Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
about
Improved activities of CREB binding protein, heterogeneous nuclear ribonucleoproteins and proteasome following downregulation of noncoding hsromega transcripts help suppress poly(Q) pathogenesis in fly modelsThe predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregationMechanism of prion propagation: amyloid growth occurs by monomer additionMolecular origin of polyglutamine aggregation in neurodegenerative diseases.Fibrillogenesis of huntingtin and other glutamine containing proteinsThe structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice modelA protein aggregation based test for screening of the agents affecting thermostability of proteinsSolvent microenvironments and copper binding alters the conformation and toxicity of a prion fragmentMisfolding of proteins with a polyglutamine expansion is facilitated by proteasomal chaperonesThe soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel.Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein.Thermodynamic parameters for salt-induced reversible protein precipitation from automated microscale experiments.Reduction of the C191-C220 disulfide of α-chymotrypsinogen A reduces nucleation barriers for aggregation.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Trinucleotide repeats: a structural perspectiveElongation kinetics of polyglutamine peptide fibrils: a quartz crystal microbalance with dissipation study.Nuclear aggresomes form by fusion of PML-associated aggregates.Nucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constantsMutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo.Dynamic imaging by fluorescence correlation spectroscopy identifies diverse populations of polyglutamine oligomers formed in vivo.Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutionsThe interplay between PolyQ and protein context delays aggregation by forming a reservoir of protofibrils.Polyglutamine expansion mutation yields a pathological epitope linked to nucleation of protein aggregate: determinant of Huntington's disease onset.Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies.Stable polyglutamine dimers can contain β-hairpins with interdigitated side chains-but not α-helices, β-nanotubes, β-pseudohelices, or steric zippers.Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formationConformational switching in PolyGln amyloid fibrils resulting from a single amino acid insertion.A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo.Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerizationMonomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionPolyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences.The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis.Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation.In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence.From the test tube to the cell: exploring the folding and aggregation of a beta-clam protein.Characterization of a possible amyloidogenic precursor in glutamine-repeat neurodegenerative diseases.An aggregation sensing reporter identifies leflunomide and teriflunomide as polyglutamine aggregate inhibitors.polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reactionA coarse-grained model for polyglutamine aggregation modulated by amphipathic flanking sequences
P2860
Q24626685-672D97AC-DB54-4457-90FA-10BBF9DBF1CAQ24650711-416EDD34-0BF7-4EBF-812A-55A0C24C7815Q24793082-912EB720-D4D1-4250-B7B5-68490DB6622DQ24816819-E6F05F93-1500-41A6-88A6-1F165BAFA2C0Q26850062-0DDBF8C9-FA88-4244-83DE-2916935F5134Q27644551-0858D48C-FED4-449B-B323-23719DC295B4Q28478940-06D23055-E40A-4B5D-8C05-E166BD1E1A88Q28538070-723E68EB-0E7E-4772-8E51-34E609A2FEB2Q28569827-2DA868EC-DBC0-443C-BE93-66C3C6A1833AQ30155509-BA3D8C05-27B1-4B72-9AEB-123FE193744DQ30159881-B04BF57F-F31D-4497-AAA8-D8BB2956FFA4Q30394139-8D61F250-2967-4F54-81E4-4F389777D8FDQ30408748-68E2896C-A4FC-4A80-A728-7C2AD5C48E65Q30427825-A58F8756-B075-44DC-A97C-2950E1A2CAFEQ30432441-4C01BCA0-B74D-4CFE-9CC6-8E8847CA7F90Q30450982-E2F3E761-8E34-4559-B178-73D1BB91FCE0Q30476220-B3388AA8-3F4E-4AE6-9C9B-E0781428AEA6Q30481896-0D701C5E-2C75-4802-B008-8A010417A384Q30494325-A3D18362-1CCD-458C-8E32-1FBC15999A20Q30523072-5E712205-F10F-455D-AB6C-8B9923497C7BQ31072074-6D2B697B-7549-4FB5-A8EB-501D1508E505Q33268282-297C6085-83C8-4606-B51B-5F14006C95B5Q33291745-160F71AF-8879-4CB0-94C6-F9DFAFBC8E31Q33427240-C82BBB67-B97A-4418-B087-95EA61839D2FQ33561356-A72525AD-9361-4EA4-A409-96E175D37705Q33675599-433485C6-59D9-4A19-BC00-68EF38D42613Q33736909-DF975804-D818-4B68-9739-6E755B479F92Q33756277-9F5FF72A-9604-4BAD-A760-32DADEF5E02BQ33761386-6A61FE9A-83DD-4EBD-B54D-38B9CDC784BBQ33788913-47790814-54EE-4737-B924-CC85855A31BEQ33818809-DE3B9FD7-B1CD-4944-9ACB-31A6B51FB183Q33838789-807CF163-BC87-48BE-A1F5-6C52FDCF260AQ33908362-3C730FC3-C2BE-4635-A65C-A992D857F5A2Q33935094-43C8F03A-454B-4E6D-B1DD-C7774491E18BQ33941017-74F933C5-F381-4662-AFF4-B60250EEB616Q33997145-FA732A57-ECF3-4C9A-BE9F-88799DDFB5A0Q34015826-87F58C1E-9AD4-460E-9066-6A3FFB1612ACQ34066654-87F11442-E1D3-49C1-AEE5-526CD0289514Q34098314-1833D540-7E8C-4676-8547-66695CB6A266Q34144086-C3F65821-AE28-4870-8633-73770228BFE0
P2860
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
description
2002 nî lūn-bûn
@nan
2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
@ast
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
@en
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
@nl
type
label
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
@ast
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
@en
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
@nl
prefLabel
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
@ast
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
@en
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
@nl
P2093
P2860
P356
P1476
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.
@en
P2093
Frank A Ferrone
Ronald Wetzel
Songming Chen
P2860
P304
11884-11889
P356
10.1073/PNAS.182276099
P407
P577
2002-08-19T00:00:00Z