Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Marie-Josèphe Rabiet"'
Autor:
Julien Verove, Cédric Bernarde, Yu-Sing Tammy Bohn, François Boulay, Marie-Josèphe Rabiet, Ina Attree, François Cretin
Publikováno v:
PLoS ONE, Vol 7, Iss 1, p e30488 (2012)
Pseudomonas aeruginosa type III secretion apparatus exports and translocates four exotoxins into the cytoplasm of the host cell. The translocation requires two hydrophobic bacterial proteins, PopB and PopD, that are found associated with host cell me
Externí odkaz:
https://doaj.org/article/a9ac1aa23e544109bef295f42c6f7d19
Autor:
Anna Karlsson, François Boulay, Claes Dahlgren, Marie-Josèphe Rabiet, Huamei Forsman, Tudor I. Oprea, Johan Bylund
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1833:1914-1923
Lipidated peptides (pepducins) can activate certain G-protein coupled receptors (GPCRs) through a unique allosteric modulation mechanism involving cytosolic receptor domains. Pepducins with the amino acid sequence of the third intracellular loop of t
Publikováno v:
Journal of Biological Chemistry. 285:14338-14345
The N-terminal part of the calcium-regulated and phospholipid-binding protein annexin AI contains peptide sequences with pro- and anti-inflammatory activities. We have earlier shown that a proinflammatory signal triggered by one of these peptides, Gl
Autor:
Huamei Forsman, François Boulay, Michael Gabl, Malene Winther, Marie-Josèphe Rabiet, Claes Dahlgren, Sarah Line Skovbakke
Publikováno v:
Biochimica et Biophysica Acta-Molecular Cell Research
Biochimica et Biophysica Acta-Molecular Cell Research, Elsevier, 2015, 1853 (1), pp.192-200. ⟨10.1016/j.bbamcr.2014.10.021⟩
Biochimica et Biophysica Acta-Molecular Cell Research, Elsevier, 2015, 1853 (1), pp.192-200. ⟨10.1016/j.bbamcr.2014.10.021⟩
International audience; Pathogenic Staphylococcus aureus strains produce N-formylmethionyl containing peptides, of which the tetrapeptide fMIFL is a potent activator of the neutrophil formyl peptide receptor 1 (FPR1) and the PSMα2 peptide is a poten
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bafbec74e8d4613adbfd39149a34abd5
https://hal.archives-ouvertes.fr/hal-03518824
https://hal.archives-ouvertes.fr/hal-03518824
Autor:
Marie-Josèphe Rabiet, François Boulay
Publikováno v:
Traffic. 6:83-86
Publikováno v:
Scandinavian Journal of Immunology. 56:470-476
Lipoxin A4 (LXA4) has been shown to bind to the leucocyte formyl peptide receptor (FPR) homologue, FPRL1, without triggering the biological activities induced by other FPRL1 agonists. We investigated the direct effect of LXA4 as well as the effect on
Publikováno v:
Blood. 100:1835-1844
A tetracycline-controlled expression system was adapted to the human promyelocytic HL-60 cell line by placement of the transactivator (tTA-off) sequence under the control of the human EF-1α promoter region. Constitutively active and dominant-inhibit
Autor:
Jean-Luc Plantier, Yolande Genoux, Elisabetta Dejana, Yves Rival, Marie-Josèphe Rabiet, Maria Grazia Lampugnani
Publikováno v:
Scopus-Elsevier
Abstract Thrombin increases endothelial permeability in a rapid and reversible way. This effect requires the catalytic activity of the enzyme and thrombin receptor engagement. Endothelial cell permeability is mostly regulated by intercellular junctio
Autor:
Jennie Karlsson, Claes Dahlgren, Huamei Forsman, Emil Andréasson, Marie-Josèphe Rabiet, François Boulay
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 189(2)
The neutrophil formyl peptide receptors, FPR1 and FPR2, play critical roles for inflammatory reactions, and receptor-specific antagonists/inhibitors can possibly be used to facilitate the resolution of pathological inflammatory reactions. A 10-aa-lon
Autor:
Ina Attree, Cédric Bernarde, Julien Verove, Marie-Josèphe Rabiet, Yu-Sing Tammy Bohn, François Boulay, François Cretin
Publikováno v:
PLoS ONE
PLoS ONE, Public Library of Science, 2020, 7 (1), pp.e30488. ⟨10.1371/journal.pone.0030488⟩
PLoS ONE, Vol 7, Iss 1, p e30488 (2012)
PLoS ONE, 2020, 7 (1), pp.e30488. ⟨10.1371/journal.pone.0030488⟩
PLoS ONE, Public Library of Science, 2020, 7 (1), pp.e30488. ⟨10.1371/journal.pone.0030488⟩
PLoS ONE, Vol 7, Iss 1, p e30488 (2012)
PLoS ONE, 2020, 7 (1), pp.e30488. ⟨10.1371/journal.pone.0030488⟩
International audience; Pseudomonas aeruginosa type III secretion apparatus exports and translocates four exotoxins into the cytoplasm of the host cell. The translocation requires two hydrophobic bacterial proteins, PopB and PopD, that are found asso