Zobrazeno 1 - 10
of 52
pro vyhledávání: '"Gilles Flatau"'
Autor:
Christoph Beitzinger, Caroline Stefani, Angelika Kronhardt, Monica Rolando, Gilles Flatau, Emmanuel Lemichez, Roland Benz
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e46964 (2012)
It is of interest to define bacterial toxin biochemical properties to use them as molecular-syringe devices in order to deliver enzymatic activities into host cells. Binary toxins of the AB(7/8)-type are among the most potent and specialized bacteria
Externí odkaz:
https://doaj.org/article/cc8517eb4d8b43369fc1b9bd17c3bc37
Autor:
Angelika Kronhardt, Monica Rolando, Christoph Beitzinger, Caroline Stefani, Michael Leuber, Gilles Flatau, Michel R Popoff, Roland Benz, Emmanuel Lemichez
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e23133 (2011)
Binary toxins are among the most potent bacterial protein toxins performing a cooperative mode of translocation and exhibit fatal enzymatic activities in eukaryotic cells. Anthrax and C2 toxin are the most prominent examples for the AB(7/8) type of t
Externí odkaz:
https://doaj.org/article/bfbaa0c9d25a471dbf8b0edf677a342b
Autor:
Musa M. Mhlanga, Amel Mettouchi, Gilles Flatau, Caroline Stefani, Ulf R. Rapp, Patrick Auberger, Emmanuel Lemichez, Monica Rolando, Antoine Galmiche
Publikováno v:
Cellular Microbiology. 12:891-905
We have investigated how Bacillus anthracis lethal toxin (LT) triggers caspase-3 activation and the formation of thick actin cables in human endothelial cells. By DNA array analysis we show that LT has a major impact on the cell transcriptome and we
Autor:
Caroline Stefani, Patrick Auberger, Emmanuel Lemichez, Gilles Flatau, Monica Rolando, Patrick Munro
Publikováno v:
Infection and Immunity. 77:3596-3601
Systemic injection of Bacillus anthracis lethal toxin (LT) produces vascular leakage and animal death. Recent studies suggest that LT triggers direct endothelial cell cytotoxicity that is responsible for the vascular leakage. LT is composed of heptam
Publikováno v:
Protein Science. 17:878-886
C3-like exoenzymes are ADP-ribosyltransferases that specifically modify some Rho GTPase proteins, leading to their sequestration in the cytoplasm, and thus inhibiting their regulatory activity on the actin cytoskeleton. This modification process goes
Autor:
Ilka Wittig, Ansgar Santel, Monica Rolando, Emmanuel Lemichez, Gilles Flatau, Ulf R. Rapp, Georg Krohne, Jochen Fueller, Antoine Galmiche, Anne Doye
Publikováno v:
Journal of Biological Chemistry. 283:14857-14866
The proteins of the RAF family (A-RAF, B-RAF, and C-RAF) are serine/threonine kinases that play important roles in development, mature cell regulation, and cancer. Although it is widely held that their localization on membranes is an important aspect
Publikováno v:
Molecular Biology of the Cell. 18:3429-3439
Apical junctional complex (AJC) plays a vital role in regulation of epithelial barrier function. Disassembly of the AJC is observed in diverse physiological and pathological states; however, mechanisms governing this process are not well understood.
Autor:
Pierre Gounon, Céline Pulcini, Patrick Munro, Luce Landraud, René L. Clément, Olivier Dussurget, Emmanuel Lemichez, Amel Mettouchi, Gilles Flatau, Anne Doye, Monica Rolando, Michel R. Popoff, Laurent Boyer
Publikováno v:
Journal of Cell Biology
Journal of Cell Biology, 2006, 173, pp.809-19. ⟨10.1083/jcb.200509009⟩
Journal of Cell Biology, Rockefeller University Press, 2006, 173, pp.809-19. ⟨10.1083/jcb.200509009⟩
The Journal of Cell Biology
Journal of Cell Biology, 2006, 173, pp.809-19. ⟨10.1083/jcb.200509009⟩
Journal of Cell Biology, Rockefeller University Press, 2006, 173, pp.809-19. ⟨10.1083/jcb.200509009⟩
The Journal of Cell Biology
The GTPase RhoA is a major regulator of the assembly of actin stress fibers and the contractility of the actomyosin cytoskeleton. The epidermal cell differentiation inhibitor (EDIN) and EDIN-like ADP-ribosyltransferases of Staphylococcus aureus catal
Autor:
Gilles Flatau, Laurent Boyer, Jean-Louis Mege, Olivier Oregioni, Emmanuel Lemichez, Luce Landraud, Anne Doye, Patrick Munro
Publikováno v:
Journal of Biological Chemistry. 279:35849-35857
The CNF1 toxin is produced by uropathogenic and meningitis-causing Escherichia coli. CNF1 penetrates autonomously into cells and confers phagocytic properties to epithelial and endothelial cells. CNF1 acts at the molecular level by constitutively act
Autor:
Amel Mettouchi, Emmanuel Lemichez, René L. Clément, Gilles Flatau, Guillaume Bossis, Caroline Buisson-Touati, Anne Doye, Laurent Gagnoux, Patrice Boquet, Marc Piechaczyk
Publikováno v:
Cell
Cell, Elsevier, 2002, 111 (4), pp.553--564. ⟨10.1016/S0092-8674(02)01132-7⟩
Cell, Elsevier, 2002, 111 (4), pp.553--564. ⟨10.1016/S0092-8674(02)01132-7⟩
CNF1 toxin is a virulence factor produced by uropathogenic Escherichia coli. Upon cell binding and introduction into the cytosol, CNF1 deamidates glutamine 63 of RhoA (or 61 of Rac and Cdc42), rendering constitutively active these GTPases. Unexpected