scispace - formally typeset
M

Motoaki Sano

Researcher at National Institute of Advanced Industrial Science and Technology

Publications -  38
Citations -  2316

Motoaki Sano is an academic researcher from National Institute of Advanced Industrial Science and Technology. The author has contributed to research in topics: Aspergillus oryzae & Gene. The author has an hindex of 12, co-authored 35 publications receiving 2188 citations. Previous affiliations of Motoaki Sano include National Institute of Technology and Evaluation & Kanazawa Institute of Technology.

Papers
More filters
Journal ArticleDOI

Genome sequencing and analysis of Aspergillus oryzae

Masayuki Machida, +64 more
- 22 Dec 2005 - 
TL;DR: Specific expansion of genes for secretory hydrolytic enzymes, amino acid metabolism and amino acid/sugar uptake transporters supports the idea that A. oryzae is an ideal microorganism for fermentation.
Journal ArticleDOI

System-level identification of transcriptional circuits underlying mammalian circadian clocks.

TL;DR: The results indicate that circadian transcriptional circuits are governed by two design principles: regulation of E/E′ boxes and RevErbA/ROR binding elements follows a repressor-precedes-activator pattern, resulting in delayed transcriptional activity, whereas regulation of DBP/E4BP4 binding elements following a repression-antiphasic-to-activators mechanism, which generates high-amplitude transcriptionalactivity.
Journal ArticleDOI

Transcriptional analysis of genes for energy catabolism and hydrolytic enzymes in the filamentous fungus Aspergillus oryzae using cDNA microarrays and expressed sequence tags.

TL;DR: The wheat-bran culture gave the richest gene expression profile of hydrolytic enzymes and the lowest expression levels of catabolic genes (EMP, TCA) among the three media tested, suggesting that A. oryzae uses both EMP and TCA for glucose metabolism under AC conditions.
Journal ArticleDOI

Plasmid-Encoded asp Operon Confers a Proton Motive Metabolic Cycle Catalyzed by an Aspartate-Alanine Exchange Reaction

TL;DR: The asp operon confers a proton motive metabolic cycle consisting of the electrogenic aspartate-alanine antiporter and the as partate decarboxylase, which keeps intracellular levels of alanine, the countersubstrate for aspartates, high.