ArticleThe Journal of biological chemistry2019
A stable tetramer is not the only oligomeric state that mitochondrial single-stranded DNA binding proteins can adopt.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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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Who cites it
4 citing papers in PubMed, 3 citations in OpenAlex.
- Regulation of Pfh1 helicase activity by nucleic acid interactions and mitochondrial SSB.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanisms of SSBP1 variants in mitochondrial disease: Molecular dynamics simulations reveal stable tetramers with altered DNA binding surfaces.DNA repair · 2021Article
- The R882H substitution in the humanThe Journal of biological chemistry · 2019Article
- The LUFS domain, its transcriptional regulator proteins, and drug resistance in the fungal pathogen Candida auris.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Mitochondrial single-stranded DNA (ssDNA)-binding proteins (mtSSBs) are required for mitochondrial DNA replication and stability and are generally assumed to form homotetramers, and this species is proposed to be the one active for ssDNA binding. However, we recently reported that the mtSSB from
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Registered trials
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