{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_00999.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01006.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01011.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_00995.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01010.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_00991.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01007.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01002.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01001.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_00994.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01005.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_00990.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_00997.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01004.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01000.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01009.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01013.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_00993.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_00998.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01003.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_00996.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01012.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_00992.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/esf2_01008.raw"],"Pepxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067066/ip-esf_115_20211216.pep.xml"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["eric_fischer@dfci.harvard.edu"],"submitter":["Eric Fischer"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["Ddx18","Protein degradation","Gluthionylation","E3 ligase","Molecular glue","Dcaf11"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067066"],"tissue":["Cell Culture"],"sample_protocol":["DMSO, CC-885 (positive control, 31.25 µM, 6 µL per well) or pools of 320 drugs (31.25 µM, 6 µL per well) were dispensed into a 96-well plate in triplicate. A total of 1 × 10⁹ frozen cells (8 × 10⁸ Expi293, 5 × 10⁷ K562, 1 × 10⁸ U937, and 5 × 10⁷ Hep3B cells) were resuspended in 20 mL of lysis buffer (50 mM Tris pH 8.0, 200 mM NaCl, 2 mM TCEP, 0.1% NP-40, 2 µL Benzonase (EMD Millipore 77664-3), and one tablet of cOmplete protease inhibitor cocktail). The suspension was sonicated on ice for 20 cycles (3 s on, 5 s off) at 25% amplitude. After centrifugation, 504 µL of each of seven bait proteins (15 µM each) were added to 9.5 mL of clarified lysate. Then, 125 µL of the lysate–protein mixture was added to each well of the pre-plated 96-well PCR plate containing compounds. The plate was incubated on ice for 1 hour, followed by addition of 50 µL pre-washed MagStrep® Strep-Tactin®XT beads (IBA 2-5090-010) to each well (final composition: 90 µL lysate, 6 µL compound pool, 25 µL protein, 50 µL resin; final concentration of each drug: 1.1 µM). The mixture was incubated for an additional hour on ice. Beads were washed using wash buffer (50 mM Tris pH 8.0, 2 mM TCEP) containing the corresponding compound pool, and elution was performed using 0.5 M NaOH. The eluate was immediately neutralized with 0.1 M Tris pH 2.0 to achieve a final pH of 8.5 and a final volume of 200 µL. Samples were reduced with TCEP (final concentration 10 mM) for 30 minutes at room temperature on a thermomixer, followed by alkylation with iodoacetamide (Sigma I1149, final concentration 15 mM) for 45 minutes, protected from light. The reaction was quenched with 1 M DTT (final concentration 10 mM). Subsequently, proteins were digested with 3 µg of Trypsin/Lys-C Mix, Mass Spec Grade (Promega V5072) overnight at 37 °C. Sample digests were acidified with formic acid to a pH of 2-3 prior to desalting using C18 solid phase extraction plates (Thermo Scientific 60307). Desalted peptides were dried in a vacuum-centrifuged and reconstituted in 0.1% formic acid for LC-MS analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data were collected using an Orbitrap Exploris 480 mass spectrometer (Thermo Fisher Scientific) coupled with a UltiMate 3000 RSLCnano System. Peptides were separated on an Aurora 25 cm x 75 μm inner diameter microcapillary column (IonOpticks), and using a 60 min gradient of 5 - 25% acetonitrile in 1.0% formic acid with a flow rate of 250 nL/min. Each analysis used a TopN data-dependent method. The data were acquired using a mass range of m/z 350 – 1200, resolution 60,000, 300% normalized AGC target, auto maximum injection time, dynamic exclusion of 30 sec, and charge states of 2-6. TopN 40 data-dependent MS2 spectra were acquired with a scan range starting at 110 m/z, resolution 15,000, isolation window of 1.4 m/z, HCD normalized collision energy (NCE) set at 30%, standard AGC target and the automatic maximum injection time. Data were collected using an Orbitrap Eclipse mass spectrometer (Thermo Fisher Scientific) coupled with a UltiMate 3000 RSLCnano System. Peptides were separated on a 50 cm 75 μm inner diameter EasySpray ES903 microcapillary column (Thermo Fisher Scientific), and using a 60 min gradient of 6 - 22% acetonitrile or a 60min gradient of 5 – 25% acetonitrile in 1.0% formic acid with a flow rate of 350 nL/min. Each analysis used a cycle time-based data-dependent acquisition method with a total cycle time of 3 s. Full MS1 scans were acquired in the orbitrap at a resolution of 120,000 over a mass range of m/z 375 – 1325, with a maximum injection time of 200 ms and AGC target of 4x105 (normalized 100). Precursors with charge states of 2-6 and intensity above 20,000 were selected for fragmentation, with 30s dynamic exclusion. MS1 scans were acquired in the orbitrap at a resolution of 30,000 using HCD fragmentation with a normalized collision energy of 35%, quadrupole isolation window of 0.5 m/z and 54 ms maximum injection time. The AGC target for MS2 scans was 5x104 (normalized 100), and data were collected in centroid mode. Proteome Discoverer 2.4 or 2.5 (Thermo Fisher Scientific) was used for .RAW file processing and controlling peptide and protein level false discovery rates, assembling proteins from peptides, and protein quantification from peptides. MS/MS spectra were searched against a Swissprot human database (January 2021) with both the forward and reverse sequences as well as known contaminants such as human keratins. Database search criteria were as follows: tryptic with two missed cleavages, a precursor mass tolerance of 10 ppm, fragment ion mass tolerance of 0.03 or 0.06 Da, static alkylation of cysteine (57.0215 Da) and variable oxidation of methionine (15.9949 Da), N-terminal acetylation (42.0106 Da) and with or without phosphorylation of serine, threonine and tyrosine (75.966 Da). Peptides were quantified using the MS1 Intensity, and peptide abundance values were summed to yield the protein abundance values. Resulting data was filtered to only include proteins that had a minimum of 2-3 counts in at least 2-3 replicates of each independent comparison of treatment sample to the DMSO control. Protein abundances were globally normalized using in-house scripts in the R framework (R Development Core Team, 2014). Proteins with missing values were imputed by random selection from a Gaussian distribution either with a mean of the non-missing values for that treatment group or with a mean equal to the median of the background (in cases when all values for a treatment group are missing). Significant changes comparing the relative protein abundance of the treatment to DMSO control comparisons were assessed by two-sided moderated t-test as implemented in the limma package within the R framework(5)."],"omics_type":["Proteomics"],"labhead":["Eric Fischer"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA., Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["eric_fischer@dfci.harvard.edu"],"submitter_affiliation":["Dana-Farber Cancer Institute"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"DCAF11-dependent molecular glue degrader activated by glutathionylation","description":"Targeted protein degradation is a powerful pharmacological strategy that harnesses the ubiquitin proteasome system to eliminate disease-relevant proteins, including otherwise undruggable proteins. Here, we report an unbiased and broadly applicable platform for the systematic discovery of molecular glues across diverse E3 ligases. Using multiplexed mass spectrometry-based chemical screening, we identified a molecular glue, M12, that reprograms the E3 ligase DCAF11 to degrade DDX18. We found that M12 functions as a prodrug, activated by glutathionylation. The glutathione moiety then directly engages DCAF11, enabling neo-substrate recruitment. We demonstrate that this mechanism readily enables targeted degradation of a range of proteins. Our studies highlight a novel approach to redirect E3 ligase function through an enzyme-activated small molecule, expanding the scope of targeted protein degradation and chemically induced proximity.","dates":{"publication":"2026-06-18","submission":"2025-08-07"},"accession":"PXD067066","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:2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