Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.
about
SH3 domains: modules of protein-protein interactions.Mapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.Characterization of oligomers of heterogeneous size as precursors of amyloid fibril nucleation of an SH3 domain: an experimental kinetics study.Early amyloidogenic oligomerization studied through fluorescence lifetime correlation spectroscopy.MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.Pressure as a denaturing agent in studies of single-point mutants of an amyloidogenic protein human cystatin c.Kinetics of amyloid aggregation: a study of the GNNQQNY prion sequence.Seminal plasma accelerates semen-derived enhancer of viral infection (SEVI) fibril formation by the prostatic acid phosphatase (PAP248-286) peptide.Non-Arrhenius protein aggregation.Role of water in protein folding, oligomerization, amyloidosis and miniprotein.A minimal conformational switching-dependent model for amyloid self-assembly.Peptide self-assembly: thermodynamics and kinetics.Amyloid nanospheres from polyglutamine rich peptides: assemblage through an intermolecular salt bridge interaction.The air-water interface determines the outcome of seeding during amyloidogenesis.Fluorescence Investigation of Interactions Between Novel Benzanthrone Dyes and Lysozyme Amyloid Fibrils.A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides.Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space.Nanopore analysis of amyloid fibrils formed by lysozyme aggregation.Insights into the Origin of Distinct Medin Fibril Morphologies Induced by Incubation Conditions and Seeding.Lysine functionalised amyloid fibrils: the design and assembly of a TTR1-based peptideDefining the Dynamic Conformational Networks of Cross-β Peptide AssemblyRecent Advances by In Silico and In Vitro Studies of Amyloid-β 1-42 Fibril Depicted a S-Shape Conformation
P2860
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P2860
Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.
description
2010 nî lūn-bûn
@nan
2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Environmental conditions affec ...... nd determine their morphology.
@ast
Environmental conditions affec ...... nd determine their morphology.
@en
type
label
Environmental conditions affec ...... nd determine their morphology.
@ast
Environmental conditions affec ...... nd determine their morphology.
@en
prefLabel
Environmental conditions affec ...... nd determine their morphology.
@ast
Environmental conditions affec ...... nd determine their morphology.
@en
P2860
P50
P1433
P1476
Environmental conditions affec ...... nd determine their morphology.
@en
P2093
Ana I Azuaga
P2860
P304
P356
10.1016/J.BPJ.2010.10.039
P407
P577
2010-12-01T00:00:00Z