ArticleFrontiers in microbiology2019
The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of
Article in Frontiers in microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Structural characterization and functional insights into the type II secretion system of the poly-extremophile Deinococcus radiodurans.The Journal of biological chemistry · 2024Article
- The structured organization ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The cryo-EM structure of the S-layer deinoxanthin-binding complex of Deinococcus radiodurans informs properties of its environmental interactions.The Journal of biological chemistry · 2022Article
- Structural insights into the main S-layer unit ofThe Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Surface (S)-layers are cryptic structures that coat the external surface of the bacterial cell in many species. The paracrystalline regularity of the S-layer is due to the self-assembling of one or more protein units. The property of self-assembling seems to be mediated by specific topologies of the S-layer proteins as well as the presence of specific ions that provide support in building and stabilizing the bi-dimensional S-layer organization. In the present study, we have investigated the self-assembling mechanism of the main S-layer protein of
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Registered trials
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