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GenomicsEphA2 receptor is a key player in the metastatic onset of Ewing sarcoma
EphA2 receptor is a key player in the metastatic onset of Ewing sarcoma
PRJNA417000 | ENA
ProteomicsAllosteric Regulation of the EphA2 Receptor Intracellular Region by Serine/Threonine Kinases
HDX-MS analysis of the intracellular portion (residues 570-976) of the human EphA2 receptor tyrosine kinase. WT and 5 mutants (S892E, S897E, T898E/S899E/S901E, S892E/S897E/T898E/S899E/S901E and E820K/E825K) were compared.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-01-04 | MSV000086658 | MassIVE
ProteomicsEphA2 regulates vascular permeability and prostate cancer metastasis via modulation of cell junction protein phosphorylation
Prostate cancer morbidity and mortality obviate a need for more effective targeted therapies. One potential target is EphA2, although paradoxically, pro- and anti-oncogenic effects have been shown to be mediated by EphA2. We demonstrate that unique activating and blocking EphA2-targeting monoclonal ...
ORGANISM(S): Homo sapiens (Human) 
2024-11-11 | PXD053835 | Pride
Afadin Shb Phosphoproteomics Epha2 Silac Eph receptor 
GenomicsEffect of Ephrin-A5 DNA Nanocalipers stimulation of EphA2 receptor signaling in U3013 cell line
Effect of Ephrin-A5 DNA Nanocalipers stimulation of EphA2 receptor signaling in U3013 cell line
PRJNA576597 | ENA
ProteomicsDefining the landscape of EPHA2 Inhibition by Clinical Kinase Inhibitors
The receptor tyrosine kinase EPHA2 plays important roles in oncogenesis, metastasis and treatment resistance but therapeutic targeting, drug discovery or investigation of EPHA2 biology is hampered by the lack of appropriate inhibitors and structural information on how these interact with the protein...
ORGANISM(S): Homo sapiens (Human) 
2016-12-23 | PXD004112 | Pride
Epha2 co-crystals Selectivity profiling Chemical proteomics Residue categorization Drug protein interactions 
ProteomicsDiscovery of dedicated EPHA2 inhibitors - Medicinal chemistry meets chemical proteomics
The receptor tyrosine kinase EPHA2 has gained interest as therapeutical drug target in cancer and infectious diseases in the past years. However, EPHA2 research and EPHA2 based therapies have been hampered by the lack of selective small molecule EPHA2 inhibitors. We report on the synthesis and evalu...
ORGANISM(S): Homo sapiens (Human) 
2017-05-30 | PXD006193 | Pride
Eph receptor Drug discovery Selectivity profiling Inhibitors Chemical proteomics 
ProteomicsProteomics uncover EPHA2 in cetuximab resistant colorectal cancer cell lines as a potential novel therapeutic target
In metastatic colorectal cancer (mCRC), primary and acquired resistance against anti-EGFR targeted monoclonal antibodies, such as cetuximab (CET), were shown to be frequently caused by activating alterations in RAS genes (KRAS or NRAS). To this day no efficient second-line treatment options have eme...
ORGANISM(S): Homo sapiens (Human) 
2023-03-10 | PXD022072 | Pride
Epha2 Cetuximab resistance Proteomics 
TranscriptomicsEphA2 receptor is a key player in the metastatic onset of Ewing sarcoma
Ewing sarcoma (ES) is the second most common bone malignancy affecting children and young adults with poor prognosis due to high metastasis incidence. Our group previously described that EphA2, a tyrosine kinase receptor, promotes angiogenesis in ES cells via ligand-dependent signaling. EphA2 ligand...
ORGANISM(S): Homo sapiens 
2018-04-11 | GSE106480 | GEO
OtherChemical proteomics uncovers EPHA2 as a mechanism of acquired resistance to small molecule EGFR kinase inhibition.
Data from ProteomeXchange, PXD ID: PXD001333. File: 000249_D01_P001442_B00_A00_R1.mzml. Published as part of J Proteome Res. 2015 May 12 . From the Abstract: {{i}} ... Here, we describe a chemical proteomic approach comprising kinase affinity purification (kinobeads) and quantitative mass spectrome...
ORGANISM(S): Homo_sapiens_viruses, Human_female 
GPM32310019962 | GPMDB
Resource Reanalysis 
UnknownProtein kinase A can block EphA2 receptor-mediated cell repulsion by increasing EphA2 S897 phosphorylation.
Not available
S-EPMC5007095 | biostudies-literature
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