{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/XO44_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/53P4_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/P4_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/DMSO_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/53XO_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/53XO_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/DMSO_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/XO44_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/P4_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/53P4_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/53P4_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/XO44_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/P4_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/DMSO_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/53XO_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/53XO_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/P4_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/53P4_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/XO44_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/DMSO_1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072258/Analysis.zip"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["nir.london@weizmann.ac.il"],"submitter":["Ronen Gabizon"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Btk","Alphafold"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072258"],"tissue":["B Cell","Blood"],"sample_protocol":["Mino cells were treated for 1 h with DMSO 0.1% or 1 \uD835\uDECDM of YS1, followed by 45 min treatment with either 1 \uD835\uDECDM Probe 4 or 2 \uD835\uDECDM XO44, in 4 replicates for each condition. The cells were harvested, washed with ice-cold PBS, and lysed with RIPA buffer (sigma, R0278) supplemented with protease inhibitor cocktail (Sigma, P8340). Protein concentration was determined using BCA protein assay (Thermo Fisher Scientific, 23225). 500 \uD835\uDECDg samples in a total volume of 200 \uD835\uDECDl were prepared. A click reaction was performed in a final volume of 250 \uD835\uDECDl, using final concentrations of 100 \uD835\uDECDM biotin-azide, 4.8 mM THPTA, 0.96 mM CuSO4 and 8 mM sodium ascorbate. Samples were reacted for 1.5 h at room-temperature, followed by methanol-chloroform precipitation. 250 \uD835\uDECDl Chloroform, 750 \uD835\uDECDl water, and 1 ml methanol were added and the samples were vortexed thoroughly and spun-down for 10 min at 4 degrees. The top layer was aspirated, followed by addition of 1 ml methanol. Samples were vortexed and spun-down again for 10 min at 4 degrees, the solution was removed, and the pellet was air-dried. The dry pellets were re-suspended in 250 \uD835\uDECDl of 2.5 % SDS in PBS with sonication (5 pulses, 2 sec on/ 2 sec off, 25% amplitude). Samples were then reduced with 1.25 \uD835\uDECDl of 1 M DTT (40 min at 37 degrees), alkylated with 4.6 \uD835\uDECDl of 0.8 M Iodoacetamide (40 min at room-temperature, protected from light), and then another 7.5 \uD835\uDECDl of 1 M DTT were added. The samples were diluted 20-fold with PBS, and 20 \uD835\uDECDl of PBS pre-washed Streptavidin beads were added (Cytiba, Streptavidin Sepharose High Performance, 17511301). The samples were rotated for 3 h in room-temperature. The samples were spun-down (2000 g, 3 min), the supernatant was removed and the beads were washed x3 times with 0.1% SDS in PBS, x5 times with 20% methanol, twice with 2M NaCl in PBS, once with PBS and x3 times with water. The beads were transferred to new tubes with 200 \uD835\uDECDl of 100 mM Ammonium bicarbonate, 1 \uD835\uDECDl of 0.5 \uD835\uDECDg/\uD835\uDECDl sequencing-grade trypsin were added (Promega, V5111), and samples were incubated overnight at 37 degrees with shaking. The samples were spun-down, and the supernatant was collected to new tubes. The beads were then washed with 200 \uD835\uDECDl of 100 mM Ammonium bicarbonate + 2M NaCl, which were combined with the previous supernatant. TFA was added to a final concentration of 0.1% to each sample, and the samples were desalted by Oasis (Waters) and dried using speed-vac.   The samples were dissolved in 30 \uD835\uDECDl of 0.1% formic acid in 3% acetonitrile, and 3 \uD835\uDECDl were injected per run. Samples were analyzed using EASY-nLC 1200 nano-flow UPLC system, using PepMap RSLC C18 column (2 µm particle size, 100 Å pore size, 75 µm diameter × 50 cm length), mounted using an EASY-Spray source onto an Exploris 240 mass spectrometer. µLC/MS-grade solvents were used for all chromatographic steps at 300 nL/min. The mobile phase was: (A) H2O + 0.1% formic acid and (B) 80% acetonitrile + 0.1% formic acid. Peptides were eluted from the column into the mass spectrometer using the following gradient: 1–40% B in 160 min, 40–100% B in 5 min, maintained at 100% for 20 min, 100 to 1% in 10 min, and finally 1% for 5 min. Ionization was achieved using a 1800 V spray voltage with an ion transfer tube temperature of 275 °C. MS1 spectra were collected at a resolution of 60,000 at 200 m/z, a mass range of 370–1450 m/z, normalized AGC of 300%, and the maximum injection time was set to 20 ms. Data were collected by data-independent acquisition, with MS2 resolution set to 30,000, with 32 isolation windows of 17 Da with a 1 Da overlap covering precursor m/z of 390-920, maximum injection time of 50 ms, and HCD collision energy at 27%. Four samples were analyzed per condition."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["he data were processed using DIA-NN (version 2.2). First, a theoretical spectral library was generated from a fasta file containing the human proteome, streptavidin, trypsin and common contaminants. The number of missed cleavage was set to 1. The data were then analyzed against this spectral library using the following additional settings: Qvalue = 0.001;  --matrix-qvalue [10]  --matrix-spec-q [10]  --restrict-fr. The rest of the settings were standard. The resulting data was analyzed using Perseus as follows: Intensity values were converted to Log2 values, the different quadruplicates were grouped and any protein for which at least 3 valid intensity values were measured for at least one of the groups was discarded from the data (968 proteins out of 4384). Missing values were then replaced with a value of 14, which corresponds to the lower limit of the measured intensity distribution. The groups were then compared using two sided t test, and the calculated differences and P-values were used to plot the volcano plots. To determine which proteins were pulled down by the probe and competed by YS1, we filtered the data to contain only proteins for which the Log2 difference between the probe treated set and DMSO-treated set was > 2 with a P-value < 0.01, and for which the Log2 difference between the probe treated set and the competed set was > 2 with a P–value < 0.01."],"omics_type":["Proteomics"],"labhead":["Nir London"],"instrument_platform":[""],"labhead_affiliation":["Department of Chemical and Structural Biology, Weizmann Institute"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["41857796 Shamir Y, Gabizon R, Rogel A, Lin DY, Andreotti AH, London N. Discovery of Covalent Ligands with AlphaFold3. J Am Chem Soc. 2026 148(12):13043-13054 10.1021/jacs.5c22222"],"submitter_mail":["ronen.gabizon@weizmann.ac.il"],"submitter_affiliation":["Department of Chemical and Structural Biology, Weizmann Institute of Science"],"submitter_country":["Israel"],"pubmed_abstract":["Covalent inhibitors are a prominent modality for research and therapeutic tools. However, a scarcity of computational methods for their discovery slows progress in this field. AI models such as AlphaFold3 (AF3) have shown accuracy in ligand pose prediction, but their applicability for virtual screening campaigns was not assessed. We show that AF3 cofolding predictions and an associated predicted confidence metric ranks true covalent binders with near-optimal classification over property-matched decoys, significantly outperforming state-of-the-art covalent docking tools for a set of protein kinases. In a prospective virtual screening campaign against the model kinase BTK, we discovered a chemically distinct, novel, covalent small molecule that displays potent inhibition <i>in vitro</i> and in cells while maintaining marked kinome and proteomic selectivity. Co-crystallography validated the subangstrom accuracy of the predicted AF3 binding mode. These results demonstrate that AF3 can be practically used to discover novel chemical matter for kinases, one of the most prolific families of drug targets."],"pubmed_title":["Discovery of Covalent Ligands with AlphaFold3."],"pubmed_authors":["Shamir Yoav Y, Gabizon Ronen R, Rogel Adi A, Lin David Yin-Wei DY, Andreotti Amy H AH, London Nir N"],"additional_accession":[]},"is_claimable":false,"name":"Discovery of novel covalent ligands with AlphaFold3","description":"Covalent inhibitors are a prominent modality for research and therapeutic tools. However, a scarcity of computational methods for their discovery slows progress in this field. AI models such as AlphaFold3 (AF3) have shown accuracy in ligand pose prediction, but their applicability for virtual screening campaigns was not assessed. We show that AF3 co-folding predictions and an associated predicted confidence metric ranks true covalent binders with near-optimal classification over property-matched decoys, significantly outperforming state-of-the-art covalent docking tools for a set of protein kinases. In a prospective virtual screening campaign against the model kinase BTK, we discovered a chemically distinct, novel, covalent small molecule that displays potent inhibition in vitro and in cells while maintaining marked kinome and proteomic selectivity. Co-crystallography validated the sub-angstrom accuracy of the predicted AF3 binding mode. These results demonstrate that AF3 can be practically used to discover novel chemical matter for kinases, one of the most prolific families of drug 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