Evidence map›Paper›PMID 26375417›Full record

ReviewBiochimica et biophysica acta2016

Assembling the puzzle: Oligomerization of α-pore forming proteins in membranes.

Katia Cosentino, Uris Ros, Ana J García-Sáez

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

34 citing papers in PubMed, 75 citations in OpenAlex.

  1. AFM to Study Pore-Forming Proteins.Methods in molecular biology (Clifton, N.J.) · 2027
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  10. Sea Anemones, Actinoporins, and Cholesterol.International journal of molecular sciences · 2022
    Review
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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

3 authors at 1 institution in 2 countries.

Katia Cosentino *Interfaculty Institute of Biochemistry (IFIB), University of Tübingen, Tübingen, Germany.
Uris Ros *Interfaculty Institute of Biochemistry (IFIB), University of Tübingen, Tübingen, Germany.
Ana J García-SáezInterfaculty Institute of Biochemistry (IFIB), University of Tübingen, Tübingen, Germany.
Max Planck Society · DE

Funding

European Research Council 309966
6 · The paper itself

Abstract

Pore forming proteins (PFPs) share the ability of creating pores that allow the passage of ions, proteins or other constituents through a wide variety of target membranes, ranging from bacteria to humans. They often cause cell death, as pore formation disrupts the membrane permeability barrier required for maintaining cell homeostasis. The organization into supramolecular complexes or oligomers that pierce the membrane is a common feature of PFPs. However, the molecular pathway of self-assembly and pore opening remains unclear. Here, we review the most recent discoveries in the mechanism of membrane oligomerization and pore formation of a subset of PFPs, the α-PFPs, whose pore-forming domains are formed by helical segments. Only now we are starting to grasp the molecular details of their function, mainly thanks to the introduction of single molecule microscopy and nanoscopy techniques. This article is part of a Special Issue entitled: Pore-forming toxins edited by Mauro Dalla Serra and Franco Gambale.

Indexed as

Protein MultimerizationAnimalsCell MembraneHumansPorinsProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryPorinsMembranePore forming proteins (PFPs)Pore forming toxins (PFTs)Pore structureProtein oligomerization

Identifiers

PMID26375417
PMCPMC4869852
OpenAlexW1670108590

What OpenQuestion holds

Textmetadata
LicenceTDM
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.