O-GlcNAc transferase

 
National Institutes of Health

Topic mentions per year

Topic mentions per year

1991-2017
0204019912017

Papers overview

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2012
2012
Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa… (More)
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Highly Cited
2010
Highly Cited
2010
Cancer cells upregulate glycolysis, increasing glucose uptake to meet energy needs. A small fraction of a cell's glucose enters… (More)
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Highly Cited
2009
Highly Cited
2009
O-linked N-acetylglucosamine transferase (OGT) reversibly modifies serine and threonine residues of many intracellular proteins… (More)
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Highly Cited
2008
Highly Cited
2008
Glucose flux through the hexosamine biosynthetic pathway leads to the post-translational modification of cytoplasmic and nuclear… (More)
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Highly Cited
2005
Highly Cited
2005
O-GlcNAcylation of serine and threonine residues is a dynamic and essential post-translational modification involved in signaling… (More)
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Highly Cited
2003
Highly Cited
2003
The ubiquitin proteasome system classically selects its substrates for degradation by tagging them with ubiquitin. Here, we… (More)
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Highly Cited
2002
Highly Cited
2002
Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine… (More)
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Highly Cited
2000
Highly Cited
2000
Nuclear and cytoplasmic protein glycosylation is a widespread and reversible posttranslational modification in eukaryotic cells… (More)
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Highly Cited
1999
Highly Cited
1999
The O-GlcNAc transferase (OGT) is a unique nuclear and cytosolic glycosyltransferase that contains multiple tetratricopeptide… (More)
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Highly Cited
1997
Highly Cited
1997
O-Linked N-acetylglucosamine (O-GlcNAc) glycosylation is a dynamic modification of eukaryotic nuclear and cytosolic proteins… (More)
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