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How to extend your (polylactosamine) antennae

The elongated antennae decorating eukaryotic glycans are built from polylactosamine repeats. Polylactosamine forms a lectin recognition site and also acts as a platform for presenting diverse additional modifications (e.g., terminal cell-surface antigens); it therefore plays important roles in cell...

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Autor principal: Kimber, Matthew S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7948483/
https://www.ncbi.nlm.nih.gov/pubmed/33453284
http://dx.doi.org/10.1016/j.jbc.2020.100212
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author Kimber, Matthew S.
author_facet Kimber, Matthew S.
author_sort Kimber, Matthew S.
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description The elongated antennae decorating eukaryotic glycans are built from polylactosamine repeats. Polylactosamine forms a lectin recognition site and also acts as a platform for presenting diverse additional modifications (e.g., terminal cell-surface antigens); it therefore plays important roles in cell adherence, development, and immunity. Two new papers present a detailed structural and mechanistic investigation of β1-3-N-acetylgucosaminyltransferase 2, a key enzyme in antennae synthesis. The resulting insights will also help decipher other members of GT31, the single largest human glycosyltransferase family.
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spelling pubmed-79484832021-03-19 How to extend your (polylactosamine) antennae Kimber, Matthew S. J Biol Chem Editors' Pick Highlight The elongated antennae decorating eukaryotic glycans are built from polylactosamine repeats. Polylactosamine forms a lectin recognition site and also acts as a platform for presenting diverse additional modifications (e.g., terminal cell-surface antigens); it therefore plays important roles in cell adherence, development, and immunity. Two new papers present a detailed structural and mechanistic investigation of β1-3-N-acetylgucosaminyltransferase 2, a key enzyme in antennae synthesis. The resulting insights will also help decipher other members of GT31, the single largest human glycosyltransferase family. American Society for Biochemistry and Molecular Biology 2021-01-14 /pmc/articles/PMC7948483/ /pubmed/33453284 http://dx.doi.org/10.1016/j.jbc.2020.100212 Text en © 2020 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Editors' Pick Highlight
Kimber, Matthew S.
How to extend your (polylactosamine) antennae
title How to extend your (polylactosamine) antennae
title_full How to extend your (polylactosamine) antennae
title_fullStr How to extend your (polylactosamine) antennae
title_full_unstemmed How to extend your (polylactosamine) antennae
title_short How to extend your (polylactosamine) antennae
title_sort how to extend your (polylactosamine) antennae
topic Editors' Pick Highlight
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7948483/
https://www.ncbi.nlm.nih.gov/pubmed/33453284
http://dx.doi.org/10.1016/j.jbc.2020.100212
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