SIGNOR: a database of causal relationships between biological entities
Autor: | Elena Santonico, Daniela Posca, Filomena Spada, Luisa Castagnoli, Luana Licata, Leonardo Briganti, Gianni Cesareni, Lucia Lisa Petrilli, Alessandra Silvestri, Daniele Peluso, Andrea Cerquone Perpetuini, Marta Iannuccelli, Anna Mattioni, Milica Marinkovic, Livia Perfetto, Francesca Langone, Theodora Pavlidou, Alberto Calderone, Stefano Pirrò |
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Rok vydání: | 2015 |
Předmět: |
0301 basic medicine
SUMO protein SIGNOR cancer causal interaction pathway network Data curation Computational biology Biology 03 medical and health sciences Databases Genetics Phosphoprotein Phosphatases Humans Database Issue Databases Protein Human proteins Phosphoprotein phosphatase Internet Settore BIO/18 Protein Intracellular Signaling Peptides and Proteins Protein Kinases Signal Transduction Directed graph Signaling network Settore BIO/18 - Genetica 030104 developmental biology Signalling Protein concentration |
Zdroj: | Nucleic Acids Research |
ISSN: | 1362-4962 |
Popis: | Assembly of large biochemical networks can be achieved by confronting new cell-specific experimental data with an interaction subspace constrained by prior literature evidence. The SIGnaling Network Open Resource, SIGNOR (available on line at http://signor.uniroma2.it), was developed to support such a strategy by providing a scaffold of prior experimental evidence of causal relationships between biological entities. The core of SIGNOR is a collection of approximately 12 000 manually-annotated causal relationships between over 2800 human proteins participating in signal transduction. Other entities annotated in SIGNOR are complexes, chemicals, phenotypes and stimuli. The information captured in SIGNOR can be represented as a signed directed graph illustrating the activation/inactivation relationships between signalling entities. Each entry is associated to the post-translational modifications that cause the activation/inactivation of the target proteins. More than 4900 modified residues causing a change in protein concentration or activity have been curated and linked to the modifying enzymes (about 351 human kinases and 94 phosphatases). Additional modifications such as ubiquitinations, sumoylations, acetylations and their effect on the modified target proteins are also annotated. This wealth of structured information can support experimental approaches based on multi-parametric analysis of cell systems after physiological or pathological perturbations and to assemble large logic models. |
Databáze: | OpenAIRE |
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