Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils.
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Mapping out the multistage fibrillation of glucagonKosmotropic anions promote conversion of recombinant prion protein into a PrPSc-like misfolded formModulation 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.Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.Revealing different aggregation pathways of amyloidogenic proteins by ultrasound velocimetry.Quartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interfaceSulfate anion delays the self-assembly of human insulin by modifying the aggregation pathway.The mechanism of enhanced insulin amyloid fibril formation by NaCl is better explained by a conformational change modelStructural transitions and interactions in the early stages of human glucagon amyloid fibrillationPolymorphic fibrillation of the destabilized fourth fasciclin-1 domain mutant A546T of the Transforming growth factor-β-induced protein (TGFBIp) occurs through multiple pathways with different oligomeric intermediates.Salts drive controllable multilayered upright assembly of amyloid-like peptides at mica/water interface.Amyloid-a state in many guises: survival of the fittest fibril fold.Ion-specific modulation of protein interactions: anion-induced, reversible oligomerization of a fusion protein.Branching in amyloid fibril growth.Amyloid structure--one but not the same: the many levels of fibrillar polymorphism.The nature of amyloid-like glucagon fibrilsRole of water in protein folding, oligomerization, amyloidosis and miniprotein.Size distribution of amyloid nanofibrils.Electrostatic effects in filamentous protein aggregation.Hydrogen exchange mass spectrometry as an analytical tool for the analysis of amyloid fibrillogenesis.Characterization of seed nuclei in glucagon aggregation using light scattering methods and field-flow fractionation.Protein fibrillation lag times during kinetic inhibition.Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy.Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions.Fibrillation of the major curli subunit CsgA under a wide range of conditions implies a robust design of aggregation.Factors affecting the physical stability (aggregation) of peptide therapeutics.Effects of environmental factors on MSP21-25 aggregation indicate the roles of hydrophobic and electrostatic interactions in the aggregation process.Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils.Spectroscopic evidence for the existence of an obligate pre-fibrillar oligomer during glucagon fibrillation.Stability of Commercially Available Glucagon Formulation for Dual-Hormone Artificial Pancreas Clinical Use.Lysine functionalised amyloid fibrils: the design and assembly of a TTR1-based peptideThe role of protonation in protein fibrillation
P2860
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P2860
Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils.
description
2006 nî lūn-bûn
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2006年の論文
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2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
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2006年论文
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2006年论文
@zh-cn
name
Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils.
@en
type
label
Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils.
@en
prefLabel
Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils.
@en
P2860
P1433
P1476
Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils.
@en
P2093
Dantcho Dikov
James M Flink
P2860
P304
P356
10.1529/BIOPHYSJ.105.070912
P407
P577
2006-03-13T00:00:00Z