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.
651
datasets available to search
ShareScore release 0.7.1
Dataset results
651 results for “autophagy”
Data from: Chronic Rapamycin administration via drinking water mitigates the pathological phenotype in a Krabbe disease mouse model through autophagy activation.
<p>ABSTRACT </p><p>Krabbe disease (KD) is a rare disorder caused by a deficiency of the lysosomal enzyme galactosylceramidase (GALC), resulting in the accumulation of the cytotoxic metabolite psychosine (PSY) in the nervous system. This accumulation triggers demyelination and neurodegeneration. Despite ongoing research, the underlying pathogenic mechanisms remain incompletely understood, and there is currently no cure available.</p><p>Previous studies from our lab revealed the presence of autophagy dysfunctions in KD pathogenesis, as evidenced by the presence of p62-tagged protein aggregates in the brains of KD mice and increased p62 levels in the KD sciatic nerve. We also demonstrated that the autophagy inducer Rapamycin (RAPA) can partially restore the wild-type (WT) phenotype in KD primary cells by reducing the number of p62 aggregates.</p><p>In this study, we tested RAPA in the Twitcher (TWI) mouse, a spontaneous KD mouse model. We administered the drug ad libitum via drinking water (15 mg/L) starting from post-natal day (PND) 21-23. We longitudinally monitored the motor performance of the mice through grip strength and rotarod tests, along with various biochemical parameters related to KD pathogenesis (i.e. autophagy markers expression, myelination, astrogliosis, and PSY accumulation).</p><p>Our findings demonstrate that RAPA significantly enhances motor functions at specific treatment time points and reduces astrogliosis in TWI brain, spinal cord, and sciatic nerves. Using western blot and immunohistochemistry, we observed a decrease in p62 aggregates in TWI nervous tissues, which corroborates our earlier in-vitro results. Furthermore, RAPA treatment partially reduces PSY levels in the spinal cord.</p><p>In conclusion, our results support the consideration of RAPA as a supportive therapy for KD. Importantly, as RAPA is already available in pharmaceutical formulations for clinical use, its potential for KD treatment can be promptly evaluated in clinical trials.</p>
Lipogenesis mediated by OGR1 regulates metabolic adaptation to acid stress in cancer cells via autophagy
<p>Malignant tumors exhibit altered metabolism resulting in a highly acidic extracellular microenvironment. Here we show that cytoplasmic lipid droplet (LD) accumulation, indicative of a lipogenic phenotype is a cellular adaption to extracellular acidity. LD marker PLIN2, is strongly associated with poor overall survival in breast cancer patients. Acid-induced LD accumulation is triggered by activation of the acid-sensing GPCR, OGR1 expressed highly in breast tumors. OGR1 depletion inhibited acid induced lipid accumulation while activation by synthetic agonist triggered LD formation. Inhibition of OGR1 downstream signaling abrogated the lipogenic phenotype which could be rescued with OGR1 ectopic expression. OGR1 depleted cells showed growth inhibition under acidic growth conditions in vitro and tumor formation in vivo. Isotope tracing showed that the source of lipid precursors is primarily autophagy-derived ketogenic amino acids. OGR1 depleted cells were defective in endoplasmic reticulum stress response and autophagy, hence failed to accumulate LDs affecting survival under acidic stress.</p>
Membrane interaction and mechanism of LC3 lipidation machinery in autophagy raw GUV data
<p>Raw GUV data of fluorescent protein imaged on a Nikon A1 confocal microscope with a 63 × Plan 359 Apochromat 1.4 NA objective. Three biological replicates were performed for each experimental 360 condition. Identical laser power and gain settings were used during the course of all conditions.</p>
Targeting autophagy: Polydatin's role in inducing cell death in AML
Open the record for dataset details and reuse information.
Development of an FKBP12-recruiting Chemical-Induced Proximity DNA-Encoded Library and its application in the discovery of an autophagy potentiator
<p><strong>Chemical inducers of proximity (CIPs) are molecules that recruit one protein to another and introduce new functionalities toward modulating protein states and activities. While CIP-mediated recruitment of E3 ligases is widely exploited for the development of degraders, other therapeutic modalities remain underexplored. We describe the first non-degrader CIP-DNA-Encoded Library (CIP-DEL) that recruits FKBP12 to target proteins using non-traditional acyclic structures, with an emphasis on introducing stereochemically-diverse and rigid connectors to attach the combinatorial library. We deployed this strategy to modulate ATG16L1 T300A, which confers genetic susceptibility to Crohn’s disease, and identified a compound that stabilizes the variant protein against Caspase-3 cleavage in a FKBP12-independent manner. We demonstrate in cellular models that this compound potentiates autophagy, reverses the xenophagy defects, and increases cytokine secretion characteristic of ATG16L1 T300A. This study provides a platform to access new chemical space for CIP design to achieve novel therapeutic modalities guided by human genetics.</strong></p>
Activation of autophagy during normothermic machine perfusion of discarded livers is associated with improved hepatocellular function
We demonstrate that ischemia-reperfusion injury occurs in all livers during NMP, though there are notable differences in gene expression between functional and nonfunctional livers. We further demonstrate that activation of the liver's repair and homeostasis mechanisms through autophagy plays a vital role in the graft's response to injury and may impact liver function. These findings indicate that liver autophagy might be a key therapeutic target for rehabilitating the function of severely injured or untransplantable livers.
Mediobasal hypothalamic FKBP51 acts as a molecular switch linking autophagy to whole-body metabolism - Dataset IC
<p>Raw data associated to the following publication: “Mediobasal hypothalamic FKBP51 acts as a molecular switch linking autophagy to whole-body metabolism".</p> <p><em>The stress-responsive FKBP51 controls body weight gain by regulating the balance between autophagy and mTOR signaling. We identified FKBP51 as a central nexus for the recruitment of the LKB1/AMPK complex to WIPI4 and TSC2 to WIPI3, thereby regulating the balance between autophagy and mTOR signaling in response to metabolic challenges. MBH FKBP51 dose-dependently regulates autophagy both in the brain as well as in peripheral metabolic tissues. Consequently, deletion of MBH FKBP51 strongly induces obesity, while its overexpression protects against high-fat diet (HFD) induced obesity.</em></p> <p>IC data in Thermo RAW data format; 2nd of 2 datasets.</p>
Mediobasal hypothalamic FKBP51 acts as a molecular switch linking autophagy to whole-body metabolism - Dataset Bz
<p>Raw data associated to the following publication: “Mediobasal hypothalamic FKBP51 acts as a molecular switch linking autophagy to whole-body metabolism".</p> <p><em>The stress-responsive FKBP51 controls body weight gain by regulating the balance between autophagy and mTOR signaling. We identified FKBP51 as a central nexus for the recruitment of the LKB1/AMPK complex to WIPI4 and TSC2 to WIPI3, thereby regulating the balance between autophagy and mTOR signaling in response to metabolic challenges. MBH FKBP51 dose-dependently regulates autophagy both in the brain as well as in peripheral metabolic tissues. Consequently, deletion of MBH FKBP51 strongly induces obesity, while its overexpression protects against high-fat diet (HFD) induced obesity.</em></p> <p>Bz data in Thermo RAW data format; 1 of 2 datasets.</p>
Supplementary materials of Brain Extract of Subacute Traumatic Brain Injury Promotes Neuronal Differentiation of Human Neural Stem Cells Via Autophagy
<p>Figure S1: Characterization of hNSCs. In proliferate medium, the embryo derived hNSCs could form the neurospheres (A). Markers of NSCs (NES, SOX2, SOX1) were detected (B). The SOX2<sup>+</sup> cells accounted for >95% of all cells (C). Bar scale: 60μm;</p> <p>Figure S2: The proliferation of hNSCs in TBI brain extracts with different phases. Differentiated hNSCs could be labeled with EdU in TBI brain extracts with different phases (A). Ratio of EdU<sup>+</sup> cells was decreased with the progression of days post-injury (B). Bar scale: 75μm; ****: P<0.0001;</p> <p>Figure S3: The GO annotations and KEGG pathway analysis of different expressed pro-teins in acute brain extract and subacute brain extract;</p> <p>Table S1: The protein profiles of brain extract in acute phase and subacute phase after TBI.</p>
Autophagosomal/autolysosomal/lysosomal dynamics of FaDu and HGFb cells affected by autophagy modulators (dataset of dual labeling of autophagosomes and labeling lysosomes, confocal microscopy)
<p>In this dataset, the impact of autophagy modulators on the auophagosomes and lysosomes in FaDu and HGF cells was investigated. Experimental details are described in the accompanying paper. This dataset contains total 702 CZI confocal image Z-stacks.</p> <p><strong>Relevant paper</strong>: HANELOVA, Klara, RAUDENSKA, Martina, KRATOCHVILOVA, Monika, NAVRATIL, Jiri, VICAR, Tomas, BUGAJOVA, Maria, GUMULEC, Jaromir, MASARIK, Michal and BALVAN, Jan. Autophagy modulators influence the content of important signalling molecules in PS-positive extracellular vesicles. <em>Cell Communication and Signaling</em>. 24 May 2023. Vol. 21, no. 1, p. 120. DOI <a href="https://doi.org/10.1186/s12964-023-01126-z">10.1186/s12964-023-01126-z</a>.</p> <div> <div> <div> </div> </div> </div> <p><strong>Model cell lines</strong></p> <p> </p> <p>The cell line FaDu (HTB-43TM), derived from a squamous cell carcinoma (SCC) of the hypopharynx, and the human gingival fibroblast cell line HGF (derived from the histologically normal gingival biopsy) were used in this study. The authenticated cell lines were purchased from the American Type Culture Collection (ATCC; Manassas, Virginia, USA) within the last five years. </p> <p><strong>Autophagy modulation</strong></p> <p>For autophagy modulation, FaDu cells were treated for 24 h with 5nM bafilomycin A1 (Sigma-Aldrich, B1793), 50 µM of hydroxychloroquine sulphate (Sigma-Aldrich, H0915), 100 µM of Cpd18 (Calbiochem), 50 nM of autophinib (Sigma, SML2632), 10 µM of EACC (MedChemExpress), 200 nM of rapamycin (Sigma-Aldrich, R0395), 3 nM of Torin-1 (MedChemExpress), or 30 nM of NVP-BEZ235 (MedChemExpress). To induce starvation, cells were cultured in DMEM F12 without glutamine and without FBS (Biosera). Modulation of autophagy did not reduce the viability of FaDu cells.</p> <p><strong>Conditioned media preparation</strong></p> <p>see details in the accompanying paper</p> <p><strong>Fluorescence Microscopy</strong><br>The autophagosomal/autolysosomal/lysosomal dynamics of affected cells were observed using the combination of PremoTM Autophagy Tandem Sensor (P36239, Invitrogen) with the far-red emitting LysoTracker® Deep Red (L12492, Invitrogen) (Ex 647 nm/Em 668 nm). By combining acid-sensitive Emerald GFP (Ex 488 nm/Em 509 nm) with acid-insensitive TagRFP (Ex 555 nm/Em 584 nm) in the PremoTM kit, autophagosomes and autolysosomes labelling (yellow and red, respectively) is possible.<br>Immediately after transduction with 12 µl PremoTM Autophagy Tandem Sensor/2ml cell suspension, cells were seeded at 5 × 10<sup>5</sup> into 35-mm glass-bottomed gelatin-coated dishes (Ibidi, μ-Dish 35 mm, high Glass Bottom) and cultured for 48 h to equilibrate expression levels. Subsequently, cells were exposed to the selected agents for 6, 12, 24 and 48 hours before imaging. LysoTracker® Deep Red staining was performed 1 h before imaging. <br>To monitor the uptake of isolated PS-EVs by fibroblasts, we stained EVs with PKH67 (Sigma, PKH67GL) and then removed the remaining dye using Exosome Spin Columns (MW 3000) (Thermo Scientific, #4484449). The stained EVs were then suspended in 400 ul of cultivation medium and added to HGFB cells growing for 24 h in Ibidi µ-Slide I Luer (Ibidi, 80176). Image acquisition was performed 24 hours after EVs addition. 1 µl of 1 µg/ml of Hoechst 33342 (Enzo) (Ex 350 nm/ Em 461 nm) nuclear stain was added 1 hour before imaging.<br>To determine the viability of the cell population prior to isolation of EVs, cells were left in a culture dish with 1 ml of culture medium to which propidium iodide (Sigma-Aldrich) and Hoechst 33342 were added 45 minutes before capturing. <br>To maximize the possibility of comparison between samples, all samples (from a single cell line) were captured on the same day in a single run using the same microscope settings. For each time and each treatment, 10–12 fields of view were captured from randomized sites of the culture dish. Epifluorescent microscopy images and confocal microscopy images were acquired using Laser scanning confocal microscope Zeiss LSM 880 with AiryscanFast module (Carl Zeiss Inc.) using a C-apochromat 40x/1.20 W and C-Apochromat 63 /1.20 W. LysoTracker® Deep Red was excited HeNe 633 nm solid-state laser and emitted light was detected at 638–759 nm. Emerald GFP was excited 488 nm ArgonRemote laser, and emitted light was detected at 493–576 nm. TagRFP was excited DPSS 561 nm laser, and emitted light was detected at 570–650 nm. Hoechst 33342 was excited with a 405 nm solid-state laser, and emitted light was detected at 410–508 nm. Fluorescence images were acquired by the transmitted light detector. <br>Images were analyzed using ImageJ software and custom MATLAB software developed in our laboratory. The analysis process consists of the segmentation of cells from the background and extraction of the intensity of fluorescence channels (TagRFP, GFP, LysoTracker) inside cells. For segmentation, a thresholding-based method was used, where a manually selected threshold was applied. Segmentation was applied to the image created as the sum of all fluorescence channels to achieve segmentation independent of the intensity of individual channels. To achieve better segmentation without noisy pixels, fluorescence images were preprocessed with median filter (7x7) and Gaussian filter (standard deviation 1); additionally, binary segmentation was post-processed with morphological closing and removal of small binary connected components (<5000px). For intensity extraction, the mean value of segmented cell pixels was used for each field of view. Besides individual fluorescence channels, the mean colocalization of TagRFP and GFP was calculated with a pixel-wise multiplication of TagRFP and GFP channels.</p> <p><strong>File Naming</strong></p> <p>CZI images are organised in folders according to cell line, treatment time, and treatment. Names include magnification, cell line measured, treatment, and time of treatment,</p> <blockquote> <p>40x_FADU_BAF_12h_BF_4.czi</p> </blockquote> <p>The abbreviations used for treatments are as follows: BAF, bafilomycin A1; HCQ, hydroxychloroquine sulphate; Cpd18; APB, autophinib; EACC; RAPA, rapamycin; TOR1, Torin-1; BEZ, NVP-BEZ235; starv, starvation; </p>
Figure 43. Autophagy after a in Jumping spiders of the Phidippus princeps group in the southeastern United States (Araneae: Salticidae: Dendryphantina)
Figure 43. Autophagy after a staged encounter between an oxyopid spider (Oxyopes) and an adult female Phidippus pulcherrimus from Nassau County, Florida. 1, Female P. pulcherrimus feeding on her own left leg I (autophagy) after removing it (auto-amputation) when it was injured during an attack on an adult female Oxyopes. 2-3, Prolateral (2) and retrolateral (3) views of the amputated leg, showing amputation proximal to the trochanter. 4, This adult female Oxyopes was killed in the attack.
Metabolic enzymes moonlight as selective autophagy receptors to protect plants against viral-induced cellular damage
<p>The dataset contains all the original raw files for the following study:</p> <p><strong>Metabolic enzymes moonlight as selective autophagy receptors </strong><strong>to protect plants against viral-induced cellular damage</strong></p> <p>Marion Clavel<sup>1,2,*</sup>, Anita Bianchi<sup>1</sup>, Roksolana Kobylinska<sup>1</sup>, Roan Groh<sup>1,3</sup>, Juncai Ma<sup>4</sup>, Ranjith K. Papareddy<sup>1</sup>, Nenad Grujic<sup>1</sup>, Lorenzo Picchianti<sup>1,3</sup>, Ethan Stewart<sup>5</sup>, Michael Schutzbier<sup>1</sup>, Karel Stejskal<sup>1</sup>, Juan Carlos de la Concepcion<sup>1</sup>, Victor Sanchez de Medina Hernandez<sup>1,3</sup>, Yoav Voichek<sup>1</sup>, Pieter Clauw<sup>1</sup><strong>, </strong>Joanna Gunis<sup>1</sup>, Gerhard Durnberger<sup>1</sup>, Jens Christian Muelders<sup>2</sup>, Annett Grimm<sup>2</sup>, Arthur Sedivy<sup>5</sup>, Mathieu Erhardt<sup>6</sup>, Victoria Vyboishchikov<sup>1</sup>, Peng Gao<sup>1</sup>, Esther Lechner<sup>6</sup>, Emilie Vantard<sup>6</sup>, Jakub Jez<sup>5</sup>, Elisabeth Roitinger<sup>1</sup>, Pascal Genschik<sup>6</sup>, Byung-Ho Kang<sup>4</sup>, Yasin Dagdas<sup>1,*</sup></p> <p><strong> </strong></p> <p><strong>Affiliations</strong></p> <p><sup>1</sup>Gregor Mendel Institute, Austrian Academy of Sciences, Vienna BioCenter, Vienna, Austria.</p> <p><sup>2</sup>Max-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm, Germany</p> <p><sup>3</sup>Vienna BioCenter PhD Program, Doctoral School of the University at Vienna and Medical University of Vienna, Vienna, Austria</p> <p><sup>4</sup>School of Life Sciences, Centre for Cell & Developmental Biology and State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China</p> <p><sup>5</sup>Vienna Biocenter Core Facilities (VBCF), Vienna, Austria</p> <p><sup>6</sup>Institut de Biologie Moléculaire des Plantes, CNRS, Université de Strasbourg, 12, rue du Général Zimmer, 67084 Strasbourg, France</p> <p> </p> <p>*Correspondence: Marion Clavel (marion.clavel@mpimp-golm.mpg.de),</p> <p> Yasin Dagdas (yasin.dagdas@gmi.oeaw.ac.at)</p> <p><strong> </strong></p> <p><strong>Abstract</strong></p> <p>RNA viruses co-opt the host endomembrane system and organelles to build replication complexes for infection. How the host responds to these membrane perturbations is poorly understood. Here, we explore the autophagic response of <em>Arabidopsis thaliana</em> to three viruses that hijack different cellular compartments. Autophagy is significantly induced within systemically infected tissues, its disruption rendering plants highly sensitive to infection. Contrary to being an antiviral defense mechanism as previously suggested, quantitative analyses of the viral loads established autophagy as a tolerance pathway. Further analysis of one of these viruses, the Turnip Crinkle Virus (TCV) that hijack mitochondria, showed that despite perturbing mitochondrial integrity, TCV does not trigger a typical mitophagy response. Instead, TCV and Turnip yellow mosaic virus (TYMV) infection activates a distinct selective autophagy mechanism, where oligomeric metabolic enzymes moonlight as selective autophagy receptors and degrade key executors of defense and cell death such as EDS1. Altogether, our study reveals an autophagy-regulated metabolic rheostat that gauges cellular integrity during viral infection and degrades cell death executors to avoid catastrophic amplification of immune signaling.</p> <p> </p> <p>One archive corresponds to one main or supplemental figure.</p>
Confocal imaging raw data files of autophagy analysis in optn and p62 zebrafish mutants during Mycobacterium marinum infection
<p>Association of fluorescent Mycobacterium marinum bacteria with Ubiquitin immunolabelling and GFP-Lc3 signal in zebrafish larvae carrying mutations in the selective autophagy receptors optnineurin and p62. Data deposited are Leica LIF files belonging bioRxiv 415463; doi: https://doi.org/10.1101/415463</p>
Study on the role of AIMP1 gene activating PINK1/Parkin pathway in mediating mitochondrial autophagy in the pathogenesis of ARHL
Open the record for dataset details and reuse information.
Structural Basis for Membrane Recruitment of ATG16L1 by WIPI2 in Autophagy Raw GUV Data
<p>Raw GUV data of fluorescent protein imaged on a Nikon A1 confocal microscope with a 63 × Plan 359 Apochromat 1.4 NA objective. Three biological replicates were performed for each experimental 360 condition. Identical laser power and gain settings were used during the course of all conditions.</p>
Human STING is a proton channel (HEK293T Autophagy Experiment)
<p>RFP-LC3 and STING-HA-expressing FIP200 KO 293T cells were seeded on Fibronectin bovine plasma coated 24-well glass-bottom plates (Greiner Bio-One) the night before stimulation. Cells were then stimulated with 20 µg/ml cGAMP (Invivogen, #tlrl-nacga23-1) with 5ug/ml digitonin (Promega, #G9441) or 1 µM DIABZI (Invivogen, #tlrl-diabzi) with or without the addition of 10 µM C53 (Cayman, #37354) for 1 hour. Cells were then fixed with 2% Paraformaldehyde (Electron Microscopy Sciences) in PHEM buffer (Electron Microscopy Sciences) for 30 minutes at 37°C, washed three times with PBS and quenched with freshly prepared 0.1M Glycine for 10 minutes. Cells were permeabilized in 100% methanol for 30 minutes and stained with anti-HA (Millipore, #11867423001) for 1 hour at room temperature in 3% BSA, washed 5 times, and then stained with Alexa 647 anti-rat IgG (H+L) (Thermo, A-21247) in 3% BSA for 1 hour. After five washes, cells were incubated in 2X SSC with 200 ng/mL DAPI (Thermo Fisher) and imaged using the Nikon microscope used for organelle pH images. Images were acquired using a 60X 1.40 NA Plan Apo λ oil immersion objective (Nikon MRD01605) with Nikon type F immersion oil with the following lasers and filters: DAPI (405 nm laser, Chroma <a href="https://www.chroma.com/products/parts/et455-50m">ET455/50</a>), RFP-LC3B (561 nm laser, Chroma ET605/52), and STING-HA (640 nm laser, Chroma ET705/72), assaying five z planes per field of view with 0.625 µm spacing. Fields of view were selected using NIS Elements software coordinates without manual preselection.</p> <p>Images are maximum projections of multiple z-stacks. Channels are: DAPI, LC3B-RFP, and STING.</p>
Exploring the connection between autophagy and heat-stress tolerance in Drosophila melanogaster
<p>Mechanisms aimed at recovering from heat-induced damages are closely associated with the ability of ectotherms to survive exposure to stressful temperatures. Autophagy, a ubiquitous stress-responsive catabolic process, has recently gained renewed attention as one of these mechanisms. By increasing the turnover of cellular structures as well as the clearance of long-lived protein and protein aggregates, the induction of autophagy has been linked to increased tolerance to a range of abiotic stressors in diverse ectothermic organisms. However, whether a link between autophagy and heat-tolerance exists in insect models remains unclear despite broad ecophysiological implications thereof. Here, we explored the putative association between autophagy and heat-tolerance using <em>Drosophila</em> <em>melanogaster</em> as a model. We hypothesized that (i) heat-stress would cause an increase of autophagy in flies' tissues, and (ii) rapamycin exposure would trigger a detectable autophagic response in adults and increase their heat-tolerance. In line with our hypothesis, we report that flies exposed to heat-stress present signs of protein aggregation and appear to trigger an autophagy-related homoeostatic response as a result. We further show that rapamycin feeding causes the systemic effect associated with target of rapamycin (TOR) inhibition, induces autophagy locally in the fly gut, and increases the heat-stress tolerance of individuals. These results argue in favour of a substantial contribution of autophagy to the heat-stress tolerance mechanisms of insects.</p>
The Impact of Intermittent Fasting on Human Metabolism and Cell Autophagy
ClinicalTrials.gov study NCT02673515. IPD Sharing: NO. Countries: 1. Publications: 3.
Study of Combination Therapy With the MEK Inhibitor, Cobimetinib, Immune Checkpoint Blockade, Atezolizumab, and the AUTOphagy Inhibitor, Hydroxychloroquine in KRAS-mutated Advanced Malignancies
ClinicalTrials.gov study NCT04214418. IPD Sharing: YES. Countries: 1. Publications: 0.
Exploring the connection between autophagy and heat-stress tolerance in Drosophila melanogaster
Open the record for dataset details and reuse information.
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.