Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse (Q28594444)

GOA release 2020-03-11

5

Andrej Sali

0 references

author name string

Jonathan C. Trinidad

1

1 reference

31 January 2017

David T. Barkan

2

1 reference

31 January 2017

Brittany F. Gulledge

3

1 reference

31 January 2017

Agnes Thalhammer

4

1 reference

31 January 2017

Ralf Schoepfer

6

1 reference

31 January 2017

Alma L. Burlingame

Molecular & Cellular Proteomics

7

1 reference

31 January 2017

1 August 2012

1 reference

31 January 2017

1 reference

31 January 2017

11

1 reference

31 January 2017

8

1 reference

31 January 2017

215–229

1 reference

31 January 2017

Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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The importance of intrinsic disorder for protein phosphorylation

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Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications

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Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain

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

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Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data

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Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis

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The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine

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Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc

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