From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.
about
The pentapeptide LQVVR plays a pivotal role in human cystatin C fibrillizationStructure of the cross-beta spine of amyloid-like fibrilsAmyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structureNeuronal response in Alzheimer's and Parkinson's disease: the effect of toxic proteins on intracellular pathwaysElectrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomicsMisfolding and amyloid aggregation of apomyoglobinUbiquitous amyloidsDeciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopyThe crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporterHigh-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopyAmyloidogenic hexapeptide fragment of medin: homology to functional islet amyloid polypeptide fragmentsSupramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.Site-specific identification of non-beta-strand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMRExperimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrilsMultiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrilsCharacterization of amyloid structures at the molecular level by solid state nuclear magnetic resonance spectroscopyHis26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosisStructure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrilsIntermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s).Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates.Self-assembly of human latexin into amyloid-like oligomers.Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide.Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy.Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.Amyloidosis and the respiratory tractSimulation of two-dimensional ultraviolet spectroscopy of amyloid fibrils.Molecular basis for amyloid fibril formation and stability.Identifying the amylome, proteins capable of forming amyloid-like fibrilsQuantitative structure-activity relationship analysis of β-amyloid aggregation inhibitors.Amyloid-like interactions within nucleoporin FG hydrogels.Amyloid-associated nucleic acid hybridisation.Hierarchical self-assembly of chiral rod-like molecules as a model for peptide beta -sheet tapes, ribbons, fibrils, and fibers.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level.Short peptide amyloid organization: stabilities and conformations of the islet amyloid peptide NFGAILDefective protein folding and aggregation as the basis of neurodegenerative diseases: the darker aspect of proteins.Formation kinetics of insulin-based amyloid gels and the effect of added metalloporphyrins.Evidence for assembly of prions with left-handed beta-helices into trimers
P2860
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P2860
From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
From the globular to the fibro ...... nversion in amyloid formation.
@ast
From the globular to the fibro ...... nversion in amyloid formation.
@en
type
label
From the globular to the fibro ...... nversion in amyloid formation.
@ast
From the globular to the fibro ...... nversion in amyloid formation.
@en
prefLabel
From the globular to the fibro ...... nversion in amyloid formation.
@ast
From the globular to the fibro ...... nversion in amyloid formation.
@en
P1476
From the globular to the fibro ...... onversion in amyloid formation
@en
P2093
P356
10.1017/S0033583598003400
P577
1998-02-01T00:00:00Z