Amyloid structure: conformational diversity and consequences.
about
Molecular chaperones: guardians of the proteome in normal and disease statesPrion strains and amyloid polymorphism influence phenotypic variationThe Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPSelf-propagation of pathogenic protein aggregates in neurodegenerative diseasesOut-of-register -sheets suggest a pathway to toxic amyloid aggregatesMolecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain TissueThe Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation.Measurement of amyloid formation by turbidity assay-seeing through the cloudBacterial amyloid formation: structural insights into curli biogensisConformational analysis of misfolded protein aggregation by FRET and live-cell imaging techniquesSpontaneous variants of the [RNQ+] prion in yeast demonstrate the extensive conformational diversity possible with prion proteinsHemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process.Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.Post-translational modifications in PrP expand the conformational diversity of prions in vivoTechniques for Monitoring Protein Misfolding and Aggregation in Vitro and in Living CellsSelenomethionine incorporation into amyloid sequences regulates fibrillogenesis and toxicityIntrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity.Biology and genetics of prions causing neurodegenerationContribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.The [Het-s] prion, an amyloid fold as a cell death activation triggerPrion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation.The effects of amino acid composition of glutamine-rich domains on amyloid formation and fragmentation.Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR studyDistinct Spacing Between Anionic Groups: An Essential Chemical Determinant for Achieving Thiophene-Based Ligands to Distinguish β-Amyloid or Tau Polymorphic AggregatesUnderstanding Aspects of Aluminum Exposure in Alzheimer's Disease Development.A retrospective analysis of the Alzheimer's disease vaccine progress - The critical need for new development strategies.Sequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology.Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission.An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution.Radically different amyloid conformations dictate the seeding specificity of a chimeric Sup35 prion.Structural determinants of phenotypic diversity and replication rate of human prions.Amyloid polymorphism: structural basis and neurobiological relevance.Peptides released by physiological cleavage of semen coagulum proteins form amyloids that enhance HIV infection.Amyloid fibril formation by the glaucoma-associated olfactomedin domain of myocilin.Kinetically competing huntingtin aggregation pathways control amyloid polymorphism and propertiesSolvent-induced tuning of internal structure in a protein amyloid protofibril.Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.Generating extracellular amyloid aggregates using E. coli cells.Structural variants of yeast prions show conformer-specific requirements for chaperone activity.
P2860
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P2860
Amyloid structure: conformational diversity and consequences.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
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
name
Amyloid structure: conformational diversity and consequences.
@ast
Amyloid structure: conformational diversity and consequences.
@en
Amyloid structure: conformational diversity and consequences.
@nl
type
label
Amyloid structure: conformational diversity and consequences.
@ast
Amyloid structure: conformational diversity and consequences.
@en
Amyloid structure: conformational diversity and consequences.
@nl
prefLabel
Amyloid structure: conformational diversity and consequences.
@ast
Amyloid structure: conformational diversity and consequences.
@en
Amyloid structure: conformational diversity and consequences.
@nl
P2860
P1476
Amyloid structure: conformational diversity and consequences.
@en
P2093
Brandon H Toyama
P2860
P304
P356
10.1146/ANNUREV-BIOCHEM-090908-120656
P577
2011-01-01T00:00:00Z