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Chemoresistance remains to be the major restriction on the clinical use of cisplatin. Aberrant changes in protein glycosylation are closely associated with the growth, invasion, metastasis, and resistance to chemotherapy of cancer cells. Comprehensive study on the role of protein glycosylation in the development of cisplatin resistance would contribute to precise elucidation of the complicated mechanism of resistance. In this work, we have integrated proteomic and N-glycoproteomic analysis for comprehensive identification of the membrane proteins, glycoproteins as well as glycans associated with cisplatin resistance of the non-small-cell lung cancer cells. Using this method, we found that alterations in the abundance and glycosylation of proteins implicated in cell adhesion, cell migration, response to drug and signal transduction occurred in the development of cisplatin resistance. We further assessed the cell migration, invasion, and cellular cisplatin accumulation of the sensitive and resistant cells. Impo