{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075129/checksum.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075129/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075129/QinZ_102623_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075129/QinZ_102623_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075129/QinZ_102623_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075129/QinZ_102623_01.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075129/2023_04_UniProt_Homo_sapiens.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD075129/MaxQuant.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["zqin@uams.edu"],"submitter":["Zhen Lin"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Kshv","Mz-1","Jq-1","Sim-1","Brd4"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075129"],"tissue":["Endothelial Cell Of Umbilical Vein"],"sample_protocol":["Protein samples were reduced, alkylated, and purified by chloroform/methanol extraction prior to digestion with sequencing grade modified porcine trypsin (Promega). Tryptic peptides were then separated by reverse phase XSelect CSH C18 2.5 um resin (Waters) on an in-line 150 x 0.075 mm column using an UltiMate 3000 RSLCnano system (Thermo). Peptides were eluted using a 90 min gradient from 98:2 to 65:35 buffer A:B ratio. Eluted peptides were ionized by electrospray (2.4 kV) followed by mass spectrometric analysis on an Orbitrap Eclipse Tribrid mass spectrometer (Thermo). MS data were acquired using the FTMS analyzer in profile mode at a resolution of 120,000 over a range of 375 to 1200 m/z. Following HCD activation, MS/MS data were acquired using the ion trap analyzer in centroid mode and normal mass range with a normalized collision energy of 30%."],"repository":["pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Proteins were identified by database search using MaxQuant (Max Planck Institute) with a parent ion tolerance of 3 ppm and a fragment ion tolerance of 0.5 Da. Scaffold Q+S (Proteome Software) was used to verify MS/MS based peptide and protein identifications. Protein identifications were accepted if they could be established with less than 1.0% false discovery and contained at least 2 identified peptides. Protein probabilities were assigned by the Protein Prophet algorithm [Anal. Chem. 75: 4646-58 (2003)]."],"omics_type":["Proteomics"],"labhead":["Zhiqiang Qin"],"instrument_platform":[""],"labhead_affiliation":["Department of Pathology Winthrop P. Rockefeller Cancer Institute University of Arkansas for Medical Sciences"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["zlin@tulane.edu"],"publication":["42224297 Chen J, Fan J, Qin M, Lin Z, Mu S, Dai L, Qin Z. Targeting BRD2 and BRD4 inhibit the growth of KSHV-infected immortalized endothelial cells through suppression of LANA translation. PLoS Pathog. 2026 22(6):e1014288 10.1371/journal.ppat.1014288"],"submitter_affiliation":["Tulane University"],"submitter_country":["United States"],"pubmed_abstract":["Kaposi's sarcoma-associated herpesvirus (KSHV) is the etiologic agent of several human cancers, including Kaposi's sarcoma (KS) and primary effusion lymphoma (PEL), both of which still lack effective treatment options. Members of the bromodomain and extra-terminal domain (BET) family, especially bromodomain-containing protein 4 (BRD4), play important roles in RNA polymerase II-mediated transcriptional regulation and are required for the expression of many tumor-driving oncogenes in various cancer cells. Therefore, BET proteins have become attractive targets for anticancer drug development. Previous studies have demonstrated the high sensitivity of PEL cells to BET inhibitors, and BRD4 silencing effectively blocks tumor cell proliferation. In contrast, KSHV-infected immortalized endothelial cells display strong resistance to BET inhibitors, including (+)-JQ1. To further develop BRD-targeted therapies for KSHV-infected immortalized endothelial cells, we identified MZ-1 and SIM-1, two BRD4 PROTAC degraders, as effective inhibitors of cell growth in these cells. Mechanistically, these inhibitory effects depend on suppression of LANA translation through increased eIF2α phosphorylation in KSHV-infected cells. Similar LANA suppression was also observed following RNAi-mediated silencing of BRD2 or BRD4. Proteomic analysis identified unique protein candidates altered in MZ-1- and SIM-1-treated KSHV-infected immortalized endothelial cells compared with (+)-JQ1-treated cells. In summary, our study develops an effective strategy against KSHV-infected immortalized endothelial cells using selective BRD PROTACs, which may help improve therapeutic outcomes for KSHV-related malignancies in the future."],"pubmed_title":["Targeting BRD2 and BRD4 inhibit the growth of KSHV-infected immortalized endothelial cells through suppression of LANA translation."],"pubmed_authors":["Chen Jungang J, Fan Jiaojiao J, Qin Margaret M, Lin Zhen Z, Mu Shengyu S, Dai Lu L, Qin Zhiqiang Z"],"additional_accession":[]},"is_claimable":false,"name":"Human proteomics analysis of BRD4 targeted small-molecules in KSHV+ cells by Orbitrap Eclipse and MaxQuant","description":"In this project, we used proteomics to identify and compare protein profile changed in SIM-1, MZ-1, or JQ-1 treated TIVE-LTC, a KSHV long-term infected immortalized endothelial cell 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