Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry
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The extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrilsStructural Insights into High Density Lipoprotein: Old Models and New FactsNew insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolismCrystal Structure of C-terminal Truncated Apolipoprotein A-I Reveals the Assembly of High Density Lipoprotein (HDL) by DimerizationSequence conservation of apolipoprotein A-I affords novel insights into HDL structure-functionAmyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosisA model of lipid-free apolipoprotein A-I revealed by iterative molecular dynamics simulationStructural and Functional Analysis of the ApolipoproteinA-I A164S VariantQuantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX.The crystal structure of the C-terminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment.Congruency between biophysical data from multiple platforms and molecular dynamics simulation of the double-super helix model of nascent high-density lipoprotein.Immunochemical Approach for Monitoring of Structural Transition of ApoA-I upon HDL Formation Using Novel Monoclonal AntibodiesSwapping the N- and C-terminal domains of human apolipoprotein E3 and AI reveals insights into their structure/activity relationshipMethods for the Analysis of High Precision Differential Hydrogen Deuterium Exchange Data.Exchange of apolipoprotein A-I between lipid-associated and lipid-free states: a potential target for oxidative generation of dysfunctional high density lipoproteinsAllosteric inhibition of complement function by a staphylococcal immune evasion protein.Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I.An experimentally robust model of monomeric apolipoprotein A-I created from a chimera of two X-ray structures and molecular dynamics simulationsDifferential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactionsConformational transitions in the membrane scaffold protein of phospholipid bilayer nanodiscsImpact of self-association on function of apolipoprotein A-IApolipoprotein A-II-mediated conformational changes of apolipoprotein A-I in discoidal high density lipoproteins.Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.Structural stability and functional remodeling of high-density lipoproteins.The "beta-clasp" model of apolipoprotein A-I--a lipid-free solution structure determined by electron paramagnetic resonance spectroscopy.Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry.Nascent high density lipoproteins formed by ABCA1 resemble lipid rafts and are structurally organized by three apoA-I monomersDirect detection of ABCA1-dependent HDL formation based on lipidation-induced hydrophobicity change in apoA-IBinding of human apoA-I[K107del] variant to TG-rich particles: implications for mechanisms underlying hypertriglyceridemia.Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.Crystal structure of Δ(185-243)ApoA-I suggests a mechanistic framework for the protein adaptation to the changing lipid load in good cholesterol: from flatland to sphereland via double belt, belt buckle, double hairpin and trefoil/tetrafoilStructural Stability and Local Dynamics in Disease-Causing Mutants of Human Apolipoprotein A-I: What Makes the Protein Amyloidogenic?Direct Measurement of the Structure of Reconstituted High-Density Lipoproteins by Cryo-EM.An Evaluation of the Crystal Structure of C-terminal Truncated Apolipoprotein A-I in Solution Reveals Structural Dynamics Related to Lipid Binding.Apolipoproteins as Differentiating and Predictive Markers for Assessing Clinical Outcomes in Patients with Small Cell Lung Cancer.The low-resolution structure of nHDL reconstituted with DMPC with and without cholesterol reveals a mechanism for particle expansion.Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks.Comparison of apoA-I helical structure and stability in discoidal and spherical HDL particles by HX and mass spectrometry.Discoidal HDL and apoA-I-derived peptides improve glucose uptake in skeletal muscle.High level of serum apolipoprotein A-I is a favorable prognostic factor for overall survival in esophageal squamous cell carcinoma.
P2860
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P2860
Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 22 October 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Helical structure and stabilit ...... exchange and mass spectrometry
@en
Helical structure and stabilit ...... xchange and mass spectrometry.
@nl
type
label
Helical structure and stabilit ...... exchange and mass spectrometry
@en
Helical structure and stabilit ...... xchange and mass spectrometry.
@nl
prefLabel
Helical structure and stabilit ...... exchange and mass spectrometry
@en
Helical structure and stabilit ...... xchange and mass spectrometry.
@nl
P2093
P2860
P356
P1476
Helical structure and stabilit ...... exchange and mass spectrometry
@en
P2093
David Stranz
Leland Mayne
Michael C Phillips
Palaniappan Sevugan Chetty
S Walter Englander
Sissel Lund-Katz
P2860
P304
19005-19010
P356
10.1073/PNAS.0909708106
P407
P577
2009-10-22T00:00:00Z