ArticleExperimental & molecular medicine2016
A phosphorylation pattern-recognizing antibody specifically reacts to RNA polymerase II bound to exons.
Article in Experimental & molecular medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- TRIP13 fosters both transcriptional silencing and DSB repair during meiosis.bioRxiv : the preprint server for biology · 2025Article
- Assessment of an scFv Antibody Fragment Against ELTD1 in a G55 Glioblastoma Xenograft Model.Translational oncology · 2020Article
- Optimized monoclonal antibody treatment against ELTD1 for GBM in a G55 xenograft mouse model.Journal of cellular and molecular medicine · 2020Article
- S100A4 released from highly bone-metastatic breast cancer cells plays a critical role in osteolysis.Bone research · 2019Article
- Next-generation sequencing enables the discovery of more diverse positive clones from a phage-displayed antibody library.Experimental & molecular medicine · 2017Article
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The C-terminal domain of RNA polymerase II is an unusual series of repeated residues appended to the C-terminus of the largest subunit and serves as a flexible binding scaffold for numerous nuclear factors. The binding of these factors is determined by the phosphorylation patterns on the repeats in the domain. In this study, we generated a synthetic antibody library by replacing the third heavy chain complementarity-determining region of an anti-HER2 (human epidermal growth factor receptor 2) antibody (trastuzumab) with artificial sequences of 7-18 amino-acid residues. From this library, antibodies were selected that were specific to serine phosphopeptides that represent typical phosphorylation patterns on the functional unit (YSPTSPS)
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