ArticleProceedings of the National Academy of Sciences of the United States of America1997
ActA is a dimer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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.
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Who cites it
9 citing papers in PubMed, 36 citations in OpenAlex.
- Review
- ActA promotes Listeria monocytogenes aggregation, intestinal colonization and carriage.PLoS pathogens · 2013Article
- Close packing of Listeria monocytogenes ActA, a natively unfolded protein, enhances F-actin assembly without dimerization.The Journal of biological chemistry · 2008Article
- Construction, characterization, and use of two Listeria monocytogenes site-specific phage integration vectors.Journal of bacteriology · 2002Article
- Actin-based motility of intracellular microbial pathogens.Microbiology and molecular biology reviews : MMBR · 2001Review
- Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility.The Journal of cell biology · 2001Article
- Three regions within ActA promote Arp2/3 complex-mediated actin nucleation and Listeria monocytogenes motility.The Journal of cell biology · 2000Article
- Interactions of Listeria monocytogenes with mammalian cells during entry and actin-based movement: bacterial factors, cellular ligands and signaling.The EMBO journal · 1998Review
- Interactions of the bacterial pathogen Listeria monocytogenes with mammalian cells: bacterial factors, cellular ligands, and signaling.Folia microbiologica · 1998Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ActA, a surface protein of Listeria monocytogenes, is able to induce continuous actin polymerization at the rear of the bacterium, in the cytosol of the infected cells. Its N-terminal domain is sufficient to induce actin tail formation and movement. Here, we demonstrate, using the yeast two-hybrid system, that the N-terminal domain of ActA may form homodimers. By using chemical cross-linking to explore the possibility that ActA could be a multimer on the surface of the bacteria, we show that ActA is a dimer. Cross-linking experiments on various L. monocytogenes strains expressing different ActA variants demonstrated that the region spanning amino acids 97-126, and previously identified as critical for actin tail formation, is also critical for dimer formation. A model of actin polymerization by L. monocytogenes, involving the ActA dimer, is presented.
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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.