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Author Correction: The active site of O-GlcNAc transferase imposes constraints on substrate sequence.

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Title: Author Correction: The active site of O-GlcNAc transferase imposes constraints on substrate sequence.
Authors: Pathak S; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK., Alonso J; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK., Schimpl M; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK., Rafie K; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK., Blair DE; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK., Borodkin VS; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK., Schüttelkopf AW; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK., Albarbarawi O; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK.; Department of Chemistry, Faculty of Science, Taibah University, Al Madenah Al Monwarah, Saudi Arabia., van Aalten DMF; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK. dmfvanaalten@dundee.ac.uk.; Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, UK. dmfvanaalten@dundee.ac.uk.
Source: Nature structural & molecular biology [Nat Struct Mol Biol] 2023 Apr; Vol. 30 (4), pp. 564.
Publication Type: Published Erratum
Journal Info: Publisher: Nature Pub. Group Country of Publication: United States NLM ID: 101186374 Publication Model: Print Cited Medium: Internet ISSN: 1545-9985 (Electronic) Linking ISSN: 15459985 NLM ISO Abbreviation: Nat Struct Mol Biol Subsets: MEDLINE; PubMed not MEDLINE
Database: MEDLINE Ultimate
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  Data: Author Correction: The active site of O-GlcNAc transferase imposes constraints on substrate sequence.
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  Data: <searchLink fieldCode="AU" term="%22Pathak+S%22">Pathak S</searchLink>; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK.<br /><searchLink fieldCode="AU" term="%22Alonso+J%22">Alonso J</searchLink>; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK.<br /><searchLink fieldCode="AU" term="%22Schimpl+M%22">Schimpl M</searchLink>; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK.<br /><searchLink fieldCode="AU" term="%22Rafie+K%22">Rafie K</searchLink>; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK.<br /><searchLink fieldCode="AU" term="%22Blair+DE%22">Blair DE</searchLink>; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK.<br /><searchLink fieldCode="AU" term="%22Borodkin+VS%22">Borodkin VS</searchLink>; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK.<br /><searchLink fieldCode="AU" term="%22Schüttelkopf+AW%22">Schüttelkopf AW</searchLink>; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK.<br /><searchLink fieldCode="AU" term="%22Albarbarawi+O%22">Albarbarawi O</searchLink>; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK.; Department of Chemistry, Faculty of Science, Taibah University, Al Madenah Al Monwarah, Saudi Arabia.<br /><searchLink fieldCode="AU" term="%22van+Aalten+DMF%22">van Aalten DMF</searchLink>; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK. dmfvanaalten@dundee.ac.uk.; Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, UK. dmfvanaalten@dundee.ac.uk.
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  Data: <searchLink fieldCode="JN" term="%22101186374%22">Nature structural & molecular biology</searchLink> [Nat Struct Mol Biol] 2023 Apr; Vol. 30 (4), pp. 564.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Nature+Pub%2E+Group%22">Nature Pub. Group </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>101186374 <i>Publication Model: </i>Print <i>Cited Medium: </i>Internet <i>ISSN: </i>1545-9985 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2215459985%22">15459985 </searchLink><i>NLM ISO Abbreviation: </i>Nat Struct Mol Biol <i>Subsets: </i>MEDLINE; PubMed not MEDLINE
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        Value: 10.1038/s41594-023-00945-5
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        Text: English
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        StartPage: 564
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              Text: 2023 Apr
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