ArticleBiophysical journal2008
Pinched multilamellar structure of aggregates of lysozyme and phosphatidylserine-containing membranes revealed by FRET.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Free-Standing Hierarchically Porous Silica Nanoparticle Superstructures: Bridging the Nano- to Microscale for Tailorable Delivery of Small and Large Therapeutics.ACS applied materials & interfaces · 2024Article
- The Minor Capsid Protein VP11 of Thermophilic Bacteriophage P23-77 Facilitates Virus Assembly by Using Lipid-Protein Interactions.Journal of virology · 2015Article
- Time-resolved fluorescence in lipid bilayers: selected applications and advantages over steady state.Biophysical journal · 2014Review
- Simple estimation of Förster Resonance Energy Transfer (FRET) orientation factor distribution in membranes.International journal of molecular sciences · 2012Article
- Two conserved residues are important for inducing highly ordered membrane domains by the transmembrane domain of influenza hemagglutinin.Biophysical journal · 2011Article
- FRET in Membrane Biophysics: An Overview.Frontiers in physiology · 2011Article
- Morphological changes of supported lipid bilayers induced by lysozyme: planar domain formation vs. multilayer stacking.Colloids and surfaces. B, Biointerfaces · 2010Article
- Membrane microheterogeneity: Förster resonance energy transfer characterization of lateral membrane domains.European biophysics journal : EBJ · 2010Review
- Quantification of protein-lipid selectivity using FRET.European biophysics journal : EBJ · 2010Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electrostatic interactions between negatively charged membranes and basic peptides/protein domains have been implicated as the driving force for several important processes, often involving membrane aggregation, fusion, or phase separation. Recently, acidic lipids were reported to both catalyze amyloid fiber formation by amyloidogenic proteins/peptides and induce formation of "amyloid-like" fibrils by nonamyloidogenic proteins. This study aims to characterize the structure of the aggregates of a basic protein (lysozyme) and negatively charged membranes (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine 4:1 mixture) at the molecular level, using Förster resonance energy transfer. It is concluded that lysozyme induced formation of a "pinched lamellar" structure, with reduced interbilayer distance in the regions where there is bound protein and increased interbilayer distance (stabilized by hydration repulsion) outside these areas.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.