ArticleNature communications2018
Bacterial dynamin-like proteins reveal mechanism for membrane fusion.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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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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.
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Who cites it
7 citing papers in PubMed.
- Host-initiated microbial association leads to stable ectosymbiosis in an ecological model.PLoS computational biology · 2026Article
- Mitochondrial flagella-like extensions (MitoFLARE) dysfunction triggers STING-mediated immune dysregulation in sepsis.Nature communications · 2026Article
- Binding of Bacillus subtilis dynamin-like protein DynA to the bacterial membrane is essential for effective phage defense.The FEBS journal · 2026Article
- Tracing the evolutionary pathway: on the origin of mitochondria and eukaryogenesis.The FEBS journal · 2025Article
- Antiviral Mx proteins have an ancient origin and widespread distribution among eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mitochondrial membrane models built from native lipid extracts: Interfacial and transport properties.Frontiers in molecular biosciences · 2022Article
- Genetic dissection of Escherichia coli's master diguanylate cyclase DgcE: Role of the N-terminal MASE1 domain and direct signal input from a GTPase partner system.PLoS genetics · 2019Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dynamin superfamily of large GTPases comprises specialized members that catalyze fusion and fission of biological membranes. While fission-specific proteins such as dynamin work as homo-oligomeric complexes, many fusion catalysts such as mitofusins or bacterial dynamin-like proteins (DLPs) act as hetero-oligomers. However, so far it was unclear how these hetero-oligomeric DLPs assemble and how they function in membrane remodeling. The group of Harry Low report now on the structure of a DLP pair from Campylobacter jejuni, allowing detailed insight into the assembly mechanism and membrane tethering activity.
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Registered trials
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