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Inhibition of N\u2010glycosylation induces endoplasmic reticulum (<jats:styled-content style=\"fixed-case\">ER<\/jats:styled-content>) stress and the unfolded protein response (<jats:styled-content style=\"fixed-case\">UPR<\/jats:styled-content>), and eventually triggers <jats:styled-content style=\"fixed-case\">ER<\/jats:styled-content> stress\u2010related apoptosis. Unfortunately, the detailed timeline of these cell responses and protein expression alterations related to N<jats:italic>\u2010<\/jats:italic>glycosylation inhibition is not explicit yet, and the pathways involved in different stages of N<jats:italic>\u2010<\/jats:italic>glycosylation inhibition still need to be characterized. In this study, the dynamic proteome alterations related to N<jats:italic>\u2010<\/jats:italic>glycosylation inhibition were investigated by further analyzing our previously published quantitative proteomics data from tunicamycin (TM)\u2010treated ovarian carcinoma (<jats:styled-content style=\"fixed-case\">OVCAR<\/jats:styled-content>\u20103) cells. The results revealed that N\u2010glycosylation inhibition not only directly affects the expression of glycosylated proteins but also alters an extended scale of proteins. Functional annotation of these altered proteins demonstrated that proteins related to <jats:styled-content style=\"fixed-case\">ER<\/jats:styled-content> stress start changing within 6\u00a0h, followed by <jats:styled-content style=\"fixed-case\">UPR<\/jats:styled-content> within 24\u00a0h, and eventually <jats:styled-content style=\"fixed-case\">ER<\/jats:styled-content> stress\u2010related apoptosis is triggered after 48\u00a0h, indicating the conversion of cellular response from positive to negative. The dynamic proteome data presented here provide important information for better understanding of the significance of N\u2010glycosylation to cell survival and TM\u2010related cancer treatment.<\/jats:p>","DOI":"10.1111\/febs.14811","type":"journal-article","created":{"date-parts":[[2019,3,19]],"date-time":"2019-03-19T04:32:05Z","timestamp":1552969925000},"page":"1594-1605","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Dynamic analysis of proteomic alterations in response to N\u2010linked glycosylation inhibition in a drug\u2010resistant ovarian carcinoma cell line"],"prefix":"10.1111","volume":"286","author":[{"given":"Jian","family":"Shu","sequence":"first","affiliation":[{"name":"College of Life Sciences Northwest University Xi'an China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Liuyi","family":"Dang","sequence":"additional","affiliation":[{"name":"College of Life Sciences Northwest 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