Evidence map›Paper›PMID 26087906›Full record

ReviewThe Journal of membrane biology2015

More Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes.

Uris Ros, Ana J García-Sáez

Abstract readReview
PubMed Publisher
In one paragraph

Review in The Journal of membrane biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 73 citations in OpenAlex.

  1. AFM to Study Pore-Forming Proteins.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. Article
  3. Review
  4. Biophysical Considerations in Cell Fusion.Advances in experimental medicine and biology · 2026
    Review
  5. Article
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  7. Review
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  9. Sea Anemones, Actinoporins, and Cholesterol.International journal of molecular sciences · 2022
    Review
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  11. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Uris RosCenter for Protein Studies, Faculty of Biology, Calle 25 # 455, Plaza de la Revolución, Havana, Cuba.
Ana J García-Sáez
Max Planck Institute for Intelligent Systems · DEUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pore-forming proteins (PFPs) punch holes in their target cell membrane to alter their permeability. Permeabilization of lipid membranes by PFPs has received special attention to study the basic molecular mechanisms of protein insertion into membranes and the development of biotechnological tools. PFPs act through a general multi-step mechanism that involves (i) membrane partitioning, (ii) insertion into the hydrophobic core of the bilayer, (iii) oligomerization, and (iv) pore formation. Interestingly, PFPs and membranes show a dynamic interplay. As PFPs are usually produced as soluble proteins, they require a large conformational change for membrane insertion. Moreover, membrane structure is modified upon PFPs insertion. In this context, the toroidal pore model has been proposed to describe a pore architecture in which not only protein molecules but also lipids are directly involved in the structure. Here, we discuss how PFPs and lipids cooperate and remodel each other to achieve pore formation, and explore new evidences of protein-lipid pore structures.

Indexed as

AnimalsCell MembraneCell Membrane PermeabilityHumansHydrophobic and Hydrophilic InteractionsMembrane LipidsModels, MolecularPore Forming Cytotoxic ProteinsPorosityProtein Structure, SecondaryMembrane LipidsPore Forming Cytotoxic Proteins

Identifiers

PMID26087906
OpenAlexW639309518

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.