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.
523
datasets available to search
ShareScore release 0.9.0
Dataset results
523 results for “actin”
FIGURE 5. Chitonaster felli. USNM 1018861. A. Abactinal surface. B. Actinal surface. C.Marginal plate series. D in Taxonomy of high-latitude Goniasteridae (Subantarctic & Antarctic): one new genus, and three new species with an overview and key to taxa
FIGURE 5. Chitonaster felli. USNM 1018861. A. Abactinal surface. B. Actinal surface. C.Marginal plate series. D. Close-up of enlarged pedicellariae on actinal intermediate surface. Scale Bar = 0.5 cm.
Polarisation camera dSTORM datasets of actin in fixed HeLa cells labeled with phalloidin-Alexa Fluor 488
<p>Polarisation camera dSTORM dataset of the actin of fixed HeLa cells labeled with phalloidin-Alexa Fluor 488.</p> <p><strong>Image acquisition was performed as follows:</strong></p> <p>Imaging was performed on a widefield microscope equipped with a polarisation camera (CS505MUP, Thorlabs). The sample was excited using a 488 nm laser at quasi-TIRF, with a measured power density at the image plane of <span>5.04 kW/cm^2</span>. A single long-pass dichroic (Di02-R488, Semrock) was used to seperate fluorescence from the excitation. The emission was filtered using a long-pass (BLP01-488R, Semrock) and a bandpass filter (FF01-582/64, Semrock) before detection. An exposure time of 30 ms was used.</p> <p><strong>Samples were prepared as follows:</strong></p> <p><span>Cell culture: </span>HeLa TDS cells were cultured in DMEM (Gibco, Invitrogen) supplemented with 10 % Fetal Bovine Serum (FBS, Life Technologies), 1 % penicillin/streptomycin (Life Technologies), and 1 % glutamine (Life Technologies) at 37 °C + 5 % CO_2. Cells were periodically tested for mycoplasma contamination and passaged 3 times per week. Cells were plated at low density on high-precision glass coverslips (MatTek, P35G-0.170-14-C) 1 day prior to fixation for dSTORM experiments.</p> <p><span>Labeling:</span> Cells were simultaneously fixed and permeabilized in cytoskeleton buffer (CBS, 10 mM MES, 138 mM KCl, 3 mM MgCl_2, 2 mM EGTA, 4.5 % sucrose w/v, pH 7.4), + 4 % paraformaldehyde (PFA) and 0.2 % Triton for 6 minutes at 37 °C, and further fixed in CBS + 4 % PFA for 14 minutes at 37 °C. Post-fixation, cells were washed x3 in PBST (PBS supplemented with 0.1 % Tween) and permeabilized a second time in PBS + 0.5 % Triton for 5 minutes at room temperature. The samples were then washed 3 times in PBST and blocked for 30 minutes in 5 % BSA. Cells were washed x3 in PBST and then incubated with Alexa Fluor™ 488 Phalloidin (A12379, Invitrogen, 1:50 in PBS) for 1 h in the dark, followed by x2 washes in PBS. Prior to dSTORM imaging, PBS was replaced with dSTORM imaging buffer (base buffer consisting of 0.56 M glucose, 50 mM Tris (pH 8.5), and 10 mM NaCl supplemented with 5 U/mL pyranose oxidase (Sigma, P4234), 10 mM cysteamine (Sigma, 30070), 40 µg/mL catalase (Sigma, C100) and 2 mM cyclooctatetraene (Sigma, 138924).</p>
Polarisation camera dSTORM datasets of actin in fixed HeLa cells labeled with phalloidin-Alexa Fluor 647
<p>Polarisation camera dSTORM dataset of the actin of fixed HeLa cells labeled with phalloidin-Alexa Fluor 647.</p> <p><strong>Image acquisition was performed as follows:</strong></p> <p>Imaging was performed on a widefield microscope equipped with a polarisation camera (CS505MUP, Thorlabs). The sample was excited using a 638 nm laser at quasi-TIRF, with a measured power density at the image plane of 3.51 kW/cm^2. A multiband dichroic (Di03-R405/488/561/635-t1, Semrock) was used to seperate fluorescence from the excitation. The emission was filtered using a long-pass filter (BLP01-635R, Semrock) before detection. An exposure time of 30 ms was used.</p> <p><strong>Samples were prepared as follows:</strong></p> <p>Cell culture: HeLa TDS cells were cultured in DMEM (Gibco, Invitrogen) supplemented with 10 % Fetal Bovine Serum (FBS, Life Technologies), 1 % penicillin/streptomycin (Life Technologies), and 1 % glutamine (Life Technologies) at 37 °C + 5 % CO_2. Cells were periodically tested for mycoplasma contamination and passaged 3 times per week. Cells were plated at low density on high-precision glass coverslips (MatTek, P35G-0.170-14-C) 1 day prior to fixation for dSTORM experiments.</p> <p>Labeling: Cells were simultaneously fixed and permeabilized in cytoskeleton buffer (CBS, 10 mM MES, 138 mM KCl, 3 mM MgCl_2, 2 mM EGTA, 4.5 % sucrose w/v, pH 7.4), + 4 % paraformaldehyde (PFA) and 0.2 % Triton for 6 minutes at 37 °C, and further fixed in CBS + 4 % PFA for 14 minutes at 37 °C. Post-fixation, cells were washed x3 in PBST (PBS supplemented with 0.1 % Tween) and permeabilized a second time in PBS + 0.5 % Triton for 5 minutes at room temperature. The samples were then washed 3 times in PBST and blocked for 30 minutes in 5 % BSA. Cells were washed x3 in PBST and then incubated with Alexa Fluor™ 647 Phalloidin (A22287, Invitrogen, 1:50 in PBS) for 1 h in the dark, followed by x2 washes in PBS. Prior to dSTORM imaging, PBS was replaced with dSTORM imaging buffer (base buffer consisting of 0.56 M glucose, 50 mM Tris (pH 8.5), and 10 mM NaCl supplemented with 5 U/mL pyranose oxidase (Sigma, P4234), 10 mM cysteamine (Sigma, 30070), 40 µg/mL catalase (Sigma, C100) and 2 mM cyclooctatetraene (Sigma, 138924).</p>
Images used for Actin nano-architecture of phagocytic podosomes
<p>Images used for Actin nano-architecture of phagocytic podosomes</p>
Source data for "Single-molecule analysis of actin filament debranching by cofilin and GMF"
<p>Source data for "Single-molecule analysis of actin filament debranching by cofilin and GMF"</p>
All-atom accelerated molecular dynamics (aMD) simulations of Filamin-A (FLNa) actin-binding Domain, immunoglobulin-like Domains 3, 4, 5, 21 and 24 to investagate the impact of known missense mutations associated with periventricular nodular heterotopia in the liveborn males
<p>Data includes all of the wild-type and mutant trajectories of accelerated all-atom molecular dynamics (aMD) simulations of Filamin-A (FLNa, the product of <em>FLNA</em> gene located on chromosome X). Wild-type proteins are from the PDB structures with IDs: 4M9P, 3HOP, 3CNK. The mutations, including R484Q that we discovered in a Turkish family, were formerly found in the liveborn males with <em>FLNA</em>-associated periventricular nodular heterotopia (PNH), who survived with the only copy of mutated <em>FLNA</em>. To understand how these mutations lead to the PNH and simultaneously allow their survival, we performed these MD simulations for the wild-type and mutant systems.</p> <p>Systems were prepared in Visual Molecular Dynamics (VMD 1.9.3) by placing them in a TIP3P water box with approximately 20 Å thickness from the protein surface and neutralizing the system by adding counter ions in the form of NaCl. Of note, only protein parts were kept for the submission to reduce the size of files. Nanoscale Molecular Dynamics (NAMD 2.13-CUDA) was used to perform MD simulations with CHARMM36m force field. For pressure and temperature controls, Nosé-Hoover Langevin barostat and Langevin thermostat were used. ShakeH algorithm of NAMD was applied for water molecule constraints. 12 Å cut-off distance was used for van der Waals interactions. Switching function starts at 10 Å and reaches zero at 14 Å. Integration time-step was 2 fs. To compute the long-range Coulomb interactions, the particle-mash Ewald method was used. After a 10000-step minimization with conjugate gradient algorithm and an equilibration for 1 ns at 298 K under NVT ensemble, production simulations were run along 100 ns. Only the production simulations were supplied in this dataset. Further details are available in the regarding configuration files.</p> <p>Resulting analysis files and scripts are included with the carbon alpha-containing dcd files of the simulations.</p> <p>This dataset is not used directly for any study, but they are preliminary results for the usage of aMD to understand rare disease mechanisms.</p> <p>Related publications:</p> <pre>Zenodo repo of classical MD for these variants: https://doi.org/10.5281/zenodo.4483108</pre> <p>Journal article based on classical MD:</p> <p>Gerlevik U, Saygı C, Cangül H, Kutlu A, Çaralan EF, Topçu Y, et al. (2022) Computational analysis of missense filamin-A variants, including the novel p.Arg484Gln variant of two brothers with periventricular nodular heterotopia. PLoS ONE 17(5): e0265400. https://doi.org/10.1371/journal.pone.0265400</p>
Light-Induced Spiking Response in Proteinoid-Actin-Kombucha System
<p>Data for the paper: 'Light-Induced Spiking Response in Proteinoid-Actin-Kombucha System'</p>
Single particle analysis supplemental files for F-actin under myosin directed forces
<p>This dataset contains supplemental files associated with the single particle analysis for F-actin under myosin directed forces. Included are neural networks used to pick particles from 2D micrographs, flexibly fit atomic models and associated maps, and variability analysis-generated maps and associated models.</p>
Denoised tomograms and filament traces for F-actin under myosin directed forces
<p>This dataset contains the neural networks used to denoise cryo-electron tomograms of F-actin filaments under myosin directed forces as well as the denoised tomograms and filament traces.</p>
FIGURE 8. Grantia arctica, spicules from the fringe. A. Triactine with unproportionally large paired actines. B–C. Triactines regular. D–D3 in On some Calcaronea (Porifera: Calcarea) from the Barents Sea and adjacent Polar Basin
FIGURE 8. Grantia arctica, spicules from the fringe. A. Triactine with unproportionally large paired actines. B–C. Triactines regular. D–D3. Diactines.
FIGURE 38. Anthenea chinensis USNM 3036. A. Abactinal. B. Abactinal-superomarginal closeup. C. Actinal. D in New Ecological Observations and Occurrence for Asteroidea and Echinoidea in Hong Kong
FIGURE 38. Anthenea chinensis USNM 3036. A. Abactinal. B. Abactinal-superomarginal closeup. C. Actinal. D. Closeup actinal surface. Scale bar: 10.0 mm=A, C. Scale bar: 5.0 mm=B, D.
Giant worm-shaped ESCRT-scaffolds surround actin-independent integrin clusters, data part 6
<p>Part 6 of data for the article Giant worm-shaped ESCRT-scaffolds surround actin-independent integrin clusters.</p>
Giant worm-shaped ESCRT-scaffolds surround actin-independent integrin clusters, data part 4
<p>Part 4 of data for the article Giant worm-shaped ESCRT-scaffolds surround actin-independent integrin clusters.</p>
Giant worm-shaped ESCRT-scaffolds surround actin-independent integrin clusters, data part 3
<p>Part 3 of data for the article <em>Giant worm-shaped ESCRT-scaffolds surround actin-independent integrin clusters.</em></p>
Giant worm-shaped ESCRT-scaffolds surround actin-independent integrin clusters, data part 5
<p>Part 5 of data for the article Giant worm-shaped ESCRT-scaffolds surround actin-independent integrin clusters.</p>
Files associated with coordination of actin plus-end dynamics paper.
<p>Files associated with coordination of actin plus-end dynamics paper.</p>
FIGURE 25. Solasteridae Gut Contents. Solaster regularis USNM 1137298 gut contents. A. Actinal view. B in New Genera, Species, and observations on the biology of Antarctic Valvatida (Asteroidea)
FIGURE 25. Solasteridae Gut Contents. Solaster regularis USNM 1137298 gut contents. A. Actinal view. B. Closeup of Anasterias (identified as GUTcon) in S. regularis gut. C. Closeup of paxillae (identified as GUTcon) in Lophaster stellans USNM 1664405 gut.
MD_Simulations_Molecular_mechanisms_of_inorganic-phosphate_release_from_the_core_and_barbed_end_of_actin_filaments
<p>This repository contains the models, protocols, datasets and Jupyter notebooks to reproduce the computational experiments in the paper:</p> <p>"Molecular mechanisms of inorganic-phosphate release from the core and<br> barbed end of actin filaments"</p> <p>by W. Oosterheert, F.E.C Blanc, A. Roy, A. Belyy, M.B. Sanders,, O. Hofnagel, G. Hummer, P. Bieling, S. Raunser</p>
A platform for dissecting force sensitivity and multivalency in actin networks (supplemental)
<p>These data support the supplemental figures in our publication "<strong>A platform for dissecting force sensitivity and multivalency in actin networks</strong>". Unzip for a README file explaining data. See DOI 8239706 for main figure data. BioRxiv: https://www.biorxiv.org/content/10.1101/2023.08.15.553463v1</p>
Evaluation of Efficacy and Safety of BF-200 ALA Used With Photodynamic Therapy in Patients With Actinic Keratosis.
ClinicalTrials.gov study NCT02799082. IPD Sharing: NO. Countries: 0. Publications: 2.
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.