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Chandra"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Human friedreich's ataxia model proteomics","Lfq"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070711"],"tissue":["Stem Cell","Fibroblast"],"sample_protocol":["Proteomics sample preparation: Human fibroblasts (Project-ID: 012949 & 013394), sensory neurons (Project-ID: 013463) or cardiomyocytes (Project-ID: 014888) treated with or without MR3 were spun down and the cell pellets were lysed with 100 μL of a 5% sodium dodecyl sulfate (SDS), 50 mM triethyl ammonium bicarbonate (TEAB) solution containing Halt Protease and Phosphatase Inhibitor Cocktail and treated with 1 μL Pierce Universal Nuclease (Thermo Scientific, San Jose CA) to disrupt residual DNA. 25 μL aliquots of each sample lysate were transferred to new 1.7 mL eppendorf tubes and normalized to 50 μL with 10%SDS/100 mM TEAB for proteolytic filter digestion.    The samples were reduced with 10 mM dithiothreitol (DTT) for 20 min at 55°C, cooled to room temperature, and then alkylated with 30 mM acrylamide for 30 min. They were then acidified to a pH ~1 with 2.6 μL of 27% phosphoric acid and resuspended in 165 μL of S-trap loading buffer (90% methanol/10% 1M TEAB) and loaded onto S-trap microcolumns (Protifi, USA). After loading, the samples were washed sequentially with 150 μL increments of 90% methanol/10% 100mM TEAB, 90% methanol/10% 20 mM TEAB, and 90% methanol/10% 5mM TEAB solutions, respectively. Samples were digested at 47°C for two hours with 600 ng of mass spectrometry grade Trypsin/LysC mix (Promega, USA). The digested peptides were then eluted with two 35 μL increments of 0.2% formic acid in water and two more 40 μL increments of 80% acetonitrile with 0.2% formic acid in water. The four eluents were consolidated in 1.5 mL S-trap recovery tubes and dried via SpeedVac (Thermo Scientific, San Jose CA). Finally, the dried peptides were reconstituted in 2% acetonitrile with 0.1% formic acid in water for LC-MS analysis.   LC-MS/MS analysis: Proteolytically digested peptides were separated using an in-house pulled and packed reversed phase analytical column (~25 cm in length, 100 microns of I.D.), with Dr. Maisch 1.9 micron C18 beads as the stationary phase. Separation was performed with an 80-minute reverse-phase gradient (2-45% B, followed by a high-B wash) on an Acquity M-Class UPLC system (Waters Corporation, Milford, MA) at a flow rate of 300 nL/min. Mobile Phase A was 0.2% formic acid in water, while Mobile Phase B was 0.2% formic acid in acetonitrile. Ions were formed by electrospray ionization and analyzed either by an Orbitrap Exploris 480 mass spectrometer (Thermo Scientific, San Jose, CA), or an Orbitrap Eclipse Tribrid mass spectrometer (Thermo Scientific, San Jose, CA). The mass spectrometer was operated in a data-dependent mode using HCD (for Orbitrap Exploris 480) or CID (for Orbitrap Eclipse) fragmentation for MS/MS spectra generation."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["All MS/MS samples were analyzed using the Maxquant platform (version 2.4.2.0) with Andromeda search engine at 10 ppm precursor ion mass tolerance against the SwissProt and TrEMBL Homo Sapiens Proteome database (205,205 entries, UniProt (http://www.uniprot.org/)). The label free quantification (LFQ) and Match Between Runs were used with the following search parameters: semi-tryptic and Lys-C digestion, fixed modification with propionamide on cysteine, dynamic oxidation of methionine, protein-N-terminal acetylation, acetylation on lysine, and deamidation on asparagine and glutamine as variable modification. Less than 1% of false discovery rate (FDR) was obtained for unique peptide as well as unique protein. LFQ intensity value were log2-transformed for further analysis including data normalization. For each group, if two out of the three replicates were detected and the third replicate was undetected, the missing value for the third replicate was filled by imputed value representing a normal distribution around the detection limit under Perseus Platform (https://maxquant.net/perseus/)."],"omics_type":["Proteomics"],"labhead":["Xinan Wang"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Stanford university"],"species":["Homo Sapiens (human)"],"submitter_mail":["sujyotic@stanford.edu"],"publication":["42259290 Chandra S, Kwak CS, Du Z, Barisano G, Nguyen KT, Vinogradov V, Wang X. Chemical modulation of Miro1 alleviates cell-type-specific vulnerabilities in Friedreich's ataxia. Cell Chem Biol. 2026:S2451-9456(26)00156-X 10.1016/j.chembiol.2026.05.004"],"submitter_affiliation":["Instructor"],"submitter_country":["United States"],"doi":["10.6019/PXD070711"],"pubmed_abstract":["Friedreich's ataxia (FA) is marked by early-onset sensory neurodegeneration and cardiomyopathy. We establish a human dual-cell model of FA by differentiating sensory neurons and cardiomyocytes from the same patients, enabling parallel molecular profiling of disease-relevant cell types. Proteomic analysis reveals distinct, cell-type-specific pathway disruptions in response to frataxin deficiency. Leveraging this platform, we investigate Miro1 reducer 3 (MR3), a selective chemical probe binding Miro1, a mitochondrial outer membrane protein implicated in redox regulation in FA. MR3 treatment modulates molecular signatures in a cell-type-dependent manner, altering pathways related to cardiac contractility in cardiomyocytes and synaptic function in sensory neurons. Mechanistically, MR3 reduces mitochondrial reactive oxygen species and restores membrane potential in FA sensory neurons via potential allosteric reshaping of Miro1 protein. We expand the chemical diversity of this scaffold by conducting ligand-based virtual screening of over 3 billion compounds and identifying previously uncharacterized Miro1 ligands with improved docking and neuroprotective capacity."],"pubmed_title":["Chemical modulation of Miro1 alleviates cell-type-specific vulnerabilities in Friedreich's ataxia."],"pubmed_authors":["Chandra Sujyoti S, Kwak Chulhwan S CS, Du Zehui Z, Barisano Giuseppe G, Nguyen Kong T KT, Vinogradov Vlad V, Wang Xinnan X"],"additional_accession":[]},"is_claimable":false,"name":"Human Friedreich's Ataxia model proteomics","description":"Friedreich’s ataxia (FA) is a multisystem neurodegenerative disorder marked by early-onset sensory neuropathy and cardiomyopathy. However, the molecular determinants of tissue-specific vulnerability remain poorly understood. Here, we establish a human dual-cell model of FA by differentiating sensory neurons and cardiomyocytes from the same patients, enabling parallel molecular profiling of disease-relevant cell types. Proteomic analysis reveals distinct, cell-type-specific pathway disruptions in response to frataxin deficiency, reflecting divergent susceptibilities to mitochondrial dysfunction. Leveraging this platform, we investigate Miro1 Reducer 3 (MR3), a selective chemical probe targeting Miro1, a mitochondrial outer membrane GTPase implicated in redox regulation in FA. MR3 treatment modulates molecular signatures in a cell-type-dependent manner, enhancing pathways related to cardiac contractility in cardiomyocytes and synaptic function and cell-cell communication in sensory neurons. Mechanistically, MR3 reduces mitochondrial reactive oxygen species and restores membrane potential in FA sensory neurons via potential allosteric reshaping of Miro1 protein. To expand the chemical diversity of this scaffold, we conducted ligand-based virtual screening of over 3 billion compounds and identified multiple new Miro1 ligands with improved neuroprotective activity. These findings underscore the power of matched, patient-derived cell model in decoding cell-type-specific disease mechanisms and therapeutic responses, and highlight Miro1-targeted modulation as a promising therapeutic strategy in FA.","dates":{"publication":"2026-06-15","submission":"2025-11-14"},"accession":"PXD070711","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:6819","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:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","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: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:156587","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:28174","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:33995","NEWT:55784","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:491","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","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: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: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:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","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: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:441772","NEWT:48106","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: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