Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments.
about
Disease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact StructureComparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin.Free-Energy Landscape of the Amino-Terminal Fragment of Huntingtin in Aqueous SolutionFibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine coreMonomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionPrion-like proteins sequester and suppress the toxicity of huntingtin exon 1.A coarse-grained model for polyglutamine aggregation modulated by amphipathic flanking sequencesHuntingtin protein interactions altered by polyglutamine expansion as determined by quantitative proteomic analysis.Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.Probing the Huntingtin 1-17 membrane anchor on a phospholipid bilayer by using all-atom simulationsInsights into Kinetics of Agitation-Induced Aggregation of Hen Lysozyme under Heat and Acidic Conditions from Various Spectroscopic Methods.Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer.Kinetically 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.Solid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils.Studying polyglutamine aggregation in Caenorhabditis elegans using an analytical ultracentrifuge equipped with fluorescence detection.The interaction of polyglutamine peptides with lipid membranes is regulated by flanking sequences associated with huntingtinLevels of supramolecular chirality of polyglutamine aggregates revealed by vibrational circular dichroism.Acetylation within the First 17 Residues of Huntingtin Exon 1 Alters Aggregation and Lipid Binding.Identification and Structural Characterization of the N-terminal Amyloid Core of Orb2 isoform A.Investigating Mutations to Reduce Huntingtin Aggregation by Increasing Htt-N-Terminal Stability and Weakening Interactions with PolyQ Domain.Structural motif of polyglutamine amyloid fibrils discerned with mixed-isotope infrared spectroscopy.Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.The role of amyloidogenic protein oligomerization in neurodegenerative disease.A serendipitous survey of prediction algorithms for amyloidogenicity.Advances in huntington disease drug discovery: novel approaches to model disease phenotypes.Polyglutamine Aggregation in Huntington Disease: Does Structure Determine Toxicity?Formation and Structure of Wild Type Huntingtin Exon-1 Fibrils.Emerging β-Sheet Rich Conformations in Supercompact Huntingtin Exon-1 Mutant Structures.Functional oligopeptide as a novel strategy for drug delivery.Inhibition of polyglutamine aggregation by SIMILAR huntingtin N-terminal sequences: Prospective molecules for preclinical evaluation in Huntington's disease.Backbone Engineering within a Latent β-Hairpin Structure to Design Inhibitors of Polyglutamine Amyloid Formation.Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease.Improved chemical synthesis of hydrophobic Aβ peptides using addition of C-terminal lysines later removed by carboxypeptidase B.C-Terminal Threonine Reduces Aβ43 Amyloidogenicity Compared with Aβ42.Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway.Aggregation behavior of chemically synthesized, full-length huntingtin exon1.
P2860
Q27677065-94386016-7F73-4A68-80BB-BCEE1CE97E8BQ30371013-D648EFD8-FD3F-4BEB-8607-7A1FFCADE25AQ31055925-88165353-D5DE-4F7A-8E3E-286C8EB5D556Q33761247-E1ADBCA5-B994-4A3C-A77B-914337E47FD5Q33788913-179CD9D6-4933-42EB-8BBE-D1EA9AF5D878Q34082859-2DF92904-81ED-4E8B-954B-F125927C9364Q34144086-C1719DFB-EC07-42B3-B1EF-E7BA71A29F94Q34274478-7DF1FD4C-8E2F-49AF-ABFC-43D60828E85EQ34414446-2D781F21-B3B4-4B9C-B3CC-9798B02D21B2Q35221894-974898EF-E93C-4896-A022-4C9A17B71F57Q35842093-F7C0C563-9404-4906-ABE8-155FB57D1009Q36043574-F1F06B32-647F-445D-B260-1D2EEB70EC1AQ36088674-5179AEFF-A0E8-4BF3-9983-B7A9B01A7C60Q36110838-AFDFF96E-C7E2-4092-A4FE-8132F586884AQ36198935-BE35D337-FEB8-4974-9C4B-22DB6BEF62F9Q36234699-3D267FA6-8DFB-4BAE-939E-3F88A3EE102BQ36277923-1510A283-BCB9-415C-B1FA-F5AE599A0AA0Q36630032-1A1ABD1F-C9FE-44D0-9F24-2A807767F0EEQ36749672-61875744-5DFB-44A6-94B9-7A943D506CEDQ36873629-D874B4B8-40E0-487E-B757-C58D9389FFCFQ36936466-5EEA0904-3BEF-4A95-81CA-8A907419E799Q37142133-A2E3B44A-7657-4A8A-A1A6-9CD333D9FCF2Q37475977-B10095B7-EFB5-479D-8EE3-480A8F064EE2Q37550841-ADBFB899-E997-476B-BB50-BD0A01B72054Q37725285-9036B6BC-AEC2-44D6-8355-383BAF2A2956Q37981477-ECE2737F-A206-41A8-B9D9-5F2AC6E8795CQ38093118-6AB41C2F-A397-45AD-9F87-4EE5D300C55BQ38124811-F4B4FF4B-3D00-42FA-BF24-EA7D20195589Q38160307-3C306FC6-5B99-4B97-843C-88C01E5CB6ECQ38261844-46ABBB03-72A0-4034-9354-11DAD7E51AC1Q38722643-C6A6F07D-5531-45FF-BB0A-B780B9047511Q38727983-30BD9B69-05F5-45B7-958E-8BC013E5F84CQ38740492-F73C11D2-FF12-478C-9678-5C88F206264CQ38838617-CB12BE16-59B3-4247-879C-251A6CAD1647Q39093738-4DC1E4B5-5AFE-4CB2-96EE-B243144431A3Q39124557-3ACAB05A-36C1-404D-88AD-8855801B732EQ39244602-FB8FF4F4-236E-4BB5-B33B-D8C4737C863AQ40785358-8B4D92A6-572A-44B6-BF40-F74395267D04Q41230841-5CDC32E6-F3C1-4F9F-937A-B1977EFE9311Q41513084-59AAC03A-350E-4C43-A391-15D7A2AD0B52
P2860
Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Slow amyloid nucleation via α- ...... ntaining huntingtin fragments.
@ast
Slow amyloid nucleation via α- ...... ntaining huntingtin fragments.
@en
type
label
Slow amyloid nucleation via α- ...... ntaining huntingtin fragments.
@ast
Slow amyloid nucleation via α- ...... ntaining huntingtin fragments.
@en
prefLabel
Slow amyloid nucleation via α- ...... ntaining huntingtin fragments.
@ast
Slow amyloid nucleation via α- ...... ntaining huntingtin fragments.
@en
P2093
P2860
P1476
Slow amyloid nucleation via α- ...... ontaining huntingtin fragments
@en
P2093
Anand Mayasundari
Ashwani K Thakur
Cynthia B Peterson
Murali Jayaraman
Rakesh Mishra
Ravindra Kodali
Ronald Wetzel
P2860
P304
P356
10.1016/J.JMB.2011.12.010
P407
P577
2011-12-09T00:00:00Z