{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_Malondialdeyde_Feb2024.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20260213_AV_500_Rebuttal.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_BenAdd_MDA_MW_160.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_BisMDA_MW_196.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_BenAdd_MW_88.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_MDA_MW_54.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_100B.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_500B.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_1000A.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_250B.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_250A.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20260213_AV_178_500_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_100A.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_1000B.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_500A.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_2000A.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20260213_AV_178_Control.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_2000B.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_Control.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20260213_AV_178_500_2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20260213_AV_500_Rebuttal.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_BenAdd_MW_88.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_MDA_MW_54.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_BenAdd_MDA_MW_160.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_BisMDA_MW_196.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067614/20250220_AV_Malondialdeyde_Feb2024.pdResult"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["monika.raj@emory.edu"],"submitter":["Riley Hughes"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067614"],"tissue":["Cell Culture"],"sample_protocol":["To 5 tubes (individual reactions) of 100 µg of lysate in 300 µL of MeCN:H2O (1:4) were treated with freshly prepared solution of MDA-Benzaldehyde intermediate (100 µM, 250 µM, 500 µM, 1 mM, and 2 mM). The reaction was stirred at 40 °C for 20 h. The proteins were acetone precipitated, followed by digestion using SMART Digest™ Trypsin Kit by Thermo Scientific. Digested samples were resuspended in Buffer A (0.1% FA in water), and the peptide amount was determined by Pierce™ Quantitative Peptide Assays & Standards (Thermo Fisher Scientific) according to manufacturer instructions. Samples were injected into the Vanquish Neo UHPLC (Thermo Scientifc) coupled to an Exploris 480 mass-spectrometer (Thermo Scientific). The peptides were loaded on a 50 cm EASY-Spray PepMap Neo C18 column (Thermo Scientific) and chromatographic separation was achieved using a linear gradient starting with a flow rate of 300 nL/min from 6% Buffer B (0.1% FA in 80% ACN) and increasing to 55% in 90 min. The mass-spectrometer operated in positive polarity for data collection using a data-dependent acquisition (DDA) mode with a 3 second cycle time. All spectra were acquired within an m/z range of 350 to 1500, and HCD collision energy was set to 30%."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw mass spectrometry (MS) files were processed using Proteome Discoverer (version 3.2; Thermo Fisher Scientific) with the integrated search engine. Database searches were performed against the human UniProt Swiss-Prot database (20,456 entries) appended with common contaminants. Variable modifications included N-terminal acetylation, methionine oxidation, and a mass shift of +196.005 Da on lysine residues or N-termini to account for the MDA-benzaldehyde adduct. Carbamidomethylation of cysteine was set as a fixed modification. Trypsin was specified as the proteolytic enzyme, allowing up to two missed cleavages. Peptides were filtered to lengths of 7–50 amino acids and masses of 500–5,000 Da. For MS2-based quantification, precursor mass tolerance was set to 20 ppm, and fragment mass tolerance to 0.02 Da. Peptide-spectrum matches (PSMs) and protein identifications were validated using Percolator within the Philosopher toolkit (version 5.0), with false discovery rates (FDRs) controlled at 1% for both PSMs and proteins. Label-free quantification was performed, using precursor ion intensities. Protein abundances were calculated based on the sum of unique peptide intensities, requiring at least two unique peptides per protein for quantification. All downstream statistical analyses were conducted in R (version 4.4.2). Protein intensities were normalized per sample to the mean intensity across all quantified peptides to account for technical variability."],"omics_type":["Proteomics"],"labhead":["Monika Raj"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Emory University, Department of Chemistry"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["riley.hughes@emory.edu"],"submitter_affiliation":["Emory University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Cooperative Aldehyde Chemistry Maps an Orthogonal Lysine Reactivity Landscape","description":"Reactive metabolites are often associated with nonspecific protein damage, if harnessed cooperatively they could be repurposed into precision tools for targeted labeling, redefining how we probe and manipulate protein function in complex biological systems. Here, we introduce a bioinspired cooperative metabolite strategy that harnesses the synergistic chemistry of malondialdehyde (MDA) and monoaldehydes to generate highly reactive intermediates that selectively modify lysine residues across proteins and proteomes. Dose-dependent chemoproteomic profiling of proteins modified by MDA-monoaldehyde complexes reveals 245 peptides and 167 unique proteins commonly modified in all doses. Among these, nearly 100 proteins feature a single modification at only hyperreactive lysine residue, indicating distinct microenvironmental features that enhance lysine reactivity and selectivity toward cooperative metabolite modification. Captured proteins were found to be linked to disease pathways and environmental exposures, revealing previously unrecognized patterns of metabolic susceptibility. ","dates":{"publication":"2026-04-14","submission":"2025-08-22"},"accession":"PXD067614","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:625351","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:6819","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:36630","NEWT:383379","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","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:410658","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:3714","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:3704","NEWT:244366","NEWT:1246791","NEWT:176597","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:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","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:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","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:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","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:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","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:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1045775","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:1028307","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","N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