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Joseph Aduse-Opoku

Researcher at King's College London

Publications -  52
Citations -  2810

Joseph Aduse-Opoku is an academic researcher from King's College London. The author has contributed to research in topics: Porphyromonas gingivalis & Protease. The author has an hindex of 28, co-authored 48 publications receiving 2562 citations. Previous affiliations of Joseph Aduse-Opoku include University of London & Queen Mary University of London.

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Selective Sorting of Cargo Proteins into Bacterial Membrane Vesicles

TL;DR: It is established that the human oral pathogen Porphyromonas gingivalis has a mechanism to selectively sort proteins into OMV, resulting in the preferential packaging of virulence factors intoOMV and the exclusion of abundant outer membrane proteins from the protein cargo.
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Molecular genetics and nomenclature of proteases of Porphyromonas gingivalis

TL;DR: It is evident, through comparison of these gene sequences and through gene inactivation studies, that the genetic structure of the proteases of this organism, particularly those with specificity for arginyl and lysyl peptide bonds, is less complicated than originally thought.
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Cysteine proteases of Porphyromonas gingivalis.

TL;DR: Some of the progress in their molecular characterization and how their putative biological roles, in relation to the in vivo growth and survival strategies of P. gingivalis, may also contribute to the periodontal disease process are described.
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LuxS-dependent quorum sensing in Porphyromonas gingivalis modulates protease and haemagglutinin activities but is not essential for virulence.

TL;DR: Results were obtained with E. coli DH5alpha transformed with luxS, suggesting that AI-2 production is not limited by a lack of LuxS protein, and was insufficient to attenuate the luxS mutant in a murine lesion model of P. gingivalis infection.
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Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50.

TL;DR: The catalytic chains of this unusual group of enzymes are shown to be differentially modified by the posttranslational addition of carbohydrate, indicating that these protease isoforms are modified not only to different extents but also with different sugars.