ReviewEuropean biophysics journal : EBJ2010
Quantification of protein-lipid selectivity using FRET.
Review in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed.
- Cooperativity in regulation of membrane protein function: phenomenological analysis of the effects of pH and phospholipids.Biophysical reviews · 2023Review
- Insights into lipid-protein interactions from computer simulations.Biophysical reviews · 2021Review
- Activation of G-protein-coupled receptors is thermodynamically linked to lipid solvation.Biophysical journal · 2021Article
- Current Methods for Detecting Cell Membrane Transient Interactions.Frontiers in chemistry · 2020Review
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Lipid-Protein Interactions Are Unique Fingerprints for Membrane Proteins.ACS central science · 2018Article
- Article
- Kinetics of peptide folding in lipid membranes.Biopolymers · 2015Review
- A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport.eLife · 2015Article
- A two-stage model for lipid modulation of the activity of integral membrane proteins.PloS one · 2012Article
- Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides.Cellular and molecular life sciences : CMLS · 2011Review
- Recent developments in molecular dynamics simulations of fluorescent membrane probes.Molecules (Basel, Switzerland) · 2011Review
- FRET in Membrane Biophysics: An Overview.Frontiers in physiology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane proteins exhibit different affinities for different lipid species, and protein-lipid selectivity regulates the membrane composition in close proximity to the protein, playing an important role in the formation of nanoscale membrane heterogeneities. The sensitivity of Förster resonance energy transfer (FRET) for distances of 10 A up to 100 A is particularly useful to retrieve information on the relative distribution of proteins and lipids in the range over which protein-lipid selectivity is expected to influence membrane composition. Several FRET-based methods applied to the quantification of protein-lipid selectivity are described herein, and different formalisms applied to the analysis of FRET data for particular geometries of donor-acceptor distribution are critically assessed.
Indexed as
Identifiers
What OpenQuestion holds
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.