Population of nonnative states of lysozyme variants drives amyloid fibril formation.
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α-Synuclein as an intrinsically disordered monomer--fact or artefact?A Nanobody Binding to Non-Amyloidogenic Regions of the Protein Human Lysozyme Enhances Partial Unfolding but Inhibits Amyloid Fibril FormationMechanism of Protein Kinetic Stabilization by Engineered Disulfide CrosslinksThe model of amyloid aggregation of Escherichia coli RNA polymerase σ70 subunit based on AFM data and in vitro assays.pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomersAnti-fibrillation propensity of a flavonoid baicalein against the fibrils of hen egg white lysozyme: potential therapeutics for lysozyme amyloidosis.Insights into Kinetics of Agitation-Induced Aggregation of Hen Lysozyme under Heat and Acidic Conditions from Various Spectroscopic Methods.Accelerated insulin aggregation under alternating current electric fields: Relevance to amyloid kineticsCharacterization of heat induced spherulites of lysozyme reveals new insight on amyloid initiation.Sodium louroyl sarcosinate (sarkosyl) modulate amyloid fibril formation in hen egg white lysozyme (HEWL) at alkaline pH: a molecular insight study.Molecular Insight into Human Lysozyme and Its Ability to Form Amyloid Fibrils in High Concentrations of Sodium Dodecyl Sulfate: A View from Molecular Dynamics SimulationsThe native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro.Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Electrostatic effects in filamentous protein aggregation.Conformation types of ubiquitin [M+8H]8+ Ions from water:methanol solutions: evidence for the N and A States in aqueous solution.A Population Shift between Sparsely Populated Folding Intermediates Determines AmyloidogenicityFactors affecting the physical stability (aggregation) of peptide therapeutics.Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation.The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme.In vitro hyperglycemic condition facilitated the aggregation of lysozyme via the passage through a molten globule state.
P2860
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P2860
Population of nonnative states of lysozyme variants drives amyloid fibril formation.
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
Population of nonnative states of lysozyme variants drives amyloid fibril formation.
@en
Population of nonnative states of lysozyme variants drives amyloid fibril formation.
@nl
type
label
Population of nonnative states of lysozyme variants drives amyloid fibril formation.
@en
Population of nonnative states of lysozyme variants drives amyloid fibril formation.
@nl
prefLabel
Population of nonnative states of lysozyme variants drives amyloid fibril formation.
@en
Population of nonnative states of lysozyme variants drives amyloid fibril formation.
@nl
P2093
P2860
P50
P356
P1476
Population of nonnative states of lysozyme variants drives amyloid fibril formation.
@en
P2093
Anne Dhulesia
Janet R Kumita
Mark E Welland
Mireille Dumoulin
Tuomas P J Knowles
P2860
P304
P356
10.1021/JA109620D
P407
P577
2011-04-29T00:00:00Z