Find research datasets worth reusing
Search datasets from major research repositories and use ShareScore to quickly assess how well each record supports discovery, access, and reuse.
69
datasets available to search
ShareScore release 0.9.0
Dataset results
69 results for “Screening assays”
HDAC6 screening dataset using tau-based substrate in an enzymatic assay yields selective inhibitors and activators
<p><strong>Structure and information of the data file</strong></p> <p>DATA SET; Contains the information to which data set this information belongs. There are four possibilities denoted 1 to 4. Data set1: Enzymatic assay of human HDAC6 with commercial peptide substrate. Data set2: Enzymatic assay of human HDAC6 with custom peptide substrate. Data set3: Hit confirmation of the active molecules of the enzymatic assay of human HDAC6 with custom peptide substrate. Data set4: Determination of IC50 values for inhibition of enzymatic assay of human HDAC6 with custom peptide substrate.</p> <p>INTERNAL NAME; An internal name which enables identification of the compound within data sets from Fraunhofer ITMP ScreeningPort.</p> <p>TYPE; Type of data. Either 'inhibition' for normalized inhibition values or 'IC50' for enzymatic IC50.</p> <p>RELATION; Relation between TYPE and VALUE, always '='.</p> <p>VALUE; Value of the normalized inhibition or the enzymatic IC50.</p> <p>UNITS; Unit of the value. Either '%' for the normalized inhibition or 'uM' for the enzymatic IC50.</p> <p>NAME; Trade name of the chemical compound.</p> <p>SMILES; The canonical Smile of the chemical compound.</p> <p> </p> <p><strong>A</strong><strong>bstract</strong></p> <p>Histone deacetylase 6 (HDAC6) and HDAC10 are unique among the other HDACs as they consist of two domains instead of one. Only in the case of HDAC6 both domains are active resulting in a number of unique deacetylase reactions. Interestingly, HDAC6 can regulate the microtubule network and plays a role in the degradation of misfolded and aggregated proteins. We therefore developed a substrate (Boc-Ile-Asp-(Dimethyl)Lys-(Ac)Lys-aminoluciferin) based on a critical acetylation site of misfolded human Tau, a hallmark of Alzheimer’s Disease. This substrate was used to screen a 5632 compound encompassing repurposing library at 10 µM in a coupled, luminescence based assay. The assay was miniaturised to 10 µL per enzymatic reaction. For comparison, a generic HDAC substrate (BOC-Gly-(Ac)Lys-aminoluciferin) was also used to screen the same library. Both substrates rely on a cascade of enzymatic reactions. First, HDAC6 deacetylates the substrate followed by cleavage of aminluciferin from the peptide by porcine Trypsin and conversion of the aminoluciferin using firefly Luciferase. Compounds with an activity of at least 75% inhibition against the custom human Tau based substrate were confirmed in triplicates at the screening concentration of 10 µM. Confirmed hits, activity of at least 75%, where analysed in 8 point or 15 point dose response curves, depending on their activity. The data presented here encompass both primary data sets including 5632 compounds as well as 249 values from hit confirmation screening against the hTau based substrate and 151 IC<sub>50</sub> values from confirmed hits.</p> <p> </p> <p><strong>Methods of data generation</strong></p> <p><strong>Enzymatic assay of human HDAC6 with commercial peptide substrate. </strong></p> <p>The assay using the commercial peptide substrate (BOC-Gly-(Ac)Lys-aminoluciferin) was obtained from Promega Inc.. In the beginning the assay buffer is thawed and the lyophilized substrate is dissolved according to the technical manual (Promega Inc.) to create the substrate reagent. HDAC6 (obtained from BPS Biosciences) is dissolved in assay buffer at 0.2 nM, which is twice the final assay concentration. Compounds and controls are added to the plates using acoustic dispensing to reach a final concentration of 10 µM in the assay followed by 5 µl enzyme solution per well. Plates are centrifuged shortly and incubated for 10 min at RT. Afterwards, 5 µL/well substrate solution are added to the wells, centrifuged shortly and incubated for 10 min prior detection of the luminescence signal on a multimode reader. Primary screening was done at one concentration (10 µM) in singlicates.</p> <p> </p> <p><strong>Enzymatic assay of human HDAC6 with custom peptide substrate. </strong></p> <p>The assay was designed based on a commercial HDAC6 assay available from Promega Inc. This luminescence assay works by an aminoluciferin coupled HDAC6 peptide substrate. Upon deacetylation of the peptidic substrate by HDAC6 (obtained from BPS Biosciences) Trypsin (obtained from Sigma-Aldrich) can cleave the aminoluciferine from the peptide which can be converted by Luciferase (obtained from AAT Bioquest) to the detected signal. First, a twofold concentrated enzyme solution was generated, consisting of 4 nM HDAC6 and 0.1% BSA in HEPES buffer (25 mM HEPES, 137 mM NaCl, 2.7 mM KCl and 1 mM MgCl2, pH 7.0). Second, a twofold peptide solution was generated containing 100 µM custom made peptide (Boc-Ile-Asp-(Dimethyl)Lys-(Ac)Lys-aminoluciferin) in HEPES buffer. Compounds and controls are added to the plates using acoustic dispensing to reach a final concentration of 10 µM in the assay followed by 5 µl enzyme solution per well. Plates are centrifuged shortly and 5 µL/well peptide solution are added to the wells, centrifuged shortly and incubated for 30 min at RT. Afterwards, 5 µL detection reagent (0.067 mg/mL Luciferase, 133.3 µM ATP, 0.133 mg/mL Trypsin in HEPES buffer) were added to each well. Plates were centrifuged shortly and measured on a multimode reader after 30 min incubation at RT in the dark. Primary screening was done at one concentration (10 µM) in singlicates.</p> <p> </p> <p><strong>Hit confirmation of the active molecules of the enzymatic assay of human HDAC6 with custom peptide substrate</strong></p> <p>The assay was designed based on a commercial HDAC6 assay available from Promega Inc. This luminescence assay works by an aminoluciferin coupled HDAC6 peptide substrate. Upon deacetylation of the peptidic substrate by HDAC6 (obtained from BPS Biosciences) Trypsin (obtained from Sigma-Aldrich) can cleave the aminoluciferine from the peptide which can be converted by Luciferase (obtained from AAT Bioquest) to the detected signal. First, a twofold concentrated enzyme solution was generated, consisting of 4 nM HDAC6 and 0.1% BSA in HEPES buffer (25 mM HEPES, 137 mM NaCl, 2.7 mM KCl and 1 mM MgCl2, pH 7.0). Second, a twofold peptide solution was generated containing 100 µM custom made peptide (Boc-Ile-Asp-(Dimethyl)Lys-(Ac)Lys-aminoluciferin) in HEPES buffer. Compounds and controls are added to the plates using acoustic dispensing to reach a final concentration of 10 µM in the assay followed by 5 µl enzyme solution per well. Plates are centrifuged shortly and 5 µL/well peptide solution are added to the wells, centrifuged shortly and incubated for 30 min at RT. Afterwards, 5 µL detection reagent (0.067 mg/mL Luciferase, 133.3 µM ATP, 0.133 mg/mL Trypsin in HEPES buffer) were added to each well. Plates were centrifuged shortly and measured on a multimode reader after 30 min incubation at RT in the dark. Hit confirmation was done at one concentration (10 µM) in triplicates.</p> <p> </p> <p><strong>Determination of IC50 values for inhibition of enzymatic assay of human HDAC6 with custom peptide substrate</strong></p> <p>The assay was designed based on a commercial HDAC6 assay available from Promega Inc. This luminescence assay works by an aminoluciferin coupled HDAC6 peptide substrate. Upon deacetylation of the peptidic substrate by HDAC6 (obtained from BPS Biosciences) Trypsin (obtained from Sigma-Aldrich) can cleave the aminoluciferine from the peptide which can be converted by Luciferase (obtained from AAT Bioquest) to the detected signal. First, a twofold concentrated enzyme solution was generated, consisting of 4 nM HDAC6 and 0.1% BSA in HEPES buffer (25 mM HEPES, 137 mM NaCl, 2.7 mM KCl and 1 mM MgCl2, pH 7.0). Second, a twofold peptide solution was generated containing 100 µM custom made peptide (Boc-Ile-Asp-(Dimethyl)Lys-(Ac)Lys-aminoluciferin) in HEPES buffer. Compounds and controls are added to the plates using acoustic dispensing to reach a final concentration of 10 µM in the assay followed by 5 µl enzyme solution per well. Plates are centrifuged shortly and 5 µL/well peptide solution are added to the wells, centrifuged shortly and incubated for 30 min at RT. Afterwards, 5 µL detection reagent (0.067 mg/mL Luciferase, 133.3 µM ATP, 0.133 mg/mL Trypsin in HEPES buffer) were added to each well. Plates were centrifuged shortly and measured on a multimode reader after 30 min incubation at RT in the dark. IC50 values were determined using 7 point dose response curves (DRCs) between 20 µM and 312 nM. In case inhibition values were not below 50% additional 7 point DRCs were measured, starting at 312 nm with a dilution factor of 2. All DRCs were recorded in triplicates.</p>
A Multiplexed Cell-Free Assay to Screen for Antimicrobial Peptides in Double Emulsion Droplets
<p>Data underlying the figures in the publication “A Multiplexed Cell-Free Assay to Screen for Antimicrobial Peptides in Double Emulsion Droplets”, published in <em>Angew. </em><em>Chem. Int. Ed.,</em> <strong>2022</strong>, e202114632.</p> <p><a href="https://onlinelibrary.wiley.com/doi/10.1002/anie.202114632">https://onlinelibrary.wiley.com/doi/10.1002/anie.202114632</a></p> <p> </p> <p>Table of contents:</p> <p><strong>1. Figure 1b</strong>: Bright-field image of the double emulsions droplets produced on the microfluidic chip (scale bar 40 μm).</p> <p><strong>2. Figure 1c</strong>: Source video of the image in <em>Figure 1c</em>. Overlaid fluorescence and bright-field image of a double emulsion in a hydrodynamic trap, containing LUVs loaded with a self-quenching concentration of SRB in the cell-free extract, showing background fluorescence (scale bar 20 μm).</p> <p><strong>3. Figure 2a</strong>: Excel file containing the experimental data for <em>Figure 2a</em>. Cell-free protein production. Cell-free production of sfGFP in double emulsion (DE) droplets. The expression and folding of sfGFP was confirmed by the increase of fluorescence at 516 nm (ex. 488 nm). The dashed ribbon represents standard deviation (n=150).</p> <p><strong>4. Figure 2c</strong>: Excel files containing the experimental data for <em>Figure 2c</em>. Mean fluorescence intensities of b) after incubation at room temperature for 16 hours. no DNA: DEs without any alpha-hemolys in plasmid DNA(n=107), α-HL:DEs with the alpha-hemolys in plasmid DNA(n=258), SDS: double emulsions without any alpha-hemolys in plasmid DNA, exposed to a solution of 0.5% SDS in buffer throughout the incubation (n=204).</p> <p><strong>5. Figure 2d</strong>: Excel file containing the experimental data for <em>Figure 2d</em>. Fluorophore leakage kinetics from mammalian-like LUVs with SRB and from bacteria-like LUVs with 6-FAM, induced by the cell-free expression of pneumolysin in a 384 well-plate, starting at time 0. Fractional fluorescence (fF) is calculated by setting the zero level to the vesicle fluorescence in the absence of DNA, and the maximum level of fluorescence, scaled to a value of 1, to the value obtained by lysing the vesicles with 0.5% SDS. Solid lines represent the average of three independent reactions visible below.</p> <p><strong>6. Figures 2e and 2f</strong>: FACS data for <em>Figures 2e</em> and <em>2f</em>.</p> <p><strong>7. Figure 3a</strong>: Excel file containing the experimental data for <em>Figure 3a</em>. Fluorophore leakage kinetics from mammalian-like LUVs with SRB and bacteria-like LUVs with 6-FAM, induced by the cell-free expression of meucin-25 in a 384 well-plate. Each well contained 8 nM of plasmid (Supporting Information Table 1). Solid lines represent the average of three technical replicates displayed as well (the lines are overlapping, thus not visible).</p> <p><strong>8. Figure 3c</strong>: Excel file containing the experimental data for <em>Figure 3c</em>. Bacterial viability assay with increasing meucin-25 concentrations, measured by flow cytometry. Propidium iodide (PI) cannot pass intact bacterial membranes and only intercalates the DNA of permeabilized dead bacteria (“PI positive”). Constitutively expressed sfGFP proteins normally efficiently retained in intact bacterial cells (“GFPpositive”) but lost in suitably permeabilized cells. Error bars indicate standard deviation (n=10000).</p> <p><strong>9. Figure SI_2</strong>: Excel files containing the experimental data for <em>Supplementary Figure 2</em>.</p> <p><strong>10. Figure SI_3</strong>: Excel file containing the experimental data for <em>Supplementary Figure 3</em>.</p> <p><strong>11. Figure SI_4a</strong>: Excel files containing the experimental data for <em>Supplementary Figure 4a</em>.</p> <p><strong>12. Figure SI_4b</strong>: Excel files containing the experimental data for <em>Supplementary Figure 4b</em>.</p> <p><strong>13. Figure SI_5</strong>: Excel files containing the experimental data for <em>Supplementary Figure 5</em>.</p> <p><strong>14. Figure SI_6</strong>: Excel files containing the experimental data for <em>Supplementary Figure 6</em>.</p> <p> </p> <p> </p>
Screening of 2694 RdRP virtual screening hits in RdRP/Nsp7/Nsp8 biochemical assay and confirmation in cellular SARS-CoV-2 assay
<p>This report describes the most relevant results of virtually screening the Janssen Pharmaceutica compound collection for potential activity against SARS-CoV-2 RNA polymerase and confirmation of potential hits in a biochemical SARS-CoV RTC assay and A549-hACE2 cell-based anti-SARS-CoV-2 assay.</p>
Analog Series of Compounds with High Frequency of Activity in Screening Assays
<p>A set of 6941 analog series and associated data are provided. These series exclusively consist of compounds that are most frequently active across public screening assays. </p>
Development of a high-throughput small molecule screening assay for phenotypical characterization of lysosomal storage disorder-affected cells, with infantile cystinosis as a proof of principle
<p>Together with the Pivot Park Screening Centre we performed a drug screen on CTNS-/- proximal tubule cells. For this we developed an assay to evaluate LC3-II positive puncta, and which may be applied for any disease in which autophagy plays an important role. The screen was optimized by the hotel for a 384 well format, making it useful for high throughput screening. The screen was performed with 1280 compounds from the Prestwick library.</p>
The process of HDAC11 Assay Development: buffer screening
<p>A buffer screen at various pH was performed to pick the buffer that gives the best activity for HDAC11. </p> <p>Note: 1. In the assay buffer, BSA conc. is 0.5 mg/ml (instead of 0.5%).</p> <p> 2. In the 7.5 ul developer solution, 40 uM of TSA (Trichostatin A) is also included.</p>
Compounds of interest identified by screening a focused library against USP5 Zf-UBD with a 19F NMR assay
<p>Screening a set of commercial compounds selected from computational docking studies against USP5 zinc finger ubiquitin binding domain (Zf-UBD) using <sup>19</sup>F NMR spectroscopy. You can find details of preliminary <sup>19</sup>F NMR experiments <a href="https://zenodo.org/record/1246807#.WxV8HkgvzIV">here</a>.</p>
Screening compounds of interest against USP5 Zf-UBD with a surface plasmon resonance assay
<p>The determination of binding affinities of compounds of interest against USP5 zinc finger ubiquitin binding domain (Zf-UBD) with a surface plasmon resonance (SPR) assay. </p>
Screening Compounds against USP5 Zf-UBD with a 19F NMR assay #2
<p>Screening compounds against USP5 zinc finger ubiquitin binding domain (Zf-UBD) using a <sup>19</sup>F NMR spectroscopy. You can find previous <sup>19</sup>F NMR experiments <a href="https://openlabnotebooks.org/co-crystal-structures-of-usp5-zf-ubd-and-weak-binding-compounds/">here</a>.</p>
Developing a Tryptophan Fluorescence Assay for Screening Ligands against USP5 Zf-UBD
<p>Development of a fluorescence based assay by measuring changes in UV tryptophan fluorescence of USP5 zinc finger ubiquitin binding domain (Zf-UBD) with addition of ligands</p>
Supplementary Information for "Semi-automated high-throughput substrate screening assay for nucleoside kinases
<p>This is the external Supplementary Information for our publication "Semi-automated high-throughput substrate screening assay for nucleoside kinases". Files are to follow soon. We apologize for the delay. Thank you for your patience.</p> <p> </p> <p>The preprint and the Supporting Information are available at ChemRxiv (https://doi.org/10.33774/chemrxiv-2021-k0w7q).</p>
High-Throughput-Methyl-Reading (HTMR) assay: A solution based on nucleotide methyl-binding proteins enables large-scale screening for DNA/RNA methyltransferases and demethylases
<p>Epigenetic therapy has significant potential for cancer treatment. However, few small potent molecules have been identified against DNA or RNA modification regulatory proteins. Current approaches for activity detection of DNA/RNA methyltransferases and demethylases are time-consuming and labor-intensive, making it difficult to subject them to high-throughput screening. Here, we developed a fluorescence polarization-based "High-Throughput Methyl Reading" (HTMR) assay to implement large-scale compound screening for DNA/RNA methyltransferases and demethylases-DNMTs, TETs, ALKBH5, and METTL3/METTL14. This assay is simple to perform in a mix-and-read manner by adding the methyl-binding proteins MBD1 or YTHDF1. The proteins can be used to distinguish FAM-labelled substrates or product oligonucleotides with different methylation statuses catalyzed by enzymes. Therefore, the extent of the enzymatic reactions can be coupled with the variation of FP binding signals. Furthermore, this assay can be effectively used to conduct a cofactor competition study. Based on the assay, we identified two natural products as candidate compounds for DNMT1 and ALKBH5. In summary, this study outlines a powerful homogeneous approach for high-throughput screening and evaluating enzymatic activity for DNA/RNA methyltransferases and demethylases that is cheap, easy, quick, and highly sensitive.</p>
Multiplexed On-Yeast Serological Assay for Immune Escape Screening of SARS-CoV-2 Variants
<p>Experimental data and scripts used for the development of a Yeast-based serological Assay:</p> <ol> <li>The<strong> Python scripts</strong> folder includes all scripts used in this study to analyze sera titers and plotting data.</li> <li>The<strong> Raw data</strong> folder includes: <ol> <li>The Y<strong>east Immunoassay development</strong> folder includes the flow cytometric data for serum depletion and reduction of ligand depletion effects.</li> <li>The <strong>Yeast serological data folder</strong> includes the raw data of all tested sera and related data for their analyses.</li> </ol> </li> <li>The <strong>Snapgene plasmid maps </strong>folder includes the plasmid maps for the three SARS-CoV-2 VOCs for Snapgene.</li> </ol> <p> </p> <p> </p>
High-Throughput-Methyl-Reading (HTMR) assay: A solution based on nucleotide methyl-binding proteins enables large-scale screening for DNA/RNA methyltransferases and demethylases
Open the record for dataset details and reuse information.
Data from: Development of a genotype-by-sequencing immunogenetic assay as exemplified by screening for variation in red fox with and without endemic rabies exposure
Pathogens are recognized as major drivers of local adaptation in wildlife systems. By determining which gene variants are favored in local interactions among populations with and without disease, spatially explicit adaptive responses to pathogens can be elucidated. Much of our current understanding of host responses to disease comes from a small number of genes associated with an immune response. High-throughput sequencing (HTS) technologies, such as genotype-by-sequencing (GBS), facilitate expanded explorations of genomic variation among populations. Hybridization-based GBS techniques can be leveraged in systems not well characterized for specific variants associated with disease outcome to "capture" specific genes and regulatory regions known to influence expression and disease outcome. We developed a multiplexed, sequence capture assay for red foxes to simultaneously assess ~300-kbp of genomic sequence from 116 adaptive, intrinsic, and innate immunity genes of predicted adaptive significance and their putative upstream regulatory regions along with 23 neutral microsatellite regions to control for demographic effects. The assay was applied to 45 fox DNA samples from Alaska, where three arctic rabies strains are geographically restricted and endemic to coastal tundra regions, yet absent from the boreal interior. The assay provided 61.5% on-target enrichment with relatively even sequence coverage across all targeted loci and samples (mean = 50×), which allowed us to elucidate genetic variation across introns, exons, and potential regulatory regions (4,819 SNPs). Challenges remained in accurately describing microsatellite variation using this technique; however, longer-read HTS technologies should overcome these issues. We used these data to conduct preliminary analyses and detected genetic structure in a subset of red fox immune-related genes between regions with and without endemic arctic rabies. This assay provides a template to assess immunogenetic variation in wildlife disease systems.
Carbon sources screening assay
<p><span>The FACS optimized GFPmut3 </span><sup><span>69</span></sup><span> was fused to promoter of interest and cloned into a plasmid pSC101. <a name="_Hlk156916219"></a><span>For the first screening, </span>overnight cultures of the strain carrying the screening system were diluted 200X in MOPS Rich <span>(Teknova EZ rich defined medium) supplemented with carbenicillin for plasmid maintenance. </span><span>The phenotype Microarray (Biolog) plates PM1 and PM2B (carbon sources), and PM3B, for a total of 198 molecules including 7 nucleosides and 6 nucleotides were used for molecules screening. Each well was filled with 100 µl of inoculated media and mixed by pipetting. Media were transferred to 96 well dark-bottom plates (Thermo Scientific). GFP fluorescence was followed on the Tecan Infinite 200 PRO (Life Science) at 37°C for 8 hours. Fluorescence induction by the substrate was calculated using the ratio </span>fluorescence (t8h-t0h) over growth (t8h-t0h OD<sub>600nm</sub>).</span></p> <p><span>For flow cytometry quantification, </span><span>overnight cultures in MH of strain carrying the screening system were diluted 200X in rich MOPS <span>(Teknova EZ rich defined medium), or MH supplemented with carbenicillin for plasmid maintenance<span> and grown overnight, and the molecule tested at 0.5% (except uracil: 0.1%, limit of solubility). Fluorescence was read on 5 µl of overnight cultures diluted in 200 µl of PBS with the B1 laser. </span></span></span></p>
Chemical screening in an estrogen receptor transactivation assay with metabolic competence
<p>The U.S. EPA continues to utilize high-throughput screening data to evaluate potential biological effects of endocrine active substances without the use of animal testing. Determining the scope and need for <em>in vitro</em> metabolism in high-throughput assays requires the generation of larger data sets that assess the impact of xenobiotic transformations on toxicity-related endpoints. The objective of the current study was to screen a set of 768 ToxCast chemicals in the VM7Luc estrogen receptor transactivation assay (ERTA) using the Alginate Immobilization of Metabolic Enzymes (AIME) hepatic metabolism method. Chemicals were screened with or without metabolism to identify estrogenic effects and metabolism-dependent changes in bioactivity. Based on estrogenic hit calls, 85 chemicals were active in both assay modes, 16 chemicals were only active without metabolism, and 27 chemicals were only active with metabolism. Using a novel metabolism curve shift method that evaluates the shift in concentration-response curves, 29 of these estrogenic chemicals were identified as bioactivated and 59 were bioinactivated. Human biotransformation routes and associated metabolites were predicted <em>in silico </em>across the chemicals to mechanistically characterize possible transformation-related ERTA effects. Overall, the study profiled novel chemicals associated with metabolism-dependent changes in ERTA bioactivity, and suggested routes of biotransformation and putative metabolites responsible for the observed estrogenic effects. The data demonstrate a range of metabolism-dependent effects across a diverse chemical library and highlight the need to evaluate the role of intrinsic xenobiotic metabolism in endocrine and other toxicity-related health effects.</p>
Virtual screening on SARS-CoV-2 Nsp14_testing of 5474 hits in a Nsp14 biochemical assay and an A549-hACE2 SARS-CoV-2 infected cells
<p> </p> <p>This report describes the most relevant results of virtually screening the Janssen Pharmaceutica compound collection for potential activity against SARS-CoV-2 Nsp14 and confirmation of potential hits in a SARS-CoV-2 Nsp10/Nsp14 biochemical exonuclease assay and in a A549-hACE2 cell-based anti-SARS-CoV-2 assay.</p>
Selecting Chemotherapy With High-throughput Drug Screen Assay Using Patient Derived Organoids in Patients With Refractory Solid Tumours (SCORE)
ClinicalTrials.gov study NCT04279509. IPD Sharing: NO. Countries: 1. Publications: 2.
Fecal Screening Assay for Taiwanese Population
ClinicalTrials.gov study NCT01341197. IPD Sharing: Not stated. Countries: 1. Publications: 1.
ScienceDex guides
Understand access before you commit
These curated guides explain access requirements, typical timelines, costs, and reuse considerations for widely used research datasets.
Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
Annotated Behaviour and Observability Dataset (ABODe)
ABODe is a University of Edinburgh DataShare dataset for behavior classification in group-housed mice using home-cage video, identities, bounding boxes, ground-plate positions, and annotator labels.
DANDI Archive for NWB datasets
DANDI is a BRAIN Initiative archive for publishing and sharing neurophysiology data, including electrophysiology, optophysiology, and behavioral data packaged as NWB and related standards.
International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.