The association−dissociation behavior of the ApoE proteins: kinetic and equilibrium studies
about
A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactions.Influence of domain stability on the properties of human apolipoprotein E3 and E4 and mouse apolipoprotein E.Swapping the N- and C-terminal domains of human apolipoprotein E3 and AI reveals insights into their structure/activity relationshipApoE: In Vitro Studies of a Small Molecule Effector.HDL mimetic peptide ATI-5261 forms an oligomeric assembly in solution that dissociates to monomers upon dilutionMass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4.Impact of self-association on function of apolipoprotein A-IHydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerizationRole of Conserved Proline Residues in Human Apolipoprotein A-IV Structure and Function.Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease.Small-angle X-ray scattering of apolipoprotein A-IV reveals the importance of its termini for structural stability.Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled AβApolipoprotein E, amyloid-beta, and neuroinflammation in Alzheimer's diseaseCharacterization of protein adsorption onto FePt nanoparticles using dual-focus fluorescence correlation spectroscopy.Improving the diffraction of apoA-IV crystals through extreme dehydration.Concerning the structure of apoEThe extent of pyrene excimer fluorescence emission is a reflector of distance and flexibility: analysis of the segment linking the LDL receptor-binding and tetramerization domains of apolipoprotein E3.Dissociation of apolipoprotein E oligomers to monomer is required for high-affinity binding to phospholipid vesicles.Fluorescence analysis of the lipid binding-induced conformational change of apolipoprotein E4.Fluorescence study of domain structure and lipid interaction of human apolipoproteins E3 and E4.ApoE: the role of conserved residues in defining functionHelical structure, stability, and dynamics in human apolipoprotein E3 and E4 by hydrogen exchange and mass spectrometry.Peptide-Level Interactions between Proteins and Small-Molecule Drug Candidates by Two Hydrogen-Deuterium Exchange MS-Based Methods: The Example of Apolipoprotein E3.Quantitative Characterization of Metastability and Heterogeneity of Amyloid Aggregates.A fast and cost-effective method for apolipoprotein E isotyping as an alternative to APOE genotyping for patient screening and stratification.
P2860
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P2860
The association−dissociation behavior of the ApoE proteins: kinetic and equilibrium studies
description
2010 nî lūn-bûn
@nan
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
2010年论文
@zh
2010年论文
@zh-cn
name
The association−dissociation b ...... inetic and equilibrium studies
@en
type
label
The association−dissociation b ...... inetic and equilibrium studies
@en
prefLabel
The association−dissociation b ...... inetic and equilibrium studies
@en
P2860
P356
P1433
P1476
The association−dissociation b ...... inetic and equilibrium studies
@en
P2093
Carl Frieden
Kanchan Garai
P2860
P304
P356
10.1021/BI101407M
P407
P577
2010-11-01T00:00:00Z