{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/diann_report.pg_matrix_chromatin.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/diann_report.pr_matrix_lysate.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/diann_report.pr_matrix_chromatin.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/diann_report.pg_matrix_lysate.tsv"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/tf_updated.csv"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_JWJ378_0-1uM_2hr_Lysate_REP3.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_JWJ378_0-1uM_6hr_Lysate_REP1.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_CG428_0-1uM_2hr_Lysate_REP2.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_JWJ378_0-1uM_6hr_Lysate_REP3.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_DMSO_6hr_Lysate_REP3.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_DMSO_2hr_Lysate_REP3.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_DMSO_6hr_Lysate_redo.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_JWJ378_0-1uM_2hr_Lysate_REP2.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_JWJ378_0-1uM_6hr_Lysate_REP2.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_CG428_0-1uM_6hr_Lysate_REP1.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_CG428_0-1uM_2hr_Lysate_REP1.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_CG428_0-1uM_6hr_Lysate_REP2.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_DMSO_2hr_Lysate_REP1.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_CG428_0-1uM_6hr_Lysate_REP3.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_JWJ378_0-1uM_2hr_Lysate_REP1.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_CG428_0-1uM_2hr_Lysate_REP3.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_DMSO_2hr_Lysate_REP2.d.tar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065035/241220_DMSO_6hr_Lysate_REP1.d.tar"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["afederation@talus.bio"],"submitter":["Sebastian Paez"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Colon Cancer"],"software":[""],"submitter_keywords":["Lc-msms","Colorectal cancer","Timstof"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065035"],"tissue":["Cell Culture","Colon"],"sample_protocol":["KM-12 cells were seeded in 96-well plates and treated with a variety of compounds at multiple concentrations and timepoints (following dataset only includes compounds, concentration, and timepoint listed in description). After treatment, cell nuclei were isolated using 10 mM Tris with 15 mM NaCl, 60 mM KCl, and benzonase prior to protein digestion. Proteins were digested into peptides using a high-throughput SP3 protocol using a KingFisher Apex. Peptides were loaded onto EvoTips and analyzed by DIA-LCMS on a timsTOF Ultra 2 mass spectrometer and separated over a 22 minute gradient."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data was analyzed using QuantMS-nextflow. In brief, the data was analyzed using DIA-NN with the attached configuration file."],"omics_type":["Proteomics"],"labhead":["Alexander Federation"],"instrument_platform":[""],"labhead_affiliation":["Talus Bio"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["spaez@talus.bio"],"publication":["41908584 Kumar S, Jiang J, Donald-Paladino MS, Chen J, Gutierrez A, Federation AJ, Szulzewsky F, Holland EC, Ferguson FM, Nabet B. Development of PROTACs for targeted degradation of oncogenic TRK fusions. RSC Chem Biol. 2026 10.1039/d6cb00008h"],"submitter_affiliation":["Talus Bioscience"],"submitter_country":["United States"],"pubmed_abstract":["Chromosomal translocations leading to the fusion of tropomyosin receptor kinases (TRKs) with diverse partner proteins have been identified as oncogenic drivers in many adult and pediatric cancers. While first-generation TRK kinase inhibitors, such as entrectinib and larotrectinib, have shown positive responses in TRK fusion-positive cancers, resistance mutations against these inhibitors in the kinase domain limit their efficacy. Second-generation inhibitors are in clinical evaluation, highlighting a need for novel therapeutic modalities to achieve durable suppression of the oncogenic activity of TRK fusions. Here, we developed heterobifunctional small molecule degraders (PROTACs) to achieve targeted degradation of TRK fusions. By conjugating entrectinib to thalidomide, we identified JWJ-01-378 as a potent and selective cereblon (CRBN)-recruiting degrader of the TPM3-TRKA fusion. JWJ-01-378 induced TPM3-TRKA degradation through the ubiquitin-proteasome system and proteomics analysis confirmed the acute selectivity of JWJ-01-378 for achieving TPM3-TRKA degradation with minimal off-target effects. Importantly, JWJ-01-378 did not degrade CRBN neosubstrates that are targeted by existing TRK PROTACs including CG-428. While JWJ-01-378 was also able to degrade wild-type TRK, it was unable to degrade TRK inhibitor resistant mutants and ALK fusions. TPM3-TRKA degradation by JWJ-01-378 suppressed downstream signaling and reduced cancer cell viability, with improved responses compared to a heterobifunctional control compound that cannot degrade TPM3-TRKA. Together, our study expands the toolbox of selective compounds for evaluating targeted degradation of TRK fusions in diseases including cancer."],"pubmed_title":["Development of PROTACs for targeted degradation of oncogenic TRK fusions."],"pubmed_authors":["Kumar Saurav S, Jiang Jiewei J, Donald-Paladino Mia S MS, Chen Joy J, Gutierrez Andrea A, Federation Alexander J AJ, Szulzewsky Frank F, Holland Eric C EC, Ferguson Fleur M FM, Nabet Behnam B"],"additional_accession":[]},"is_claimable":false,"name":"KM-12 Whole Cell Lysate Proteomics","description":"The KM-12 cell line, representative of colorectal cancer indications, was used to explore the effect that multiple compounds would have in the profile of transcription factor occupancy. Cells were dosed with 3 concentrations of each of the 5 compounds provided for 3 different timepoints. Both a chromatin fraction (ChESS) and a whole cell lysate preparation were performed. Resulting proteins were digested via SP3 digestion and resulting peptides were analyzed by data independent acquisition liquid chromatography mass spectrometry. (DIA-LCMS) in order to determine the effects of each of the provided compounds in both chromatin and whole cell lysate matrices on a variety of transcription factor proteins. The following dataset includes data corresponding to peptides resulting from nuclear isolation after a 6 hour treatment with 100 nanomolar concentration CG-428 (positive control, published TRK PROTAC), JWJ-378 (novel PROTAC developed by Nabet lab), and DMSO (negative 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