Related Experiment Video
Updated: Mar 31, 2026

An Improved and High Throughput Respiratory Syncytial Virus RSV Micro-neutralization Assay
Published on: January 26, 2019
RNF138 joins the HR team
Simon Bekker-Jensen1, Niels Mailand1
1Ubiquitin Signaling Group, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.
Abstract:
Two studies show that the E3 ubiquitin ligase RNF138 is recruited to DNA double-strand break sites, where it ubiquitylates key repair factors to promote DNA-end resection and homologous recombination. These findings add insights into the multilayered regulatory mechanisms underlying DNA double-strand break repair pathway choice in mammalian cells.
More Related Videos
06:10A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases
Published on: December 23, 2013
13:00A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA
Published on: December 2, 2009
Related Concept Videos
Homologous Recombination
RNA Polymerase II Accessory Proteins
RNA Polymerase II Accessory Proteins
Transcriptional Regulation: Riboswitches
Transducer Mechanism: Nuclear Receptors
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
Riboswitches
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...