Polymorphism in the intermediates and products of amyloid assembly.
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The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathwayPrions, protein homeostasis, and phenotypic diversityMapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerizationMolecular basis for passive immunotherapy of Alzheimer's diseaseMonoclinic form of isopentenyl diphosphate isomerase: a case of polymorphism in biomolecular crystalsAtomic structure of the cross-β spine of islet amyloid polypeptide (amylin)β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkagesCrystallographic analysis of metal-ion binding to human ubiquitinOut-of-register -sheets suggest a pathway to toxic amyloid aggregatesAtomic View of a Toxic Amyloid Small OligomerA multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35Curcumin promotes A-beta fibrillation and reduces neurotoxicity in transgenic DrosophilaThe Japanese Mutant Aβ (ΔE22-Aβ1−39) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence: Seeding of Wild-Type Aβ1−40into Atypical Fibrils by ΔE22-Aβ1−39β-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Effect of beta-sheet propensity on peptide aggregation.Comparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin.Intrinsic fibrillation of fast-acting insulin analogs.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Polymorphism of β2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanolThe polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP.Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity.A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins.Amyloid β-Protein C-Terminal Fragments: Formation of Cylindrins and β-Barrels.Prion protein insertional mutations increase aggregation propensity but not fiber stability.Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity.Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spineConfocal fluorescence detected linear dichroism imaging of isolated human amyloid fibrils. Role of supercoiling.Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing α-synuclein oligomeric species toxicityAmyloid structure and assembly: insights from scanning transmission electron microscopy.Intrinsic linear heterogeneity of amyloid β protein fibrils revealed by higher resolution mass-per-length determinations.Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.Spatial extent of charge repulsion regulates assembly pathways for lysozyme amyloid fibrilsAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence.Orthogonal cross-seeding: an approach to explore protein aggregates in living cells.Mysterious oligomerization of the amyloidogenic proteinsPolymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Transmission electron microscopy characterization of fluorescently labelled amyloid β 1-40 and α-synuclein aggregatesUnraveling the early events of amyloid-β protein (Aβ) aggregation: techniques for the determination of Aβ aggregate size.
P2860
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P2860
Polymorphism in the intermediates and products of amyloid assembly.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Polymorphism in the intermediates and products of amyloid assembly.
@ast
Polymorphism in the intermediates and products of amyloid assembly.
@en
type
label
Polymorphism in the intermediates and products of amyloid assembly.
@ast
Polymorphism in the intermediates and products of amyloid assembly.
@en
prefLabel
Polymorphism in the intermediates and products of amyloid assembly.
@ast
Polymorphism in the intermediates and products of amyloid assembly.
@en
P1476
Polymorphism in the intermediates and products of amyloid assembly.
@en
P2093
Ravindra Kodali
Ronald Wetzel
P356
10.1016/J.SBI.2007.01.007
P577
2007-01-23T00:00:00Z