{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/combined_peptide.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/combined_protein.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/Read_Me.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F2_1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F25_2.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F10_2.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F51_3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_DMSO_3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F37_1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/fragpipe.workflow","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F51_1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_DMSO_1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/fragger.params","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_2.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F10_1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F37_3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F25_1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F2_3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F25_3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_DMSO_2.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F2_2.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F10_3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F51_2.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072598/HeLa_IAA_F37_2.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["A.S.Nelson@leeds.ac.uk"],"submitter":["Julian Chesti"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Cervix Carcinoma"],"software":[""],"submitter_keywords":["Covalent fragment screening","Pull-down proteomics","Dda-pasef","Pentafluorobenzenesulfonamide","Label-free quantification","Iodoacetamide alkyne"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072598"],"tissue":["Epithelial Cell","Hela Cell"],"sample_protocol":["HeLa cell lysate (440 µg, 1 mg/mL) was treated with a corresponding pentafluorobenzenesulfonamide reactive fragment (50 µM) for 1 hr at 25 °C, followed by a 1 hr incubation with N-hex-5-ynyl-2-iodo-acetamide (25 µM). Trypsin cleavable biotin azide (AzRB) was then conjugated to the alkyne, and the labelled proteome was enriched with high-capacity NeutrAvidin beads. Affinity-enriched proteins were denatured on-bead with TCEP (12.5 mM) and alkylated with iodoacetamide (18.75 mM). Peptides generated from an overnight trypsin (5 µg) digestion were then analysed by timsTOF LC-MS/MS in DDA-PASEF mode."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["DDA data was processed on Fragpipe (version 22.0) with  MSFragger, IonQuant, diaTracer, DIA-NN, Python, Database Splitting and Spectral Library Generation add-ins. The built-in workflow LFQ-MBR was used with the following modifications:  Under the Database tab the appropriate .fasta file was uploaded from UniProt (UP000005640 Homo sapiens (Human)) and decoys were added.  Under the MSFragger tab Run MSFragger was checked, and in Common Options > Peak Matching > Precursor mass tolerance, Da was selected from the dropdown menu and the range was set to -150 - 1,000. Fragment mass tolerance was set to 20 PPM. Protein Digestion under Enzyme name 1, trypsin was added. Under No Cuts 1, P was added and under Mixed Cleavages 1, 2 was added. Under Modifications > Variable Modifications, Cysteine was added and checked. This was achieved by inserting C under Site (editable), 57.02146 under Mass (editable), and 3 was selected under the Max occurrences (editable) column. Under Fixed Modifications, Cysteine remained unchecked in the available menu.   In the tab Validation > Crystal-C was unchecked together with RunMSBoost under Rescoring Using Deep Learning Prediction.   Under Quant (MS1) > Advanced Options > Match between runs (MBR) > MBR top runs was set to 2.   Perseus (version 2.0.7.0) was used to analyse data outputs from FragPipe by opening the combined_protein.tsv file. The following workflow was used;  MaxLFQ Intensity of relative samples were selected and moved to the column Main using the provided arrows. Protein, Protein ID, Description and Gene were added to the Text column in the same manner.   Contaminants were removed by selecting the Filter rows based on text column in the Filter rows drop down menu. In the new interface under Search string, contam was added.  A log2 transformation was then carried out on the data. Further processing was carried out by selecting Filter rows based on valid values, under Min. Valids > Min. Number was set to 3.   Missing values in the dataset were then replaced by using the Replace missing values from normal distribution function. Finally, experimental replicates were then combined using Annot. rows > Categorical annotation rows. IAA-treated control samples were combined separately to samples treated with the competitors followed IAA. To visualise the results, either depletion or enrichment of the proteome, a t-test and volcano plot were generated by selecting the appropriate icon. For the visualisation of depleted proteins, under Grouping > First group (right), the competition sample was selected. In the Second group (left) the IAA-treated controls were selected to generate the volcano plot."],"omics_type":["Proteomics"],"labhead":["Adam Nelson"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Professor of Chemical Biology, School of Chemistry, University of Leeds, United Kingdom"],"species":["Homo Sapiens (human)"],"submitter_mail":["nmsv885@leeds.ac.uk"],"publication":["10.1002/CHEM.202600009"],"submitter_affiliation":["University of Leeds"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Proteome-wide Profiling of Diverse Pentafluorobenzenesulfonamide Reactive Fragments","description":"A unified synthesis of diverse pentafluorobenzenesulfonamide reactive fragments was developed which was based on the reaction between diverse, readily-available substrates and rhodium nitrenoid intermediates formed from pentafluorobenzenesulfonamide.  The approach enabled the synthesis of 21 reactive fragments whose diversity stemmed from both that of the substrates, and the rich chemistry of rhodium nitrenoids.  Five of the reactive fragments were profiled against HeLa cell lysate, which demonstrated that the constellation of modified proteins was critically dependent on the specific reactive fragment 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