Motivation: Mass spectrometry-based phosphoproteomics can routinely identify and quantify thousands of phosphorylated peptides from a single experiment. However interrogating possible upstream kinases and identifying key literature for phosphorylation sites is laborious and time-consuming. Results: Here, we present Phosphomatics—a publicly available web resource for interrogating phosphoproteomics data. Phosphomatics allows researchers to upload phosphoproteomics data and interrogate possible relationships from a substrate-, kinase- or pathway-centric viewpoint.
Leeming, M., O'Callaghan, S., Licata, L., Iannuccelli, M., Lo Surdo, P., Micarelli, E., et al. (2020). Phosphomatics: interactive interrogation of substrate-kinase networks in global phosphoproteomics datasets. BIOINFORMATICS, 37(11), 1635-1636 [10.1093/bioinformatics/btaa916].
Phosphomatics: interactive interrogation of substrate-kinase networks in global phosphoproteomics datasets
Licata L;Iannuccelli M;Lo Surdo P;Micarelli E;
2020-01-01
Abstract
Motivation: Mass spectrometry-based phosphoproteomics can routinely identify and quantify thousands of phosphorylated peptides from a single experiment. However interrogating possible upstream kinases and identifying key literature for phosphorylation sites is laborious and time-consuming. Results: Here, we present Phosphomatics—a publicly available web resource for interrogating phosphoproteomics data. Phosphomatics allows researchers to upload phosphoproteomics data and interrogate possible relationships from a substrate-, kinase- or pathway-centric viewpoint.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
