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  1. Purification and detection of Shigella type III secretion needle complex.

    Methods in Enzymology 358:385 (2002) PMID 12474402

  2. Characterization of the biosynthetic gene cluster for the ribosomally synthesized cyclic peptide ustiloxin B in Aspergillus flavus.

    Fungal Genetics and Biology 68:23 (2014) PMID 24841822

    We observed the production of this compound by Aspergillus flavus, and identified two A. flavus genes responsible for ustiloxin B biosynthesis (Umemura et al., 2013). The compound is a cyclic tetrapeptide of Tyr-Ala-Ile-Gly, whose tyrosine is modified with a non-protein coding amino acid, norvaline....
  3. Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length.

    Journal of Bacteriology 184(5):1244 (2002) PMID 11844752 PMCID PMC134865

    We show that Spa32, encoded by one of the spa genes, is an essential protein translocated via the type III secretion system and is involved in the control of needle length as well as type III secretion activity. When the spa32 gene was mutated, the type III secretion complexes possessed needles of v...
  4. Identification and characterization of genes responsible for biosynthesis of kojic acid, an industrially important compound fromAspergillus ...

    Fungal Genetics and Biology 47(12):953 (2010) PMID 20849972

    Kojic acid is produced in large amounts by Aspergillus oryzae as a secondary metabolite and is widely used in the cosmetic industry. Glucose can be converted to kojic acid, perhaps by only a few steps, but no genes for the conversion have thus far been revealed. Using a DNA microarray, g...
  5. Increased production of fatty acids and triglycerides in Aspergillus oryzae by enhancing expressions of fatty acid synthesis-related genes.

    Applied Microbiology and Biotechnology 97(1):269 (2013) PMID 22733113

    We investigate enhancing expression of enzymes involved in the production of fatty acids and triglycerides as a means to increase production of these compounds in Aspergillus oryzae. Examination of the A. oryzae genome demonstrates that it contains two fatty acid synthases and several other genes th...
  6. Use of the Aspergillus oryzae actin gene promoter in a novel reporter system for exploring antifungal compounds and their target genes.

    Applied Microbiology and Biotechnology 87(5):1829 (2010) PMID 20464390

    We used Aspergillus oryzae as a model to construct a reporter system for exploring novel antifungal compounds and their target genes. The comprehensive gene expression analysis showed that the actin-encoding actB gene was transcriptionally highly induced by benomyl treatment. We therefore used the a...
  7. The beta-1,3-exoglucanase gene exgA (exg1) of Aspergillus oryzae is required to catabolize extracellular glucan, and is induced in growth on...

    Bioscience, Biotechnology, and Biochemistry 71(4):926 (2007) PMID 17420593

    The biological role of ExgA (Exg1), a secretory beta-1,3-exoglucanase of Aspergillus oryzae, and the expression pattern of the exgA (exg1) gene were analyzed. The exgA disruptant and the exgA-overexpressing mutant were constructed, and phenotypes of both mutants were compared. Higher mycelial growth...
  8. Genomics of industrial Aspergilli and comparison with toxigenic relatives.

    Food Additives & Contaminants: Part A - Chemist... 25(9):1147 (2008) PMID 18798040

    Aspergillus oryzae has been used in Japanese fermentation industries for more than a thousand years. The species produces large amounts of various hydrolytic enzymes and has been successfully applied to modern biotechnology. The size of the A. oryzae genome (37.5 Mb) is very close to that of A. flav...
  9. Transcriptional regulation of genes on the non-syntenic blocks ofAspergillus oryzaeand its functional relationship to solid-state cultivatio...

    Fungal Genetics and Biology 45(2):139 (2008) PMID 17967552

    These results strongly suggest that the genes on NSBs play an important role on solid-state fermentation....
  10. Improvement of the lectin-antibody enzyme immunoassay of the alphafetoprotein carbohydrate chain for automation with the enzyme immunoassay ...

    Bioscience, Biotechnology, and Biochemistry 69(8):1616 (2005) PMID 16116296

    We improved the technique of the assay for automation. Consequently, alphafetoprotein-L3 and total alphafetoprotein were detected with two lectins using an automatic paramagnetic bead handling robot. This indicates that the improved method is potentially applicable to the automated enzyme immunoassa...