ReviewMini reviews in medicinal chemistry2011
Attachment of rod-like (BAR) proteins and membrane shape.
Review in Mini reviews in medicinal chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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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
16 citing papers in PubMed, 39 citations in OpenAlex.
- Dynamin-like Proteins Combine Mechano-constriction and Membrane Remodeling to Enable Two-Step Mitochondrial Fission via a "Snap-through" Instability.Journal of the American Chemical Society · 2025Article
- Formation of protein-mediated bilayer tubes is governed by a snapthrough transition.Soft matter · 2023Article
- On the Role of Curved Membrane Nanodomains, and Passive and Active Skeleton Forces in the Determination of Cell Shape and Membrane Budding.International journal of molecular sciences · 2021Article
- Cellular Blebs and Membrane Invaginations Are Coupled through Membrane Tension Buffering.Biophysical journal · 2019Article
- Modeling Membrane Curvature Generation due to Membrane⁻Protein Interactions.Biomolecules · 2018Review
- Multipole analysis of the strain-mediated coupling between proteins adsorbed at tubular lipid membrane surface.The European physical journal. E, Soft matter · 2016Article
- Membrane tubule formation by banana-shaped proteins with or without transient network structure.Scientific reports · 2016Article
- Effects of magnetic cobalt ferrite nanoparticles on biological and artificial lipid membranes.International journal of nanomedicine · 2014Article
- Interaction between dipolar lipid headgroups and charged nanoparticles mediated by water dipoles and ions.International journal of molecular sciences · 2013Article
- On the role of anisotropy of membrane components in formation and stabilization of tubular structures in multicomponent membranes.PloS one · 2013Article
- Stability of membranous nanostructures: a possible key mechanism in cancer progression.International journal of nanomedicine · 2012Article
- The role of cholesterol-sphingomyelin membrane nanodomains in the stability of intercellular membrane nanotubes.International journal of nanomedicine · 2012Article
- Fusion pore diameter regulation by cations modulating local membrane anisotropy.TheScientificWorldJournal · 2012Article
- Exploring the binding dynamics of BAR proteins.Cellular & molecular biology letters · 2011Article
- Nanoparticles isolated from blood: a reflection of vesiculability of blood cells during the isolation process.International journal of nanomedicine · 2011Article
- Phenomenology based multiscale models as tools to understand cell membrane and organelle morphologies.Advances in planar lipid bilayers and liposomesArticle
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies have shown that cellular function depends on rod-like membrane proteins, among them Bin/Amphiphysin/Rvs (BAR) proteins may curve the membrane leading to physiologically important membrane invaginations and membrane protrusions. The membrane shaping induced by BAR proteins has a major role in various biological processes such as cell motility and cell growth. Different models of binding of BAR domains to the lipid bilayer are described. The binding includes hydrophobic insertion loops and electrostatic interactions between basic amino acids at the concave region of the BAR domain and negatively charged lipids. To shed light on the elusive binding dynamics, a novel experiment is proposed to expand the technique of single-molecule AFM for the traction of binding energy of a single BAR domain.
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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.