Recent Advances in the Chemical Biology of <i>N</i>-Glycans
Asparagine-linked <i>N</i>-glycans on proteins have diverse structures, and their functions vary according to their structures. In recent years, it has become possible to obtain high quantities of <i>N</i>-glycans via isolation and chemical/enzymatic/chemoenzymatic synthesis....
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MDPI AG
2021-02-01
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Series: | Molecules |
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Online Access: | https://www.mdpi.com/1420-3049/26/4/1040 |
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author | Asuka Shirakawa Yoshiyuki Manabe Koichi Fukase |
author_facet | Asuka Shirakawa Yoshiyuki Manabe Koichi Fukase |
author_sort | Asuka Shirakawa |
collection | DOAJ |
description | Asparagine-linked <i>N</i>-glycans on proteins have diverse structures, and their functions vary according to their structures. In recent years, it has become possible to obtain high quantities of <i>N</i>-glycans via isolation and chemical/enzymatic/chemoenzymatic synthesis. This has allowed for progress in the elucidation of <i>N</i>-glycan functions at the molecular level. Interaction analyses with lectins by glycan arrays or nuclear magnetic resonance (NMR) using various <i>N</i>-glycans have revealed the molecular basis for the recognition of complex structures of <i>N</i>-glycans. Preparation of proteins modified with homogeneous <i>N</i>-glycans revealed the influence of <i>N</i>-glycan modifications on protein functions. Furthermore, <i>N</i>-glycans have potential applications in drug development. This review discusses recent advances in the chemical biology of <i>N</i>-glycans. |
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issn | 1420-3049 |
language | English |
last_indexed | 2024-03-09T00:49:33Z |
publishDate | 2021-02-01 |
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series | Molecules |
spelling | doaj.art-6768972c560e4a428589ed12576d6c072023-12-11T17:18:48ZengMDPI AGMolecules1420-30492021-02-01264104010.3390/molecules26041040Recent Advances in the Chemical Biology of <i>N</i>-GlycansAsuka Shirakawa0Yoshiyuki Manabe1Koichi Fukase2Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, JapanDepartment of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, JapanDepartment of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka, Osaka 560-0043, JapanAsparagine-linked <i>N</i>-glycans on proteins have diverse structures, and their functions vary according to their structures. In recent years, it has become possible to obtain high quantities of <i>N</i>-glycans via isolation and chemical/enzymatic/chemoenzymatic synthesis. This has allowed for progress in the elucidation of <i>N</i>-glycan functions at the molecular level. Interaction analyses with lectins by glycan arrays or nuclear magnetic resonance (NMR) using various <i>N</i>-glycans have revealed the molecular basis for the recognition of complex structures of <i>N</i>-glycans. Preparation of proteins modified with homogeneous <i>N</i>-glycans revealed the influence of <i>N</i>-glycan modifications on protein functions. Furthermore, <i>N</i>-glycans have potential applications in drug development. This review discusses recent advances in the chemical biology of <i>N</i>-glycans.https://www.mdpi.com/1420-3049/26/4/1040<i>N</i>-glycanchemical biologyglycan arrayNMRglycoproteinlectin |
spellingShingle | Asuka Shirakawa Yoshiyuki Manabe Koichi Fukase Recent Advances in the Chemical Biology of <i>N</i>-Glycans Molecules <i>N</i>-glycan chemical biology glycan array NMR glycoprotein lectin |
title | Recent Advances in the Chemical Biology of <i>N</i>-Glycans |
title_full | Recent Advances in the Chemical Biology of <i>N</i>-Glycans |
title_fullStr | Recent Advances in the Chemical Biology of <i>N</i>-Glycans |
title_full_unstemmed | Recent Advances in the Chemical Biology of <i>N</i>-Glycans |
title_short | Recent Advances in the Chemical Biology of <i>N</i>-Glycans |
title_sort | recent advances in the chemical biology of i n i glycans |
topic | <i>N</i>-glycan chemical biology glycan array NMR glycoprotein lectin |
url | https://www.mdpi.com/1420-3049/26/4/1040 |
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