{"database":"JPOST Repository","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["https://storage.jpostdb.org/JPST003525/files/240530QE_Total_Mock_2.raw","https://storage.jpostdb.org/JPST003525/files/240529QE_phospho_Mock_2.raw","https://storage.jpostdb.org/JPST003525/files/240524HF_Boncat_IAV_1.raw","https://storage.jpostdb.org/JPST003525/files/240524HF_Boncat_IAV_3.raw","https://storage.jpostdb.org/JPST003525/files/240530QE_Total_IAV_2.raw","https://storage.jpostdb.org/JPST003525/files/240524HF_Boncat_Mock_2.raw","https://storage.jpostdb.org/JPST003525/files/240529QE_phospho_IAV_2.raw","https://storage.jpostdb.org/JPST003525/files/240530QE_Total_Mock_1.raw","https://storage.jpostdb.org/JPST003525/files/240530QE_Total_Mock_3.raw","https://storage.jpostdb.org/JPST003525/files/240529QE_phospho_Mock_1.raw","https://storage.jpostdb.org/JPST003525/files/240529QE_phospho_Mock_3.raw","https://storage.jpostdb.org/JPST003525/files/240530QE_Total_IAV_1.raw","https://storage.jpostdb.org/JPST003525/files/240524HF_Boncat_IAV_2.raw","https://storage.jpostdb.org/JPST003525/files/240529QE_phospho_IAV_1.raw","https://storage.jpostdb.org/JPST003525/files/240524HF_Boncat_Mock_1.raw","https://storage.jpostdb.org/JPST003525/files/240524HF_Boncat_Mock_3.raw","https://storage.jpostdb.org/JPST003525/files/240529QE_phospho_IAV_3.raw","https://storage.jpostdb.org/JPST003525/files/240530QE_Total_IAV_3.raw"],"Mgf":["https://storage.jpostdb.org/JPST003525/files/20240529%20Phospho_Mock%20vs%20IAV_limit500.mgf","https://storage.jpostdb.org/JPST003525/files/20240530_Total_Mock%20vs%20IAV.mgf"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Yayoi Kimura"],"species":["Homo Sapiens (human)"],"full_dataset_link":["https://repository.jpostdb.org/entry/JPST003525"],"submitter_affiliation":["Yokohama City University"],"sample_protocol":[""],"repository":["jPOST"],"data_protocol":[""],"pubmed_abstract":["Profiling of newly synthesized proteins (NSPs) provides access to dynamic changes in protein production that accompany acute cellular responses. Bioorthogonal noncanonical amino acid tagging (BONCAT)-based approaches enable selective labeling of NSPs; however, their broader application remains constrained by labor-intensive enrichment workflows and limited sensitivity for direct peptide-level analysis. Here, we developed a workflow termed \"Phos-tag Click Tip\" by integrating a phosphorylated variant of bicyclononyne (pBCN) with Phos-tag affinity purification to selectively capture azidohomoalanine (AHA)-labeled peptides for newly synthesized proteome analysis (NSProteomics). This approach overcomes key limitations of conventional proteomics and BONCAT-based strategies by enabling efficient enrichment and sensitive detection of NSP-derived peptides. Using this workflow, we performed comprehensive NSP profiling of host cells during influenza A virus infection. We identified dynamic changes in distinct NSP profiles associated with viral replication, host restriction, and immune responses, many of which were not readily detected with conventional whole-cell- or phospho-proteomic analyses. Overall, the Phos-tag Click Tip workflow provides a complementary approach for stimulus-responsive NSP profiling, offering functionally relevant insights into host-virus interactions and cellular response mechanisms."],"pubmed_title":["Selective Enrichment of Newly Synthesized Proteins Using Phos-Tag Click Tip Enables Nascent Proteome Analysis in Influenza A Virus Infection."],"pubmed_authors":["Kimura Yayoi Y, Akiyama Tomoko T, Kobashi Tatsuhiro T, Hosotani Maiko M, Ino Yoko Y, Shin Jihye J, Nakamura Naotoshi N, Kinoshita Eiji E, Miyakawa Kei K, Ryo Akihide A"],"additional_accession":[]},"is_claimable":false,"name":"Selective Enrichment of Newly Synthesized Proteins using Phos-tag Click Tip Enables Nascent Proteome Analysis in Influenza A Virus Infection","description":"Bioorthogonal non-canonical amino acid tagging (BONCAT)-based approaches enable selective labeling of newly synthesized proteins (NSPs). We developed a workflow termed the “Phos-tag Click Tip” by integrating a phosphorylated variant of bicyclononyne (pBCN) with Phos-tag affinity purification to selectively capture azidohomoalanine (AHA)-labeled peptides.\nApplying this workflow, we performed comprehensive NSP profiling of host cells during influenza A virus (IAV) infection. We identified dynamic changes in NSP profiles associated with viral replication, host restriction, and immune responses, many of which were not readily detected by conventional whole-cell or phosphoproteomic analyses.\n","dates":{"publication":"Wed Sep 09 00:00:00 BST 2026"},"accession":"PXD059239","cross_references":{"TAXONOMY":["9606"],"pubmed":["42695899"]}}