Mitsutaka Ogawa

Nagoya, 4668550, Japan

Last Updated: 09/26/2026

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Found 20 publications

Evidence that only EWS among the FET proteins acquires a low partitioning property for the hyperosmotic stress response by O-GlcNAc glycosylation on its low-complexity domain.

Evidence that only EWS among the FET proteins acquires a low partitioning property for the hyperosmotic stress response by O-GlcNAc glycosylation on its low-complexity domain.

Journal: Experimental cell research

Published: December 16, 2022

Glycoproteomics of NOTCH1 EGF repeat fragments overexpressed with different glycosyltransferases in HEK293T cells reveals insights into O-GlcNAcylation of NOTCH1.

Glycoproteomics of NOTCH1 EGF repeat fragments overexpressed with different glycosyltransferases in HEK293T cells reveals insights into O-GlcNAcylation of NOTCH1.

Journal: Glycobiology

Published: December 15, 2021

Bioinformatics and Functional Analyses Implicate Potential Roles for EOGT and L-fringe in Pancreatic Cancers.

Bioinformatics and Functional Analyses Implicate Potential Roles for EOGT and L-fringe in Pancreatic Cancers.

Journal: Molecules (Basel, Switzerland)

Published: January 05, 2021

Glycoproteomic analysis identifies cryptdin-related sequence 1 as O-glycosylated protein modified with α1,2-fucose in the small intestine.

Glycoproteomic analysis identifies cryptdin-related sequence 1 as O-glycosylated protein modified with α1,2-fucose in the small intestine.

Journal: Archives of biochemistry and biophysics

Published: September 22, 2020

Contribution of extracellular O-GlcNAc to the stability of folded epidermal growth factor-like domains and Notch1 trafficking.

Contribution of extracellular O-GlcNAc to the stability of folded epidermal growth factor-like domains and Notch1 trafficking.

Journal: Biochemical and biophysical research communications

Published: February 25, 2020

N-Glycans on EGF domain-specific O-GlcNAc transferase (EOGT) facilitate EOGT maturation and peripheral endoplasmic reticulum localization.

N-Glycans on EGF domain-specific O-GlcNAc transferase (EOGT) facilitate EOGT maturation and peripheral endoplasmic reticulum localization.

Journal: The Journal of biological chemistry

Published: December 11, 2019

Structure and function of extracellular O-GlcNAc.

Structure and function of extracellular O-GlcNAc.

Journal: Current opinion in structural biology

Published: October 04, 2018

Dissection and Whole Mount Staining of Retina from Neonatal Mice.

Dissection and Whole Mount Staining of Retina from Neonatal Mice.

Journal: Bio-protocol

Published: July 25, 2018

Structural Divergence in O-GlcNAc Glycans Displayed on Epidermal Growth Factor-like Repeats of Mammalian Notch1.

Structural Divergence in O-GlcNAc Glycans Displayed on Epidermal Growth Factor-like Repeats of Mammalian Notch1.

Journal: Molecules (Basel, Switzerland)

Published: June 20, 2018

Protocol for Notch-ligand Binding Assays Using Dynabeads.

Protocol for Notch-ligand Binding Assays Using Dynabeads.

Journal: Bio-protocol

Published: June 16, 2017

O-GlcNAc on NOTCH1 EGF repeats regulates ligand-induced Notch signaling and vascular development in mammals.

O-GlcNAc on NOTCH1 EGF repeats regulates ligand-induced Notch signaling and vascular development in mammals.

Journal: eLife

Published: December 22, 2016

Neogenin, Defined as a GD3-associated Molecule by Enzyme-mediated Activation of Radical Sources, Confers Malignant Properties via Intracytoplasmic Domain in Melanoma Cells.

Neogenin, Defined as a GD3-associated Molecule by Enzyme-mediated Activation of Radical Sources, Confers Malignant Properties via Intracytoplasmic Domain in Melanoma Cells.

Journal: The Journal of biological chemistry

Published: December 07, 2015

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Last Updated: 09/26/2026