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Copley"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Rna","Hydrogen/deuterium-exchange mass spectrometry","Tdp-43"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD071117"],"sample_protocol":["WT TDP-43 and TDP-435FL constructs containing C-terminal maltose binding protein (MBP) and 6x-Histidine (His) tags were expressed in E. coli, then purified via affinity purification with nickel-NTA resin followed by amylose resin. Clip34 RNA was purchased from Integrated DNA Technologies (IDT). Deuterium on-exchange was performed at 25°C by mixing 10 µL of sample (non-deuterated buffer; 20 µM TDP-43-MBP-His, 150 mM NaCl, 20 mM HEPES-NaOH, 1 mM DTT, 0 µM or 40 µM Clip34 RNA) with 40 µL of deuterium on-exchange buffer (D2O-based; 150 mM NaCl, 20 mM HEPES-NaOD, 1 mM DTT), resulting in a D2O concentration of 80%. For nondeuterated samples, 10 µL of sample was mixed with 40 µL of Non-Deuterated Buffer. For the fully deuterated sample, 10 µL of sample was mixed with 40 µL of on-exchange buffer, then incubated at 30°C for ~18 hr.  HX measurements from 20 s to 14.5 hr were performed at pH 7.0 (with HEPES-NaOH pH 7.0). To measure less protected, faster exchanging parts of the protein, another set of measurements was performed with HEPES-NaOH pH 6.0 buffer. Due to the direct dependence of the intrinsic exchange rate on OH- concentration, these measurements can be put on the same time axis as the pH 7.0 measurements by dividing the actual exchange time by 10. All 1 s, 2 s, 6 s, and 18 s timepoints were collected utilizing pH 6.0 buffer; 1 min and 3 min timepoints were collected with some replicates utilizing pH 6.0 buffer and others utilizing pH 7.0 buffer; 20 s, and 10 min and longer timepoints were collected utilizing pH 7.0 buffer. For example, the “1 min” timepoints were measured by 1 min of on-exchange at pH 7.0, or 10 min of on-exchange at pH 6.0. At the indicated timepoint, the exchange reaction was quenched by addition of 10 µL of ice-cold 250 mM phosphoric acid (for pH 7.0 buffer) or 145 mM phosphoric acid (for pH 6.0 buffer), to achieve a final pH of pH 2.5. For MS analysis, the sample was digested by loading 50 µL onto a homemade pepsin column maintained at 0°C, where pepsin was immobilized by coupling to POROS 20 AL support (Applied Biosystems) and packed into a column housing of 2 mm x 2 cm (64 µL) (Upchurch). The protease-generated fragments were then collected onto a TARGA C8 5 µM Piccolo HPLC column (1.0 x 5.0 mm, Higgins Analytical) and separated on a C8 analytical column utilizing a shaped 10-45% Buffer B gradient at 8 µL/min (Buffer A: 0.1% formic acid; Buffer B: 0.1% formic acid, 99.9% acetonitrile). The effluent was electrosprayed into the mass spectrometer."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peptides were identified from non-deuterated samples by MS/MS (Thermo Q Exactive), by analyzing MS/MS data using SEQUEST Proteome Discoverer (ThermoFisher). Deuterated samples, and additional non-deuterated reference samples, were analyzed by MS (Thermo Q Exactive or Thermo Exactive Plus EMR). HDExaminer software was utilized to process and analyze the HXMS data. The timepoints for samples performed at pH 6.0 were input as one-tenth of the actual on-exchange time. ExMS2, a MATLAB-based program, was used to prepare the peptide pool used by HDExaminer, from the SEQUEST output files for MS/MS data analysis. HDExaminer uses a non-deuterated sample as the reference for identifying deuterated peptides. Manual adjustment of retention times and m/z windows was performed as needed to correct any initial errors. Each deuterated peptide is corrected for back exchange after quenching, by normalizing to the maximal deuteration level of that peptide as detected in the fully deuterated sample. For calculating the peptide deuteration level at each timepoint, HDExaminer identifies the peptide envelope centroid values for both the non-deuterated and deuterated peptides. For visualizing the difference in peptide deuteration levels for each peptide, the HDExaminer data was visualized using MATLAB. At each timepoint, the average deuteration percent for a peptide in either the free or bound condition was calculated by taking the average deuteration percent of all replicates for the peptide at that timepoint that were identified with medium or high confidence. These values were then analyzed in MATLAB by subtracting the average deuteration percent of the peptide in the Clip34-bound state from the average deuteration percent of the peptide in the free state. This data is plotted in MATLAB. Peptides of the same sequence but different charge states are plotted to allow visualization of the agreement across separate charge states for a unique peptide sequence. To generate plots of consensus exchange difference for each timepoint, the exchange differences of the peptides at that timepoint were manually analyzed, with the consensus exchange difference determined based on the average classification of all peptides including a specific residue. This was done via a scoring system, where a peptide with a difference of less than 10% receives a score of 0, a peptide with a difference of ≥ 10% receives a score of -1, a peptide with a difference of ≥ 20% receives a score of -2, a peptide with a difference of ≥ 30% receives a score of -3, a peptide with a difference of ≤ -10% receives a score of +1, a peptide with a difference of ≤ -20% receives a score of +2, and a peptide with a difference of ≤ -30% receives a score of +3. As peptides were binned according to this scoring system, the displayed consensus percentage differences in exchange do not report the exact value of the percentage difference for each peptide, and do not report the proximity of each peptide’s behavior to the cutoff value for each score. The average score for each residue was rounded to the nearest whole number, and this data was plotted in GraphPad Prism, with the rounded score value for each residue colored according to the same scoring system. To generate plots of HX data for representative peptides displaying exchange as the number of deuterons, the HDExaminer output of this data was visualized using GraphPad Prism. For a peptide, the values for the number of deuterons from HDExaminer was taken for each replicate with high or medium confidence at each timepoint, for both free and bound states. This was then plotted in GraphPad Prism. To generate plots of mass spectra, HDExaminer output was visualized in GraphPad Prism. The raw mass spectrum data for a particular replicate of a specific timepoint in either the free or bound state was copied into GraphPad Prism. This data was manually analyzed to determine the signal that corresponded to the desired peptide, based on the signal corresponding to the appropriate m/z values. All signal is displayed in the mass spectra plots, but the signal determined to correspond to the correct peptide is colored red, for ease of visualization. Dashed guidelines for visualization are also displayed, with the blue line corresponding to the value of the monoisotopic peak for that peptide, and the purple line corresponding to the centroid value of the peptide in the fully deuterated condition. Representative spectra for each state at each timepoint were chosen by determining the average value of the centroid for all replicates with peptides of high or medium confidence, for that state and timepoint. The spectrum displayed as the representative spectrum corresponds to the replicate with the centroid value closest to the average of these centroid values."],"omics_type":["Proteomics"],"labhead":["James Shorter"],"instrument_platform":[""],"labhead_affiliation":["Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)","Escherichia Coli"],"submitter_mail":["katie.copley@yale.edu"],"publication":["42096556 Copley KE, Mauna JC, Danielson HL, Chen Q, Ozguney B, Ngo M, Xie L, Smirnov A, Davis M, Mayne L, Linsenmeier M, Rubien JD, Bergmann CA, Portz B, Lee BL, Odeh HM, Lai L, Chang YW, Hallegger M, Ule J, Pasinelli P, Poon Y, Mittal J, Fawzi NL, Black BE, Donnelly CJ, Jensen BK, Shorter J. Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration. Science. 2026 392(6798):eadv3301 10.1126/science.adv3301"],"submitter_affiliation":["Yale University"],"submitter_country":["United States"],"pubmed_abstract":["Aberrant aggregation of the prion-like RNA binding protein TDP-43 drives several fatal neurodegenerative proteinopathies, including amyotrophic lateral sclerosis (ALS). In this work, we define how short, specific RNAs solubilize TDP-43. These short RNAs engage and stabilize the TDP-43 RNA recognition motifs, which allosterically destabilizes a conserved helical region in the prion-like domain, thereby promoting aggregation-resistant conformers. Sequence-space mining identified short RNA chaperones with enhanced activity against TDP-43 and disease-linked variants. Enhanced short RNA chaperones mitigated aberrant TDP-43 phenotypes in optogenetic models and in ALS patient-derived and control motor neurons. In mice with cytoplasmic TDP-43 aggregation and motor neuron loss, an enhanced short RNA chaperone reduced pathological aggregation, restored TDP-43 function, and conferred neuroprotection. These results define a mechanistic and therapeutic framework for RNA-based strategies to counter TDP-43 proteinopathies."],"pubmed_title":["Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration."],"pubmed_authors":["Copley Katie E KE, Mauna Jocelyn C JC, Danielson Helen L HL, Chen Qizan Q, Ozguney Busra B, Ngo Marilyn M, Xie Longxin L, Smirnov Ashleigh A, Davis Matt M, Mayne Leland L, Linsenmeier Miriam M, Rubien Jack D JD, Bergmann Cristian A CA, Portz Bede B, Lee Bo Lim BL, Odeh Hana M HM, Lai Longsheng L, Chang Yi-Wei YW, Hallegger Martina M, Ule Jernej J, Pasinelli Piera P, Poon Yan Y, Mittal Jeetain J, Fawzi Nicolas L NL, Black Ben E BE, Donnelly Christopher J CJ, Jensen Brigid K BK, Shorter James J"],"additional_accession":[]},"is_claimable":false,"name":"Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration","description":"Aberrant aggregation of the prion-like RNA-binding protein TDP-43 drives several fatal neurodegenerative proteinopathies, including amyotrophic lateral sclerosis (ALS). Here, we define how short, specific RNAs solubilize TDP-43. These short RNAs engage and stabilize the TDP-43 RNA-recognition motifs, which allosterically destabilizes a conserved helical region in the prion-like domain, thereby promoting aggregation-resistant conformers. Sequence-space mining identified short RNA chaperones with enhanced activity against TDP-43 and disease-linked variants. Enhanced short RNA chaperones mitigate aberrant TDP-43 phenotypes in optogenetic models and in ALS patient–derived and control motor neurons. In mice experiencing cytoplasmic TDP-43 aggregation and motor neuron loss, an enhanced short RNA chaperone reduces pathological aggregation, restores TDP-43 function, and confers neuroprotection. These findings define a mechanistic and therapeutic framework for RNA-based strategies to counter TDP-43 proteinopathies.","dates":{"publication":"2026-05-15","submission":"2025-11-24"},"accession":"PXD071117","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:193528","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:10031","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:1190602","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:2767842","NEWT:314345","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3710","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:32201","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:2902907","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3707","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","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:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:1195466","NEWT:2483192","NEWT:85698","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:427924","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:29471","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","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:480020","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:518","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:7375","NEWT:300641","NEWT:39655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