-
1
-
-
0027480960
-
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
-
The Huntington's Disease Collaborative Research Group
-
M.E. MacDonald, C.M. Ambrose, M.P. Duyao, R.H. Myers, C. Lin The Huntington's Disease Collaborative Research Group A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes Cell 72 1993 971 983
-
(1993)
Cell
, vol.72
, pp. 971-983
-
-
Macdonald, M.E.1
Ambrose, C.M.2
Duyao, M.P.3
Myers, R.H.4
Lin, C.5
-
2
-
-
26944478180
-
Huntingtin is cleaved by caspases in the cytoplasm and translocated to the nucleus via perinuclear sites in Huntington's disease patient lymphoblasts
-
A. Sawa, and E. Nagata S.H. Snyder Huntingtin is cleaved by caspases in the cytoplasm and translocated to the nucleus via perinuclear sites in Huntington's disease patient lymphoblasts Neurobiol. Dis. 20 2005 267 274
-
(2005)
Neurobiol. Dis.
, vol.20
, pp. 267-274
-
-
Sawa, A.1
Nagata, E.2
Snyder, S.H.3
-
3
-
-
33745003424
-
Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
-
R.K. Graham, and Y. Deng M.R. Hayden Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin Cell 125 2006 1179 1191
-
(2006)
Cell
, vol.125
, pp. 1179-1191
-
-
Graham, R.K.1
Deng, Y.2
Hayden, M.R.3
-
4
-
-
35648936428
-
Flanking polyproline sequences inhibit β-sheet structure in polyglutamine segments by inducing PPII-like helix structure
-
G. Darnell, and J.P.R.O. Orgel S.C. Meredith Flanking polyproline sequences inhibit β-sheet structure in polyglutamine segments by inducing PPII-like helix structure J. Mol. Biol. 374 2007 688 704
-
(2007)
J. Mol. Biol.
, vol.374
, pp. 688-704
-
-
Darnell, G.1
Orgel, J.P.R.O.2
Meredith, S.C.3
-
5
-
-
69849086690
-
Secondary structure of Huntingtin amino-terminal region
-
M.W. Kim, and Y. Chelliah I. Bezprozvanny Secondary structure of Huntingtin amino-terminal region Structure 17 2009 1205 1212
-
(2009)
Structure
, vol.17
, pp. 1205-1212
-
-
Kim, M.W.1
Chelliah, Y.2
Bezprozvanny, I.3
-
6
-
-
0032475931
-
Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
-
F. Saudou, and S. Finkbeiner M.E. Greenberg Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions Cell 95 1998 55 66
-
(1998)
Cell
, vol.95
, pp. 55-66
-
-
Saudou, F.1
Finkbeiner, S.2
Greenberg, M.E.3
-
7
-
-
13244258435
-
Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
-
E.J. Bennett, and N.F. Bence R.R. Kopito Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation Mol. Cell 17 2005 351 365
-
(2005)
Mol. Cell
, vol.17
, pp. 351-365
-
-
Bennett, E.J.1
Bence, N.F.2
Kopito, R.R.3
-
8
-
-
59649095699
-
Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
-
P.-H. Ren, and J.E. Lauckner R.R. Kopito Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates Nat. Cell Biol. 11 2009 219 225
-
(2009)
Nat. Cell Biol.
, vol.11
, pp. 219-225
-
-
Ren, P.-H.1
Lauckner, J.E.2
Kopito, R.R.3
-
9
-
-
67649856863
-
Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
-
Y. Nekooki-Machida, and M. Kurosawa M. Tanaka Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity Proc. Natl. Acad. Sci. USA 106 2009 9679 9684
-
(2009)
Proc. Natl. Acad. Sci. USA
, vol.106
, pp. 9679-9684
-
-
Nekooki-Machida, Y.1
Kurosawa, M.2
Tanaka, M.3
-
10
-
-
33750361540
-
A century-old debate on protein aggregation and neurodegeneration enters the clinic
-
P.T. Lansbury, and H.A. Lashuel A century-old debate on protein aggregation and neurodegeneration enters the clinic Nature 443 2006 774 779
-
(2006)
Nature
, vol.443
, pp. 774-779
-
-
Lansbury, P.T.1
Lashuel, H.A.2
-
11
-
-
33847662852
-
Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
-
C. Haass, and D.J. Selkoe Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide Nat. Rev. Mol. Cell Biol. 8 2007 101 112
-
(2007)
Nat. Rev. Mol. Cell Biol.
, vol.8
, pp. 101-112
-
-
Haass, C.1
Selkoe, D.J.2
-
12
-
-
77951988103
-
Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo
-
J. Legleiter, and E. Mitchell P.J. Muchowski Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo J. Biol. Chem. 285 2010 14777 14790
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 14777-14790
-
-
Legleiter, J.1
Mitchell, E.2
Muchowski, P.J.3
-
13
-
-
77954379810
-
Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool
-
M.A. Olshina, and L.M. Angley D.M. Hatters Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool J. Biol. Chem. 285 2010 21807 21816
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 21807-21816
-
-
Olshina, M.A.1
Angley, L.M.2
Hatters, D.M.3
-
14
-
-
77953567262
-
A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis
-
G. Ossato, and M.A. Digman E. Gratton A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis Biophys. J. 98 2010 3078 3085
-
(2010)
Biophys. J.
, vol.98
, pp. 3078-3085
-
-
Ossato, G.1
Digman, M.A.2
Gratton, E.3
-
15
-
-
34347356574
-
Solution structure of an amyloid-forming protein during photoinitiated hexamer-dodecamer transitions revealed through small-angle neutron scattering
-
A.C. Hamill, S.-C. Wang, and C.T. Lee Jr. Solution structure of an amyloid-forming protein during photoinitiated hexamer-dodecamer transitions revealed through small-angle neutron scattering Biochemistry 46 2007 7694 7705
-
(2007)
Biochemistry
, vol.46
, pp. 7694-7705
-
-
Hamill, A.C.1
Wang, S.-C.2
Lee, Jr.C.T.3
-
16
-
-
59849109485
-
A universal pathway for amyloid nucleus and precursor formation for insulin
-
A. Nayak, and M. Sorci G. Belfort A universal pathway for amyloid nucleus and precursor formation for insulin Proteins 74 2009 556 565
-
(2009)
Proteins
, vol.74
, pp. 556-565
-
-
Nayak, A.1
Sorci, M.2
Belfort, G.3
-
17
-
-
79959682444
-
Structural formation of huntingtin exon 1 aggregates probed by small-angle neutron scattering
-
C.B. Stanley, T. Perevozchikova, and V. Berthelier Structural formation of huntingtin exon 1 aggregates probed by small-angle neutron scattering Biophys. J. 100 2011 2504 2512
-
(2011)
Biophys. J.
, vol.100
, pp. 2504-2512
-
-
Stanley, C.B.1
Perevozchikova, T.2
Berthelier, V.3
-
18
-
-
12144288251
-
Venezuelan kindreds reveal that genetic and environmental factors modulate Huntington's disease age of onset
-
U.S.-Venezuela Collaborative Research Project
-
N.S. Wexler, J. Lorimer B. Landwehrmeyer U.S.-Venezuela Collaborative Research Project Venezuelan kindreds reveal that genetic and environmental factors modulate Huntington's disease age of onset Proc. Natl. Acad. Sci. USA 101 2004 3498 3503
-
(2004)
Proc. Natl. Acad. Sci. USA
, vol.101
, pp. 3498-3503
-
-
Wexler, N.S.1
Lorimer, J.2
Landwehrmeyer, B.3
-
19
-
-
0033551063
-
Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: Implications for Huntington's disease pathology
-
E. Scherzinger, and A. Sittler E.E. Wanker Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology Proc. Natl. Acad. Sci. USA 96 1999 4604 4609
-
(1999)
Proc. Natl. Acad. Sci. USA
, vol.96
, pp. 4604-4609
-
-
Scherzinger, E.1
Sittler, A.2
Wanker, E.E.3
-
20
-
-
0037062561
-
Amyloid-like features of polyglutamine aggregates and their assembly kinetics
-
S. Chen, and V. Berthelier R. Wetzel Amyloid-like features of polyglutamine aggregates and their assembly kinetics Biochemistry 41 2002 7391 7399
-
(2002)
Biochemistry
, vol.41
, pp. 7391-7399
-
-
Chen, S.1
Berthelier, V.2
Wetzel, R.3
-
21
-
-
0032849874
-
Quantification of β-sheet amyloid fibril structures with thioflavin T
-
H. LeVine III Quantification of β-sheet amyloid fibril structures with thioflavin T Methods Enzymol. 309 1999 274 284
-
(1999)
Methods Enzymol.
, vol.309
, pp. 274-284
-
-
Levine III, H.1
-
22
-
-
85055706702
-
Absolute calibration of small-angle neutron scattering data
-
G.D. Wignall, and F.S. Bates Absolute calibration of small-angle neutron scattering data J. Appl. Cryst. 20 1987 28 40
-
(1987)
J. Appl. Cryst.
, vol.20
, pp. 28-40
-
-
Wignall, G.D.1
Bates, F.S.2
-
23
-
-
0029185933
-
CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
-
D.I. Svergun, C. Barberato, and M.H.J. Koch CRYSOL - a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Cryst. 28 1995 768 773
-
(1995)
J. Appl. Cryst.
, vol.28
, pp. 768-773
-
-
Svergun, D.I.1
Barberato, C.2
Koch, M.H.J.3
-
24
-
-
28344442377
-
The polymerization of actin: Structural changes from small-angle neutron scattering
-
A.I. Norman, and R. Ivkov S.C. Greer The polymerization of actin: structural changes from small-angle neutron scattering J. Chem. Phys. 123 2005 154904
-
(2005)
J. Chem. Phys.
, vol.123
, pp. 154904
-
-
Norman, A.I.1
Ivkov, R.2
Greer, S.C.3
-
25
-
-
34249028643
-
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
-
B. Vestergaard, and M. Groenning D.I. Svergun A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils PLoS Biol. 5 2007 e134
-
(2007)
PLoS Biol.
, vol.5
, pp. 134
-
-
Vestergaard, B.1
Groenning, M.2
Svergun, D.I.3
-
27
-
-
0001280698
-
Approximations leading to a unified exponential/power-law approach to small-angle scattering
-
G. Beaucage Approximations leading to a unified exponential/power-law approach to small-angle scattering J. Appl. Cryst. 28 1995 717 728
-
(1995)
J. Appl. Cryst.
, vol.28
, pp. 717-728
-
-
Beaucage, G.1
-
28
-
-
77954487129
-
A new Guinier-Porod model
-
B. Hammouda A new Guinier-Porod model J. Appl. Cryst. 43 2010 716 719
-
(2010)
J. Appl. Cryst.
, vol.43
, pp. 716-719
-
-
Hammouda, B.1
-
30
-
-
0026910457
-
Determination of the regularization parameter in indirect-transform methods using perceptual criteria
-
D.I. Svergun Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Cryst. 25 1992 495 503
-
(1992)
J. Appl. Cryst.
, vol.25
, pp. 495-503
-
-
Svergun, D.I.1
-
31
-
-
79953067377
-
The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils
-
V.N. Sivanandam, and M. Jayaraman P.C. van der Wel The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils J. Am. Chem. Soc. 133 2011 4558 4566
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 4558-4566
-
-
Sivanandam, V.N.1
Jayaraman, M.2
Van Der Wel, P.C.3
-
32
-
-
84866419575
-
Structural features and domain organization of huntingtin fibrils
-
C.W. Bugg, and J.M. Isas R. Langen Structural features and domain organization of huntingtin fibrils J. Biol. Chem. 287 2012 31739 31746
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 31739-31746
-
-
Bugg, C.W.1
Isas, J.M.2
Langen, R.3
-
33
-
-
67349278762
-
The predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregation
-
N.W. Kelley, and X. Huang V.S. Pande The predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregation J. Mol. Biol. 388 2009 919 927
-
(2009)
J. Mol. Biol.
, vol.388
, pp. 919-927
-
-
Kelley, N.W.1
Huang, X.2
Pande, V.S.3
-
34
-
-
77649271684
-
Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin
-
T.E. Williamson, and A. Vitalis R.V. Pappu Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin J. Mol. Biol. 396 2010 1295 1309
-
(2010)
J. Mol. Biol.
, vol.396
, pp. 1295-1309
-
-
Williamson, T.E.1
Vitalis, A.2
Pappu, R.V.3
-
35
-
-
80053923210
-
Secondary structures of native and pathogenic huntingtin N-terminal fragments
-
M. Długosz, and J. Trylska Secondary structures of native and pathogenic huntingtin N-terminal fragments J. Phys. Chem. B 115 2011 11597 11608
-
(2011)
J. Phys. Chem. B
, vol.115
, pp. 11597-11608
-
-
Długosz, M.1
Trylska, J.2
-
36
-
-
80053259405
-
Conformations of the Huntingtin N-term in aqueous solution from atomistic simulations
-
G. Rossetti, and P. Cossio P. Carloni Conformations of the Huntingtin N-term in aqueous solution from atomistic simulations FEBS Lett. 585 2011 3086 3089
-
(2011)
FEBS Lett.
, vol.585
, pp. 3086-3089
-
-
Rossetti, G.1
Cossio, P.2
Carloni, P.3
-
37
-
-
84868142101
-
All-atom stability and oligomerization simulations of polyglutamine nanotubes with and without the 17-amino-acid N-terminal fragment of the Huntingtin protein
-
S. Côté, G. Wei, and N. Mousseau All-atom stability and oligomerization simulations of polyglutamine nanotubes with and without the 17-amino-acid N-terminal fragment of the Huntingtin protein J. Phys. Chem. B 116 2012 12168 12179
-
(2012)
J. Phys. Chem. B
, vol.116
, pp. 12168-12179
-
-
Côté, S.1
Wei, G.2
Mousseau, N.3
-
38
-
-
84862700907
-
Disease-associated polyglutamine stretches in monomeric huntingtin adopt a compact structure
-
C. Peters-Libeu, and J. Miller S. Finkbeiner Disease-associated polyglutamine stretches in monomeric huntingtin adopt a compact structure J. Mol. Biol. 421 2012 587 600
-
(2012)
J. Mol. Biol.
, vol.421
, pp. 587-600
-
-
Peters-Libeu, C.1
Miller, J.2
Finkbeiner, S.3
-
39
-
-
0037174879
-
Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
-
M.A. Poirier, and H. Li C.A. Ross Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization J. Biol. Chem. 277 2002 41032 41037
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 41032-41037
-
-
Poirier, M.A.1
Li, H.2
Ross, C.A.3
-
40
-
-
16544383250
-
Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
-
J.L. Wacker, and M.H. Zareie P.J. Muchowski Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer Nat. Struct. Mol. Biol. 11 2004 1215 1222
-
(2004)
Nat. Struct. Mol. Biol.
, vol.11
, pp. 1215-1222
-
-
Wacker, J.L.1
Zareie, M.H.2
Muchowski, P.J.3
-
41
-
-
64049119303
-
Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
-
A.K. Thakur, and M. Jayaraman R. Wetzel Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism Nat. Struct. Mol. Biol. 16 2009 380 389
-
(2009)
Nat. Struct. Mol. Biol.
, vol.16
, pp. 380-389
-
-
Thakur, A.K.1
Jayaraman, M.2
Wetzel, R.3
-
42
-
-
33745757474
-
The kinetics of nucleated polymerizations at high concentrations: Amyloid fibril formation near and above the "supercritical concentration"
-
E.T. Powers, and D.L. Powers The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration" Biophys. J. 91 2006 122 132
-
(2006)
Biophys. J.
, vol.91
, pp. 122-132
-
-
Powers, E.T.1
Powers, D.L.2
-
43
-
-
79952360891
-
Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent
-
K. Kar, and M. Jayaraman 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
Wetzel, R.3
-
44
-
-
34249290108
-
Atomic structures of amyloid cross-β spines reveal varied steric zippers
-
M.R. Sawaya, and S. Sambashivan D. Eisenberg Atomic structures of amyloid cross-β spines reveal varied steric zippers Nature 447 2007 453 457
-
(2007)
Nature
, vol.447
, pp. 453-457
-
-
Sawaya, M.R.1
Sambashivan, S.2
Eisenberg, D.3
-
45
-
-
73649140576
-
The common architecture of cross-β amyloid
-
T.R. Jahn, and O.S. Makin L.C. Serpell The common architecture of cross-β amyloid J. Mol. Biol. 395 2010 717 727
-
(2010)
J. Mol. Biol.
, vol.395
, pp. 717-727
-
-
Jahn, T.R.1
Makin, O.S.2
Serpell, L.C.3
-
46
-
-
33744831968
-
Polymorphic fibril formation by residues 10-40 of the Alzheimer's β-amyloid peptide
-
A.K. Paravastu, A.T. Petkova, and R. Tycko Polymorphic fibril formation by residues 10-40 of the Alzheimer's β-amyloid peptide Biophys. J. 90 2006 4618 4629
-
(2006)
Biophys. J.
, vol.90
, pp. 4618-4629
-
-
Paravastu, A.K.1
Petkova, A.T.2
Tycko, R.3
|