ArticlePloS one2011
Bacterial transmembrane proteins that lack N-terminal signal sequences.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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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
10 citing papers in PubMed, 21 citations in OpenAlex.
- Identification of novel tail-anchored membrane proteins integrated by the bacterial twin-arginine translocase.Microbiology (Reading, England) · 2024Article
- A comparative genomics methodology reveals a widespread family of membrane-disrupting T6SS effectors.Nature communications · 2020Article
- Identification of new components of the RipC-FtsEX cell separation pathway of Corynebacterineae.PLoS genetics · 2019Article
- Neutralization of Junín virus by single domain antibodies targeted against the nucleoprotein.Scientific reports · 2018Article
- Comprehensive subcellular topologies of polypeptides in Streptomyces.Microbial cell factories · 2018Article
- Tail-Anchored Inner Membrane Protein ElaB Increases Resistance to Stress While Reducing Persistence in Escherichia coli.Journal of bacteriology · 2017Article
- Cohesive Properties of themBio · 2017Article
- The Glutaminase-Dependent System Confers Extreme Acid Resistance to New Species and Atypical Strains ofFrontiers in microbiology · 2017Article
- New insights into the targeting of a subset of tail-anchored proteins to the outer mitochondrial membrane.Frontiers in plant science · 2014Article
- Truncated hemoglobin, HbN, is post-translationally modified in Mycobacterium tuberculosis and modulates host-pathogen interactions during intracellular infection.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Tail-anchored membrane proteins (TAMPs), a class of proteins characterized by their lack of N-terminal signal sequence and Sec-independent membrane targeting, play critical roles in apoptosis, vesicle trafficking and other vital processes in eukaryotic organisms. Until recently, this class of membrane proteins has been unknown in bacteria. Here we present the results of bioinformatic analysis revealing proteins that are superficially similar to eukaryotic TAMPs in the bacterium Streptomyces coelicolor. We demonstrate that at least four of these proteins are bona fide membrane-spanning proteins capable of targeting to the membrane in the absence of their N-terminus and the C-terminal membrane-spanning domain is sufficient for membrane targeting. Several of these proteins, including a serine/threonine kinase and the SecE component of the Sec translocon, are widely conserved in bacteria.
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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.