Search Results - (Author, Cooperation:S. P. Holloway)
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1C. L. Valentim ; D. Cioli ; F. D. Chevalier ; X. Cao ; A. B. Taylor ; S. P. Holloway ; L. Pica-Mattoccia ; A. Guidi ; A. Basso ; I. J. Tsai ; M. Berriman ; C. Carvalho-Queiroz ; M. Almeida ; H. Aguilar ; D. E. Frantz ; P. J. Hart ; P. T. LoVerde ; T. J. Anderson
American Association for the Advancement of Science (AAAS)
Published 2013Staff ViewPublication Date: 2013-11-23Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Amino Acid Sequence ; Animals ; Drug Resistance/*genetics ; Gene Knockdown Techniques ; Genetic Linkage ; Helminth Proteins/*genetics ; Humans ; Molecular Sequence Data ; Mutation ; Oxamniquine/*pharmacology ; Phylogeny ; Protein Conformation ; Quantitative Trait Loci ; RNA Interference ; Schistosoma mansoni/*drug effects/*genetics ; Schistosomicides/*pharmacology ; Sulfotransferases/chemistry/classification/*geneticsPublished by: -
2Holloway, S. P. ; Sims, P. F. G. ; Delves, C. J. ; Scaife, J. G. ; Hyde, J. E.
Oxford, UK : Blackwell Publishing Ltd
Published 1989Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: As a step towards indentifying exploitable differences between host and parasite at the molecular level, we have isolated and sequenced genomic clones encompassing an entire α-tubulin gene (designated α-tubulin I) from the human malaria parasite, Plasmodium falciparum. The gene, which contains two introns, encodes a product with a predicted length of 453 amino acid residues (50.3 kD). The protein sequence shows a high degree of homology to other α-tubulins, particularly that of the coccidian parasite, Toxoplasma gondii (94%), whose gene carries introns in identical positions. Only one copy of the α-tubulin I gene itself was found, although a second gene designated α-II was also identified which is closely related but which differs at both the nucleotide and amino acid sequence levels. The α-I and β-tubulin genes were found to reside on different chromosomes.Type of Medium: Electronic ResourceURL: -
3Delves, C. J. ; Ridley, R. G. ; Goman, M. ; Holloway, S. P. ; Hyde, J. E. ; Scaife, J. G.
Oxford, UK : Blackwell Publishing Ltd
Published 1989Staff ViewISSN: 1365-2958Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyMedicineNotes: We describe the isolation and characterization of a gene for β-tubulin from the malaria parasite, Plasmodium falciparum. This organism appears to contain a single gene encoding β-tubulin. A single transcript from this gene can be detected in the total RNA of the parasite's asexual blood stages. The complete sequence for the gene has been elucidated. It has two introns, one of which has a position identical to that of a related parasite, Toxoplasma gondii. The gene shows the usual preference for codons with A or T in the third position. The predicted amino acid sequence is compared with that of T. gondii and the human host. Further comparisons between these and fungal sequences of β-tubulins resistant to benomyl, a drug binding this protein, highlight differences that could be exploited in the development of parasite-specific anti-tubulin drugs.Type of Medium: Electronic ResourceURL: -
4Minko, I. ; Holloway, S. P. ; Nikaido, S. ; Carter, M. ; Odom, O. W. ; Johnson, C. H. ; Herrin, D. L.
Springer
Published 1999Staff ViewISSN: 1617-4623Keywords: Key words Bioluminescence ; Chlamydomonas ; Chloroplast transformation ; Chloroplast translation ; Vital reporterSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Abstract The use of luciferases as reporters of gene expression in living cells has been extended to the chloroplast genome. We show that the luciferase from the soft coral Renilla reniformis (Rluc) can be successfully expressed in the chloroplast of Chlamydomonas reinhardtii. Expression of the rluc cDNA was driven by the promoter and 5′ untranslated regions of the atpA gene. Western analysis with an anti-Rluc antibody detected a single polypeptide of 38 kDa in the luminescent cells. This is 3 kDa larger than native Rluc, and suggests that translation of the chimeric mRNA begins at the atpA start codon, 29 codons upstream from the rluc start site. We also show that the luminescence of the transformants was sufficient to enable imaging of colonies using a cooled CCD camera.Type of Medium: Electronic ResourceURL: