{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E3_4586_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E2_4554_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E2_4554_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E3_4586_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E3_4586_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E3_4586_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E2_4554_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E2_4554_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E3_4586_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E2_4554_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E2_4554_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E3_4586_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E3_4586_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E2_4554_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E2_4554_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/E3_4586_02.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/PRIDE_4586.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD075266/PRIDE_4554.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["jan.riemer@uni-koeln.de"],"submitter":["Proteomics Facility"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["Mitochondria","Oxidative protein folding","Heme biosynthesis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075266"],"tissue":["Cell Culture"],"sample_protocol":["For the interactome data an in-gel digest was performed. The native IP was performed as described in the respective section. After the native IP was performed the beads were dried and boiled in 20 µl reducing Laemmli buffer (without bromphenolblue) for 10 min. The samples were reduced by addition of DTT with a final concentration of 5 mM and incubated at 56 °C for 30 min. Free cysteine thiols were alkylated by addition of CAA to a final concentration of 40 mM to the samples which were then incubated for 30 min at room temperature in the dark. The samples were run on SDS-PAGE until the samples migrated for 1 cm into the separation gel. Then the gels were fixed for 1 h in fixing solution (10% Acetic acid / 20% Methanol in water). The gel bands were cut in smaller pieces and were transferred to individual tubes. 100 µl of 50 mM ABC/50% Acetonitrile was added to the gel pieces and were incubated for 20 min at room temperature. The solution was exchanged with fresh 50 mM ABC/50% Acetonitrile and remaining solution was discarded after 20 min incubation. The gel pieces were covered with 100 µl acetonitrile and incubated for 10 min. The gel pieces were then dried in a speedvac for approximately 5 min. A digestion solution of 10 ng/μL of 90 % trypsin and 10 % LysC in 50 mM ammonium bicarbonate (ABC) was added to the gel pieces until the gel pieces were fully covered. The gel pieces were incubated for 30 min at 4°C with the digest solution. After the incubation time, excessive digest solution was removed and 50 mM ABC buffer was used to cover the gel pieces. The samples were incubated overnight at 37°C while shaking at 750 rpm. The next day, the supernatant of the gel pieces were transferred into new tubes. The gel pieces were covered with 100 µl 30% ACN/3% TFA and incubated for 20 min at room temperature. The extract was combined with the supernatant of the previous step. The gel pieces were covered with 100 µl 100% acetonitrile and again incubated for 20 min at room temperature. The extract was also combined with the supernatant from the previous step and the organic solvents of the samples were reduced in the speedvac until a remaining volume of 50 µl was reached. The samples were acidified by addition of formic acid to a final concentration of 1% and the STAGE tip purification protocol as it is described in the section “Determination of cellular protein levels by quantitative label-free proteomics” was performed. The STAGE tips were stored at 4°C. The mass spectrometry was performed and analysed by the proteomics core facility Cologne."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Samples were analyzed by the CECAD Proteomics Facility on an Orbitrap Exploris 480 (Thermo Scientific, granted by the German Research Foundation under INST 216/1163-1 FUGG) mass spectrometer that was coupled to an Vanquish neo in trap-and-elute setup (Thermo Scientific). Samples were loaded onto a precolumn (Acclaim 5µm PepMap 300 µ Cartridge) with a flow of 60 µl/min before reverse-flushed onto an in-house packed analytical column (30 cm length, 75 µm inner diameter, filled with 2.7 µm Poroshell EC120 C18, Agilent). Peptides were chromatographically separated with an initial flow rate of 400 nL/min and the following gradient: initial 2% B (0.1% formic acid in 80 % acetonitrile), up to 6 % in 3 min. Then, flow was reduced to 300 nl/min and B increased to 20% B in 26 min, up to 35% B within 15 min and up to 98% solvent B within 1.0 min while again increasing the flow to 400 nl/min, followed by column wash with 95% solvent B and reequilibration to initial condition. The mass spectrometer was operated in data-dependent acquisition with a cycle time of 1 s with MS1 scans acquired from 350 m/z to 1400 m/z at 60k resolution and an AGC target of 300%. MS2 scans were acquired at 15 k resolution with a maximum injection time of 118 ms and an normalized AGC target of 50% in a 2 Th window and a fixed first mass of 110 m/z. All MS1 scans were stored as profile, all MS2 scans as centroid.   All mass spectrometric raw data were processed with Maxquant (version 2.6, Tyanova et al. NatProt) using default parameters against the Uniprot canonical human database (UP5640, downloaded 15.01.2025) with the match-between-runs option enabled between replicates. Follow-up analysis was done in Perseus 1.6.15 (Tyanova et al. NatMet). Protein groups were filtered for potential contaminants and insecure identifications. Remaining IDs were filtered for data completeness in at least one group and missing values imputed by sigma downshift (0.3 σ width, 1.8 σ downshift). Afterwards, FDR-controlled two-sided t-tests were performed."],"omics_type":["Proteomics"],"labhead":["Jan Riemer"],"instrument_platform":[""],"labhead_affiliation":["Redox Metabolism, Institute for Biochemistry, University of Cologne"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["proteomics-facility@uni-koeln.de"],"publication":["Not available"],"submitter_affiliation":["CECAD Research Center"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"ALR Couples IMS Redox and Heme Biosynthesis Beyond the Disulfide Relay","description":"Denaturing pulldown of ALR-HA from HEK293 cells to identify the covalent interaction partners of ALR. One half of the samples were treated with DTT during the Co-IP protocol to verify that the interactions are disulfide related. Accordingly, no Mock-cell lines was used. One half of the samples from the same cell line were treated with DTT during the IP and the other half was 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