Primary Literature
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- Qiao S, et al. (2022) Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation. Nat Commun 13(1):3041 PMID: 35650207
- Fechtner L and Pfirrmann T (2021) The GID ubiquitin ligase complex just reached the next level of complexity. Mol Cell 81(11):2270-2272 PMID: 34087177
- Sherpa D, et al. (2021) GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme. Mol Cell 81(11):2445-2459.e13 PMID: 33905682
- Dong C, et al. (2020) Recognition of nonproline N-terminal residues by the Pro/N-degron pathway. Proc Natl Acad Sci U S A 117(25):14158-14167 PMID: 32513738
- Qiao S, et al. (2020) Interconversion between Anticipatory and Active GID E3\xa0Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly. Mol Cell 77(1):150-163.e9 PMID: 31708416
- Melnykov A, et al. (2019) Gid10 as an alternative N-recognin of the Pro/N-degron pathway. Proc Natl Acad Sci U S A 116(32):15914-15923 PMID: 31337681
- Oh JH, et al. (2017) A reference-based protein degradation assay without global translation inhibitors. J Biol Chem 292(52):21457-21465 PMID: 29122887
- Park EJ, et al. (2014) Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Cell Metab 20(3):448-57 PMID: 25066056
- Menssen R, et al. (2012) Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes. J Biol Chem 287(30):25602-14 PMID: 22645139
- Braun B, et al. (2011) Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation. FEBS Lett 585(24):3856-61 PMID: 22044534
- Regelmann J, et al. (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63 PMID: 12686616