Ordway JM, Tallaksen-Greene S, Gutekunst CA, Bernstein EM, Cearley JA, et al. (1997) Ectopically expressed CAG repeats cause intranuclear inclusions and a progressive late onset neurological phenotype in the mouse. Cell 91: 753-763.
Robitaille Y, Lopes-Cendes I, Becher M, Rouleau G, Clark AW, (1997) The neuropathology of CAG repeat diseases: review and update of genetic and molecular features. Brain Pathol 7: 901-926.
Zoghbi HY, Orr HT, (2000) Glutamine repeats and neurodegeneration. Annu Rev Neurosci 23: 217-247.
Robertson AL, Bottomley SP, (2010) Towards the treatment of polyglutamine diseases: the modulatory role of protein context. Curr Med Chem 17: 3058-3068.
Diaz-Hernandez M, Moreno-Herrero F, Gomez-Ramos P, Moran MA, Ferrer I, et al. (2004) Biochemical, ultrastructural, and reversibility studies on huntingtin filaments isolated from mouse and human brain. J Neurosci 24: 9361-9371.
Sanchez I, Mahlke C, Yuan J, (2003) Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 421: 373-379.
Williams AJ, Paulson HL, (2008) Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci 31: 521-528.
Ross CA, (1997) Intranuclear neuronal inclusions: a common pathogenic mechanism for glutamine-repeat neurodegenerative diseases? Neuron 19: 1147-1150.
Yang W, Dunlap JR, Andrews RB, Wetzel R, (2002) Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum Mol Genet 11: 2905-2917.
Nagai Y, Inui T, Popiel HA, Fujikake N, Hasegawa K, et al. (2007) A toxic monomeric conformer of the polyglutamine protein. Nat Struct Mol Biol 14: 332-340.
Mukai H, Isagawa T, Goyama E, Tanaka S, Bence NF, et al. (2005) Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells. Proc Natl Acad Sci U S A 102: 10887-10892.
Olshina MA, Angley LM, Ramdzan YM, Tang J, Bailey MF, et al. (2010) Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool. J Biol Chem 285: 21807-21816.
Takahashi T, Kikuchi S, Katada S, Nagai Y, Nishizawa M, et al. (2008) Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic. Hum Mol Genet 17: 345-356.
Wetzel R, (2010) Misfolding and aggregation in Huntington disease and other expanded Polyglutamine repeat diseases. In: Ramirez-Alvarado M, Kelly JW, Dobson CM, editors. Protein Misfolding Diseases: Current and Emerging Principles and Therapies John Wiley and sons, Inc pp. 305-324.
Perutz MF, Johnson T, Suzuki M, Finch JT, (1994) Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci U S A 91: 5355-5358.
Ignatova Z, Thakur AK, Wetzel R, Gierasch LM, (2007) In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence. J Biol Chem 282: 36736-36743.
Tanaka M, Morishima I, Akagi T, Hashikawa T, Nukina N, (2001) Intra- and intermolecular beta-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases. J Biol Chem 276: 45470-45475.
Thakur AK, Jayaraman M, Mishra R, Thakur M, Chellgren VM, et al. (2009) Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. Nat Struct Mol Biol 16: 380-389.
Johnson SM, Wiseman RL, Sekijima Y, Green NS, Adamski-Werner SL, et al. (2005) Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses. Acc Chem Res 38: 911-921.
Dumoulin M, Kumita JR, Dobson CM, (2006) Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants. Acc Chem Res 39: 603-610.
Dumoulin M, Last AM, Desmyter A, Decanniere K, Canet D, et al. (2003) A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature 424: 783-788.
Bhattacharyya A, Thakur AK, Chellgren VM, Thiagarajan G, Williams AD, et al. (2006) Oligoproline effects on polyglutamine conformation and aggregation. J Mol Biol 355: 524-535.
Sharma D, Sharma S, Pasha S, Brahmachari SK, (1999) Peptide models for inherited neurodegenerative disorders: conformation and aggregation properties of long polyglutamine peptides with and without interruptions. FEBS Lett 456: 181-185.
Bulone D, Masino L, Thomas DJ, San Biagio PL, Pastore A, (2006) The interplay between PolyQ and protein context delays aggregation by forming a reservoir of protofibrils. PLoS ONE 1: e111.
Hollenbach B, Scherzinger E, Schweiger K, Lurz R, Lehrach H, et al. (1999) Aggregation of truncated GST-HD exon 1 fusion proteins containing normal range and expanded glutamine repeats. Philos Trans R Soc Lond B Biol Sci 354: 991-994.
Nozaki K, Onodera O, Takano H, Tsuji S, (2001) Amino acid sequences flanking polyglutamine stretches influence their potential for aggregate formation. Neuroreport 12: 3357-3364.
Cooper JK, Schilling G, Peters MF, Herring WJ, Sharp AH, et al. (1998) Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture. Hum Mol Genet 7: 783-790.
Martindale D, Hackam A, Wieczorek A, Ellerby L, Wellington C, et al. (1998) Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates. Nat Genet 18: 150-154.
Ignatova Z, Gierasch LM, (2006) Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein. J Biol Chem 281: 12959-12967.
Ellisdon AM, Thomas B, Bottomley SP, (2006) The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step. J Biol Chem 281: 16888-16896.
Ellisdon AM, Pearce MC, Bottomley SP, (2007) Mechanisms of ataxin-3 misfolding and fibril formation: kinetic analysis of a disease-associated polyglutamine protein. J Mol Biol 368: 595-605.
Robertson AL, Bate MA, Buckle AM, Bottomley SP, (2011) The rate of polyQ-mediated aggregation is dramatically affected by the number and location of surrounding domains. J Mol Biol 413: 879-887.
Robertson AL, Horne J, Ellisdon AM, Thomas B, Scanlon MJ, et al. (2008) The structural impact of a polyglutamine tract is location-dependent. Biophys J 95: 5922-5930.
Saunders HM, Gilis D, Rooman M, Dehouck Y, Robertson AL, et al. (2011) Flanking domain stability modulates the aggregation kinetics of a polyglutamine disease protein. Protein Sci 20: 1675-1681.
Tobelmann MD, Murphy RM, (2011) Location trumps length: polyglutamine-mediated changes in folding and aggregation of a host protein. Biophys J 100: 2773-2782.
Bennett MJ, Huey-Tubman KE, Herr AB, West AP Jr, Ross SA, et al. (2002) Inaugural Article: A linear lattice model for polyglutamine in CAG-expansion diseases. Proc Natl Acad Sci U S A 99: 11634-11639.
Masino L, Kelly G, Leonard K, Trottier Y, Pastore A, (2002) Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins. FEBS Lett 513: 267-272.
Tobelmann MD, Kerby RL, Murphy RM, (2008) A strategy for generating polyglutamine 'length libraries' in model host proteins. Protein Eng Des Sel 21: 161-164.
Klein FA, Pastore A, Masino L, Zeder-Lutz G, Nierengarten H, et al. (2007) Pathogenic and non-pathogenic polyglutamine tracts have similar structural properties: towards a length-dependent toxicity gradient. J Mol Biol 371: 235-244.
Knox JR, Moews PC, (1991) Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2 Å resolution and analysis of hydration. J Mol Biol 220: 435-455.
Matagne A, Misselyn-Bauduin AM, Joris B, Erpicum T, Granier B, et al. (1990) The diversity of the catalytic properties of class A beta-lactamases. Biochem J 265: 131-146.
Vandevenne M, Filee P, Scarafone N, Cloes B, Gaspard G, et al. (2007) The Bacillus licheniformis BlaP beta-lactamase as a model protein scaffold to study the insertion of protein fragments. Protein Sci 16: 2260-2271.
Vandevenne M, Gaspard G, Yilmaz N, Giannotta F, Frère JM, et al. (2008) Rapid and easy development of versatile tools to study protein/ligand interactions. Protein Eng Des Sel 21: 443-451.
Ladurner AG, Fersht AR, (1997) Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates. J Mol Biol 273: 330-337.
Harper JD, Lansbury PT Jr, (1997) 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: 385-407.
Serpell LC, Fraser PE, Sunde M, (1999) X-ray fiber diffraction of amyloid fibrils. Methods Enzymol 309: 526-536.
Scherzinger E, Lurz R, Turmaine M, Mangiarini L, Hollenbach B, et al. (1997) Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 90: 549-558.
Chen S, Berthelier V, Yang W, Wetzel R, (2001) Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. J Mol Biol 311: 173-182.
DiFiglia M, Sapp E, Chase KO, Davies SW, Bates GP, et al. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277: 1990-1993.
Crick SL, Jayaraman M, Frieden C, Wetzel R, Pappu RV, (2006) Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions. Proc Natl Acad Sci U S A 103: 16764-16769.
Lakhani VV, Ding F, Dokholyan NV, (2010) Polyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences. PLoS computational biology 6: e1000772.
Vitalis A, Wang X, Pappu RV, (2007) Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories. Biophys J 93: 1923-1937.
Kim MW, Chelliah Y, Kim SW, Otwinowski Z, Bezprozvanny I, (2009) Secondary structure of Huntingtin amino-terminal region. Structure 17: 1205-1212.
Ordway JM, Detloff PJ, (1996) In vitro synthesis and cloning of long CAG repeats. Biotechniques 21: 609-610, 612.
Han KK, Tetaert D, Debuire B, Dautrevaux M, Biserte G, (1977) [Sequential Edman degredation]. Biochimie 59: 557-576.
Dumoulin M, Conrath K, Van Meirhaeghe A, Meersman F, Heremans K, et al. (2002) Single-domain antibody fragments with high conformational stability. Protein Sci 11: 500-515.
Pace CN, Scholtz M, (1997) Measuring the conformational stability of a protein. In: Creighton TE, editors. Protein structure: a pratical approach. Second Edition ed IRL press pp. 299-321.
Pace CN, (1990) Measuring and increasing protein stability. Trends Biotechnol 8: 93-98.
Santoro MM, Bolen DW, (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27: 8063-8068.
Vandenameele J, Lejeune A, Di Paolo A, Brans A, Frère JM, et al. (2010) Folding of class A beta-lactamases is rate-limited by peptide bond isomerization and occurs via parallel pathways. Biochemistry 49: 4264-4275.
El Hajjaji H, Dumoulin M, Matagne A, Colau D, Roos G, et al. (2009) The zinc center influences the redox and thermodynamic properties of Escherichia coli thioredoxin 2. J Mol Biol 386: 60-71.
Mossuto MF, Dhulesia A, Devlin G, Frare E, Kumita JR, et al. (2010) The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity. J Mol Biol 402: 783-796.
Ambler RP, Coulson AF, Frère JM, Ghuysen JM, Joris B, et al. (1991) A standard numbering scheme for the class A beta-lactamases. Biochem J 276 (Pt 1): 269-270.
