J
Josef Deutscher
Researcher at Université Paris-Saclay
Publications - 152
Citations - 11743
Josef Deutscher is an academic researcher from Université Paris-Saclay. The author has contributed to research in topics: PEP group translocation & Catabolite repression. The author has an hindex of 61, co-authored 152 publications receiving 11068 citations. Previous affiliations of Josef Deutscher include Max Planck Society & Institut national de la recherche agronomique.
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Journal ArticleDOI
How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria
TL;DR: The known protein phosphorylation-related regulatory functions of the PTS are summarized, which shows that the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.
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The mechanisms of carbon catabolite repression in bacteria
TL;DR: The major CCR mechanisms operative in Enterobacteriaceae and Firmicutes are quite different, but in both types of organisms components of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) and protein phosphorylation play a major role.
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Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria
TL;DR: Glycolytic intermediates, stimulating the corresponding protein kinase and the P‐ser‐HPr/CcpA complex formation, provide a link between glycolysis activity and carbon catabolite repression.
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The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions
Josef Deutscher,Francine Moussan Désirée Aké,Meriem Derkaoui,Arthur Constant Zébré,Thanh Nguyen Cao,Houda Bouraoui,Takfarinas Kentache,Abdelhamid Mokhtari,Eliane Milohanic,Philippe Joyet +9 more
TL;DR: A large variety of signal transduction mechanisms allows the PTS to regulate numerous proteins and to form a vast regulatory network responding to the phosphorylation state of various PTS components.
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ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes
Josef Deutscher,Milton H. Saier +1 more
TL;DR: Observations lead us to suggest that phosphorylation of a seryl residue in HPr is involved in the regulation of sugar transport in the bacteria cell.