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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Autores principales: Sally Esmail, Morris F. Manolson
Formato: article
Lenguaje:EN
Publicado: Elsevier 2021
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Acceso en línea:https://doaj.org/article/2b42ae9b895c4685aa4a5dd7be8c7d9c
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spelling 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)
institution DOAJ
collection DOAJ
language EN
topic N-glycan
Immunotherapy
Glycoediting
Biomarker
Cancer
Rheumatoid arthritis
Cytology
QH573-671
spellingShingle 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
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