 1765
J.M. Ordway Ectopically expressed CAG repeats cause intranuclear inclusions and a progressive late onset neurological phenotype in the mouse Cell 91 6 1997 753 763
Y.W. Chen, K. Stott, and M.F. Perutz Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat Proc. Natl. Acad. Sci. U. S. A. 96 4 1999 1257 1261
C.A. Ross Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders Neuron 35 5 2002 819 822
J.B. Penney Jr. CAG repeat number governs the development rate of pathology in Huntington's disease Ann. Neurol. 41 5 1997 689 692
L. Schols Autosomal dominant cerebellar ataxias: clinical features, genetics, and pathogenesis Lancet Neurol. 3 5 2004 291 304
S.W. Davies Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation Cell 90 3 1997 537 548
R. Wetzel Misfolding and aggregation in Huntington disease and other expanded Polyglutamine repeat diseases K.J. D.C., and M. Ramirez-Alvarado Protein Misfolding Diseases: Current and Emerging Principles and Therapies 2010 305 324
C.A. Ross Intranuclear neuronal inclusions: a common pathogenic mechanism for glutamine-repeat neurodegenerative diseases? Neuron 19 6 1997 1147 1150
A. Bhattacharyya Oligoproline effects on polyglutamine conformation and aggregation J. Mol. Biol. 355 3 2006 524 535
K. Nozaki Amino acid sequences flanking polyglutamine stretches influence their potential for aggregate formation Neuroreport 12 15 2001 3357 3364
L. Masino Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins FEBS Lett. 513 2-3 2002 267 272
D. Bulone The interplay between PolyQ and protein context delays aggregation by forming a reservoir of protofibrils PLoS ONE 1 2006 e111
M.F. Perutz Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases Proc. Natl. Acad. Sci. U. S. A. 91 12 1994 5355 5358
A.K. Thakur Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism Nat. Struct. Mol. Biol. 16 4 2009 380 389
A.L. Robertson The rate of polyQ-mediated aggregation is dramatically affected by the number and location of surrounding domains J. Mol. Biol. 413 4 2011 879 887
A.L. Robertson The structural impact of a polyglutamine tract is location-dependent Biophys. J. 95 12 2008 5922 5930
A.L. Robertson, and S.P. Bottomley Towards the treatment of polyglutamine diseases: the modulatory role of protein context Curr. Med. Chem. 17 27 2010 3058 3068
M. Tanaka Intra- and intermolecular beta-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases J. Biol. Chem. 276 48 2001 45470 45475
R.P. Menon Mapping the self-association domains of ataxin-1: identification of novel non overlapping motifs Peer J. 2 2014 e323
A.M. Ellisdon, B. Thomas, and S.P. Bottomley The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step J. Biol. Chem. 281 25 2006 16888 16896
S.L. Crick Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation Proc. Natl. Acad. Sci. U. S. A. 110 50 2013 20075 20080
M.D. Tobelmann, and R.M. Murphy Location trumps length: polyglutamine-mediated changes in folding and aggregation of a host protein Biophys. J. 100 11 2011 2773 2782
S. Chen, F.A. Ferrone, and R. Wetzel Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation Proc. Natl. Acad. Sci. U. S. A. 99 18 2002 11884 11889
A.L. Robertson, and S.P. Bottomley Molecular pathways to polyglutamine aggregation Adv. Exp. Med. Biol. 769 2012 115 124
K. Sugaya, and S. Matsubara Nucleation of protein aggregation kinetics as a basis for genotype-phenotype correlations in polyglutamine diseases Mol. Neurodegener. 4 2009 29
E. Scherzinger Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology Proc. Natl. Acad. Sci. U. S. A. 96 8 1999 4604 4609
S. Barton The length dependence of the polyQ-mediated protein aggregation J. Biol. Chem. 282 35 2007 25487 25492
J.D. Harper, and P.T. Lansbury Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 66 1997 385 407
M.F. Perutz Glutamine repeats and inherited neurodegenerative diseases: molecular aspects Curr. Opin. Struct. Biol. 6 6 1996 848 858
N. Slepko Normal-repeat-length polyglutamine peptides accelerate aggregation nucleation and cytotoxicity of expanded polyglutamine proteins Proc. Natl. Acad. Sci. U. S. A. 103 39 2006 14367 14372
R.H. Walters Elongation kinetics of polyglutamine peptide fibrils: a quartz crystal microbalance with dissipation study J. Mol. Biol. 421 2-3 2012 329 347
C. Huynen Class a-lactamases as versatile scaffolds to create hybrid enzymes: applications from basic research to medicine Biomed. Res. Int. 2013 2013 827621
A.K. Buell, C.M. Dobson, and M.E. Welland Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances Methods Mol. Biol. 849 2012 101 119
T.P. Knowles Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass Proc. Natl. Acad. Sci. U. S. A. 104 24 2007 10016 10021
N. Scarafone Amyloid-like fibril formation by polyQ proteins: a critical balance between the polyQ length and the constraints imposed by the host protein PLoS ONE 7 3 2012 e31253
R.P. Ambler A standard numbering scheme for the class A beta-lactamases Biochem. J. 276 Pt 1 1991 269 270
M. Vandevenne The Bacillus licheniformis BlaP beta-lactamase as a model protein scaffold to study the insertion of protein fragments Protein Sci. 16 10 2007 2260 2271
A.K. Buell Surface attachment of protein fibrils via covalent modification strategies J. Phys. Chem. B 114 34 2010 10925 10938
W.P. Hu Kinetic analysis of beta-amyloid peptide aggregation induced by metal ions based on surface plasmon resonance biosensing J. Neurosci. Methods 154 1-2 2006 190 197
A.K. Buell Population of nonnative states of lysozyme variants drives amyloid fibril formation J. Am. Chem. Soc. 133 20 2011 7737 7743
M.B. Hovgaard Quartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interface Biophys. J. 93 6 2007 2162 2169
J.A. Kotarek, K.C. Johnson, and M.A. Moss Quartz crystal microbalance analysis of growth kinetics for aggregation intermediates of the amyloid-beta protein Anal. Biochem. 378 1 2008 15 24
A.K. Buell Electrostatic effects in filamentous protein aggregation Biophys. J. 104 5 2013 1116 1126
G. Sauerbrey Verwendung von Schwingquarzen zur Wägung dünner Schichten und zur Mikrowägung Z. Phys. 155 1959 206 222
T.C.T. Michaels Quantitative analysis of diffusive reactions at the solid-liquid interface in finite systems J. Phys. Chem. Lett. 5 2014 695 699
K.K. Sweers Atomic force microscopy under controlled conditions reveals structure of C-terminal region of alpha-synuclein in amyloid fibrils ACS Nano 6 7 2012 5952 5960
R. Khurana A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy Biophys. J. 85 2 2003 1135 1144
S. Chen Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity J. Mol. Biol. 311 1 2001 173 182
K. Kar d-polyglutamine amyloid recruits l-polyglutamine monomers and kills cells J. Mol. Biol. 426 4 2014 816 829
E. Preisinger Evidence for a recruitment and sequestration mechanism in Huntington's disease Philos. Trans. R. Soc. Lond. B Biol. Sci. 354 1386 1999 1029 1034
M.K. Perez Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation J. Cell Biol. 143 6 1998 1457 1470
K. Kar Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent Nat. Struct. Mol. Biol. 18 3 2011 328 336
B.S. Heck, F. Doll, and K. Hauser Length-dependent conformational transitions of polyglutamine repeats as molecular origin of fibril initiation Biophys. Chem. 185 2014 47 57
E. Landrum, and R. Wetzel Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formation J. Biol. Chem. 289 15 2014 10254 10260
J.R. Knox, and P.C. Moews Beta-lactamase of Bacillus licheniformis 749/C Refinement at 2A resolution and analysis of hydration J Mol Biol 202 2 1991 435 455
