Browsing by Author "Fernandez-Recio, Juan"
Now showing items 1-5 of 5
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Characteritzation of protein-protein interfaces and identification of transient cavities for its modulation
Rosell, Mireia; Fernandez-Recio, Juan (Barcelona Supercomputing Center, 2015-05-05)
Conference report
Open AccessProtein-protein interactions (PPIs) play an essential role in many biological processes, including disease conditions. Strategies to modulate PPIs with small molecules have therefore attracted increasing interest over the ... -
Exploring the relationship between gene expression and topological properties of Arabidopsis thaliana interactome network.
Gimenez, Silvia M.; Rodrigo, Guillermo; Jiménez, Brian; Fernandez-Recio, Juan (Barcelona Supercomputing Center, 2017-05-04)
Conference report
Open AccessThe aim of this study is to integrate and link up transcriptomic data with biological networks approaches. The main objective was to determinate the correlation of transcriptomic profiles with PPI topology, seeking to ... -
Intrinsically active MEK variants are differentially regulated by proteinases and phosphatases
Ordan, Merav; Pallara, Chiara; Maik-Rachline, Galia; Hanoch, Tamar; Gervasio, Francesco L.; Glaser, Fabian; Fernandez-Recio, Juan; Seger, Rony (Nature Publishing Group, 2018-08-07)
Article
Open AccessMAPK/ERK kinase (MEK) 1/2 are central signaling proteins that serve as specificity determinants of the MAPK/ERK cascade. More than twenty activating mutations have been reported for MEK1/2, and many of them are known to ... -
pyDock performance in 5th CAPRI edition: from docking and scoring to binding affinity predictions and other challenges
Pallara, Chiara; Jiménez-García, Brian; Romero, Miguel; Fernandez-Recio, Juan (Barcelona Supercomputing Center, 2015-05-05)
Conference report
Open AccessProteins form the executive machinery underlying all the biological processes that occur within and between cells, from DNA replication to protein degradation. Although genome-scale technologies enable to clarify their ... -
Substrate specificity of human metallocarboxypeptidase D: Comparison of the two active carboxypeptidase domains
García-Pardo, Javier; Tanco, Sebastian; Diaz, Lucia; Dasgupta, Sayani; Fernandez-Recio, Juan; Lorenzo, Julia; Aviles, Francesc X.; Fricker, Lloyd D. (Public Library of Science, 2017-11-13)
Article
Open AccessMetallocarboxypeptidase D (CPD) is a membrane-bound component of the trans-Golgi network that cycles to the cell surface through exocytic and endocytic pathways. Unlike other members of the metallocarboxypeptidase family, ...