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Geoffrey B. Severin

Researcher at Michigan State University

Publications -  23
Citations -  508

Geoffrey B. Severin is an academic researcher from Michigan State University. The author has contributed to research in topics: Vibrio cholerae & Cyclic di-GMP. The author has an hindex of 9, co-authored 19 publications receiving 334 citations.

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Oligoribonuclease is the primary degradative enzyme for pGpG in Pseudomonas aeruginosa that is required for cyclic-di-GMP turnover

TL;DR: This work identifies oligoribonuclease (Orn) as the primary PDE-B enzyme that removes pGpG, which is necessary to complete the final step in the c-di-GMP degradation pathway, and demonstrates that Orn is the primary source of Pde-B activity in Pseudomonas aeruginosa.
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Direct activation of a phospholipase by cyclic GMP-AMP in El Tor Vibrio cholerae

TL;DR: It is demonstrated that cGAMP activates CapV phospholipase activity to target the cell membrane and suggested that acquisition of this second messenger signaling pathway may contribute to the emergence of the El Tor biotype as the etiological agent behind the seventh cholera pandemic.
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The Vibrio cholerae diguanylate cyclase VCA0965 has an AGDEF active site and synthesizes cyclic di-GMP

TL;DR: It is concluded that VCA0965 is capable of c-di-GMP synthesis and that the first amino acid of the GG(D/E)EF motif is more tolerant of substitutions than currently appreciated.
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Feedback regulation of Caulobacter crescentus holdfast synthesis by flagellum assembly via the holdfast inhibitor HfiA.

TL;DR: The data support a model in which flagellum assembly feeds back to control holdfast synthesis via HfiA expression in a c‐di‐GMP‐dependent manner under defined nutrient conditions, and show that flagella are not necessarily required for C. crescentus surface sensing in the absence of flow.
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Cyclic di-GMP Regulates TfoY in Vibrio cholerae To Control Motility by both Transcriptional and Posttranscriptional Mechanisms

TL;DR: The results suggest that the c-di-GMP signaling network of V. cholerae can exist in at least three distinct states to regulate biofilm formation and motility.