| Name | ERG2 |
|---|---|
| Synonyms | ERG; P55; ERG1; ERG 2; ERG2; ERG/EWS fusion gene; ERG/FUS fusion gene; Erg 3… |
| Name | fenpropimorph |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 8988026 | Moebius FF, Bermoser K, Reiter RJ, Hanner M, Glossmann H: Yeast sterol C8-C7 isomerase: identification and characterization of a high-affinity binding site for enzyme inhibitors. Biochemistry. 1996 Dec 24;35(51):16871-8. Indeed the sigma ligands [3H] haloperidol (Kd = 0.3 nM) and [3H] ifenprodil (Kd = 1.4 nM) bound to a single population of sites in ERG2 wild type yeast microsomes (Bmax values of 77 and 61 pmol/mg of protein, respectively), whereas binding activity was absent in strains carrying ERG2 gene mutations or disruptions. [3H] Ifenprodil binding was inhibited by sterol isomerase inhibitors such as fenpropimorph (Ki = 0.05 nM), (Ki = 0.09 nM), MDL28,815 (Ki = 0.44 nM), triparanol (Ki = 1.5 nM), and AY-9944 (Ki = 5.8 nM). [3H] Haloperidol specifically photoaffinity-labeled a protein with an apparent molecular weight of 27400, in agreement with the molecular mass of the sterol C8-C7 isomerase (24900 Da). 9E10 c-myc antibodies specifically immunoprecipitated the c-myc tagged protein after [3H] haloperidol photolabeling, unequivocally proving that the drug binding site is localized on the ERG2 gene product. |
83(1,1,1,3) | Details |
| 10734216 | Soustre I, Dupuy PH, Silve S, Karst F, Loison G: Sterol metabolism and ERG2 gene regulation in the yeast Saccharomyces cerevisiae. FEBS Lett. 2000 Mar 24;470(2):102-6. |
4(0,0,0,4) | Details |
| 9146879 | Moebius FF, Reiter RJ, Hanner M, Glossmann H: High affinity of sigma 1-binding sites for sterol isomerization inhibitors: evidence for a pharmacological relationship with the yeast sterol C8-C7 isomerase. Br J Pharmacol. 1997 May;121(1):1-6. The sigma-drug binding site of guinea-pig liver is carried by a protein which shares significant amino acid sequence similarities with the yeast sterol C8-C7 isomerase (ERG2 protein). Among the compounds which bound with high affinity to native hepatic and cerebral as well as to yeast expressed sigma 1-binding sites were the agricultural fungicide fenpropimorph (Ki 0.005 nM), the antihypocholesterinaemic drugs triparanol (Ki 7.0 nM), AY-9944 (Ki, 0.46 nM) and MDL28,815 (Ki 0.16 nM), the enantiomers of the ovulation inducer clomiphene (Ki 5.5 and 12 nM, respectively) and the antioestrogene tamoxifen (Ki 26 nM). 3. |
1(0,0,0,1) | Details |
| 8125337 | Lai MH, Bard M, Pierson CA, Alexander JF, Goebl M, Carter GT, Kirsch DR: The identification of a gene family in the Saccharomyces cerevisiae biosynthesis pathway. Gene. 1994 Mar 11;140(1):41-9. The Saccharomyces cerevisiae ERG24 gene, encoding sterol delta 14 reductase (Erg24p), was cloned by selecting strains carrying sequences on a 2 mu-based vector for resistance to the morpholine fungicide, fenpropimorph (Fp). Although Fp is reported to inhibit activity of Erg24p and sterol delta 8-delta 7 isomerase (Erg2p; encoded by ERG2), none of the inserts had restriction maps resembling ERG2. |
1(0,0,0,1) | Details |
| 12384361 | Smith WL, Edlind TD: Histone deacetylase inhibitors enhance Candida albicans sensitivity to azoles and related antifungals: correlation with reduction in CDR and ERG upregulation. Antimicrob Agents Chemother. 2002 Nov;46(11):3532-9. Both antifungals induced to various levels the expression of ERG1, ERG11, CDR1, and CDR2; addition of TSA reduced this upregulation 50 to 100%. Similar effects were observed with other HDA inhibitors and with the antifungals terbinafine and fenpropimorph, which target, as do azoles, enzymes in the biosynthetic pathway. |
1(0,0,0,1) | Details |
| 7988864 | Kelly DE, Rose ME, Kelly SL: Investigation of the role of sterol delta 8--> 7-isomerase in the sensitivity of Saccharomyces cerevisiae to fenpropimorph. FEMS Microbiol Lett. 1994 Oct 1;122(3):223-6. |
0(0,0,0,0) | Details |