Advances in understanding N-glycosylation structure, function, and regulation in health and disease
N-linked glycosylation is a post-translational modification crucial for membrane protein folding, stability and other cellular functions. Alteration of membrane protein N-glycans is implicated in wide range of pathological conditions including cancer metastasis, chronic inflammatory diseases, and vi...
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Elsevier
2021
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oai:doaj.org-article:2b42ae9b895c4685aa4a5dd7be8c7d9c2021-11-26T04:23:46ZAdvances in understanding N-glycosylation structure, function, and regulation in health and disease0171-933510.1016/j.ejcb.2021.151186https://doaj.org/article/2b42ae9b895c4685aa4a5dd7be8c7d9c2021-09-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S0171933521000376https://doaj.org/toc/0171-9335N-linked glycosylation is a post-translational modification crucial for membrane protein folding, stability and other cellular functions. Alteration of membrane protein N-glycans is implicated in wide range of pathological conditions including cancer metastasis, chronic inflammatory diseases, and viral pathogenesis. Even though the roles of N-glycans have been studied extensively, our knowledge of their mechanisms remains unclear due to the lack of detailed structural analysis of the N-glycome. Mapping the N-glycome landscape will open new avenues to explore disease mechanisms and identify novel therapeutic targets. This review discusses the diverse structure of N-linked glycans, the function and regulation of N-glycosylation in health and disease, and ends with a focus on recent approaches to target N-glycans in rheumatoid arthritis and cancer metastasis.Sally EsmailMorris F. ManolsonElsevierarticleN-glycanImmunotherapyGlycoeditingBiomarkerCancerRheumatoid arthritisCytologyQH573-671ENEuropean Journal of Cell Biology, Vol 100, Iss 7, Pp 151186- (2021) |
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N-glycan Immunotherapy Glycoediting Biomarker Cancer Rheumatoid arthritis Cytology QH573-671 |
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N-glycan Immunotherapy Glycoediting Biomarker Cancer Rheumatoid arthritis Cytology QH573-671 Sally Esmail Morris F. Manolson Advances in understanding N-glycosylation structure, function, and regulation in health and disease |
description |
N-linked glycosylation is a post-translational modification crucial for membrane protein folding, stability and other cellular functions. Alteration of membrane protein N-glycans is implicated in wide range of pathological conditions including cancer metastasis, chronic inflammatory diseases, and viral pathogenesis. Even though the roles of N-glycans have been studied extensively, our knowledge of their mechanisms remains unclear due to the lack of detailed structural analysis of the N-glycome. Mapping the N-glycome landscape will open new avenues to explore disease mechanisms and identify novel therapeutic targets. This review discusses the diverse structure of N-linked glycans, the function and regulation of N-glycosylation in health and disease, and ends with a focus on recent approaches to target N-glycans in rheumatoid arthritis and cancer metastasis. |
format |
article |
author |
Sally Esmail Morris F. Manolson |
author_facet |
Sally Esmail Morris F. Manolson |
author_sort |
Sally Esmail |
title |
Advances in understanding N-glycosylation structure, function, and regulation in health and disease |
title_short |
Advances in understanding N-glycosylation structure, function, and regulation in health and disease |
title_full |
Advances in understanding N-glycosylation structure, function, and regulation in health and disease |
title_fullStr |
Advances in understanding N-glycosylation structure, function, and regulation in health and disease |
title_full_unstemmed |
Advances in understanding N-glycosylation structure, function, and regulation in health and disease |
title_sort |
advances in understanding n-glycosylation structure, function, and regulation in health and disease |
publisher |
Elsevier |
publishDate |
2021 |
url |
https://doaj.org/article/2b42ae9b895c4685aa4a5dd7be8c7d9c |
work_keys_str_mv |
AT sallyesmail advancesinunderstandingnglycosylationstructurefunctionandregulationinhealthanddisease AT morrisfmanolson advancesinunderstandingnglycosylationstructurefunctionandregulationinhealthanddisease |
_version_ |
1718409890972565504 |