ERG7/YHR072W Literature Guide Help

Other names published for ERG7: lanosterol synthase ERG7, YHR072W

ERG7 - Primary Literature (38)

Results: 1 - 30 of 38 records
   1  2 
ReferenceOther Genes Addressed
Gerstein AC  (2013) Mutational effects depend on ploidy level: all else is not equal. Biol Lett 9(1):20120614
Layer JV, et al.  (2013) Characterization of a mutation that results in independence of oxidosqualene cyclase (Erg7) activity from the downstream 3-ketoreductase (Erg27) in the yeast ergosterol biosynthetic pathway. Biochim Biophys Acta 1831(2):361-9
Chang CH, et al.  (2012) The cysteine 703 to isoleucine or histidine mutation of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae generates an iridal-type triterpenoid. Biochimie 94(11):2376-81
Gerstein AC, et al.  (2012) Parallel genetic changes and nonparallel gene-environment interactions characterize the evolution of drug resistance in yeast. Genetics 192(1):241-52
Liu YT, et al.  (2012) Protein engineering of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase into parkeol synthase. Org Lett 14(20):5222-5
Ta TM, et al.  (2012) Accumulation of squalene is associated with the clustering of lipid droplets. FEBS J 279(22):4231-44
Oliaro-Bosso S, et al.  (2011) Characterization of the channel constriction allowing the access of the substrate to the active site of yeast oxidosqualene cyclase. PLoS One 6(7):e22134
Wallace IM, et al.  (2011) Compound prioritization methods increase rates of chemical probe discovery in model organisms. Chem Biol 18(10):1273-83
Wu TK, et al.  (2011) Mutation of isoleucine 705 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae affects lanosterol's C/D-ring cyclization and 17alpha/beta-exocyclic side chain stereochemistry. Org Biomol Chem 9(4):1092-7
Joffrion TM, et al.  (2010) Functional characterization and localization of Pneumocystis carinii lanosterol synthase. Eukaryot Cell 9(1):107-15
Taramino S, et al.  (2010) Interactions of oxidosqualene cyclase (Erg7p) with 3-keto reductase (Erg27p) and other enzymes of sterol biosynthesis in yeast. Biochim Biophys Acta 1801(2):156-162
Wu TK, et al.  (2010) Alteration of the Substrate's Prefolded Conformation and Cyclization Stereochemistry of Oxidosqualene-Lanosterol Cyclase of Saccharomyces cerevisiae by Substitution at Phenylalanine 699. Org Lett 12(3):500-3
Balliano G, et al.  (2009) Oxidosqualene cyclase from Saccharomyces cerevisiae, Trypanosoma cruzi, Pneumocystis carinii and Arabidopsis thaliana expressed in yeast: a model for the development of novel antiparasitic agents. Bioorg Med Chem Lett 19(3):718-23
Endo A, et al.  (2009) Involvement of ergosterol in tolerance to vanillin, a potential inhibitor of bioethanol fermentation, in Saccharomyces cerevisiae. FEMS Microbiol Lett 299(1):95-9
Teske B, et al.  (2008) Genetic analyses involving interactions between the ergosterol biosynthetic enzymes, lanosterol synthase (Erg7p) and 3-ketoreductase (Erg27p), in the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1781(8):359-66
Wu TK, et al.  (2008) Importance of Saccharomyces cerevisiae Oxidosqualene-Lanosterol Cyclase Tyrosine 707 Residue for Chair-Boat Bicyclic Ring Formation and Deprotonation Reactions. Org Lett 10(21):4959-62
Wu TK, et al.  (2008) Protein plasticity: a single amino acid substitution in the Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase generates protosta-13(17),24-dien-3beta-ol, a rearrangement product. Org Lett 10(12):2529-32
Oliaro-Bosso S, et al.  (2007) Inhibitory effect of umbelliferone aminoalkyl derivatives on oxidosqualene cyclases from S. cerevisiae, T. cruzi, P. carinii, H. sapiens, and A. thaliana: a structure-activity study. ChemMedChem 2(2):226-33
Sawai S, et al.  (2006) Plant lanosterol synthase: divergence of the sterol and triterpene biosynthetic pathways in eukaryotes. Plant Cell Physiol 47(5):673-7
Tansakul P, et al.  (2006) Dammarenediol-II synthase, the first dedicated enzyme for ginsenoside biosynthesis, in Panax ginseng. FEBS Lett 580(22):5143-9
Wu TK, et al.  (2006) Phenylalanine 445 within Oxidosqualene-Lanosterol Cyclase from Saccharomyces cerevisiae Influences C-Ring Cyclization and Deprotonation Reactions. Org Lett 8(21):4691-4
Wu TK, et al.  (2006) Site-Saturated Mutagenesis of Histidine 234 of Saccharomyces cerevisiae Oxidosqualene-Lanosterol Cyclase Demonstrates Dual Functions in Cyclization and Rearrangement Reactions. J Am Chem Soc 128(19):6414-9
Buurman ET, et al.  (2005) Utilization of target-specific, hypersensitive strains of Saccharomyces cerevisiae to determine the mode of action of antifungal compounds. Antimicrob Agents Chemother 49(6):2558-60
Germann M, et al.  (2005) Characterizing sterol defect suppressors uncovers a novel transcriptional signaling pathway regulating zymosterol biosynthesis. J Biol Chem 280(43):35904-13
Oliaro-Bosso S, et al.  (2005) Access of the Substrate to the Active Site of Yeast Oxidosqualene Cyclase: An Inhibition and Site-Directed Mutagenesis Approach. Chembiochem 6(12):2221-2228
Lum PY, et al.  (2004) Discovering modes of action for therapeutic compounds using a genome-wide screen of yeast heterozygotes. Cell 116(1):121-37
Mullner H, et al.  (2004) Targeting of proteins involved in sterol biosynthesis to lipid particles of the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1663(1-2):9-13
Mo C, et al.  (2003) In yeast sterol biosynthesis the 3-keto reductase protein (Erg27p) is required for oxidosqualene cyclase (Erg7p) activity. Biochim Biophys Acta 1633(1):68-74
Milla P, et al.  (2002) Yeast oxidosqualene cyclase (Erg7p) is a major component of lipid particles. J Biol Chem 277(4):2406-12
Segura MJ, et al.  (2002) Directed evolution experiments reveal mutations at cycloartenol synthase residue His477 that dramatically alter catalysis. Org Lett 4(25):4459-62
Results: 1 - 30 of 38 records
   1  2