Other names published for PEP4: PHO9, PRA1, yscA, YPL154C
PEP4 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
PEP4 - Protein-protein Interactions (7)
| Reference | Other Genes Addressed |
|---|---|
| Nevzglyadova OV, et al. (2009) Prion-associated proteins in yeast: comparative analysis of isogenic [PSI(+)] and [psi(-)] strains. Yeast 26(11):611-31 | |
| Padron-Garcia JA, et al. (2009) Quantitative structure activity relationship of IA3-like peptides as aspartic proteinase inhibitors. Proteins 75(4):859-69 | |
| Narayanan R, et al. (2008) Kinetics of Folding and Binding of an Intrinsically Disordered Protein: The Inhibitor of Yeast Aspartic Proteinase YPrA. J Am Chem Soc 130(34):11477-85 | |
| Ganesh OK, et al. (2006) Characterizing the residue level folding of the intrinsically unstructured IA3. Biochemistry 45(45):13585-96 | |
| Green TB, et al. (2004) IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution. Biochemistry 43(14):4071-81 | |
| Badasso MO, et al. (2000) Purification, co-crystallization and preliminary X--ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae. Acta Crystallogr D Biol Crystallogr 56(Pt 7):915-7 | |
| Li M, et al. (2000) The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. Nat Struct Biol 7(2):113-7 |



