![Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation | Nature Communications Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation | Nature Communications](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs41467-022-30803-9/MediaObjects/41467_2022_30803_Fig1_HTML.png)
Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation | Nature Communications
GitHub - KratosMultiphysics/GiDInterface: The graphical user interface of Kratos for GiD. Featuring CFD, CSM, DEM, PFEM, etc
![The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation | eLife The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation | eLife](https://iiif.elifesciences.org/lax/35528%2Felife-35528-fig1-v2.tif/full/1500,/0/default.jpg)