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277 results for “novel proteins”
A novel approach to the detection of unusual mitochondrial protein change suggests hypometabolism of ancestral simians: Supplemental Files
<p><strong>Supplementary Fig. S1</strong>: θ<sub>evo</sub> calculated for each analyzed edge for specific OXPHOS complexes. Analyses were performed as in fig. 1F, except that SPCSs calculated from mtDNA-encoded protein positions in Complex I, Complex III, Complex IV, or Complex V were used to generate θevo values.</p> <p><strong>Supplementary Fig. S2</strong>: Mammalian orders differ in their propensity for potentially efficacious mitochondrial protein substitutions within specific OXPHOS complexes (median calculations). Analysis was performed as in fig. 2A, except that θ<sub>evo</sub> values were obtained by analysis of mtDNA-encoded Complex I, Complex III, Complex IV, or Complex V polypeptides.</p> <p><strong>Supplementary Fig. S3</strong>: Mammalian orders differ in their propensity for potentially efficacious mitochondrial protein substitutions within specific OXPHOS complexes (median confidence intervals). Analysis was performed as in (<em>A</em>) fig. 2B or (<em>B</em>) fig. 2C, except that θ<sub>evo</sub> values were obtained by analysis of mtDNA-encoded Complex I, Complex III, Complex IV, or Complex V proteins.</p> <p><strong>Supplementary Fig. S4</strong>: Mammalian families differ in their propensity for potentially efficacious mitochondrial protein substitutions at specific OXPHOS complexes (median calculations). Analysis was performed as in fig. 3A, except that θ<sub>evo</sub> values were obtained by analysis of mtDNA-encoded Complex I, Complex III, Complex IV, or Complex V subunits.</p> <p><strong>Supplementary Fig. S5</strong>: Mammalian families differ in their propensity for potentially efficacious mitochondrial protein substitutions at specific OXPHOS complexes (median confidence intervals ordered by lower 90% median confidence limit). Analysis was performed as in fig. 3B, except that θ<sub>evo</sub> values were obtained by analysis of mtDNA-encoded Complex I, Complex III, Complex IV, or Complex V proteins.</p> <p><strong>Supplementary Fig. S6</strong>: Mammalian families differ in their propensity for potentially efficacious mitochondrial protein substitutions at specific OXPHOS complexes (median confidence intervals ordered by upper 90% median confidence limit). Analysis was performed as in fig. 3C, except that θ<sub>evo</sub> values were obtained by analysis of mtDNA-encoded Complex I, Complex III, Complex IV, or Complex V polypeptides.</p> <p>---</p> <p><strong>Supplementary File 1</strong>: All predicted protein substitutions along all edges at positions containing less than 2% gaps across input and ancestral sequences are listed, along with associated taxonomy information, TSS, and branch length. All alignment positions refer to Bos taurus reference sequences.</p> <p><strong>Supplementary File 2</strong>: The TSS calculated for each mitochondrial protein alignment position. All alignment positions refer to Bos taurus reference sequences.</p> <p><strong>Supplementary File 3</strong>: SPCS and θevo outputs are provided for analyses across all mitochondria-encoded positions, as well as for focused analyses of specific OXPHOS complexes and individual proteins.</p> <p><strong>Supplementary File 4</strong>: A GenBank flat file containing RefSeq entries for mammalian mtDNAs, as well as the entry for the reptile Anolis punctatus.</p> <p><strong>Supplementary File 5</strong>: A maximum likelihood inferred tree generated by a RAxML-NG analysis of concatenated and aligned protein coding sequences from mammalian and Anolis punctatusmtDNAs.</p> <p><strong>Supplementary File 6</strong>: Bootstrap replicates were generated from the alignment of concatenated protein coding sequences. Felsenstein’s Bootstrap Proportions (Felsenstein 1985) were calculated and used to label the maximum likelihood inferred tree of mammalian mtDNAs.</p> <p><strong>Supplementary File 7</strong>: Bootstrap replicates were generated using concatenated mammalian mtDNA coding sequences. Transfer Bootstrap Expectations (Lemoine 2018) were calculated and used to label the maximum likelihood inferred tree of mammalian mtDNAs.</p> <p><strong>Supplementary File 8</strong>: PAGAN tree output produced using aligned amino acid sequences and the rooted maximum likelihood inferred tree as input.</p>
Scored protein-protein interactions accompanying "A pan-plant protein complex map reveals deep conservation and novel assemblies"
<p><a href="http://plants.proteincomplexes.org/static/data/panplant_cfms_scores_annot.txt.gz">All scored pairwise protein-protein interactions with CF-MS scores (3,076,999 unique pairwise interactions)</a></p> <ul> <li>Description: Scores between Orthogroups with the corresponding CF-MS score and eggNOG generated orthogroup descriptions.</li> <li>Note: Only the highest scoring pairs are considered significant. A CF-MS score >= 0.509 corresponds to 10% FDR, >= 0.207 corresponds to 50% FDR</li> <li>Format: OrthogroupID1 [tab] OrthogroupID2 [tab] Score [tab] Annotation1 [tab] Annotation2</li> </ul>
Data for the article: "Molecular Modelling Reveals Eight Novel Druggable Binding Sites in SARS-CoV-2's Spike Protein" by Ilke Ugur and Antoine Marion
<p>This upload contains data related to the article<br> published as a preprint on ChemRxiv with DOI<br> https://doi.org/10.26434/chemrxiv.13292768</p> <p>"Molecular Modelling Reveals Eight Novel Druggable Binding Sites in SARS-CoV-2's Spike Protein"<br> by Ilke Ugur and Antoine Marion (2020)<br> Department of Chemistry, Middle East Technical University, Ankara, Turkey.</p> <p>For further information, please contact:<br> ilkeugur@metu.edu.tr ; amarion@metu.edu.tr</p> <p>The manuscript is currently under peer-review.</p> <p>Content:</p> <p>Library of molecules derived from DrugBank v 5.1.5:<br> - DrugBank_2020_5.1.5/ # All necessary files for the docking and refinement of the library of molecules.<br> -- DB_5.1.5_pH7.4_pdbqt/ ## PDBQT readily usable for docking with AutoDock Vina.<br> -- DB_5.1.5_pH7.4_mol2amber/ ## mol2 files containing assigned GAFF atom types and Gasteiger atomic charges.<br> -- DB_5.1.5_pH7.4_frcmod/ ## frcmod files containing missing molecular mechanics parameters<br> -- dbID_name.dat ## DrugBank ID to generic name dictionary</p> <p>Note: The files were prepared automatically via a series of operations handling openbabel and antechamber.<br> The protonation state of ionizable groups as well as Gasteiger atomic charges were assigned by openbabel for a pH of 7.4<br> mol2 and frcmod files can be used readily via the tleap module of AmberTools to produce topology files.</p> <p><br> Receptor structures:<br> - receptors/ # PDB files for the four structures of the spike protein considered in this work<br> -- CS00ns.pdb ## Closed state after the remodelling of missing loops (PDB ID 6vxx)<br> -- OS00ns.pdb ## Open state after the remodelling of missing loops (PDB ID 6vyb)<br> -- CS25ns.pdb ## Closed state after 25 ns of molecular dynamics in explicit water<br> -- OS25ns.pdb ## Open state after 25 ns of molecular dynamics in explicit water</p> <p>Note: All structures are aligned to CS00ns.pdb and can be converted to pdbqt for docking with AutoDock Vina</p> <p><br> Docking grid centers:<br> - dockingCenters/ # XYZ files containing the coordinates of each docking grid center considered in this work</p> <p>Note: The coordinates are given in the same frame as that of the four structures of the receptor.</p> <p><br> Binding sites:<br> - bindingSites/ # XYZ files with the coordinates of the representative atomic centres<br> # of each binding site identified in this work (A-H).</p> <p>Note: These files can be used to get a clearer picture of the binding sites within the structures<br> of the spike protein shared in the receptors directory.</p> <p><br> Final modelling results:<br> - allData.txt # data for all molecules in the set (approved and investigational)<br> - appData.txt # data for approved molecules only<br> - data.xlsx # data for all molecules in the set (approved and investigational)<br> # as a formatted excel spreadsheet</p> <p>Note: The columns are delimited with semi-colons ";".<br> The files contain the results for the best pose of all approved molecules for which<br> molecular mechanics-based geometry optimization succeeded, regardless of their score.<br> For other molecules, the result of their best pose is reported only for those complexes<br> having MM interaction energy lower or equal to -22.00 kcal/mol.</p> <p><br> Visualization:<br> - bs.pse # pymol session representing the binding sites within the<br> # closed state structure of the spike protein (CS00ns)<br> - pt.pse # pymol session representing the docking grid centres within<br> # closed statestructure of the spike protein (CS00ns)</p> <p>Note: the PSE files should be compatible with version 7.0 of pymol and later</p>
Protein elution profiles accompanying "A pan-plant protein complex map reveals deep conservation and novel assemblies"
<p>Key to files</p> <p><strong>Experiment_Order.csv</strong></p> <ul> <li>Description: Meta details of each experiment.</li> <li>Format: experiment_name,ExperimentID_order,tissue,experiment_type,spec,ExperimentID</li> </ul> <p><strong>Fraction_Details.csv</strong></p> <ul> <li>Description: Meta details of each fraction</li> <li>Format:FractionID,frac_order,ExperimentID</li> </ul> <p><strong>plant_virNOG_orthology.csv.gz</strong></p> <ul> <li>Description: Conversion between orthogroup and protein IDs.</li> <li>Format:ID,ProteinID,spec</li> </ul> <p><strong>orthogroup_annotation.csv.gz</strong></p> <ul> <li>Description: Orthogroup annotations</li> <li>Format:ID,Annotation,arath_genenames,arath_Entries,arath_Entry_names,arath_Protein_names,disruptions,tair_disruptions,lloyd2012_LOFs,arath_functions,arath_misc,pathway,unipathway,BioCyc,Reactome,BRENDA,kegg_pws,ec,arath_masses,arath_protein_names,arath_GO,devstages,tissues,tair,araport,orysj_genenames,orysj_Entries,orysj_Entry_names,orysj_Protein_names,orysj_disruptions,orysj_functions,orysj_misc</li> </ul> <p><strong>panplant_tidy_elution_virNOG.csv.gz</strong></p> <ul> <li>Description: Tidy (long format) table of counts of peptide spectral matches (PSMs) for all observed <strong>orthogroups</strong> for all experiments. Includes parts per million in each fraction. </li> <li>Format: ExperimentID,FractionID,ID,Total_PeptideCount,spec,ExperimentID_order,FractionID_order,abundance_ppm</li> </ul> <p><strong>panplant_tidy_elution_protcount.csv.gz</strong></p> <ul> <li>Description: Tidy (long format) table of counts of peptide spectral matches (PSMs) for all observed <strong>proteins</strong> for all experiments. </li> <li>Format: ExperimentID,FractionID,ProteinID,ProteinCount,spec,ExperimentID_order,FractionID_order</li> </ul> <p><strong>panplant_wide_elution_virNOG.csv.gz</strong></p> <ul> </ul> <ul> <li>Description: Table of concatenated elution profiles of raw counts of peptide spectral matches (PSMs) for all observed <strong>orthogroups</strong></li> <li>Format: OrthogroupID,[Fractions]</li> </ul> <p><strong>panplant_wide_elution_virNOG_annot.csv.gz</strong></p> <ul> </ul> <ul> <li>Description: Table of concatenated elution profiles of raw counts of peptide spectral matches (PSMs) for all observed <strong>orthogroups</strong>, includes annotation columns.</li> <li>Format: OrthogroupID,[Annotations],[Fractions]</li> </ul> <p><strong>panplant_wide_elution_expnorm.csv.gz</strong></p> <ul> </ul> <ul> <li>Description: Table of concatenated elution profiles reporting per-fractionation experiment-normalized peptide spectral matches (PSMs) for all observed<strong> orthogroups</strong></li> <li>Format: OrthogroupID,[Fractions]</li> </ul> <p><strong>panplant_wide_elution_expnorm_annot.csv.gz</strong></p> <ul> </ul> <ul> <li>Description: Table of concatenated elution profiles reporting per-fractionation experiment-normalized peptide spectral matches (PSMs) for all observed<strong> orthogroups</strong>, including columns with annotations</li> <li>Format: OrthogroupID,[Annotations],[Fractions]</li> </ul> <p><strong>[experiment_name].virNOG.wide.gz</strong></p> <ul> <li>Description: Elution profile of raw counts of peptide spectral matches (PSMs) for all observed<strong> orthogroups</strong> in one experiment</li> <li>Format: OrthogroupID,[Fractions]</li> </ul> <ul> </ul> <p><strong>[experiment_name].protcount.wide.gz</strong></p> <ul> <li>Description: Elution profile of raw counts of peptide spectral matches (PSMs) counts for all observed <strong>proteins </strong>in one experiment</li> <li>Format: ProteinID,[Fractions]</li> </ul> <p><strong>[species]_specconcat.virNOG.wide.gz</strong></p> <ul> <li>Description: Table of concatenated elution profiles of raw counts of peptide spectral matches (PSMs) for all observed <strong>orthogroups </strong>from a particular species. Only present for species with more than one experiment. </li> <li>Format: OrthogroupID,[Fractions]</li> </ul> <p><strong>[species]_specconcat.protcount.wide.gz</strong></p> <ul> <li>Description: Table of concatenated elution profiles of raw counts of peptide spectral matches (PSMs) for all observed <strong>proteins</strong> from a particular species. Only present for species with more than one experiment. </li> <li>Format: ProteinID,[Fractions]</li> </ul> <p> </p> <ul> </ul> <p>Species codes</p> <p>|Code | Species | Common name | Use |<br> |---|---|---|<br> | arath | Arabidopsis Thaliana | Arabidopsis | <br> | braol | Brassica oleracea | Broccoli |<br> | cansa | Cannabis sativa | hemp | <br> | cerri | Ceratopteris richardii | C-fern | <br> | chlre | Chlamydomonas reinhardtii | Chlamydomonas |<br> | chqui | Chenopodium quinoa | Quinoa | <br> | orysj | Oryza sativa var. japonica | Rice |<br> | selml | Selaginella moellendorffii | Selaginella | <br> | sollc | Solanum lycopersicum | Tomato | <br> | wheat | Triticum Aestivum | Wheat | <br> | soybn | Glycine max | Soybean | <br> | cocnu | Cocos nucifera | Coconut | </p> <p>| maize | MAIZE | maize | </p> <p> </p>
Data from: Convergent rates of protein evolution identify novel targets of sexual selection in primates
<p>Sexual selection is the differential reproductive success of individuals, resulting from competition for mates, mate choice, or success in fertilization. In primates, this selective pressure often leads to the development of exaggerated traits which play a role in sexual competition and successful reproduction. In order to gain insight into the mechanisms driving the development of sexually selected traits, we used an unbiased genome-wide approach across 21 primate species to correlate individual rates of protein evolution to relative testes size and sexual dimorphism in body size, two anatomical hallmarks of sexual selection in mammals. Among species with presumed high levels of sperm competition, we detected strong conservation of testes-specific proteins responsible for spermatogenesis and ciliary form and function. In contrast, we identified accelerated evolution of female reproductive proteins expressed in the vagina, cervix, and fallopian tubes in these same species. Additionally, we found accelerated protein evolution in lymphoid tissue, indicating that adaptive immune functions may also be influenced by sexual selection. This study demonstrates the distinct complexity of sexual selection in primates revealing contrasting patterns of protein evolution between male and female reproductive tissues.</p>
Data and Analysis Scripts for "Diviner uncovers hundreds of novel human (and other) exons through comparative analysis of proteins"
<p>This compressed directory contains the complete set of data and analysis scripts represented in "<em>Diviner</em> uncovers novel coding regions on eukaryotic genomes using targeted homology search."</p> <p> </p>
Data from: Convergent rates of protein evolution identify novel targets of sexual selection in primates
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the supplementary of Novel plastid genome characteristics in Fugacium kawagutii and accelerated evolution of plastid proteins in dinoflagellates
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Sensitization of FOLFOX-resistant colorectal cancer cells via the modulation of a novel pathway involving protein phosphatase 2A
<p>The treatment of colorectal cancer (CRC) with FOLFOX shows some efficacy, but these tumors quickly develop resistance to this treatment. We have observed an increased phosphorylation of AKT1/mTOR/4EBP1 and levels of p21 in FOLFOX-resistant CRC cells. We have identified a small molecule, NSC49L, that stimulates protein phosphatase 2A (PP2A) activity, downregulates the AKT1/mTOR/4EBP1-axis, and inhibits p21 translation. We have provided evidence that NSC49L- and TRAIL-mediated sensitization is synergistically induced in p21-knockdown CRC cells, which is reversed in p21-overexpressing cells. p21 binds with procaspase 3 and prevents activation of caspase 3. We have shown that TRAIL induces apoptosis through the activation of caspase 3 by NSC49L-mediated downregulation of p21 translation, and thereby cleavage of procaspase 3 into caspase 3. NSC49L does not affect global protein synthesis. These studies provide a mechanistic understanding of NSC49L as a PP2A agonist, and how its combination with TRAIL sensitizes FOLFOX-resistant CRC cells.</p>
Evolution of a novel female reproductive strategy in Drosophila melanogaster populations subjected to long term protein restriction
<p>Reproductive output is often constrained by availability of macronutrients, especially protein. Long term protein restriction, therefore, is expected to select for traits maximizing reproduction even under nutritional challenge. We subjected four replicate populations of <em>Drosophila melanogaster</em> to a complete deprivation of yeast supplement, thereby mimicking a protein restricted ecology. Following 24 generations, compared to their matched controls, females from experimental populations showed increased reproductive output early in life, both in presence and absence of yeast supplement. The observed increase in reproductive output was without associated alterations in egg size, development time, pre-adult survivorship, body mass at eclosion, and lifespan of the females. Further, selection was ineffective on lifelong cumulative fecundity. However, females from experiment regime were found to have a significantly faster rate of reproductive senescence following the attainment of the reproductive peak early in life. Therefore, adaptation to yeast deprivation ecology in our study involved a novel reproductive strategy whereby females attained higher reproductive output early in life followed by faster reproductive aging. To the best of our knowledge, this is one of the cleanest demonstration of optimization of fitness by fine tuning of reproductive schedule during adaptation to a prolonged nutritional deprivation.</p>
Substrates and a novel component in hSnd2-dependent ER protein targeting
<p>Protein import into the endoplasmic reticulum (ER) is essential for about 30% of the human proteome. It involves targeting of precursor proteins to the ER and insertion into or translocation across the ER membrane. Furthermore, it relies on signals in the precursor polypeptides and components, which read the signals and facilitate their targeting to a protein-conducting channel in the ER membrane, the Sec61 complex. Compared to the SRP- and TRC-dependent pathways, little is known about the SRP-independent/SND pathway. Our aim was to identify additional components and characterize the client spectrum of the human SND pathway. The established strategy of combining depletion of the central hSnd2-component from HeLa cells with proteomic- and differential protein abundance-analysis was used. The SRP and TRC targeting pathways were analyzed in comparison. TMEM109 was characterized as hSnd3. Unlike SRP but similar to TRC, the SND clients are predominantly membrane proteins with N-terminal, central, or C-terminal targeting signals.</p>
Novel cropping system strategies in China can increase plant protein with higher economic value but lower greenhouse gas emissions and water use
<p> This database contains the average crop residue, manure nitrogen, manure organic carbon, net greenhouse gas emissions, and cropland area for 17 cropping systems at prefecture level during the period 2014-2018. In addition, it contained the changes of net greenhouse gas emissions caused by the optimization at prefecture level and province level.</p> <p> We also shared the key code for optimizing cropping systems at prefecture level and provided the all data. Users can run it the Matlab platform.</p>
Data from: A novel protein-based fruit fly trap in melon flies Bactrocera cucurbitae for effective pest control management
<p>Agriculture remains a major source of subsistence for local communities in India. However, agricultural yield can be strongly affected by agricultural pest outbreaks. This can result in economic losses for small-scale farmers who already experience socioeconomic challenges, such as lack of appropriate infrastructure and subsidies. Sophisticated pest management techniques (e.g., sterile insect technique) are less accessible to small farmers in developing countries and therefore, alternative cost-effective approaches for pest management are needed. Here, we report our findings of a three-year-long field trial (2018 to 2020) in India which was designed to test for the potential effectiveness of a novel, slow-release formulation protein-based trap, compared to standard Cuelure traps against melon flies <em>Bactrocera</em> <em>cucurbitae</em> (Diptera: Tephritidae). Protein-bait traps can attract flies from both sexes (as opposed to males-only, chemical traps), bearing the potential to have greater long-term impact on pest populations by decreasing future reproductive potential of trapped individuals. We found that Cuelure had overall higher trapping performance, while protein-bait traps, despite trapping at lower efficiency, were equally effective for males and females. Simulations with our field data revealed that protein-bait traps can have an 'inclusive' advantage by trapping females and thereby preventing future individuals. Overall, our study highlights the potential benefits of using this alternative trapping technique to supplement pest management in developing countries.</p>
Novel Blood Test to Predict Safe Foods for Infants and Toddlers With Food Protein-induced Enterocolitis Syndrome (FPIES)
ClinicalTrials.gov study NCT04644783. IPD Sharing: NO. Countries: 1. Publications: 1.
Data from: BioID2-based tau interactome reveals novel and known protein interactions associated with multiple cellular pathways
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Data from: A novel sperm-derived seminal fluid protein in Caenorhabditis nematodes
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Data from: A novel protein-based fruit fly trap in melon flies Bactrocera cucurbitae for effective pest control management
Open the record for dataset details and reuse information.
Evolution of a novel female reproductive strategy in Drosophila melanogaster populations subjected to long term protein restriction
Open the record for dataset details and reuse information.
A massive proteogenomic screen identifies thousands of novel human protein coding sequences
<p>Accurate annotation of genes in the human genome is fundamental for biomedical research and genomic data interpretation. The Ensembl, RefSeq, and GENCODE consortiums continuously update the human genome annotations based on new computational and experimental evidence, and new proteins were identified constantly. The Genotype-Tissue Expression (GTEx) project has generated more than 15,000 RNA sequencing dataset from multiple-tissues of more than 800 donors which allows to model almost all transcripts and proteins in the human genome. Using proteins translated from the GTEx transcript model, more than 21 million in-silico trypsin-digested peptides were generated. To identify high-confidence novel proteins with proteomic support, we screened more than 2,000 proteomic projects in the PRIDE database and selected more than 50,000 mass spectrometry (MS) runs from 923 projects. These MS data were used to validate the predicted novel peptides. With a stringent standard, we identified almost 20,000 novel peptides. </p> <p>This dataset include files used in the the above analysis. More details can be found in the GitHub page (https://github.com/ATPs/human_novo_protein_2022). </p>
Data from: Molecular docking and dynamics studies to identify novel active compounds targeting potential breast cancer receptor proteins from an indigenous herb Euphorbia thymifolia Linn
<p>Breast cancer has become most prevalent disease and their incidence has doubled in Indian scenario. Targeted therapy with the novel compounds derived from plants could be the promising approach for the development of drugs. <em>Euphorbia thymifolia</em> L is a widely growing tropical herb which has been reported for its various ethnopharmacological properties, including anticancer properties. The aim of the present study was to identify the active phytocompounds present in the methanolic extract using an <em>I</em><em>n-silico</em> approach. The methanolic extract of <em>E. thymifolia</em> (ME.ET) was subjected to GC-MS analysis and the identified compounds were docked with potential protein targets implicated in breast cancer such as ERK1, AKT, EGFR/HER2, ER, MELK, PLK1, PTK6. Compounds with good docking score were further subjected to dynamics study to understand the protein ligand binding stability, ligand pathway calculation, molecular mechanics energies combined with Poisson-Boltzmann (MM/PBSA) calculation using Schrodinger suite. Out of 219 unique phytocompounds subjected to docking, two compounds namely, 3,6,9,12-tetraoxatetradecane-1,14-diyl dibenzoate (TTDB) and succinic acid, 2-(dimethylamino)ethyl 4-isopropylphenyl ester (SADPE) showed good docking score. Molecular dynamics study showed high affinity and low binding energy for TTDB with HER2, ERK1 and SADPE with ER. Hence this is the first study to identify and report active compounds from <em>E.thymifolia</em> linn. Further <em>invitro</em> and <em>invivo</em> anticancer studies can be performed to confirm these results and understand the molecular mechanism by which TTDB and SADPE exhibit anticancer activity against breast cancer.</p>
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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.