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Hisashi Ashida

Researcher at Kindai University

Publications -  87
Citations -  8668

Hisashi Ashida is an academic researcher from Kindai University. The author has contributed to research in topics: Bifidobacterium bifidum & Bifidobacterium longum. The author has an hindex of 35, co-authored 83 publications receiving 7220 citations. Previous affiliations of Hisashi Ashida include Osaka University & Kyoto University.

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Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Two distinct α-l-fucosidases from Bifidobacterium bifidum are essential for the utilization of fucosylated milk oligosaccharides and glycoconjugates

TL;DR: It is suggested that AfcA and AfcB play essential roles in degradingalpha1,2- and alpha1,3/4-fucosylated milk oligosaccharides, respectively, and also glycoconjugates, in the gastrointestinal tracts.
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Longevity in Mice Is Promoted by Probiotic-Induced Suppression of Colonic Senescence Dependent on Upregulation of Gut Bacterial Polyamine Production

TL;DR: This study demonstrated increased longevity in mice following probiotic treatment with LKM512, possibly due to the suppression of chronic low-grade inflammation in the colon induced by higher PA levels, indicating that ingestion of specific probiotics may be an easy approach for improving intestinal health and increasing lifespan.
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Mutants of Mucor hiemalis Endo-β-N-acetylglucosaminidase Show Enhanced Transglycosylation and Glycosynthase-like Activities

TL;DR: The site-directed mutagenesis on residues in the putative catalytic region of Endo-M is described to generate mutants with superior transglycosylation activity and the first glycosynthase derived from endo-β-N-acetylglucosaminidases that proceed via a substrate-assisted mechanism is described.