Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation

The ubiquitin clan: A protein family essential for life

(2011) Dieter H. Wolf   FEBS LETTERS

Cdc48: a power machine in protein degradation

(2011) Alexandra Stolz et al.   TRENDS IN BIOCHEMICAL SCIENCES

The Cdc48–Ufd1–Npl4 complex is central in ubiquitin–proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase

(2010) Lise Barbin et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

The Hsp70 chaperone Ssa1 is essential for catabolite induced degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase

(2010) Jeannette Juretschke et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

RING Domain E3 Ubiquitin Ligases

(2009) Raymond J. Deshaies et al.   Annual Review of Biochemistry

The Vacuole Import and Degradation Pathway Utilizes Early Steps of Endocytosis and Actin Polymerization to Deliver Cargo Proteins to the Vacuole for Degradation

(2009) C. Randell Brown et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Structures of the cIAP2 RING Domain Reveal Conformational Changes Associated with Ubiquitin-conjugating Enzyme (E2) Recruitment

(2008) Peter D. Mace et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Polyubiquitylation of Histone H2B

(2008) Fuqiang Geng et al.   MOLECULAR BIOLOGY OF THE CELL

The Yeast GID Complex, a Novel Ubiquitin Ligase (E3) Involved in the Regulation of Carbohydrate Metabolism

(2008) Olivier Santt et al.   MOLECULAR BIOLOGY OF THE CELL