Evidence map›Paper›PMID 34387717›Full record

ReviewCellular and molecular life sciences : CMLS2021

Beyond pore formation: reorganization of the plasma membrane induced by pore-forming proteins.

Magdalena Kulma, Gregor Anderluh

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  12. Evaluating Biofilm Inhibitory Potential in Fish Pathogen,Antibiotics (Basel, Switzerland) · 2023
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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 1 institution in 1 country.

Magdalena KulmaDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1001, Ljubljana, Slovenia. magdalena.kulma@ki.si.ORCID http://orcid.org/0000-0002-4407-1447
Gregor AnderluhDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1001, Ljubljana, Slovenia.
National Institute of Chemistry · SI

Funding

Javna Agencija za Raziskovalno Dejavnost RS ARRS-NRU/N1-0120-0104-2020/1Javna Agencija za Raziskovalno Dejavnost RS P1-0391Polish National Agency for Academic Exchange PPN/BEK/2018/1/00327/U/00001
6 · The paper itself

Abstract

Pore-forming proteins (PFPs) are a heterogeneous group of proteins that are expressed and secreted by a wide range of organisms. PFPs are produced as soluble monomers that bind to a receptor molecule in the host cell membrane. They then assemble into oligomers that are incorporated into the lipid membrane to form transmembrane pores. Such pore formation alters the permeability of the plasma membrane and is one of the most common mechanisms used by PFPs to destroy target cells. Interestingly, PFPs can also indirectly manipulate diverse cellular functions. In recent years, increasing evidence indicates that the interaction of PFPs with lipid membranes is not only limited to pore-induced membrane permeabilization but is also strongly associated with extensive plasma membrane reorganization. This includes lateral rearrangement and deformation of the lipid membrane, which can lead to the disruption of target cell function and finally death. Conversely, these modifications also constitute an essential component of the membrane repair system that protects cells from the lethal consequences of pore formation. Here, we provide an overview of the current knowledge on the changes in lipid membrane organization caused by PFPs from different organisms.

Indexed as

Cell MembraneCell Membrane PermeabilityComplement Membrane Attack ComplexEndocytosisHumansMembrane LipidsPore Forming Cytotoxic ProteinsPorinsComplement Membrane Attack ComplexMembrane LipidsPore Forming Cytotoxic ProteinsPorinsLipid distributionMembrane organizationPlasma membranePore-forming proteins

Identifiers

PMID34387717
PMCPMC11073440
OpenAlexW3188789931

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.