{"doi":"10.1016/j.jprot.2011.05.019","title":"Distinct cell surface proteome profiling by biotin labeling and glycoprotein capturing","abstract":null,"journal":"Journal of Proteomics","year":2011,"id":637925,"datarank":0.40620753016533157,"base_score":2.70805020110221,"endowment":2.70805020110221,"self_citation_contribution":0.40620753016533157,"citation_network_contribution":0.0,"self_endowment_contribution":0.40620753016533157,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":14,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1656623,"name":"Takashi Shinkawa","orcid":null,"position":1,"is_corresponding":false},{"id":1656624,"name":"Kuniyasu Kato","orcid":null,"position":2,"is_corresponding":false},{"id":1656625,"name":"Noriyuki Inomata","orcid":null,"position":3,"is_corresponding":false},{"id":1656626,"name":"Nami Yabuki","orcid":null,"position":4,"is_corresponding":false},{"id":1656627,"name":"Masayuki Haramura","orcid":null,"position":5,"is_corresponding":false},{"id":1656622,"name":"Kohji Nagano","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Distinct cell surface proteome profiling by biotin labeling and glycoprotein capturing","abstract":"We performed here MS-based cell surface proteome profiling of HCT-116 cells by two distinct methods based on biotin labeling and glycoprotein capturing. In total, 742 biotinylated and 219 glycosylated proteins were identified by the biotin labeling and glycoprotein capturing, of which 224 and 138 proteins known to be located on plasma membrane were included, respectively, according to ingenuity pathway analysis. Although 104 plasma membrane proteins were identified by both methods, the rest of 154 were identified only by one. Almost all the identified plasma membrane proteins possessed consensus N-glycosylation sites, and proteins having various numbers of glycosylation sites were identified by both methods. Thus, the discrepancies of the identified proteins obtained from those two methods might not be only due to the number of glycosylation sites, but also to the expression and/or glycosylation level of the cell surface proteins. We also identified 312 N-glycosylated proteins from xenograft samples by glycoprotein capturing of which 135 were known as plasma membrane proteins. Although a number of highly-expressed plasma membrane proteins were common between culture and xenograft cells, some proteins showed culture- or xenograft-specific expression, suggesting that those proteins might contribute to grow in different environment.","is_dataset_classified":null,"base_score":2.70805020110221,"endowment":2.70805020110221,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"21621025","pmcid":null,"openalex_id":"https://openalex.org/W2155671594","authors":[],"funders":[],"total_grants":0,"fwci":0.158,"citation_percentile":0.53960565,"influential_citations":0,"citation_trend":[{"year":2014,"count":1},{"year":2017,"count":2},{"year":2019,"count":5},{"year":2020,"count":1},{"year":2021,"count":1},{"year":2022,"count":3},{"year":2023,"count":1}],"oa_status":"closed","license":"https://www.elsevier.com/tdm/userlicense/1.0/","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S1874391911002107?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S1874391911002107?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.jprot.2011.05.019","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/21621025","host_type":"repository"}],"fields_of_study":["Advanced Proteomics Techniques and Applications","Glycosylation and Glycoproteins Research","Peptidase Inhibition and Analysis","Animals","Biotinylation","Chromatography, Liquid","Glycoproteins","Glycosylation","HCT116 Cells","Humans","Membrane Proteins","Mice","Proteomics","Tandem Mass Spectrometry","Transplantation, Heterologous"],"mesh_terms":["Animals","Chromatography, Liquid","Glycoproteins","Glycosylation","Humans","Membrane Proteins","Transplantation, Heterologous","Biotinylation","Proteomics","HCT116 Cells","Mice","Tandem Mass Spectrometry"],"keywords":["Glycoprotein","Proteome","Glycosylation","Biotinylation","Membrane protein","Membrane glycoproteins","Biotin","Chemistry","Blood proteins","Biochemistry","Proteomics","Cell","Cell biology","Biology","Membrane","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-06T19:45:11.748050Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}