<p>(A) corresponds to a silver stained SDS-PAGE of O-GlcNAc proteins purified by RL-2 immunoprecipitation before (a) or after (b) an hexosaminidase treatment; (c) corresponds to immunoprecipitation protocol realized without proteins sample, and (d) to 25 µg of contractile proteins extract. O-GlcNAc proteins were purified by RL-2 immuno-precipitation followed by an electrophoretic separation on 7.5% (B) or 10–20% (C) SDS-PAGE. Gels were colloïdal blue stained. Each well-resolved bands were submitted to a mass spectrometry-based identification. Numbers on the two panels indicates the different identified proteins; note that the corresponding identifications are summarized in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pon...
The modification of proteins with O-linked N-acetylglucosamine residues (O-GlcNAc) is found on many ...
Glycosylation is a widespread PTM of proteins; the carbohydrate moieties provide various functional,...
<p>(A and B) Whole cell lysates from HEK293 cells transfected with siRNA targeting OGT or control si...
<p>O-GlcNAc contractile proteins extracted from soleus were enriched using RL-2 immunoprecipitation ...
<p>Proteins extracted from skinned biopsies were RL-2 immunoprecipitated and separated on 10–20% SDS...
O-linked N-acetylglucosaminylation (O-GlcNAc) is a reg-ulatory post-translational modification of nu...
The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in t...
The attachment of N-acetylglucosamine to serine or thre-onine residues (O-GlcNAc) is a post-translat...
<p>Soleus contractile proteins (lanes 1 and 2), proteins extracted from skinned biopsies (lanes 3 an...
O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucia...
Protein O-GlcNAcylation is a non-canonical glycosylation of nuclear, mitochondrial, and cytoplasmic ...
We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell...
The post-translational modification of proteins with <i>N</i>-acetylglucosamine (<i>O</i>-GlcNAc) is...
There are many tools available for the study of post-translational modifications. The majority of th...
O-GlcNAcylation is the only sugar modification for proteins present in the cytoplasm and nucleus and...
The modification of proteins with O-linked N-acetylglucosamine residues (O-GlcNAc) is found on many ...
Glycosylation is a widespread PTM of proteins; the carbohydrate moieties provide various functional,...
<p>(A and B) Whole cell lysates from HEK293 cells transfected with siRNA targeting OGT or control si...
<p>O-GlcNAc contractile proteins extracted from soleus were enriched using RL-2 immunoprecipitation ...
<p>Proteins extracted from skinned biopsies were RL-2 immunoprecipitated and separated on 10–20% SDS...
O-linked N-acetylglucosaminylation (O-GlcNAc) is a reg-ulatory post-translational modification of nu...
The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in t...
The attachment of N-acetylglucosamine to serine or thre-onine residues (O-GlcNAc) is a post-translat...
<p>Soleus contractile proteins (lanes 1 and 2), proteins extracted from skinned biopsies (lanes 3 an...
O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucia...
Protein O-GlcNAcylation is a non-canonical glycosylation of nuclear, mitochondrial, and cytoplasmic ...
We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell...
The post-translational modification of proteins with <i>N</i>-acetylglucosamine (<i>O</i>-GlcNAc) is...
There are many tools available for the study of post-translational modifications. The majority of th...
O-GlcNAcylation is the only sugar modification for proteins present in the cytoplasm and nucleus and...
The modification of proteins with O-linked N-acetylglucosamine residues (O-GlcNAc) is found on many ...
Glycosylation is a widespread PTM of proteins; the carbohydrate moieties provide various functional,...
<p>(A and B) Whole cell lysates from HEK293 cells transfected with siRNA targeting OGT or control si...