Name | ERG2 |
---|---|
Synonyms | ERG; P55; ERG1; ERG 2; ERG2; ERG/EWS fusion gene; ERG/FUS fusion gene; Erg 3… |
Name | tridemorph |
---|---|
CAS | tridemorph |
PubMed | Abstract | RScore(About this table) | |
---|---|---|---|
12133002 | Nes WD, Zhou W, Dennis AL, Li H, Jia Z, Keith RA, Piser TM, Furlong ST: Purification, characterization and catalytic properties of human sterol 8-isomerase. Biochem J. 2002 Nov 1;367(Pt 3):587-99. The resulting native protein was overexpressed in erg 2 yeast cells and purified to apparent homogeneity. |
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 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. Tests with a panel of fungicides indicated that pML100 conferred significant resistance only to compounds (Fp, tridemorph, fenpropidin and azasterol) which have a shared site of action, Erg24p. |
biosynthesis pathway. Gene. 1994 Mar 11;140(1):41-9.1(0,0,0,1) | Details |
15638242 | Valachovic M, Wilcox LI, Sturley SL, Bard M: A mutation in sphingolipid synthesis suppresses defects in yeast metabolism. Lipids. 2004 Aug;39(8):747-52. A mutation in an otherwise nonessential ERG2 gene is synthetically lethal when combined with mutations in two transcription factors encoded by the UPC2 and ECM22 genes. In an expression study on tridemorph-containing medium, using the inducible GAL1 promoter fused to the ELO3 open reading frame, we demonstrated that suppression occurred only when ELO3 was not expressed. |
1(0,0,0,1) | Details |
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 (Ki = 0.05 nM), tridemorph (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. |
33(0,1,1,3) | Details |
8082205 | Keon JP, James CS, Court S, Baden-Daintree C, Bailey AM, Burden RS, Bard M, Hargreaves JA: Isolation of the ERG2 gene, encoding sterol delta 8--> delta 7 isomerase, from the rice blast fungus Magnaporthe grisea and its expression in the maize smut pathogen Ustilago maydis. Curr Genet. 1994 Jun;25(6):531-7. The delta 8--> delta 7 sterol isomerase produced by the M. grisea ERG2 gene exhibited a level of sensitivity to the sterol biosynthesis inhibitor, tridemorph, similar to that of the enzyme derived from the U. maydis ERG2 gene. |
85(1,1,1,5) | Details |