Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin.
about
A decade and a half of protein intrinsic disorder: biology still waits for physicsTrinucleotide repeats: a structural perspectiveElongation kinetics of polyglutamine peptide fibrils: a quartz crystal microbalance with dissipation study.Improved atomistic Monte Carlo simulations demonstrate that poly-L-proline adopts heterogeneous ensembles of conformations of semi-rigid segments interrupted by kinks.Free-Energy Landscape of the Amino-Terminal Fragment of Huntingtin in Aqueous SolutionPolyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences.The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.Investigating the structural impact of the glutamine repeat in huntingtin assembly.Hamiltonian Switch Metropolis Monte Carlo Simulations for Improved Conformational Sampling of Intrinsically Disordered Regions Tethered to Ordered Domains of Proteins.Cystamine and intrabody co-treatment confers additional benefits in a fly model of Huntington's disease.A coarse-grained model for polyglutamine aggregation modulated by amphipathic flanking sequencesAssessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptidesUnmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation.Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome.Location trumps length: polyglutamine-mediated changes in folding and aggregation of a host proteinOpposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.Probing the Huntingtin 1-17 membrane anchor on a phospholipid bilayer by using all-atom simulationsPolyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopyStructural transitions and oligomerization along polyalanine fibril formation pathways from computer simulationsAn Analysis of Biomolecular Force Fields for Simulations of Polyglutamine in SolutionKinetically competing huntingtin aggregation pathways control amyloid polymorphism and propertiesThe emerging role of the first 17 amino acids of huntingtin in Huntington's diseaseHuntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues.Structural features and domain organization of huntingtin fibrils.CAMELOT: A machine learning approach for coarse-grained simulations of aggregation of block-copolymeric protein sequences.Conformational properties of polyglutamine sequences in guanidine hydrochloride solutionsMolecular dynamics analysis of the aggregation propensity of polyglutamine segmentsSlow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments.Solid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils.An N-terminal nuclear export signal regulates trafficking and aggregation of Huntingtin (Htt) protein exon 1.The interaction of polyglutamine peptides with lipid membranes is regulated by flanking sequences associated with huntingtinAcetylation within the First 17 Residues of Huntingtin Exon 1 Alters Aggregation and Lipid Binding.Investigating Mutations to Reduce Huntingtin Aggregation by Increasing Htt-N-Terminal Stability and Weakening Interactions with PolyQ Domain.Neurotoxic protein oligomerisation associated with polyglutamine diseases.Huntington's disease, calcium, and mitochondria.Intrinsically unstructured proteins and neurodegenerative diseases: conformational promiscuity at its best.Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature.
P2860
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P2860
Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Modulation of polyglutamine co ...... the N-terminus of huntingtin.
@en
Modulation of polyglutamine co ...... the N-terminus of huntingtin.
@nl
type
label
Modulation of polyglutamine co ...... the N-terminus of huntingtin.
@en
Modulation of polyglutamine co ...... the N-terminus of huntingtin.
@nl
prefLabel
Modulation of polyglutamine co ...... the N-terminus of huntingtin.
@en
Modulation of polyglutamine co ...... the N-terminus of huntingtin.
@nl
P2093
P2860
P1476
Modulation of polyglutamine co ...... the N-terminus of huntingtin.
@en
P2093
Andreas Vitalis
Rohit V Pappu
Scott L Crick
Tim E Williamson
P2860
P304
P356
10.1016/J.JMB.2009.12.017
P407
P577
2009-12-21T00:00:00Z