Zobrazeno 1 - 10
of 62
pro vyhledávání: '"Antoine Jégou"'
Autor:
Tommi Kotila, Hugo Wioland, Muniyandi Selvaraj, Konstantin Kogan, Lina Antenucci, Antoine Jégou, Juha T. Huiskonen, Guillaume Romet-Lemonne, Pekka Lappalainen
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-18 (2022)
The authors report here the structure-function analysis of highly divergent actin from Leishmania parasite. The study reveals remarkably rapid dynamics of parasite actin as well as the underlying molecular basis, thus providing insight into evolution
Externí odkaz:
https://doaj.org/article/b51e8c37b37c487a80e957a5cb198fc3
Autor:
Tommi Kotila, Hugo Wioland, Giray Enkavi, Konstantin Kogan, Ilpo Vattulainen, Antoine Jégou, Guillaume Romet-Lemonne, Pekka Lappalainen
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
The cofilin family proteins are actin disassembly factors but the disassembly mechanism is poorly understood. Here authors show that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearl
Externí odkaz:
https://doaj.org/article/a7e7c8a65f604e56a1377651d6ef54c8
Autor:
Nicolas Vignier, Maria Chatzifrangkeskou, Luca Pinton, Hugo Wioland, Thibaut Marais, Mégane Lemaitre, Caroline Le Dour, Cécile Peccate, Déborah Cardoso, Alain Schmitt, Wei Wu, Maria-Grazia Biferi, Naïra Naouar, Coline Macquart, Maud Beuvin, Valérie Decostre, Gisèle Bonne, Guillaume Romet-Lemonne, Howard J. Worman, Francesco Saverio Tedesco, Antoine Jégou, Antoine Muchir
Publikováno v:
Cell Reports, Vol 36, Iss 8, Pp 109601- (2021)
Summary: Cofilins are important for the regulation of the actin cytoskeleton, sarcomere organization, and force production. The role of cofilin-1, the non-muscle-specific isoform, in muscle function remains unclear. Mutations in LMNA encoding A-type
Externí odkaz:
https://doaj.org/article/c556bebb8808453e8abeba29fd9a8cdb
Autor:
Pierre Montaville, Antoine Jégou, Julien Pernier, Christel Compper, Bérengère Guichard, Binyam Mogessie, Melina Schuh, Guillaume Romet-Lemonne, Marie-France Carlier
Publikováno v:
PLoS Biology, Vol 12, Iss 2, p e1001795 (2014)
In mammalian oocytes, three actin binding proteins, Formin 2 (Fmn2), Spire, and profilin, synergistically organize a dynamic cytoplasmic actin meshwork that mediates translocation of the spindle toward the cortex and is required for successful fertil
Externí odkaz:
https://doaj.org/article/9860aee1054444d0928bc5248cce29f7
Autor:
Antoine Jégou, Thomas Niedermayer, József Orbán, Dominique Didry, Reinhard Lipowsky, Marie-France Carlier, Guillaume Romet-Lemonne
Publikováno v:
PLoS Biology, Vol 9, Iss 9, p e1001161 (2011)
The hydrolysis of ATP associated with actin and profilin-actin polymerization is pivotal in cell motility. It is at the origin of treadmilling of actin filaments and controls their dynamics and mechanical properties, as well as their interactions wit
Externí odkaz:
https://doaj.org/article/612c657b5a7545f7bc421a5a23e5a2bb
Autor:
Jahnavi Chikireddy, Léana Lengagne, Rémi Le Borgne, Hugo Wioland, Guillaume Romet-Lemonne, Antoine Jégou
Actin filament turnover plays a central role in shaping actin networks, yet the feedback mechanism between network architecture and filament assembly dynamics remains unclear. The activity of ADF/cofilin, the main protein family responsible for filam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4240691ea71df030b32baef0fd35d230
https://doi.org/10.1101/2023.05.19.541460
https://doi.org/10.1101/2023.05.19.541460
Autor:
Adrien Schahl, Louis Lagardère, Brandon Walker, Pengyu Ren, Antoine Jégou, Matthieu Chavent, Jean-Philip Piquemal
Depository gathering all the relevant data for the work published in the following preprint: β-actin plasticity is modulated by coordinated actions of histidine 73 methylation, nucleotide type, and ions (https://doi.org/10.1101/2022.12.16.520803) Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e6ad2a38c8830d22e3d22daad1d63b43
Autor:
Adrien Schahl, Louis Lagardere, Brandon Walker, Pengyu Ren, Antoine Jégou, Matthieu Chavent, Jean-Philip Piquemal
Actin undergoes important structural changes to transition from the G-actin to the F-actin form. Furthermore, mammals express different isoforms, with only slight variations at the amino acid level. While theα-skeletal actin isoform was thoroughly s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47437e55a40ba9e631b5ebc169967a00
https://hal.science/hal-03904639
https://hal.science/hal-03904639
Autor:
Julien Maufront, Bérengère Guichard, Lu-Yan Cao, Aurélie Di Cicco, Antoine Jégou, Guillaume Romet-Lemonne, Aurélie Bertin
The fine regulation of actin polymerization is essential to control cell motility, architecture and to perform essential cellular functions. Formins are key regulators of actin filament assembly, known to processively elongate filament barbed ends an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9f851046364c5de9624045983d0df70
https://doi.org/10.1101/2022.06.28.497909
https://doi.org/10.1101/2022.06.28.497909
Publikováno v:
Nature reviews. Molecular cell biology. 23(12)
Polymerization of actin filaments against membranes produces force for numerous cellular processes, such as migration, morphogenesis, endocytosis, phagocytosis and organelle dynamics. Consequently, aberrant actin cytoskeleton dynamics are linked to v