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Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody

Amino Acids, 2010
The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues. These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc ...
Scott A, Yuzwa   +5 more
openaire   +2 more sources

Roles of O-GlcNAc in chronic diseases of aging

Molecular Aspects of Medicine, 2016
O-GlcNAcylation, a dynamic nutrient and stress sensitive post-translational modification, occurs on myriad proteins in the cell nucleus, cytoplasm and mitochondria. O-GlcNAcylation serves as a nutrient sensor to regulate signaling, transcription, translation, cell division, metabolism, and stress sensitivity in all cells.
Partha S, Banerjee   +2 more
openaire   +2 more sources

O-GlcNAc modification of nucleocytoplasmic proteins and diabetes

Medical Molecular Morphology, 2005
Nuclear and cytosolic proteins are glycosylated on serine or threonine residues by O-linked beta-N-acetylglucosamine (O-GlcNAc). O-GlcNAc modification is one of various posttranslational modifications and seems to be involved in the modulation of transcription and signal transduction.
Yoshihiro, Akimoto   +3 more
openaire   +2 more sources

O-Glcnac Glycans in the Mammalian Extracellular Environment

Carbohydrate Research
Extracellular O-GlcNAc is a unique post-translational modification that occurs in the epidermal growth factor-like (EGF) domain of the endoplasmic reticulum (ER) lumen. The EGF domain-specific O-GlcNAc transferase (EOGT), catalyzes the transfer of O-GlcNAc to serine/threonine residues of the C-terminal EGF domain.
Yohei Tsukamoto, Tetsuya Okajima
openaire   +2 more sources

The O-GlcNAc Modification of Recombinant Tau Protein and Characterization of the O-GlcNAc Pattern for Functional Study

The neuronal microtubule-associated tau protein is characterized in vivo by a large number of post-translational modifications along the entire primary sequence that modulates its function. The primary modification of tau is phosphorylation of serine/threonine or tyrosine residues that is involved in the regulation of microtubule binding and ...
El Hajjar, Léa   +5 more
openaire   +2 more sources

Chapter 15 O-GlcNAc Proteomics: Mass Spectrometric Analysis of O-GlcNAc Modifications on Proteins

2008
Publisher Summary This chapter reviews the specific functions of O-linked N-acetylglucosamine (O-GlcNAc) to establish its biological significance. The reason this modification has been historically difficult to detect is provided and the recent efforts to develop methods/techniques allowing for effective mass spectrometry (MS)-based site-specific O ...
Robert J. Chalkley   +2 more
openaire   +1 more source

Immunological Detection of O-GlcNAc

2003
Monika, Rex-Mathes   +4 more
openaire   +2 more sources

O-GlcNAc in the dark

Nature Chemical Biology, 2012
openaire   +1 more source

O-GlcNAc Transferase

RCSB Protein Data Bank, 2011
openaire   +1 more source

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