J
Jean-Pierre Gorvel
Researcher at Aix-Marseille University
Publications - 239
Citations - 16211
Jean-Pierre Gorvel is an academic researcher from Aix-Marseille University. The author has contributed to research in topics: Brucella & Endosome. The author has an hindex of 67, co-authored 231 publications receiving 15005 citations. Previous affiliations of Jean-Pierre Gorvel include Centre national de la recherche scientifique & Aberystwyth University.
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Journal ArticleDOI
The Cytoplasmic Tail of Invariant Chain Regulates Endosome Fusion and Morphology
Tommy W. Nordeng,Tommy W. Nordeng,Tone F. Gregers,Thomas L. Kongsvik,Stéphane Méresse,Jean-Pierre Gorvel,Fabrice Jourdan,Andrea Motta,Oddmund Bakke +8 more
TL;DR: In this article, the major histocompatibility complex class II associated invariant chain (Ii) has been shown to inhibit endocytic transport and to increase the size of endosomes.
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Invariant Chain Induces a Delayed Transport from Early to Late Endosomes
TL;DR: The results strongly suggest that invariant chain induces a retention mechanism in the endocytic pathway, and Rab5 and Rab7 GTPases as markers of early and late endosomes are identified.
Journal Article
Modulation of endocytosis in nuclear factor IL-6(-/-) macrophages is responsible for a high susceptibility to intracellular bacterial infection.
TL;DR: Addition of the granulocyte- CSF (G-CSF), whose induction is impaired in NF-IL-6(-/-) macrophages, restores both endocytosis and the morphology of endosomes, together with bactericidal activity.
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Localization by immunofluorescence and histochemical labeling of aminopeptidase N in relation to its biosynthesis in rabbit and pig enterocytes
TL;DR: Antibodies raised against highly purified rabbit intestinal brush border aminopeptidase N were found in certain rabbits or pigs to crossreact with human blood-grouplike substances present in goblet cells and at the surface of the basolateral membrane of enterocytes.
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Identification of Salmonella functions critical for bacterial cell division within eukaryotic cells
TL;DR: It is shown here that blockage in the bacterial division process is sulA‐independent and takes place after FtsZ‐ring assembly, and it is demonstrated that SL1344 filamentation is a result of hisG mutation, requires the activity of an enzyme of the histidine biosynthetic pathway HisFH and is specific for the vacuolar environment.