Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Goran Bich"'
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
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
Publikováno v:
PDZ Mediated Interactions
PDZ Mediated Interactions, 2256, Springer US, pp.61-74, 2021, Methods in Molecular Biology, ⟨10.1007/978-1-0716-1166-1_4⟩
Methods in Molecular Biology ISBN: 9781071611654
PDZ Mediated Interactions, 2256, Springer US, pp.61-74, 2021, Methods in Molecular Biology, ⟨10.1007/978-1-0716-1166-1_4⟩
Methods in Molecular Biology ISBN: 9781071611654
The holdup assay is an automated high-throughput comparative chromatographic retention approach that allows to measure quantitative binding intensities (BI) for a large number of domain-motif pairs and deduce equilibrium binding affinity constants. W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f21a2c41d72bb7b3db778900f0eadbd
https://hal.archives-ouvertes.fr/hal-03406173
https://hal.archives-ouvertes.fr/hal-03406173
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2256
The holdup assay is an automated high-throughput comparative chromatographic retention approach that allows to measure quantitative binding intensities (BI) for a large number of domain-motif pairs and deduce equilibrium binding affinity constants. W
Autor:
Yves Nominé, Virginie Girault, Célia Caillet-Saguy, Nicolas Wolff, Renaud Vincentelli, Goran Bich, Gilles Travé, Gergő Gógl, Camille Kostmann, Pascal Eberling, Pau Jane
Publikováno v:
PLoS ONE
PLoS ONE, Public Library of Science, 2020, 15 (12), pp.e0244613. ⟨10.1371/journal.pone.0244613⟩
PLoS ONE, 2020, 15 (12), pp.e0244613. ⟨10.1371/journal.pone.0244613⟩
PLoS ONE, Vol 15, Iss 12, p e0244613 (2020)
PLoS ONE, Public Library of Science, 2020, 15 (12), pp.e0244613. ⟨10.1371/journal.pone.0244613⟩
PLoS ONE, 2020, 15 (12), pp.e0244613. ⟨10.1371/journal.pone.0244613⟩
PLoS ONE, Vol 15, Iss 12, p e0244613 (2020)
International audience; 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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7eeb75649b819ef18e1dc11403dd703
https://hal.archives-ouvertes.fr/hal-03099990
https://hal.archives-ouvertes.fr/hal-03099990
Autor:
Camille Kostmann, Gergo Gogl, Renaud Vincentelli, Nikolai N. Sluchanko, Célia Caillet-Saguy, Goran Bich, Nicolas Wolff, László Nyitray, Yves Nominé, Gilles Travé, Pau Jane, Alexandra Cousido-Siah
Publikováno v:
Structure
Structure, 2020, 28 (7), pp.747. ⟨10.1016/j.str.2020.03.010⟩
Structure, Elsevier (Cell Press), 2020, ⟨10.1016/j.str.2020.03.010⟩
Structure, 2020, 28 (7), pp.747. ⟨10.1016/j.str.2020.03.010⟩
Structure, Elsevier (Cell Press), 2020, ⟨10.1016/j.str.2020.03.010⟩
International audience; Protein-protein interaction motifs are often alterable by post-translational modifications. For example, 19% of predicted human PDZ domain-binding motifs (PBMs) have been experimentally proven to be phosphorylated, and up to 8
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fd03d011e663acf98c2a5544f37e1fb
https://hal.science/hal-02545805/document
https://hal.science/hal-02545805/document