ArticleProteomics2011
Identifying transient protein-protein interactions in EphB2 signaling by blue native PAGE and mass spectrometry.
Article in Proteomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 91 citations in OpenAlex.
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- A Proteomic Glance at the Bovine Intervertebral Disc.Advances in experimental medicine and biology · 2026Review
- Mass Spectrometry for Proteomics-Based Investigation.Advances in experimental medicine and biology · 2026Review
- Sarcomeric tropomyosin expression during human iPSC differentiation into cardiomyocytes.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Methods to Investigate the Secretome of Senescent Cells.Methods and protocols · 2024Review
- Complex effects of the exo-xis region of the Shiga toxin-converting bacteriophage Φ24Journal of applied genetics · 2024Article
- Contribution of Nischarin/IRAS in CNS development, injury and diseases.Journal of advanced research · 2023Review
- A Proteomics Investigation of Salivary Profiles as Potential Biomarkers for Autism Spectrum Disorder (ASD).The protein journal · 2023Article
- Proteomics Analysis of Lymphoblastoid Cell Lines from Patients with Amyotrophic Lateral Sclerosis.Molecules (Basel, Switzerland) · 2023Article
- Article
- Tropomyosin Isoform Diversity in the Cynomolgus Monkey Heart and Skeletal Muscles Compared to Human Tissues.Biochemistry research international · 2023Article
- Characterizing Transient Protein-Protein Interactions by Trp-Cys Quenching and Computer Simulations.The journal of physical chemistry letters · 2022Article
- Investigation of the effects of overexpression of jumping translocation breakpoint (JTB) protein in MCF7 cells for potential use as a biomarker in breast cancer.American journal of cancer research · 2022Article
- Investigation of the effects of downregulation of jumping translocation breakpoint (JTB) protein expression in MCF7 cells for potential use as a biomarker in breast cancer.American journal of cancer research · 2022Article
- House dust mite sensitization drives cross-reactive immune responses to homologous helminth proteins.PLoS pathogens · 2021Article
- Proteomic Analysis Identifies Dysregulated Proteins in Butanol-Tolerant Gram-PositiveACS omega · 2021Article
- Identification of a novel TPM4 isoform transcript and comparison to the expression of other tropomyosin isoforms in bovine cardiac and skeletal muscles.International journal of biochemistry and molecular biology · 2021Article
- Exploring dynamic protein-protein interactions in cassava through the integrative interactome network.Scientific reports · 2020Article
- Lactoferrin translocates to the nucleus of bovine rectal epithelial cells in the presence of Escherichia coli O157:H7.Veterinary research · 2019Article
- Qualitative and quantitative evaluation of TPM transcripts and proteins in developing striated chicken muscles indicate TPM4α is the major sarcomeric cardiac tropomyosin from early embryonic life to adulthood.Cytoskeleton (Hoboken, N.J.) · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Receptor tyrosine kinases (RTKs) are proteins that upon ligand stimulation undergo dimerization and autophosphorylation. Eph receptors (EphRs) are RTKs that are found in different cell types, from both tissues that are developing and from mature tissues, and play important roles in the development of the central nervous system and peripheral nervous system. EphRs also play roles in synapse formation, neural crest formation, angiogenesis and in remodeling the vascular system. Interaction of EphRs with their ephrin ligands lead to activation of signal transduction pathways and formation of many transient protein-protein interactions that ultimately leads to cytoskeletal remodeling. However, the sequence of events at the molecular level is not well understood. We used blue native PAGE and MS to analyze the transient protein-protein interactions that resulted from the stimulation of EphB2 receptors by their ephrinB1-Fc ligands. We analyzed the phosphotyrosine-containing protein complexes immunoprecipitated from the cell lysates of both unstimulated (-) and ephrinB1-Fc-stimulated (+) NG108 cells. Our experiments allowed us to identify many signaling proteins, either known to be part of EphB2 signaling or new for this pathway, which are involved in transient protein-protein interactions upon ephrinB1-Fc stimulation. These data led us to investigate the roles of proteins such as FAK, WAVEs and Nischarin in EphB2 signaling.
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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.