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Mapping protein glycosylation through oxocarbenium ion generation
Mass spectrometry allows the pattern of glycosylation in proteins to be mapped, but can be limited by the lability of glycosidic bonds. Now, a method exploiting this lability allows for direct mapping of glycan moieties in glycoproteins.
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9814829/ https://www.ncbi.nlm.nih.gov/pubmed/36703321 http://dx.doi.org/10.1038/s42004-020-00352-7 |
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author | Bissette, Andrew J. |
author_facet | Bissette, Andrew J. |
author_sort | Bissette, Andrew J. |
collection | PubMed |
description | Mass spectrometry allows the pattern of glycosylation in proteins to be mapped, but can be limited by the lability of glycosidic bonds. Now, a method exploiting this lability allows for direct mapping of glycan moieties in glycoproteins. |
format | Online Article Text |
id | pubmed-9814829 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-98148292023-01-10 Mapping protein glycosylation through oxocarbenium ion generation Bissette, Andrew J. Commun Chem Research Highlight Mass spectrometry allows the pattern of glycosylation in proteins to be mapped, but can be limited by the lability of glycosidic bonds. Now, a method exploiting this lability allows for direct mapping of glycan moieties in glycoproteins. Nature Publishing Group UK 2020-08-07 /pmc/articles/PMC9814829/ /pubmed/36703321 http://dx.doi.org/10.1038/s42004-020-00352-7 Text en © Sprinter Nature Limited 2020 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Research Highlight Bissette, Andrew J. Mapping protein glycosylation through oxocarbenium ion generation |
title | Mapping protein glycosylation through oxocarbenium ion generation |
title_full | Mapping protein glycosylation through oxocarbenium ion generation |
title_fullStr | Mapping protein glycosylation through oxocarbenium ion generation |
title_full_unstemmed | Mapping protein glycosylation through oxocarbenium ion generation |
title_short | Mapping protein glycosylation through oxocarbenium ion generation |
title_sort | mapping protein glycosylation through oxocarbenium ion generation |
topic | Research Highlight |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9814829/ https://www.ncbi.nlm.nih.gov/pubmed/36703321 http://dx.doi.org/10.1038/s42004-020-00352-7 |
work_keys_str_mv | AT bissetteandrewj mappingproteinglycosylationthroughoxocarbeniumiongeneration |