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- Publications
- Influence
MitoNEET-dependent formation of intermitochondrial junctions
- Alexandre Vernay, A. Marchetti, +6 authors P. Cosson
- Biology, Medicine
- Proceedings of the National Academy of Sciences
- 17 July 2017
Significance Mitochondria form dynamic networks in eukaryotic cells by constantly fusing with and separating from each other. Alterations in the mitochondrial network are observed in many… Expand
TM9 family proteins control surface targeting of glycine-rich transmembrane domains
- J. Perrin, Marion le Coadic, +4 authors P. Cosson
- Biology, Medicine
- Journal of Cell Science
- 1 July 2015
ABSTRACT TM9 family proteins (also named Phg1 proteins) have been previously shown to control cell adhesion by determining the cell surface localization of adhesion proteins such as the Dictyostelium… Expand
Immunofluorescence labeling of cell surface antigens in Dictyostelium
- Alexandre Vernay, P. Cosson
- Biology, Medicine
- BMC Research Notes
- 12 August 2013
BackgroundImmunolocalization of cellular antigens typically requires fixation and permeabilization of cells, prior to incubation with antibodies.FindingsAssessing a test protein abundantly present at… Expand
Role of the HIV-1 envelope transmembrane domain in intracellular sorting
- J. Perrin, Aurélie Bary, Alexandre Vernay, P. Cosson
- Biology, Medicine
- BMC Cell Biology
- 15 March 2018
BackgroundThe envelope protein of lentiviruses are type I transmembrane proteins, and their transmembrane domain contains conserved potentially charged residues. This highly unusual feature would be… Expand
Abstract 3323:In situmultiplex analysis of resident microglia and infiltrating macrophages in glioblastoma
- Nicolas Goulange, A. Finan-Marchi, +5 authors Renaud Burrer
- Medicine
- 15 August 2020
TM9SF4 levels determine sorting of transmembrane domains in the early secretory pathway
- Alexandre Vernay, O. Lamrabet, J. Perrin, P. Cosson
- Biology, Medicine
- Journal of Cell Science
- 1 November 2018
ABSTRACT Previous studies have shown that TM9SF4 interacts with glycine-rich transmembrane domains (TMDs) and promotes their surface localization, presumably by escorting them along the secretory… Expand