Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation
- Hangil Park, Tadashi Suzuki, W. Lennarz
- BiologyProceedings of the National Academy of Sciences…
- 18 September 2001
Two-hybrid library screening by using mouse PNGase as the target yielded several PNGase-interacting proteins that previously had been implicated in proteasome-dependent protein degradation, suggesting that PNGase may be required for efficient proteasomesome-mediated degradation of misfolded glycoproteins in mammalian cells.
Glycosylation quality control by the Golgi structure
- Yanzhuang Wang, Shijiao Huang, Tadashi Suzuki
- BiologyJournal of Molecular Biology
- 14 August 2016
Endo-β-N-acetylglucosaminidase forms N-GlcNAc protein aggregates during ER-associated degradation in Ngly1-defective cells
- Chengcheng Huang, Yoichiro Harada, Tadashi Suzuki
- BiologyProceedings of the National Academy of Sciences
- 20 January 2015
This study identified the dysregulation of ER-associated degradation (ERAD) in cells that were defective in the cytosolic deglycosylating enzyme, Ngly1, and provides a potential mechanism underlying the phenotypic consequences of a newly emerging genetic disorder caused by mutation of the human NGLY1 gene.
Peptides Glycosylated in the Endoplasmic Reticulum of Yeast Are Subsequently Deglycosylated by a Soluble Peptide: N-Glycanase Activity*
- Tadashi Suzuki, Hangil Park, K. Kitajima, W. Lennarz
- BiologyJournal of Biological Chemistry
- 21 August 1998
The occurrence of a soluble PNGase activity in Saccharomyces cerevisiae was reported, which was recovered in the cytosolic fraction, has a neutral pH optimum, and dithiothreitol is required for activity.
Complex, Two-way Traffic of Molecules Across the Membrane of the Endoplasmic Reticulum*
- Tadashi Suzuki, Q. Yan, W. Lennarz
- BiologyJournal of Biological Chemistry
- 24 April 1998
In this review, it is clear that two-way traffic occurs, involving not only movement of molecules from the cytosol into the lumen of the ER but also out of theLumen into the cytOSol.
Glycometabolic Regulation of the Biogenesis of Small Extracellular Vesicles.
- Yoichiro Harada, K. Nakajima, I. Maruyama
- BiologyCell Reports
- 13 October 2020
Physiological importance of NGLY1, as revealed by rodent model analyses.
- Haruhiko Fujihira, Makoto Asahina, Tadashi Suzuki
- BiologyJournal of Biochemistry (Tokyo)
- 27 September 2021
P phenotypic consequences that have been reported for various Ngly1-deficient rodent models are summarized, and future perspectives are discussed to provide more insights into the physiological functions of NGLY1.
Assay for the peptide:N-glycanase/NGLY1 and disease-specific biomarkers for diagnosing NGLY1 deficiency.
- Hiroto Hirayama, Tadashi Suzuki
- BiologyJournal of Biochemistry (Tokyo)
- 18 November 2021
Progress made in the development of various assay methods for NGLy1 activity, as well as a recent progress in the identification of NGLY1 deficiency-specific biomarkers are summarized.
Siblings with MAN1B1-CDG Showing Novel Biochemical Profiles
- N. Okamoto, T. Ohto, Tadashi Suzuki
- Medicine, BiologyCells
- 1 November 2021
A HPLC analysis of sialylated N-linked glycans released from total plasma proteins and characterized the α1,2-mannosidase I activity of the lymphocyte microsome fraction observed in MAN1B1-deficient patients indicated N-glycan-processing defects.
A method for assaying peptide: N-glycanase/N-glycanase 1 activities in crude extracts using an N-glycosylated cyclopeptide
- Hiroto Hirayama, Y. Tachida, Junichi Seino, Tadashi Suzuki
- BiologyGlycobiology
- 10 November 2021
Method for measuring endogenous NGLY1 activity in crude extracts derived from cultured cells, patients’ fibroblasts, iPS cells or peripheral blood mononuclear cells (PBMCs), using a glycosylated cyclopeptide that exhibited resistance to the endogenous proteases in the extract promises to be applicable for its diagnosis.
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