Zobrazeno 1 - 10
of 32
pro vyhledávání: '"F G van der Goot"'
Autor:
I. Castanon, J. T. Hannich, L. Abrami, F. Huber, M. Dubois, M. Müller, F. G. van der Goot, M. Gonzalez-Gaitan
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
During development, oriented cell division is important to proper body axis extension. Here, the authors show that sphingolipids are required to direct spindle rotation and oriented mitosis via Anthrax receptor palmitoylation in zebrafish gastrulatio
Externí odkaz:
https://doaj.org/article/8a8ca64a3ec14891b6839f3bf319ba3c
Autor:
F. G. van der Goot, Martina Audagnotto, Sylvia Ho, M. Anward, Laurence Abrami, Maria J. Marcaida, Florence Pojer, M. Dal Peraro, Giulia Fonti, Patrick A. Sandoz, Francisco Mesquita
Many biochemical reactions occur at the membrane interfaces. The proper control of these reactions requires spatially and temporally controlled recruitment of protein complexes. These assemblies are largely regulated by post-translational modificatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b14a6af6de54544e39e26fcdce16529
https://doi.org/10.1101/2020.06.18.157545
https://doi.org/10.1101/2020.06.18.157545
Autor:
F. G. van der Goot, Yulia Tsitrin, Marie-Claire Velluz, Patrick Paumard, Catherine El Bez, Michael W. Parker, Salvatore Lanzavecchia, Jacques Dubochet, Marc Adrian, Craig J. Morton
Publikováno v:
Nature Structural Biology. 9:729-733
Proteins exist in one of two generally incompatible states: either membrane associated or soluble. Pore-forming proteins are exceptional because they are synthesized as a water-soluble molecule but end up being located in the membrane -- that is, the
Publikováno v:
Journal of Biological Chemistry, Vol. 273, No 29 (1998) pp. 18122-18129
Aerolysin is a pore-forming toxin that plays a key role in the pathogenesis of Aeromonas hydrophila infections. In this study, we have analyzed the effect of aerolysin on human granulocytes (HL-60 cells). Proaerolysin could bind to these cells, was p
Autor:
Susanne C. Feil, S M Raja, Jamie Rossjohn, J T Buckley, Michael W. Parker, F. G. van der Goot, K L Nelson
Publikováno v:
Biochemistry, Vol. 37, No 2 (1998) pp. 741-746
Aerolysin is a channel-forming toxin that must oligomerize in order to become insertion-competent. Modeling based on the crystal structure of the proaerolysin dimer and electron microscopic images of the oligomer indicated that a loop in domain 3 mus
Autor:
I. Castanon, L. Abrami, L. Holtzer, C. P. Heisenberg, F. G. van der Goot, M. Gonzxe1lez-Gaitxe1n
Publikováno v:
NATURE CELL BIOLOGY, Volume 1,5 Number 1.
Autor:
Thomas Harder, F. G. van der Goot
Publikováno v:
Seminars in immunology. 13(2)
While the existence of cholesterol/sphingolipid (raft) membrane domains in the plasma membrane is now supported by strong experimental evidence, the structure of these domains, their size, their dynamics, and their molecular composition remain to be
Publikováno v:
Nature. 354:408-410
THE 'molten' globular conformation of a protein is compact with a native secondary structure but a poorly defined tertiary structure1,2. Molten globular states are intermediates in protein folding and unfolding3–5 and they may be involved in the tr
Autor:
M, Hribar, A, Bloc, F G, van der Goot, L, Fransen, P, De Baetselier, G E, Grau, H, Bluethmann, M A, Matthay, Y, Dunant, J, Pugin, R, Lucas
Publikováno v:
European journal of immunology. 29(10)
Herein, we show that TNF exerts a pH-dependent increase in membrane conductance in primary lung microvascular endothelial cells and peritoneal macrophages. This effect was TNF receptor-independent, since it also occurred in cells isolated from mice d
Publikováno v:
Biochemistry, Vol. 38, No 14 (1999) pp. 4296-4302
The alpha-toxin from Staphylococcus aureus undergoes several conformational changes from the time it is released from the bacterium to the moment it forms a channel in the plasma membrane of its target cell. It is initially a soluble monomer, which u