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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...

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Detalles Bibliográficos
Autores principales: Struwe, Weston B, Robinson, Carol V
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2019
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.
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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
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