Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Marine Houdou"'
Autor:
Zoé Durin, Marine Houdou, Willy Morelle, Lydia Barré, Aurore Layotte, Dominique Legrand, Mohamed Ouzzine, François Foulquier
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 10 (2022)
Glycosylation is a ubiquitous and universal cellular process in all domains of life. In eukaryotes, many glycosylation pathways occur simultaneously onto proteins and lipids for generating a complex diversity of glycan structures. In humans, severe g
Externí odkaz:
https://doaj.org/article/eac89051963b4e6c9bec41f0bc6d1671
Autor:
Marine Houdou, Nathalie Jacobs, Jonathan Coene, Mujahid Azfar, Roeland Vanhoutte, Chris Van den Haute, Jan Eggermont, Veronique Daniëls, Steven H. L. Verhelst, Peter Vangheluwe
Publikováno v:
Biomolecules, Vol 13, Iss 2, p 337 (2023)
Cells acquire polyamines putrescine (PUT), spermidine (SPD) and spermine (SPM) via the complementary actions of polyamine uptake and synthesis pathways. The endosomal P5B-type ATPases ATP13A2 and ATP13A3 emerge as major determinants of mammalian poly
Externí odkaz:
https://doaj.org/article/f58ce20d84b2469ebda98b8c2723a99b
Publikováno v:
Annual Review of Biochemistry. 92
The polyamines putrescine, spermidine, and spermine are abundant polycations of vital importance in mammalian cells. Their cellular levels are tightly regulated by degradation and synthesis, as well as by uptake and export. Here, we discuss the delic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3a36e6e5e833e496879f21ca7b67ed6
https://doi.org/10.1146/annurev-biochem-071322-021330
https://doi.org/10.1146/annurev-biochem-071322-021330
Autor:
Mujahid Azfar, Sarah van Veen, Marine Houdou, Norin Nabil Hamouda, Jan Eggermont, Peter Vangheluwe
Polyamines (PAs) are physiologically relevant molecules that are ubiquitous in all organisms. The vitality of PAs to the healthy functioning of a cell is due to their polycationic nature causing them to interact with a vast plethora of cellular playe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::359a43442333fec517efce4eadec32eb
https://lirias.kuleuven.be/handle/20.500.12942/701399
https://lirias.kuleuven.be/handle/20.500.12942/701399
Autor:
Charlotte Toustou, Marie‐Laure Walet‐Balieu, Marie‐Christine Kiefer‐Meyer, Marine Houdou, Patrice Lerouge, François Foulquier, Muriel Bardor
Publikováno v:
Biological Reviews
Biological Reviews, Wiley, In press, ⟨10.1111/brv.12820⟩
Biological Reviews, 2022, 97, pp.732-748. ⟨10.1111/brv.12820⟩
Biological Reviews, Wiley, In press, ⟨10.1111/brv.12820⟩
Biological Reviews, 2022, 97, pp.732-748. ⟨10.1111/brv.12820⟩
N-glycosylation is an important post-translational modification of proteins that has been highly conserved during evolution and is found in Eukaryota, Bacteria and Archaea. In eukaryotes, N-glycan processing is sequential, involving multiple specific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8d1a3a236d9fec4c1e5f8c45fa359d0
https://hal-normandie-univ.archives-ouvertes.fr/hal-03468527/file/2021-Toustou-et-al-Biological-reviews.pdf
https://hal-normandie-univ.archives-ouvertes.fr/hal-03468527/file/2021-Toustou-et-al-Biological-reviews.pdf
Autor:
Marine, Houdou, François, Foulquier
Publikováno v:
Medecine sciences : M/S. 36(8-9)
Glycosylation is an essential and complex cellular process where monosaccharides are added one by one onto an acceptor molecule, most of the time a protein or a lipid, so called glycoprotein or glycolipid. This cellular process is found in every livi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a7d876131cb3ca93582f40ad7b2a125e
https://pubmed.ncbi.nlm.nih.gov/32821050
https://pubmed.ncbi.nlm.nih.gov/32821050
Autor:
Marine Houdou, François Foulquier
Publikováno v:
médecine/sciences
médecine/sciences, EDP Sciences, 2020, 36 (8-9), pp.735-746. ⟨10.1051/medsci/2020128⟩
médecine/sciences, 2020, 36 (8-9), pp.735-746. ⟨10.1051/medsci/2020128⟩
médecine/sciences, EDP Sciences, 2020, 36 (8-9), pp.735-746. ⟨10.1051/medsci/2020128⟩
médecine/sciences, 2020, 36 (8-9), pp.735-746. ⟨10.1051/medsci/2020128⟩
La glycosylation est un processus cellulaire complexe conduisant à des transferts successifs de monosaccharides sur une molécule acceptrice, le plus souvent une protéine ou un lipide. Ce processus est universel chez tous les organismes vivants et
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cb30d16d3519bba00d775c8a5d7ad4f
https://hal.archives-ouvertes.fr/hal-02919329/document
https://hal.archives-ouvertes.fr/hal-02919329/document
Autor:
Eudoxie Dulary, Thorsten Marquardt, Willy Morelle, Marie-Ange Krzewinski-Recchi, Marine Houdou, Romain Péanne, Corentin Spriet, Dorothée Vicogne, André Klein, François Foulquier, Geoffroy de Bettignies, Vladimir Lupashin, Sven Potelle, Sandrine Duvet, Leslie K. Climer, Gert Matthijs, Pierre Morsomme, Elodie Lebredonchel
Publikováno v:
Biochemical Journal
Biochemical Journal, 2017, 474 (9), pp.1481-1493. ⟨10.1042/BCJ20160910⟩
Biochemical Journal, 2017, 474 (9), pp.1481-1493. ⟨10.1042/BCJ20160910⟩
International audience; TMEM165 deficiencies lead to one of the congenital disorders of glycosylation (CDG), a group of inherited diseases where the glycosylation process is altered. We recently demonstrated that the Golgi glycosylation defect due to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::048fb21e2ed76d0764baac6f15bfad07
https://doi.org/10.1042/bcj20160910
https://doi.org/10.1042/bcj20160910
Autor:
Kateryna Kondratska, Charles M. Rice, André Klein, Hans-Heinrich Hoffmann, Dorothée Vicogne, Marie-Ange Krzewinski, François Foulquier, Marine Houdou, Elodie Lebredonchel
Publikováno v:
Biochemical Journal
Biochemical Journal, 2019, 476 (21), pp.3281-3293. ⟨10.1042/BCJ20190488⟩
Biochemical Journal, Portland Press, 2019, 476 (21), pp.3281-3293. ⟨10.1042/BCJ20190488⟩
Biochemical Journal, 2019, 476 (21), pp.3281-3293. ⟨10.1042/BCJ20190488⟩
Biochemical Journal, Portland Press, 2019, 476 (21), pp.3281-3293. ⟨10.1042/BCJ20190488⟩
TMEM165 was highlighted in 2012 as the first member of the Uncharacterized Protein Family 0016 (UPF0016) related to human glycosylation diseases. Defects in TMEM165 are associated with strong Golgi glycosylation abnormalities. Our previous work has s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f361681ab077ff3189fa0229bef1cd80
http://hdl.handle.net/20.500.12210/34219
http://hdl.handle.net/20.500.12210/34219
Autor:
Elodie, Lebredonchel, Marine, Houdou, Sven, Potelle, Geoffroy, de Bettignies, Céline, Schulz, Marie-Ange, Krzewinski Recchi, Vladimir, Lupashin, Dominique, Legrand, André, Klein, François, Foulquier
Publikováno v:
Biochimie. 165
Since 2012, the interest for TMEM165 increased due to its implication in a rare genetic human disease named TMEM165-CDG (Congenital Disorder(s) of Glycosylation). TMEM165 is a Golgi localized protein, highly conserved through evolution and belonging
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bfe89dc61a01af11cdca1d8c20da8d6a
https://pubmed.ncbi.nlm.nih.gov/31351090
https://pubmed.ncbi.nlm.nih.gov/31351090