RMD5/YDR255C Literature Guide Help

Other names published for RMD5: GID2, ubiquitin-protein ligase RMD5, YDR255C

RMD5 - Mutants/Phenotypes (10)

ReferenceOther Genes Addressed
Theodoraki MA, et al.  (2012) A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast. J Biol Chem 287(28):23911-22
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
Piggott N, et al.  (2011) Genome-wide Fitness Profiles Reveal a Requirement for Autophagy During Yeast Fermentation. G3 (Bethesda) 1(5):353-67
Santt O, et al.  (2008) The Yeast GID Complex, a Novel Ubiquitin Ligase (E3) Involved in the Regulation of Carbohydrate Metabolism. Mol Biol Cell 19(8):3323-33
Snowdon C, et al.  (2008) Components of the Vid30c are needed for the rapamycin-induced degradation of the high-affinity hexose transporter Hxt7p in Saccharomyces cerevisiae. FEMS Yeast Res 8(2):204-16
Pitre S, et al.  (2006) PIPE: a protein-protein interaction prediction engine based on the re-occurring short polypeptide sequences between known interacting protein pairs. BMC Bioinformatics 7():365
Hung GC, et al.  (2004) Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. J Biol Chem 279(47):49138-50
Enyenihi AH and Saunders WS  (2003) Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics 163(1):47-54
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
Hammerle M, et al.  (1998) Proteins of newly isolated mutants and the amino-terminal proline are essential for ubiquitin-proteasome-catalyzed catabolite degradation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. J Biol Chem 273(39):25000-5