Emory University (complete)
High-throughput Protein-protein Interaction Analysis for Hippo Pathway Profiling
Principal Investigator
Haian Fu, Ph.D.
Contact
Andrey Ivanov
Reference
Mo et al. (J Mol Cell Biol, 2016)
Data
The CTD2 Center at Emory University used high-throughput protein-protein interaction (PPI) mapping for Hippo signaling pathway profiling to rapidly unveil promising PPIs as potential therapeutic targets and advance functional understanding of signaling circuitry in cells.
LC-MS Analysis of PRAS40 Protein-protein Interactions
Principal Investigator
Haian Fu, Ph.D.
Contact
Andrey Ivanov
Reference
Havel et al. (Oncogene, 2015)
Data
This study focuses on subcellular localization and interactome of nuclear PRAS40 in HeLa cells.
High-throughput Protein-protein Interaction Dataset for Lung Cancer-associated Genes
Principal Investigator
Haian Fu, Ph.D.
Contact
Andrey Ivanov
Reference
Li, Ivanov, Su et al. (Nat Commun, 2017)
Data
To discover novel PPI signaling hubs for lung cancer, CTD2 Center at Emory utilized large-scale genomics datasets and literature to compile a set of lung cancer-associated genes.
A library of expression vectors were generated for these genes and utilized for detecting pairwise PPIs with cell lysate-based TR-FRET assays in high-throughput screening format.
MEDICI (Mining Essentiality Data to Identify Critical Interactions) for Cancer Drug Target Discovery and Development
Principal Investigator
Haian Fu, Ph.D.
Contact
Andrey Ivanov
Reference
Harati et al. (PLoS One, 2017)
Data
The CTD2 Center at Emory University has developed a computational methodology to combine high-throughput knockdown data with known protein network topologies to infer the importance of protein-protein interactions (PPIs) for the survival of cancer cells.
Applying these data to the Achilles shRNA results, the CCLE cell line characterizations, and known and newly identified PPIs provides novel insights for potential new drug targets for cancer therapies and identifies important PPI hubs.
Discovery of Novel MYC Protein Interactors with NanoPCA High-throughput Protein-protein Interaction Screening
Principal Investigator
Haian Fu, Ph.D.
Contact
Andrey Ivanov
Reference
Mo et al. (Mol Pharmacol, 2017)
Data
The CTD2 Center at Emory has developed a new NanoLuc®-based protein-fragment complementation assay (NanoPCA) which allows the detection of novel protein-protein interactions (PPI).
NanoPCA allows the study of PPI dynamics with reversible interactions.
mRNA-seq Analysis of Formalin-fixed, Paraffin-embedded Prostate Cancer Tissues
Principal Investigator
Haian Fu, Ph.D.
Contact
Carlos Moreno
Reference
Long, Xu et al. (Cancer Res, 2014)
Data
Global RNA sequencing was used to identify a novel panel of biomarkers for prostate cancer.
Identification of Protein-protein Interaction Inhibitors as Potential Anti-tumor Immunity Enhancers
In order to examine the functional consequences of immune response-associated potential PPI targets, the CTD2 Center at Emory University developed a high-throughput immunomodulator phenotypic (HTiP) screening platform to explore its capability in discovery of chemicals, including PPI inhibitors, as immunomodulators.
From the screening of Emory's bnriched Bioactive library, HTiP revealed IAP antagonists, a class of PPI inhibitors, as potent anti-tumor immunity enhancers.
Discovering Protein-protein Interaction (PPI) Inducers to Restore the Lost Function of a Tumor Suppressor
Principal Investigator
Haian Fu, Ph.D.
Contact
Andrey Ivanov
Reference
Tang et al. (Cell Chem Biol, 2020)
Data
In order to examine the feasibility of direct targeting loss-of-function tumor suppressor genes, the CTD2 Center at Emory University developed a high-throughput TR-FRET assay to identify mutation-directed PPI inducers to restore the tumor suppressor loss of function.
From a proof-of-concept study, the Emory team identified a small molecule, Ro-31-8220, that can induce SMAD4R361H-SMAD3 interaction and restore the lost function of SMAD4 mutation in tumor suppressive TGF-beta signaling pathway.
Discovery of the First Chemical Tools to Regulate MKK3-mediated MYC Activation in Cancer
Principal Investigator
Haian Fu, Ph.D.
Contact
Andrey Ivanov
Reference
Yang et al. (Bioorg Med Chem., 2021)
Data
The mitogen-activated protein kinase kinase 3 (MKK3) binds and activates MYC in different cell types, and disruption of MKK3-MYC protein-protein interaction may provide a new strategy to target MYC-driven programs.
However, there is no perturbagen available to interrogate and control this signaling arm.
In this study, we assessed the drugability of the MKK3-MYC complex and discovered the first chemical tools to regulate MKK3-mediated MYC activation using a high-throughput screening approach.
Systematic Discovery of Mutation-Directed Neo-Protein-Protein Interactions in Cancer
Emory CTD² team has developed a quantitative High Throughput differential Screening (qHT-dS) platform to discover mutation-directed protein-protein interactions (neoPPIs) in cancer.
Pan cancer analysis unveils widespread driver-mutation-directed gain-of-interactions, informing variant-mediated rewiring of oncogenic programs and therapeutic approaches for precision medicine.