ArticleJournal of proteome research2006
Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC).
Article in Journal of proteome research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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.
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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.
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Who cites it
27 citing papers in PubMed, 76 citations in OpenAlex.
- Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) for Quantitative Proteomics.Advances in experimental medicine and biology · 2026Review
- Mass Spectrometry-Based Identification of Post-Translational Modifications (PTMs) of Proteins.Advances in experimental medicine and biology · 2026Article
- Mass Spectrometry for Proteomics-Based Investigation.Advances in experimental medicine and biology · 2026Review
- Atrial electrophysiological and molecular remodelling induced by obstructive sleep apnoea.Journal of cellular and molecular medicine · 2017Article
- Sphingosine kinase 1 isoform-specific interactions in breast cancer.Molecular endocrinology (Baltimore, Md.) · 2014Article
- A functional approach to uncover the low-temperature adaptation strategies of the archaeon Methanosarcina barkeri.Applied and environmental microbiology · 2013Article
- A quantitative proteomic analysis uncovers the relevance of CUL3 in bladder cancer aggressiveness.PloS one · 2013Article
- Quantitative proteomics with siRNA screening identifies novel mechanisms of trastuzumab resistance in HER2 amplified breast cancers.Molecular & cellular proteomics : MCP · 2013Article
- TSLP signaling network revealed by SILAC-based phosphoproteomics.Molecular & cellular proteomics : MCP · 2012Article
- Label-free quantitation of protein modifications by pseudo selected reaction monitoring with internal reference peptides.Journal of proteome research · 2012Article
- Eph/ephrin signaling: genetic, phosphoproteomic, and transcriptomic approaches.Seminars in cell & developmental biology · 2012Review
- Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling.Journal of proteome research · 2011Article
- Identifying transient protein-protein interactions in EphB2 signaling by blue native PAGE and mass spectrometry.Proteomics · 2011Article
- Phosphoproteomics in cancer.Molecular oncology · 2010Review
- Article
- Ephrin-B1 forward signaling regulates craniofacial morphogenesis by controlling cell proliferation across Eph-ephrin boundaries.Genes & development · 2010Article
- Hyperglycemia alters the schwann cell mitochondrial proteome and decreases coupled respiration in the absence of superoxide production.Journal of proteome research · 2010Article
- Evaluation of the variation in sample preparation for comparative proteomics using stable isotope labeling by amino acids in cell culture.Journal of proteome research · 2009Article
- Use of stable isotope labeling by amino acids in cell culture (SILAC) for phosphotyrosine protein identification and quantitation.Methods in molecular biology (Clifton, N.J.) · 2009Review
- Quantitative proteomic profiling of host-pathogen interactions: the macrophage response to Mycobacterium tuberculosis lipids.Journal of proteome research · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Eph-related receptor tyrosine kinases (RTK) have been implicated in several biological functions including synaptic plasticity, axon guidance, and morphogenesis, yet the details of the signal transduction pathways that produce these specific biological functions after ligand-receptor interaction remain unclear. We used Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) in combination with LC-MS/MS to characterize cellular signaling following stimulation by ephrinB1-Fc of NG-108 cells that overexpress EphB2 receptors. Because tyrosine phosphorylation functions as a key regulatory event in RTK signaling, we used anti-phosphotyrosine immunoprecipitation (pY IP) of cell lysates to isolate potential participants in the EphB2 pathway. Our SILAC experiments identified 127 unique proteins, 40 of which demonstrated increased abundance in pY IPs from ephrinB1-Fc stimulated cells as compared with unstimulated cells. Six proteins demonstrated decreased abundance, and 81 did not change significantly in relative abundance. Western blotting analysis of five proteins after pY IP verified their SILAC results. On the basis of previously published work and use of PathwayAssist software, we proposed an interaction network downstream of EphB2 for the proteins with changed ratios.
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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.