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Tadashi Suzuki

Researcher at Saitama University

Publications -  97
Citations -  8348

Tadashi Suzuki is an academic researcher from Saitama University. The author has contributed to research in topics: Endoplasmic reticulum & Glycan. The author has an hindex of 31, co-authored 93 publications receiving 7564 citations. Previous affiliations of Tadashi Suzuki include Kanazawa University & Osaka University.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
Journal ArticleDOI

PNG1, a Yeast Gene Encoding a Highly Conserved Peptide:N-Glycanase

Tadashi Suzuki, +4 more
- 29 May 2000 - 
TL;DR: Sequencing of expressed sequence tag clones revealed that Png1p is highly conserved in a wide variety of eukaryotes including mammals, suggesting that the enzyme has an important function.
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The Png1-Rad23 complex regulates glycoprotein turnover.

Ikjin Kim, +6 more
- 16 Jan 2006 - 
TL;DR: It is demonstrated that the efficient degradation of glycosylated ricin A chain requires the Png1–Rad23 complex, suggesting that this complex couples protein deglycosylation and degradation.
Journal ArticleDOI

Rad23 Provides a Link between the Png1 Deglycosylating Enzyme and the 26 S Proteasome in Yeast

Tadashi Suzuki, +3 more
- 15 Jun 2001 - 
TL;DR: A model in which Rad23p functions as an escort protein to link the 26 S proteasome with proteins such as Rad4p or Png1p to regulate their cellular activities is proposed.
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Crystal structure of mammalian α1,6-fucosyltransferase, FUT8

Hideyuki Ihara, +13 more
- 01 May 2007 - 
TL;DR: The present findings of FUT8 suggest that the conserved residues in the three conserved regions participate in the Rossmann fold and act as the donor binding site, or in catalysis, thus playing key roles in the fucose-transferring reaction.