Other names published for ERG11: CYP51, sterol 14-demethylase, YHR007C
ERG11 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
ERG11 - Protein Sequence Features (8)
| Reference | Other Genes Addressed |
|---|---|
| Valentine SJ, et al. (2011) Using ion mobility data to improve peptide identification: intrinsic amino acid size parameters. J Proteome Res 10(5):2318-29 | |
| Lewis DF, et al. (1999) Molecular modelling of lanosterol 14 alpha-demethylase (CYP51) from Saccharomyces cerevisiae via homology with CYP102, a unique bacterial cytochrome P450 isoform: quantitative structure-activity relationships (QSARs) within two related series of antifungal azole derivatives. J Enzyme Inhib 14(3):175-92 | |
| Boscott PE and Grant GH (1994) Modeling cytochrome P450 14 alpha demethylase (Candida albicans) from P450cam. J Mol Graph 12(3):185-92, 195 | |
| Mayuzumi H, et al. (1993) Effect of mutations of ionic amino acids of cytochrome P450 1A2 on catalytic activities toward 7-ethoxycoumarin and methanol. Biochemistry 32(21):5622-8 | |
| Tuck SF, et al. (1992) Active site topology of Saccharomyces cerevisiae lanosterol 14 alpha-demethylase (CYP51) and its G310D mutant (cytochrome P-450SG1). J Biol Chem 267(19):13175-9 | |
| Chen C, et al. (1988) Primary structure of the cytochrome P450 lanosterol 14 alpha-demethylase gene from Candida tropicalis. DNA 7(9):617-26 | |
| Ishida N, et al. (1988) A single amino acid substitution converts cytochrome P450(14DM) to an inactive form, cytochrome P450SG1: complete primary structures deduced from cloned DNAS. Biochem Biophys Res Commun 155(1):317-23 | |
| Kalb VF, et al. (1987) Primary structure of the P450 lanosterol demethylase gene from Saccharomyces cerevisiae. DNA 6(6):529-37 | |



