An engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptides
Protein glycosylation is an essential post-translational modification which analysis is complicated by the diversity of glycan composition and heterogeneity at individual attachment sites. Here the authors describe a method to selectively enrich N-linked glycopeptides to facilitate the detection of...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2017-05-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms15487 |
| _version_ | 1819126540829458432 |
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| author | Minyong Chen Xiaofeng Shi Rebecca M. Duke Cristian I. Ruse Nan Dai Christopher H. Taron James C. Samuelson |
| author_facet | Minyong Chen Xiaofeng Shi Rebecca M. Duke Cristian I. Ruse Nan Dai Christopher H. Taron James C. Samuelson |
| author_sort | Minyong Chen |
| collection | DOAJ |
| description | Protein glycosylation is an essential post-translational modification which analysis is complicated by the diversity of glycan composition and heterogeneity at individual attachment sites. Here the authors describe a method to selectively enrich N-linked glycopeptides to facilitate the detection of micro-heterogeneity in N-glycosylation. |
| first_indexed | 2024-12-22T07:57:40Z |
| format | Article |
| id | doaj.art-63d113807aad4b368c472143cfecb909 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-22T07:57:40Z |
| publishDate | 2017-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-63d113807aad4b368c472143cfecb9092022-12-21T18:33:19ZengNature PortfolioNature Communications2041-17232017-05-018111510.1038/ncomms15487An engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptidesMinyong Chen0Xiaofeng Shi1Rebecca M. Duke2Cristian I. Ruse3Nan Dai4Christopher H. Taron5James C. Samuelson6New England Biolabs Inc.New England Biolabs Inc.New England Biolabs Inc.New England Biolabs Inc.New England Biolabs Inc.New England Biolabs Inc.New England Biolabs Inc.Protein glycosylation is an essential post-translational modification which analysis is complicated by the diversity of glycan composition and heterogeneity at individual attachment sites. Here the authors describe a method to selectively enrich N-linked glycopeptides to facilitate the detection of micro-heterogeneity in N-glycosylation.https://doi.org/10.1038/ncomms15487 |
| spellingShingle | Minyong Chen Xiaofeng Shi Rebecca M. Duke Cristian I. Ruse Nan Dai Christopher H. Taron James C. Samuelson An engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptides Nature Communications |
| title | An engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptides |
| title_full | An engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptides |
| title_fullStr | An engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptides |
| title_full_unstemmed | An engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptides |
| title_short | An engineered high affinity Fbs1 carbohydrate binding protein for selective capture of N-glycans and N-glycopeptides |
| title_sort | engineered high affinity fbs1 carbohydrate binding protein for selective capture of n glycans and n glycopeptides |
| url | https://doi.org/10.1038/ncomms15487 |
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