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The four oxidant conditions used were no oxidant, 1.2 mM PMSF and 40 mM Na3VO4, 4 mM PMSF and 60 mM Na3VO4, and 5 mM pervanadate. On day 2, 2x stocks of IGEPAL lysis buffers were prepared without PMSF or Na3VO4 and with Tris pH 8.0 for eventual lysis with no oxidant or 5 mM pervanadate and with Tris pH 6.0 for eventual lysis in 1.2 mM PMSF plus 40 mM Na3VO4 or 4 mM PMSF plus 60 mM Na3VO4 because Na3VO4 is basic. See “Lysis buffer components: 0.5% IGEPAL lysis buffer” for making 1x IGEPAL lysis buffer. 40 mM pervanadate was prepared fresh for each technical replicate and immediately prior to use as described in “Preparation of select reagents: Preparation of pervanadate”. 1x lysis buffers for each oxidant condition were prepared immediately prior to lysis of each technical replicate by adding water, PMSF, Na3VO4, and/or pervanadate aliquots of the 2x IGEPAL lysis buffer. Within each technical replicate, cells were washed once on ice in cold PBS, then lysed on ice in the fume hood in 1 ml/plate of the respective lysis buffer. Cells were immediately scraped and approximately 5 minutes after lysis, 990 ul lysate was added to a 1.5 ml sample tube containing 10 µl of 100 mM N-hex-5-ynyl-2-iodoacetamide (iodoacetamide-alkyne, IAA; Oakwood Chemicals, 95226) for a final concentration of 1 mM IAA. Samples were incubated for 15 minutes in the dark at room temperature, with shaking at 750 rpm on an Eppendorf ThermoMixer C, prior to snap freezing in liquid nitrogen.   IAA-labeled proteins were thawed and conjugated to DADPS-biotin-azide to enable streptavidin enrichment and acid-mediated peptide release, thereby improving proteomic depth by eliminating endogenously biotinylated species. After protein quantification, 1.1 mg of total protein from each sample was subjected to biotinylation. Samples were adjusted to a final volume of 700 µL with lysis buffer. To derivatize biotin on labeled cysteine residues, 15 µL of 50 mM dialkoxydiphenylsilane (DADPS) biotin azide (Vector Laboratories, Cat# CCT-1330) and 300 µL of copper-catalyzed click reaction premix were added to initiate the copper click reaction. The premix consisted of 100 µL 100 mM Tris-hydroxypropyltriazolylmethylamine, 100 µL 20 mM CuSO₄, and 100 µL 300 mM sodium ascorbate. Click chemistry reactions were done for 1.5 h at 25 °C in the dark with agitation at 750 rpm. To remove unreacted chemicals, 600 µL ice-cold methanol and 100 µL chloroform were added, and the mixture was vortexed briefly. White and cloudy precipitated proteins were centrifuged at 20,000 × g for 10 min at 4 °C, and the upper aqueous phase was carefully discarded. The protein pellet was washed with 1,000 µL ice-cold methanol, then centrifuged (20,000 × g, 10 min, 4 °C) and the supernatant removed. This methanol wash step was repeated, and the protein pellet was subsequently air-dried for at least 15 min. [Bead enrichment] The dried protein pellet was reconstituted in 600 µL 2.5% SDS/PBS buffer and allowed to dissolve completely (typically 30 min, variable by sample). After quantification, the same amount of biotinylated samples was taken, and the volume was adjusted to the same using 2.5% SDS/PBS buffer. The sample was transferred to a 15 mL conical tube and diluted with PBS to reduce SDS concentration to below 0.125%. Streptavidin Sepharose High Performance beads (200 µL) were added, and samples were incubated overnight at 4 °C with rotation. Beads were pelleted by centrifugation at 1,700 ×g for 5 min, washed sequentially (2 times each) with 1% SDS/PBS (1 mL), PBS (1 mL), 6 M urea (1 mL), and PBS (1 mL), with centrifugation at 1,700 × g for 3 min between washes. Beads were resuspended in 700 µL 100 mM ammonium bicarbonate (ABC). Proteins were subsequently incubated with 7 µL of 0.5 M DTT at room temperature (RT) for 30 min at 750 rpm and 14 µL of 0.5 M iodoacetamide in the dark at RT for 30 min. Next, 0.7 µL of 1 M CaCl₂ and 2 µg MS-grade trypsin were added, and digestion proceeded overnight at 37 °C (16 h). [Elution] After digestion, the beads were centrifuged again at 1,700 × g for 3 min, and the supernatant was carefully removed without disturbing the beads. Beads were washed twice with PBS, followed by two washes with LC-grade H2O washing. The beads were resuspended in 1 mL of 2% formic acid and incubated for 2 hours in a thermomixer (25 ºC, 1250 rpm). The formic acid solution containing eluted peptides was transferred to a new 1.5 mL LoBind Eppendorf microtube after the beads were pelleted (2,000 x g, 5 min). The beads were additionally incubated with 300 µL 1:1 acetonitrile:2% formic acid solution for 30 min, and the solution was collected in the same microtube. The eluted peptide (total 1.4 mL) was lyophilized under speed-vac and desalted using a C18 column before going on injection to the mass spectrometry."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["[DIA Database Search & Quantification] Raw DIA data were processed and analyzed using Spectronaut version 18 (Biognosys AG, Switzerland) with default parameters. Searches were performed against the Homo sapiens proteome (UniProtKB/Swiss-Prot Reviewed; UP000005640_9606, 20,654 entries). Retention time prediction was performed using dynamic iRT calibration. Spectronaut dynamically determined optimal extraction windows based on extensive mass calibration, iRT alignment, and gradient stability. False discovery rate (FDR) thresholds were set to 1% at both the precursor and protein levels. Decoy generation was configured as “mutated,” in which a random number of amino acid position swaps (minimum of 2, maximum of half the peptide length) were introduced. Local normalization was applied for quantitative analysis. Peptides passing the 1% Q-value cutoff were used to calculate protein group intensities using the MaxLFQ algorithm. For N-hex-5-ynyl-2-iodoacetamide-labeled cysteine residues, C₁₄H₂₄N₄O₂ (m/z 280.19047) was included as a variable modification. Non-imputable peptides identified under the background imputation setting were regarded as background noise and excluded from the dataset. [Data processing] Cysteine residue numbers were appended to each peptide by matching the associated protein IDs against the reviewed and unreviewed canonical sequences in UP000005640. If the peptide matched to more than on protein ID, the cysteine location in both IDs is reported. If an ID was not present in the reference proteome, the position was reported as “ambiguous” and the peptide was matched against the entire proteome, with its location in each matched protein reported.  Cysteines that were fully oxidized would not be labeled by iodoacetamide and therefore not detected in the mass spectrometry analysis. To filter out noise in this context, peptides were kept for further analysis if all three replicates within at least one condition had detected peak areas (i.e. not “NaN”). 1,229 peptides of the original 33,525 were removed with this filter. Missed trypsinization events were then accounted for if peptides shared the same Uniprot ID, cysteine position(s), and modification(s) by summing peak area intensities per sample and compressing the combined peptides into one line of data. A “ | “ between peptides in columns D and E of Table indicates the peak area data are a summation of those peptides from the Spectronaut output. This compressed the data by 6,431 rows to 25,865."],"omics_type":["Proteomics"],"labhead":["Iok In Christine Chio"],"instrument_platform":[""],"labhead_affiliation":["Institute of Cancer Genetics, Columbia University Medical Center"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["jn2837@cumc.columbia.edu"],"submitter_affiliation":["Columbia University Medical Center"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"PMSF/vanadate oxidation effect on Human PANC-1 cells","description":"Cysteines play critical roles in redox regulation and can be covalently engaged by electrophiles to inform on cysteine function and targetability. Here, we compare cysteine engagement by a PMSF/orthovanadate-derived oxidant with that of pervanadate, another vanadium-based 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