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Relating glycoprotein structural heterogeneity to function – insights from native mass spectrometry
Glycosylation is the most complex and prevalent protein modification that influences attributes ranging from cellular localization and signaling to half-life and proteolysis. Glycoconjugates are fundamental for cellular function and alterations in their structure are often observed in pathological s...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7104348/ https://www.ncbi.nlm.nih.gov/pubmed/31326232 http://dx.doi.org/10.1016/j.sbi.2019.05.019 |
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author | Struwe, Weston B Robinson, Carol V |
author_facet | Struwe, Weston B Robinson, Carol V |
author_sort | Struwe, Weston B |
collection | PubMed |
description | Glycosylation is the most complex and prevalent protein modification that influences attributes ranging from cellular localization and signaling to half-life and proteolysis. Glycoconjugates are fundamental for cellular function and alterations in their structure are often observed in pathological states. Most biotherapeutic proteins are glycosylated, which influences drug safety and efficacy. Therefore, the ability to characterize glycoproteins is important in all areas of biomolecular and medicinal research. Here we discuss recent advances in native mass spectrometry that have significantly improved our ability to characterize heterogeneous glycoproteins and to relate glycan structure to protein function. |
format | Online Article Text |
id | pubmed-7104348 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
record_format | MEDLINE/PubMed |
spelling | pubmed-71043482020-03-30 Relating glycoprotein structural heterogeneity to function – insights from native mass spectrometry Struwe, Weston B Robinson, Carol V Curr Opin Struct Biol Article Glycosylation is the most complex and prevalent protein modification that influences attributes ranging from cellular localization and signaling to half-life and proteolysis. Glycoconjugates are fundamental for cellular function and alterations in their structure are often observed in pathological states. Most biotherapeutic proteins are glycosylated, which influences drug safety and efficacy. Therefore, the ability to characterize glycoproteins is important in all areas of biomolecular and medicinal research. Here we discuss recent advances in native mass spectrometry that have significantly improved our ability to characterize heterogeneous glycoproteins and to relate glycan structure to protein function. 2019-10-01 2019-07-18 /pmc/articles/PMC7104348/ /pubmed/31326232 http://dx.doi.org/10.1016/j.sbi.2019.05.019 Text en http://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 | Article Struwe, Weston B Robinson, Carol V Relating glycoprotein structural heterogeneity to function – insights from native mass spectrometry |
title | Relating glycoprotein structural heterogeneity to function – insights from native mass spectrometry |
title_full | Relating glycoprotein structural heterogeneity to function – insights from native mass spectrometry |
title_fullStr | Relating glycoprotein structural heterogeneity to function – insights from native mass spectrometry |
title_full_unstemmed | Relating glycoprotein structural heterogeneity to function – insights from native mass spectrometry |
title_short | Relating glycoprotein structural heterogeneity to function – insights from native mass spectrometry |
title_sort | relating glycoprotein structural heterogeneity to function – insights from native mass spectrometry |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7104348/ https://www.ncbi.nlm.nih.gov/pubmed/31326232 http://dx.doi.org/10.1016/j.sbi.2019.05.019 |
work_keys_str_mv | AT struwewestonb relatingglycoproteinstructuralheterogeneitytofunctioninsightsfromnativemassspectrometry AT robinsoncarolv relatingglycoproteinstructuralheterogeneitytofunctioninsightsfromnativemassspectrometry |