ArticleNature communications2019
The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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
48 citing papers in PubMed, 84 citations in OpenAlex.
- Anchoring of perforin-2 via the transmembrane domain is required for antigen escape into the cytosol.The EMBO journal · 2026Article
- Molecular mechanism of pore formation by Plasmodium Perforin-like Protein 2.Nature communications · 2026Article
- Deciphering Membrane Pore Formation Mechanisms of Plasmodium falciparum Perforin-Like Protein 1 (PfPLP1).The Journal of membrane biology · 2026Article
- Perforin-2 enhances antigen-specific CTL immune response by promoting cross presentation.Cell death & disease · 2026Article
- Disrupting membranes, controlling cell fate: the role of pore-forming proteins in cell death and therapy.Apoptosis : an international journal on programmed cell death · 2025Review
- A new age in structural S-layer biology: Experimental and in silico milestones.The Journal of biological chemistry · 2025Review
- Structural basis for the pore-forming activity of a complement-like toxin.Science advances · 2025Article
- Mapping O- and N-Glycosylation in Transmembrane and Interface Regions of Proteins: Insights from a Database Search Study.International journal of molecular sciences · 2025Article
- Proliferating Microglia Exhibit Unique Transcriptional and Functional Alterations in Alzheimer's Disease.ASN neuro · 2025Article
- Whole genome sequencing reveals candidate causal genetic variants for spastic syndrome in Holstein cattle.Scientific reports · 2024Article
- Encoding extracellular modification of artificial cell membranes using engineered self-translocating proteins.Nature communications · 2024Article
- Cryo-EM reconstruction of oleate hydratase bound to a phospholipid membrane bilayer.Journal of structural biology · 2024Article
- Article
- Enhancing cryo-EM structure prediction with DeepTracer and AlphaFold2 integration.Briefings in bioinformatics · 2024Article
- Visible Light Control over the Cytolytic Activity of a Toxic Pore-Forming Protein.ACS chemical biology · 2024Article
- Structure and assembly of a bacterial gasdermin pore.bioRxiv : the preprint server for biology · 2023Article
- Structural journey of an insecticidal protein against western corn rootworm.Nature communications · 2023Article
- Article
- Perforin-2 is a pore-forming effector of endocytic escape in cross-presenting dendritic cells.Science (New York, N.Y.) · 2023Article
- Cryo-EM structures of perforin-2 in isolation and assembled on a membrane suggest a mechanism for pore formation.The EMBO journal · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
18 authors at 6 institutions in 4 countries.
Funding
Abstract
Macrophage-expressed gene 1 (MPEG1/Perforin-2) is a perforin-like protein that functions within the phagolysosome to damage engulfed microbes. MPEG1 is thought to form pores in target membranes, however, its mode of action remains unknown. We use cryo-Electron Microscopy (cryo-EM) to determine the 2.4 Å structure of a hexadecameric assembly of MPEG1 that displays the expected features of a soluble prepore complex. We further discover that MPEG1 prepore-like assemblies can be induced to perforate membranes through acidification, such as would occur within maturing phagolysosomes. We next solve the 3.6 Å cryo-EM structure of MPEG1 in complex with liposomes. These data reveal that a multi-vesicular body of 12 kDa (MVB12)-associated β-prism (MABP) domain binds membranes such that the pore-forming machinery of MPEG1 is oriented away from the bound membrane. This unexpected mechanism of membrane interaction suggests that MPEG1 remains bound to the phagolysosome membrane while simultaneously forming pores in engulfed bacterial targets.
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.