Zobrazeno 1 - 10
of 93
pro vyhledávání: '"Gilles, Travé"'
Autor:
Gergo Gogl, Boglarka Zambo, Camille Kostmann, Alexandra Cousido-Siah, Bastien Morlet, Fabien Durbesson, Luc Negroni, Pascal Eberling, Pau Jané, Yves Nominé, Andras Zeke, Søren Østergaard, Élodie Monsellier, Renaud Vincentelli, Gilles Travé
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-7 (2022)
Externí odkaz:
https://doaj.org/article/dff796c0f95b474fb39f559dd5885404
Autor:
Gergo Gogl, Boglarka Zambo, Camille Kostmann, Alexandra Cousido-Siah, Bastien Morlet, Fabien Durbesson, Luc Negroni, Pascal Eberling, Pau Jané, Yves Nominé, Andras Zeke, Søren Østergaard, Élodie Monsellier, Renaud Vincentelli, Gilles Travé
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-18 (2022)
Protein networks have been widely explored but most binding affinities remain unknown, limiting the quantitative interpretation of interactomes. Here the authors measure affinities of 65,000 interactions involving human PDZ domains and target sequenc
Externí odkaz:
https://doaj.org/article/2abf01b5330741a686c599e55cea0dee
Autor:
Márton A. Simon, Éva Bartus, Beáta Mag, Eszter Boros, Lea Roszjár, Gergő Gógl, Gilles Travé, Tamás A. Martinek, László Nyitray
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-11 (2022)
Abstract S100 proteins are small, typically homodimeric, vertebrate-specific EF-hand proteins that establish Ca2+-dependent protein–protein interactions in the intra- and extracellular environment and are overexpressed in various pathologies. There
Externí odkaz:
https://doaj.org/article/f6b5fe266e7147c194ea5da698e147da
Autor:
Monica Castro-Cruz, Frédérique Lembo, Jean-Paul Borg, Gilles Travé, Renaud Vincentelli, Pascale Zimmermann
Publikováno v:
Membranes, Vol 13, Iss 8, p 737 (2023)
PSD95-disc large-zonula occludens (PDZ) domains are globular modules of 80–90 amino acids that co-evolved with multicellularity. They commonly bind to carboxy-terminal sequences of a plethora of membrane-associated proteins and influence their traf
Externí odkaz:
https://doaj.org/article/2bb4023ef6f74d009e669a65338f2c4d
Autor:
Pau Jané, Gergő Gógl, Camille Kostmann, Goran Bich, Virginie Girault, Célia Caillet-Saguy, Pascal Eberling, Renaud Vincentelli, Nicolas Wolff, Gilles Travé, Yves Nominé
Publikováno v:
PLoS ONE, Vol 15, Iss 12, p e0244613 (2020)
Protein domains often recognize short linear protein motifs composed of a core conserved consensus sequence surrounded by less critical, modulatory positions. PTEN, a lipid phosphatase involved in phosphatidylinositol 3-kinase (PI3K) pathway, contain
Externí odkaz:
https://doaj.org/article/7bab4add76df4cae8c81a28d0fb5edf1
Autor:
Anna Bonhoure, Auguste Demenge, Camille Kostmann, Leticia San José, Eva De la Cal, Pilar Armisen, Yves Nominé, Gilles Travé
Publikováno v:
Microbial Cell Factories, Vol 17, Iss 1, Pp 1-14 (2018)
Abstract Background Bacterial expression and purification of recombinant proteins under homogeneous active form is often challenging. Fusion to highly soluble carrier proteins such as Maltose Binding Protein (MBP) often improves their folding and sol
Externí odkaz:
https://doaj.org/article/d61863bc3d74444badf6851c8591d32f
Autor:
Hanne Hollås, Juan Ramirez, Yves Nominé, Camille Kostmann, Angelo Toto, Stefano Gianni, Gilles Travé, Anni Vedeler
Publikováno v:
Biophysical Journal
Annexins (Anxs) are a family of highly homologous proteins that bind and aggregate lipid vesicles in the presence of calcium. All members of the family contain a variable N-terminus determining specific functions, followed by a conserved core region
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46a80e0ed9c3719dcd487037cd2ffd65
https://doi.org/10.1016/j.bpj.2022.10.043
https://doi.org/10.1016/j.bpj.2022.10.043
Publikováno v:
Bioinformatics Advances. 3
Motivation Studies of sets of proteins are a central point in biology. In particular, the application of omics in the last decades has generated lists of several hundreds or thousands of proteins or genes. However, these lists are often not inspected
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::078b10cedcd31d80c8e32a35a99c4fa0
https://doi.org/10.1093/bioadv/vbad022
https://doi.org/10.1093/bioadv/vbad022
Autor:
François Delalande, Gergo Gogl, Aurélien Rohrbacher, Camille Kostmann, Pascal Eberling, Christine Carapito, Gilles Travé, Elodie Monsellier
The accurate description and subsequent modeling of protein interactomes requires quantification of their affinities at proteome-wide scale. Here we develop and validate the Holdup Multiplex, a versatile assay for high-throughput measurement of prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::041ea022aed1350e2429a857dd54ca85
https://doi.org/10.1101/2022.12.08.519103
https://doi.org/10.1101/2022.12.08.519103
Autor:
Valentin Bauer, Yves Nominé, Natacha Rochel, Jozica Dolenc, Gergő Gógl, Vladimir Yu. Torbeev, Gilles Travé, Andre Mitschler, Boris Schmidtgall, Judit Osz, Alexandra Cousido-Siah, Camille Kostmann, Bruno Kieffer
Publikováno v:
Chemical Science
Chemical Science, The Royal Society of Chemistry, 2021, 12 (3), pp.1080-1089. ⟨10.1039/d0sc04482b⟩
Chemical Science, 2021, 12 (3), pp.1080-1089. ⟨10.1039/D0SC04482B⟩
Chemical Science, 12 (3)
Chemical Science, The Royal Society of Chemistry, 2021, 12 (3), pp.1080-1089. ⟨10.1039/d0sc04482b⟩
Chemical Science, 2021, 12 (3), pp.1080-1089. ⟨10.1039/D0SC04482B⟩
Chemical Science, 12 (3)
Intrinsically disordered proteins (IDPs) constitute a large portion of “Dark Proteome” – difficult to characterize or yet to be discovered protein structures. Here we used conformationally constrained α-methylated amino acids to bias the confo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d6d58921d1aed4d1ea9ab820be41c3d
https://doi.org/10.1039/d0sc04482b
https://doi.org/10.1039/d0sc04482b