Characterizing the conformational ensemble of monomeric polyglutamine.
about
A systematic survey identifies prions and illuminates sequence features of prionogenic proteinsThe structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice modelSecondary Structure of Huntingtin Amino-Terminal RegionBeta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residuesDisease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact StructureA decade and a half of protein intrinsic disorder: biology still waits for physicsExtended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein.Understanding protein non-folding.Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.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 solutionsIntramolecular cohesion of coils mediated by phenylalanine--glycine motifs in the natively unfolded domain of a nucleoporin.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 expansionDescribing sequence-ensemble relationships for intrinsically disordered proteins.Net charge per residue modulates conformational ensembles of intrinsically disordered proteinsIn-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence.Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptidesTandem repeats discovery service (TReaDS) applied to finding novel cis-acting factors in repeat expansion diseases.Are long-range structural correlations behind the aggregration phenomena of polyglutamine diseases?Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.An intrinsically disordered linker plays a critical role in bacterial cell divisionA natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures.Sequence-dependent stability test of a left-handed β-helix motif.Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories.An Analysis of Biomolecular Force Fields for Simulations of Polyglutamine in SolutionThe emerging role of the first 17 amino acids of huntingtin in Huntington's diseaseConformational dynamics and self-association of intrinsically disordered Huntingtin exon 1 in cells.Molecular dynamics analysis of the aggregation propensity of polyglutamine segmentsSlow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments.The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3.Understanding protein aggregation from the view of monomer dynamicsFunctional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions.N-terminal inactivation domains of beta subunits are protected from trypsin digestion by binding within the antechamber of BK channels.ABSINTH: a new continuum solvation model for simulations of polypeptides in aqueous solutions.Single homopolypeptide chains collapse into mechanically rigid conformations.A platform to view huntingtin exon 1 aggregation flux in the cell reveals divergent influences from chaperones hsp40 and hsp70.Molecular simulations of protein disorder.Low-complexity sequences and single amino acid repeats: not just "junk" peptide sequences.Finding order within disorder: elucidating the structure of proteins associated with neurodegenerative disease.
P2860
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P2860
Characterizing the conformational ensemble of monomeric polyglutamine.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Characterizing the conformational ensemble of monomeric polyglutamine.
@en
Characterizing the conformational ensemble of monomeric polyglutamine.
@nl
type
label
Characterizing the conformational ensemble of monomeric polyglutamine.
@en
Characterizing the conformational ensemble of monomeric polyglutamine.
@nl
prefLabel
Characterizing the conformational ensemble of monomeric polyglutamine.
@en
Characterizing the conformational ensemble of monomeric polyglutamine.
@nl
P2093
P356
P1433
P1476
Characterizing the conformational ensemble of monomeric polyglutamine
@en
P2093
Andreas Vitalis
Rohit V Pappu
Xiaoling Wang
P304
P356
10.1002/PROT.20761
P407
P577
2006-05-01T00:00:00Z