FBA1/YKL060C Literature Guide Help

Other names published for FBA1: LOT1, fructose-bisphosphate aldolase FBA1, YKL060C

FBA1 - Primary Literature (27)

ReferenceOther Genes Addressed
Bang SY, et al.  (2013) Candidate target genes for the Saccharomyces cerevisiae transcription factor, Yap2. Folia Microbiol (Praha) ()
Foyn H, et al.  (2013) Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo. Mol Cell Proteomics 12(1):42-54
Miura N, et al.  (2012) Tracing putative trafficking of the glycolytic enzyme enolase via SNARE-driven unconventional secretion. Eukaryot Cell 11(8):1075-82
Kim KH, et al.  (2011) Effect of Saccharomyces cerevisiae ret1-1 mutation on glycosylation and localization of the secretome. Mol Cells 31(2):151-8
Rachfall N, et al.  (2011) 5'TRU: identification and analysis of translationally regulative 5'untranslated regions in amino acid starved yeast cells. Mol Cell Proteomics 10(6):M110.003350
Wang S, et al.  (2011) Switch between Life History Strategies Due to Changes in Glycolytic Enzyme Gene Dosage in Saccharomyces cerevisiae. Appl Environ Microbiol 77(2):452-9
Araiza-Olivera D, et al.  (2010) The association of glycolytic enzymes from yeast confers resistance against inhibition by trehalose. FEMS Yeast Res 10(3):282-9
Sarry JE, et al.  (2007) Analysis of the vacuolar luminal proteome of Saccharomyces cerevisiae. FEBS J 274(16):4287-305
Brandina I, et al.  (2006) Enolase takes part in a macromolecular complex associated to mitochondria in yeast. Biochim Biophys Acta 1757(9-10):1217-1228
Rinnerthaler M, et al.  (2006) MMI1 (YKL056c, TMA19), the yeast orthologue of the translationally controlled tumor protein (TCTP) has apoptotic functions and interacts with both microtubules and mitochondria. Biochim Biophys Acta 1757(5-6):631-8
Waingeh VF, et al.  (2006) Glycolytic enzyme interactions with yeast and skeletal muscle F-actin. Biophys J 90(4):1371-84
Flick K and Wittenberg C  (2005) Multiple pathways for suppression of mutants affecting G1-specific transcription in Saccharomyces cerevisiae. Genetics 169(1):37-49
King DA, et al.  (2004) HOCl-mediated cell death and metabolic dysfunction in the yeast Saccharomyces cerevisiae. Arch Biochem Biophys 423(1):170-81
Kumar A, et al.  (2002) Subcellular localization of the yeast proteome. Genes Dev 16(6):707-19
Matic S, et al.  (2001) Interaction between phosphofructokinase and aldolase from Saccharomyces cerevisiae studied by aqueous two-phase partitioning. J Chromatogr B Biomed Sci Appl 751(2):341-8
Zhang L, et al.  (2001) Multiple mechanisms regulate expression of low temperature responsive (LOT) genes in Saccharomyces cerevisiae. Biochem Biophys Res Commun 283(2):531-5
Rasmussen SW  (1994) Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and TOA2 genes, an open reading frame (ORF) similar to a translationally controlled tumour protein, one ORF containing motifs also found in plant storage proteins and 13 ORFs with weak or no homology to known proteins. Yeast 10 Suppl A:S63-8
Compagno C, et al.  (1991) The promoter of Saccharomyces cerevisiae FBA1 gene contains a single positive upstream regulatory element. FEBS Lett 293(1-2):97-100
Schwelberger HG, et al.  (1989) Molecular cloning, primary structure and disruption of the structural gene of aldolase from Saccharomyces cerevisiae. Eur J Biochem 180(2):301-8
Dickinson JR and Williams AS  (1986) A genetic and biochemical analysis of the role of gluconeogenesis in sporulation of Saccharomyces cerevisiae. J Gen Microbiol 132(9):2605-10
Lobo Z  (1984) Saccharomyces cerevisiae aldolase mutants. J Bacteriol 160(1):222-6
Kadonaga JT and Knowles JR  (1983) Role of mono- and divalent metal cations in the catalysis by yeast aldolase. Biochemistry 22(1):130-6
Midelfort CF, et al.  (1976) Fructose 1,6-bisphosphate: isomeric composition, kinetics, and substrate specificity for the aldolases. Biochemistry 15(10):2178-85
Rabega C, et al.  (1976) [Study of purified aldolase from Saccharomyces cerevisiae, using irradiated fructose-1,6-diphosphate] Rev Ig Bacteriol Virusol Parazitol Epidemiol Pneumoftiziol Bacteriol Virusol 21(1):37-41
Schray KJ, et al.  (1975) The anomeric form of D-fructose 1,6-bisphosphate used as substrate in the muscle and yeast aldolase reactions. J Biol Chem 250(13):4883-7
RICHARDS OC and RUTTER WJ  (1961) Comparative properties of yeast and muscle aldolase. J Biol Chem 236:3185-92
ROSE IA and RIEDER SV  (1958) Studies on the mechanism on the aldolase reaction; isotope exchange reactions of muscle and yeast aldolase. J Biol Chem 231(1):315-29