These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
329 related articles for article (PubMed ID: 26831073)
1. Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core. Hoop CL; Lin HK; Kar K; Magyarfalvi G; Lamley JM; Boatz JC; Mandal A; Lewandowski JR; Wetzel R; van der Wel PC Proc Natl Acad Sci U S A; 2016 Feb; 113(6):1546-51. PubMed ID: 26831073 [TBL] [Abstract][Full Text] [Related]
2. Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core. Lin HK; Boatz JC; Krabbendam IE; Kodali R; Hou Z; Wetzel R; Dolga AM; Poirier MA; van der Wel PCA Nat Commun; 2017 May; 8():15462. PubMed ID: 28537272 [TBL] [Abstract][Full Text] [Related]
3. Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance. Hoop CL; Lin HK; Kar K; Hou Z; Poirier MA; Wetzel R; van der Wel PC Biochemistry; 2014 Oct; 53(42):6653-66. PubMed ID: 25280367 [TBL] [Abstract][Full Text] [Related]
4. β-hairpin-mediated nucleation of polyglutamine amyloid formation. Kar K; Hoop CL; Drombosky KW; Baker MA; Kodali R; Arduini I; van der Wel PC; Horne WS; Wetzel R J Mol Biol; 2013 Apr; 425(7):1183-97. PubMed ID: 23353826 [TBL] [Abstract][Full Text] [Related]
5. Solid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils. Isas JM; Langen R; Siemer AB Biochemistry; 2015 Jun; 54(25):3942-9. PubMed ID: 26020223 [TBL] [Abstract][Full Text] [Related]
6. Polyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences. Lakhani VV; Ding F; Dokholyan NV PLoS Comput Biol; 2010 Apr; 6(4):e1000772. PubMed ID: 20442863 [TBL] [Abstract][Full Text] [Related]
7. Structural Basis of Huntingtin Fibril Polymorphism Revealed by Cryogenic Electron Microscopy of Exon 1 HTT Fibrils. Nazarov S; Chiki A; Boudeffa D; Lashuel HA J Am Chem Soc; 2022 Jun; 144(24):10723-10735. PubMed ID: 35679155 [TBL] [Abstract][Full Text] [Related]
13. Mutational analysis implicates the amyloid fibril as the toxic entity in Huntington's disease. Drombosky KW; Rode S; Kodali R; Jacob TC; Palladino MJ; Wetzel R Neurobiol Dis; 2018 Dec; 120():126-138. PubMed ID: 30171891 [TBL] [Abstract][Full Text] [Related]
14. Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer. Sahoo B; Arduini I; Drombosky KW; Kodali R; Sanders LH; Greenamyre JT; Wetzel R PLoS One; 2016; 11(6):e0155747. PubMed ID: 27271685 [TBL] [Abstract][Full Text] [Related]
15. Exploding the Repeat Length Paradigm while Exploring Amyloid Toxicity in Huntington's Disease. Wetzel R Acc Chem Res; 2020 Oct; 53(10):2347-2357. PubMed ID: 32975927 [TBL] [Abstract][Full Text] [Related]
16. Solid-state nuclear magnetic resonance in the structural study of polyglutamine aggregation. van der Wel PCA Biochem Soc Trans; 2024 Apr; 52(2):719-731. PubMed ID: 38563485 [TBL] [Abstract][Full Text] [Related]
17. Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology. Scherzinger E; Sittler A; Schweiger K; Heiser V; Lurz R; Hasenbank R; Bates GP; Lehrach H; Wanker EE Proc Natl Acad Sci U S A; 1999 Apr; 96(8):4604-9. PubMed ID: 10200309 [TBL] [Abstract][Full Text] [Related]
18. Structure of a single-chain Fv bound to the 17 N-terminal residues of huntingtin provides insights into pathogenic amyloid formation and suppression. De Genst E; Chirgadze DY; Klein FA; Butler DC; Matak-Vinković D; Trottier Y; Huston JS; Messer A; Dobson CM J Mol Biol; 2015 Jun; 427(12):2166-78. PubMed ID: 25861763 [TBL] [Abstract][Full Text] [Related]
19. Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. Poirier MA; Li H; Macosko J; Cai S; Amzel M; Ross CA J Biol Chem; 2002 Oct; 277(43):41032-7. PubMed ID: 12171927 [TBL] [Abstract][Full Text] [Related]