ReviewEMBO reports2002
Attraction within the membrane. Forces behind transmembrane protein folding and supramolecular complex assembly.
Review in EMBO reports, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 48 citations in OpenAlex.
- The lipid bilayer strengthens the cooperative network of membrane proteins.Science advances · 2025Article
- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Review
- Ferroquine and its derivatives: new generation of antimalarial agents.European journal of medicinal chemistry · 2015Review
- Respiratory supercomplexes: plasticity and implications.Frontiers in bioscience (Landmark edition) · 2015Review
- Competition between homodimerization and cholesterol binding to the C99 domain of the amyloid precursor protein.Biochemistry · 2013Article
- MPlot--a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins.Nucleic acids research · 2010Article
- Protein folding in membranes.Cellular and molecular life sciences : CMLS · 2010Review
- Interaction and conformational dynamics of membrane-spanning protein helices.Protein science : a publication of the Protein Society · 2009Review
- Ferroquine, an ingenious antimalarial drug: thoughts on the mechanism of action.Molecules (Basel, Switzerland) · 2008Article
- Sorting of streptavidin protein coats on phase-separating model membranes.Biophysical journal · 2008Article
- Structure elucidation of dimeric transmembrane domains of bitopic proteins.Cell adhesion & migrationReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biological membranes are fascinating two-dimensional microenvironments that exhibit unique solvent behaviours due to their varying lipid composition. Although many important bioenergetic and signalling events involve the transient or permanent assembly of membrane protein complexes, the characterization of the thermodynamic and kinetic properties behind this assembly is just beginning. In particular, the molecular forces that govern protein association within these structures remain poorly understood. An understanding of the docking of transmembrane proteins to supramolecular complexes, which will make possible the development of predictive computational tools, will require detailed knowledge of interaction forces at the atomistic or residue level. Here, I review current data on supramolecular complexes in membrane environments and make a tentative comparison between assembly processes in membranes and those driven by the hydrophobic effect in water. This comparison suggests that, in addition to being controlled by specific characteristics of the lipid molecules themselves, molecular assembly in the membrane milieu also depends more generally on the entropy of the lipid fraction.
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.