High impact information on Ceratitis capitata

• The rate is 2.7 times greater when Drosophila and Chymomyza species are compared; and about 5 times greater when any of those species are compared with the medfly Ceratitis capitata [1].
• In fact, the PRR analog of the medfly Ceratitis capitata Ccs36 gene directs expression in a manner similar to the D. melanogaster s36 PRR [2].
• The medfly Ceratitis capitata contains a gene (Cctra) with structural and functional homology to the Drosophila melanogaster sex-determining gene transformer (tra) [3].
• Here we describe the isolation of achaete-scute homologues in Ceratitis capitata, a species of acalyptrate Schizophora whose bristle pattern differs slightly from that of Drosophila [4].
• Here we report that, in contrast to Drosophila, the Sxl homologue in the Medfly, Ceratitis capitata, expresses the same mRNAs and protein isoforms in both XX and XY animals irrespective of the primary sex-determining signal [5].

Biological context of Ceratitis capitata

• We have undertaken the study of actin gene organization and expression in the genome of the Mediterranean fruit fly (medfly), Ceratitis capitata [6].
• Bioinvasions of the medfly Ceratitis capitata: source estimation using DNA sequences at multiple intron loci [7].
• To study the transcriptional regulation of the genes MSSP-alpha2 and MSSP-beta2, overlapping fragments of their promoters, containing the 5' UTRs and 5' flanking regions, were fused to the lacZ reporter gene and introduced into the medfly genome via Minos-mediated germline transformation [8].
• The Medfly actin gene also has a single intervening sequence, and an intron is found at the same position in the 79B and 88F actin genes [9].
• Chlorocyclohexane insecticides and male medfly attractants: similar stereospecificity for neuroactivity and interactions with a housefly [35S]t-butylbicyclophosphorothionate binding site [10].

Anatomical context of Ceratitis capitata

• Bacterial lipopolysaccharide (LPS) can function on isolated hemocytes from Ceratitis capitata larvae, inducing their spreading and degranulation [11].
• Adenylate cyclase activation by GTP and octopamine as well as basal activity (in the presence of Mg2+) have been studied as a function of membrane structure in plasma membranes from brain of the dipterous Ceratitis capitata [12].
• Interestingly, the medfly CcP0 seems to be the only P0 protein of higher eukaryotic organisms with basic character (pI 8.5), as shown by electrofocusing of purified ribosomes [13].
• Methyl palmitate: a novel product of the Medfly (Ceratitis capitata) corpus allatum [14].
• Effect of proteolytic and lipolytic enzymes on the adenylate cyclase activity from brain membranes of Ceratitis capitata [15].

Associations of Ceratitis capitata with chemical compounds

• Similar results were obtained with the Sxl homologue of Ceratitis capitata (Saccone, G., Peluso, I., Artiaco, D. , Giodano, E., Bopp, D. and Polito, L. C. (1998) Development 125, 1495-1500) suggesting that, in these non-drosophilid species, Sxl performs a function different from that in sex determination [16].
• Differential effects of fluoride and a non-hydrolysable GTP analogue on adenylate cyclase and G-proteins in Ceratitis capitata neural tissue [17].
• Public anxiety of near panic proportions was created by the announcement of a plan to commence aerial application of malathion bait over a large urban area in California for the eradication of the Mediterranean fruit fly within four days [18].
• Octopamine-sensitive adenylyl cyclase and G proteins in Ceratitis capitata brain during aging [19].
• Biosynthesis of polyprenol phosphate sugars by Ceratitis capitata extracts [20].

Gene context of Ceratitis capitata

• A cluster of vitellogenin genes in the Mediterranean fruit fly Ceratitis capitata: sequence and structural conservation in dipteran yolk proteins and their genes [21].
• Cloning and characterization of CcEcR. An ecdysone receptor homolog from the mediterranean fruit fly ceratitis capitata [22].
• The Drosophila alcohol dehydrogenase gene may have evolved independently of the functionally homologous medfly, olive fly, and flesh fly genes [23].
• The olive fly peptide sequence is more closely related to medfly ADH-2 [23].
• We present the coding nucleotide sequence of the Cu,Zn superoxide dismutase gene (Sod) for 15 species, which include the medfly Ceratitis capitata (family Tephritidae), the genera Chymomyza and Zaprionus, and representatives of the subgenera Dorsilopha, Drosophila, Hirtodrosophila, Scaptodrosophila, and Sophophora [24].

Analytical, diagnostic and therapeutic context of Ceratitis capitata

• In this report, we used an RT-PCR fragment of D. melanogaster RpS21 mRNA to clone a RpS21 cDNA from the Mediterranean fruit fly, Ceratitis capitata [25].
• The complete amino acid sequence of cytochrome c from the Dipterous Ceratitis capitata (serie Acalypterae) has been determined by combining automatic and manual methods of sequence analysis [26].
• Salt and pH-dependent effects on the local conformation of the two tyrosine residues of the histone H1 from the fruit fly Ceratitis capitata have been studied by difference spectroscopy, circular dichroism (CD), fluorescence emission and quenching of tyrosine emission by KI [27].

References