ArticleBiochemistry2010
Structure-activity relationship analysis of peptides targeting the EphA2 receptor.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed, 60 citations in OpenAlex.
- EPHA2 Receptor as a Possible Therapeutic Target in Viral Infections.Current medicinal chemistry · 2024Review
- A computational and laboratory approach for the investigation of interactions of peptide conjugated natural terpenes with EpHA2 receptor.Journal of molecular modeling · 2023Article
- Targefrin: A Potent Agent Targeting the Ligand Binding Domain of EphA2.Journal of medicinal chemistry · 2022Article
- Hunting for Novel Routes in Anticancer Drug Discovery: Peptides against Sam-Sam Interactions.International journal of molecular sciences · 2022Review
- Effective Tumor Targeting by EphA2-Agonist-Biotin-Streptavidin Conjugates.Molecules (Basel, Switzerland) · 2021Article
- RETRACTED: Prostate Cancer Metastases Are Strongly Inhibited by Agonistic Epha2 Ligands in an Orthotopic Mouse Model.Cancers · 2020Article
- The EphA2 and cancer connection: potential for immune-based interventions.Molecular biology reports · 2020Review
- Therapeutic Targeting of Pancreatic Cancer via EphA2 Dimeric Agonistic Agents.Pharmaceuticals (Basel, Switzerland) · 2020Article
- Engineering nanomolar peptide ligands that differentially modulate EphA2 receptor signaling.The Journal of biological chemistry · 2019Article
- Pinpointed Stimulation of EphA2 Receptors via DNA-Templated Oligovalence.International journal of molecular sciences · 2018Article
- Structure-Based Design of Novel EphA2 Agonistic Agents with Nanomolar Affinity in Vitro and in Cell.ACS chemical biology · 2018Article
- Reduction of Circulating Cancer Cells and Metastases in Breast-Cancer Models by a Potent EphA2-Agonistic Peptide-Drug Conjugate.Journal of medicinal chemistry · 2018Article
- Targeted delivery of YSA-functionalized and non-functionalized polymeric nanoparticles to injured pulmonary vasculature.Artificial cells, nanomedicine, and biotechnology · 2018Article
- The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures.Communications biology · 2018Article
- Article
- Secondary nuclear targeting of mesoporous silica nano-particles for cancer-specific drug delivery based on charge inversion.Oncotarget · 2016Article
- Protein kinase A can block EphA2 receptor-mediated cell repulsion by increasing EphA2 S897 phosphorylation.Molecular biology of the cell · 2016Article
- A small peptide promotes EphA2 kinase-dependent signaling by stabilizing EphA2 dimers.Biochimica et biophysica acta · 2016Article
- Comparative Analysis of Virtual Screening Approaches in the Search for Novel EphA2 Receptor Antagonists.Molecules (Basel, Switzerland) · 2015Article
- Design and Characterization of Novel EphA2 Agonists for Targeted Delivery of Chemotherapy to Cancer Cells.Chemistry & biology · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The EphA2 receptor tyrosine kinase has emerged as a promising new therapeutic target in cancer because of its high level of expression in tumors. EphA2-specific antibodies have been used to deliver drugs and toxins to tumor cells, leading to inhibition of tumor growth and metastatic dissemination. We previously identified two related peptides, YSA and SWL, that selectively bind to the ligand-binding domain of EphA2 but not other Eph receptors and could therefore be useful as selective targeting agents. Here we characterize the two peptides and a series of derivatives. On the basis of systematic amino acid replacements, only five YSA residues appear to be critical for high-affinity receptor binding. Furthermore, a peptide comprising only the first five residues of YSA retains selectivity for EphA2. Similar to ephrin-A1, the physiological ligand for EphA2, both YSA and SWL activate EphA2 and inhibit downstream oncogenic signaling pathways in PC3 cancer cells. The two peptides and derivatives are quite stable in conditioned cell culture medium and show promise for delivering drugs and imaging agents to EphA2-expressing tumors.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.