* denotes a publication that resulted from CTD2 intra-Network collaborations
CTD2 researchers at DFCI developed CERES, a computational approach to improve the specificity of genome-wide loss-of-function CRISPR-Cas9 screens by decreasing the discovery of false-positives.
CTD2 scientists at Emory University developed the OncoPPi Portal, an interactive web resource to explore cancer-relevant protein-protein interactions that were experimentally identified in cancer cell lines.
CTD2 scientists used Project Achilles (RNAi screening) data in a community DREAM challenge (that assessed computational models focused on biomedical research problems) to predict the gene essentiality. This study provides insights into factors influencing the ability to predict gene essentiality.
CTD2 scientists at UCSF (1), Broad Institute, and TGen have identified that drug-tolerant persister cancer cells from multiple tumor types that survive chemotherapy were found to be vulnerable to chemical inhibition or genetic loss of function of GPX4.
UCSF (1) researchers identified genetic alterations that assist primary drivers, as co-drivers, that promote tumor growth and drug resistance in advanced-stage EGFR-mutant lung cancers.
CTD2 scientists at UT MD Anderson Cancer Center developed a user-friendly bioinformatic resource, The Cancer Proteome Atlas (TCPA). This resource contains the expression levels of key cancer proteins (characterized by reverse-phase protein arrays) from patient tumors and cancer cell lines.
CTD2 comprehensive molecular analysis of TCGA muscle-invasive (metastasis) bladder cases aid in subtyping and may inform optimal treatment options.
Scientists found that overexpression of PRAS40 in lung adenocarcinoma and cutaneous melanoma was associated with poor prognosis. This study describes a novel protein interaction signaling node where PRAS40 can increase NF-κB transcriptional activity through physical association with P65.
Scientists use hydrocarbon peptide stapling to develop cell permeable and stabile peptides capable of blocking RAB25-FIP complex formation. These peptides inhibit RAB25-depenent (pro- and anti-tumorigenic) phenotypes in cancer cells.