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Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-sp...

Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-sp...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_osti_scitechconnect_1042524

Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets

About this item

Full title

Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2012-05, Vol.109 (19), p.7280-7285

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

O-linked N-acetylglucosamine (O-GlcNAc) is a reversible posttranslational modification of Ser and Thr residues on cytosolic and nuclear proteins of higher eukaryotes catalyzed by O-GlcNAc transferase (OGT). O-GlcNAc has recently been found on Notch1 extracellular domain catalyzed by EGF domain-specific OGT. Aberrant O-GlcNAc modification of brain p...

Alternative Titles

Full title

Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_osti_scitechconnect_1042524

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_osti_scitechconnect_1042524

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1200425109

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