{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/bLacLysMS1_FLASHDeconv.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/bLacBSAMS1_FLASHDeconv.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/LysozymeMS1_FLASHDeconv.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Mix_bLacLys_MS2_HCD.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS3_997p87_PTCR.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS2_1060p18.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/BSA_highres_MS1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS3_1060p18_1130p85.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Mix_bLacLys_MS2_PTCR.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS2_HCD_final.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Mix_bLacLys_MS1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Mix_bLacBSA_MS2_HCD.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Mix_bLacBSA_MS3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Mix_bLacBSA_MS1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS2_997p87.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS2_1060p18_PTCR.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS3_997p87_1060p24.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS2_892p94.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Mix_bLacLys_MS3_Lysozyme.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS3_892p94_PTCR.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS3_892p94_942p49.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Mix_bLacLys_MS3_bLac.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Lysozyme_MS2_PTCR.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074730/Mix_bLacBSA_MS2_PTCR.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["a.tholey@iem.uni-kiel.de"],"submitter":["Andreas Tholey"],"technology_type":["Mass Spectrometry","Top-down proteomics"],"software":["Not available"],"submitter_keywords":["Proton transfer charge reduction","Proteoform","Quantification","Top-down proteomics","Isobaric labeling"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074730"],"sample_protocol":["Model proteins (bovine serum albumin (BSA), lysozyme, and β-lactoglobulin), chemical reagents, and solvents were purchased from Sigma-Aldrich (St. Louis, Missouri, USA) if not stated otherwise. Cysteine-directed tandem mass tags (iodoTMT, sixplex) was from Thermo Fisher Scientific (San Jose, USA). Deionized water (18.2 MΩ cm-1) was prepared by an Arium611 VF system (Sartorius, Göttingen, Germany).  The cysteine-iodoTMT sixplex labeling was performed as previously described. In brief, each of the three model proteins was aliquoted to 2×40 µg in 40 µl 6.4 M guanidinium hydrochloride, 200 mM triethylammonium bicarbonate (pH=8.5). Proteoform reduction was performed by adding 1 µl 100 mM TCEP (37 °C, 800 rpm, 50 min). Each one of the aliquots was labeled with iodoTMT channels 128 and 130, respectively. Only two reporter channels were selected because the objective of this study was to assess the quantitative performance rather than to demonstrate multiplexing capacity. For labeling, the iodoTMT reagents were first dissolved in 20 µl of methanol, and 5 µl were added to the samples. Then, the samples were incubated for 50 min at 20 °C and 800 rpm in the dark. Quenching of the reaction was performed by adding 1 µl 100 mM DTT (20 °C, 800 rpm, 50 min). The labelled proteins were combined (channels 128:130; lysozyme 1:1 (v/v), BSA 2:1, β-lactoglobulin 1:2) and purified by methanol-chloroform-water precipitation. Prior to MS analysis, the proteins were resuspended in 50% (v/v) acetonitrile, 1% (v/v) formic acid to a final concentration of ~0.2 mg/ml. Direct-infusion mass spectrometry experiments were performed using an Orbitrap Eclipse Tribrid mass spectrometer (Thermo Fisher Scientific, San Jose, USA) equipped with a heated electrospray ionization source. A flow rate of 3-5 µl/min was delivered using a syringe pump (model F100T2, Chemyx Inc, Stafford, Texas, USA). The typical ion source settings were: spray voltage of +3.5 kV, ion transfer tube temperature of 275 °C, and sheath and auxiliary gas enabled.  The mass spectrometer was operated in “peptide mode” (i.e., the gas pressure in the ion-routing multipole (IRM) was 0.008 torr). Note that lower IRM pressures (i.e., as utilized in the “protein mode”) result in the loss of reporter ions.6 Typical MS settings were for MS1 scans 120,000 resolution, 246 ms maximum injection time, 100% AGC target, and 2 microscans (except for the BSA sample, for which the data were acquired using a resolution of 7,500 and 8 microscans); for MS2 PTCR scans, 1.6-5 m/z isolation window, 5 ms PTCR reaction time (200,000 PTR reagent target, 200 ms maximum PTR reagent time), 120,000 resolution, 246 ms maximum injection time, 1,000% AGC target, 1-8 microscans; for the MS2 and MS3 HCD scans, 1.6.-5 m/z isolation window, 80 V collision energy, 30,000 resolution, 54 ms maximum injection time, 1,000% AGC target, and 1-8 microscans"],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The acquired mass spectra were analyzed using FreeStyle (v1.8 SP1, Thermo Fisher). Monoisotopic masses were determined by FLASHDeconv within FLASHApp."],"omics_type":["Proteomics"],"labhead":["Andreas Tholey"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Systematic Proteome Research & Bioanalytics, Institute for Experimental Medicine, Christian-Albrechts-Universität zu Kiel, 24105 Kiel, Germany"],"species":["Bos Taurus (bovine)","Gallus Gallus (chicken)"],"publication":["42018648 Kaulich PT, Tholey A. Proton Transfer Charge Reduction Enables Isobaric Labeling-Based Proteoform Quantification of Overlapping Signals in Top-Down Mass Spectrometry. J Am Soc Mass Spectrom. 2026 37(5):1289-1294 10.1021/jasms.6c00060"],"submitter_mail":["a.tholey@iem.uni-kiel.de"],"submitter_affiliation":["Systematic Proteome Research & Bioanalytics, University of Kiel"],"submitter_country":["Germany"],"pubmed_abstract":["Top-down mass spectrometry provides a powerful approach for analyzing and quantifying intact proteoforms, i.e., the distinct molecular forms of proteins. Isobaric labeling-based quantification strategies offer the advantages of multiplexing and increased analytical depth. However, a major challenge remains the quantification of proteoforms when their precursor signals overlap, leading to mixed reporter ion intensities. In this proof-of-concept study, we employed proton transfer charge reduction (PTCR) at the MS2 level to resolve overlapping precursor signals, allowing selective isolation of individual proteoforms and subsequently, their accurate reporter ion quantification at the MS3 level. Using direct infusion mass spectrometry of model proteins labeled with cysteine-directed tandem mass tags, we demonstrate that this approach enables accurate, interference-free reporter ion-based quantification in the presence of overlapping proteoforms and spectrally congested backgrounds. This work highlights PTCR as a versatile gas-phase separation strategy to enhance the quantitative capabilities of labeling-based top-down mass spectrometry, offering a path toward precise, proteoform-resolved quantification across diverse experimental approaches, such as large-scale top-down proteomics."],"pubmed_title":["Proton Transfer Charge Reduction Enables Isobaric Labeling-Based Proteoform Quantification of Overlapping Signals in Top-Down Mass Spectrometry."],"pubmed_authors":["Kaulich Philipp T PT, Tholey Andreas A"],"additional_accession":[]},"is_claimable":false,"name":"Proton Transfer Charge Reduction Enables Isobaric Labeling-Based Proteoform Quantification of Overlapping Signals in Top-Down Mass Spectrometry","description":"Top-down mass spectrometry provides a powerful approach for analyzing and quantifying intact proteoforms, i.e., the distinct molecular forms of proteins. Isobaric labeling-based quantification strategies offer the advantages of multiplexing and increased analytical depth. However, a major challenge remains the quantification of proteoforms when their precursor signals overlap, leading to mixed reporter ion intensities. In this proof-of-concept study, we employed proton transfer charge reduction (PTCR) at the MS2 level to resolve overlapping precursor signals, allowing selective isolation of individual proteoforms and subsequently, their accurate reporter ion quantification at the MS3 level. Using direct infusion mass spectrometry of model proteins labeled with cysteine-directed tandem mass tags, we demonstrate that this approach enables accurate, interference-free reporter ion-based quantification in the presence of overlapping proteoforms and spectrally congested backgrounds. This work highlights PTCR as a versatile gas-phase separation strategy to enhance the quantitative capabilities of labeling-based top-down mass spectrometry, offering a path toward precise, proteoform-resolved quantification across diverse experimental approaches.","dates":{"publication":"2026-06-08","submission":"2026-02-23"},"accession":"PXD074730","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:28930","NEWT:202914","NEWT:27602","NEWT:502779","NEWT:297246","NEWT:483139","NEWT:101491","NEWT:8639","NEWT:8637","NEWT:1114970","NEWT:285272","NEWT:192222","NEWT:9963","NEWT:197911","NEWT:197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