ArticleMolecular microbiology2011
The double life of a bacterial lipoprotein.
Article in Molecular microbiology, 2011. 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, 8 citations in OpenAlex.
- Escherichia coli lipoprotein binds human plasminogen via an intramolecular domain.Frontiers in microbiology · 2015Article
- Analyzing the molecular mechanism of lipoprotein localization in Brucella.Frontiers in microbiology · 2015Review
- Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond.Biochimica et biophysica acta · 2014Review
- Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC.Journal of molecular biology · 2012Article
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1 author at 1 institution in 1 country.
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Abstract
It has been known for many years that the small lipoprotein Lpp, which is the most abundant protein in E. coli, exists in two forms. The 'bound' form of the protein is tethered to the outer membrane (OM) by its N-terminal lipid moiety and covalently attached to the cell wall by its C-terminal lysine residue. The exact location of the 'free' form, however, has never been determined. In this issue of Molecular Microbiology, Cowles et al. demonstrate that the free form of Lpp is an integral OM protein whose C-terminus is exposed on the cell surface. The new study provides the first example of a lipoprotein that has a dual localization and adds to a growing body of evidence that lipoproteins can span the OM despite the lack of an obvious transmembrane segment. Furthermore, the new results raise intriguing questions about the assembly of both lipoproteins and other types of OM proteins.
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