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1,204 results for “enzymes”
Proteolytic Enzyme Activity in Temperate Forest Soils at Harvard Forest and Pisgah State Forest 2007-2010
The objective of this research is to investigate the processes that limit or promote the activity and production of proteolytic enzymes in temperate forest soils. To meet this objective, we performed a series of integrated observations and experiments to investigate a conceptual model of proteolytic enzyme activity whereby activity is a function of the interaction between four parameters: soil temperature and moisture, substrate concentration, and the enzyme pool size. We used four dominant temperate forest tree species that differ in SOM chemistry and the enzymatic capabilities of their fungal symbionts as a model system. These four species differed in mycorrhizal association, with white ash (Fraxinus americana) and sugar maple (Acer saccharum) supporting arbuscular mycorrhizal (AM) fungi and eastern hemlock (Tsuga canadensis) and American beech (Fagus grandifolia) supporting ectomycorrhizal (ECM) fungi. Further, the ECM associated species have leaf litter and SOM that is characterized by higher ratios of C:N than the AM associated. Soil samples were collected two sites, one located at the Prospect Hill Tract of the Harvard Forest and the other at the Pisgah State Forest. The sites have similar land use history and stand age. Soils at both sites are inceptisols classified as Typic Dystrochrepts derived from glacial till overlying granite-schist-gneiss bedrock. Experimental plots dominated by one of four target tree species were established at each site. Stands of sugar maple (Acer saccharum) and American beech (Fagus grandifolia) were located in Pisgah. Stands of Eastern hemlock (Tsuga canadensis) and white ash (Fraxinus americana) were located in Harvard Forest. At a later date, plots were also established in a red oak (Quercus rubra) stand on Prospect Hill in the MES tower footprint. At each site we located six replicate, 8 m radius, monodominant plots that were based on the following criteria: (1) more than 80% of the standing basal area was composed of the targ
Extracellular Enzyme Activity in Rhizosphere Soil at Harvard Forest and Pisgah State Forest 2010
The exudation of carbon (C) by tree roots stimulates microbial activity and the production of extracellular enzymes in the rhizosphere. Here, we investigated whether the strength of rhizosphere processes differed between temperate forest trees that vary in soil organic matter (SOM) chemistry and associate with either ectomycorrhizal (ECM) or arbuscular mycorrhizal (AM) fungi. We measured rates of microbial and extracellular enzyme activity, and nitrogen (N) availability in samples of rhizosphere and bulk soil influenced by four temperate forest tree species (i.e., to estimate a rhizosphere effect). The magnitude of the rhizosphere effects could not be easily characterized by mycorrhizal associations or SOM chemistry. Ash had the lowest rhizosphere effects and beech had the highest rhizosphere effects, representing one AM and one ECM species, respectively. Hemlock and sugar maple had equivalent rhizosphere effects on enzyme activity. However, the form of N produced in the rhizosphere varied with mycorrhizal association. Enhanced enzyme activity primarily increased amino acid availability in ECM rhizospheres and increased inorganic N availability in AM rhizospheres. These results show that the exudation of C by roots can enhance extracellular enzyme activity and soil-N cycling. This work suggests that global changes that alter belowground C allocation have the potential to impact the form and amount of N to support primary production in ECM and AM stands.
Alignments used in "The evolution of the phenylpropanoid pathway entailed pronounced radiations and divergences of enzyme families"
<p>Alignments used in de Vries et al. (2021) "The evolution of the phenylpropanoid pathway entailed pronounced radiations and divergences of enzyme families" published as</p> <p>(1) a pre-print: https://doi.org/10.1101/2021.05.27.445924</p> <p>(2) in Plant Journal (in press)</p>
Dataset for "Reduction-responsive immobilised and protected enzymes" research article
<p>The dataset for the paper titled "Reduction-responsive immobilised and protected enzymes".<br>The dataset includes the following items:<br><br>1. Unprocessed tif files (4 items) of the scanning electron microscopy (SEM) micrographs;<br>These SEM micrographs are presented in Fig. 3a and Fig. 3b in the manuscript and also in Fig. S1a and Fig. S1b in the supporting information document.<br><br>2. "Reduction-responsive immobilised and protected enzymes" xls file (1 file) including 4 datasheets;<br>- The "<strong>Cell experiment" </strong>sheet includes the cell viability results in Fig. 5d and Fig. S5.<br>- The "<strong>Enzyme activity - B-Gal"</strong> sheet includes all the results regarding the B-Gal enzyme activity in Fig. 4, main text, and Fig. S3.<br>- The "<strong>Enzyme activity - ASNase"</strong> sheet includes all the results regarding the ASNase enzyme activity in Fig. 5b, Fig. 5c, and Fig. S4.<br>- The<strong> "B-Gal and ASNase layer growth"</strong> sheet includes all the results regarding the layer growth reactions and kinetics of B-Gal and ASNase enzymes in Fig. 3d, Fig. 5a, and Fig. S1d.<br><br>3. "SNP and layer growth analysis" xls file (1 file) including 13 datasheets;<br>These datasheets contain the raw data of the size measurements of the silica nanoparticles conducted on the SEM micrographs before and after layer growth for each sampling timepoint for both B-Gal and ASNase enzymes with glutaraldehyde (Glu) and DSP as linkers.<br>Note: These data were used to make the graphs in the "<strong>B-Gal and ASNase layer growth" </strong>sheet.</p>
Data set for the journal article: Site-Specific Protein Ubiquitylation Using an Engineered, Chimeric E1 Activating Enzyme and E2 SUMO Conjugating Enzyme Ubc9
<p>Mutations observed in evolved chimeric E1 variants. Top row (1.X to 4.X) describes rounds of evolutions with respective variants in the round. </p> <p>Residues that appear to be enriched are highlighted with gray fill. Star (★) marks residues subjected to saturation mutagenesis in the round 4.</p>
Soil enzyme activities and soil chemistry near and away from alder collected at sites along the Sagavanirktok River, BNZ LTER sites UP3a-c, and sites near BNZ LTER site WDI6, collected June and July 2019
This dataset contains the data and R code associated with Heslop et al. 2021 "Soil Enzymes Illustrate the Effects of Alder Nitrogen Fixation on Soil Carbon Processes in Arctic and Boreal Ecosystems" published in Ecosphere. Activities of acid phosphatase, beta-glucosidase, and phenoloxidase, as well as %N, C, P, and Mo, 15N and 13C natural abundance, resin extractable P, and SOM chemsitry using FTIR spectroscopy were measured for soils taken under alder (Alnus viridis ssp. fruticosa) canopies and 5 m away. Samples were collected in the Arctic at sites near Sagwon Bluffs and the Lupine-Sagavanirktok river confluence as well as in the boreal forest at BNZ LTER sites UP3a-c and at sites located near BNZ LTER site WDI6.
SEA01 Soil extracellular enzyme activity data from the Belowground Plot Experiment
Data describe the activity of soil extracellular enzymes collected approximately every month in 2015 from the Belowground Plot Experiment. The measured enzymes depolymerize soil organic matter to release labile carbon, nitrogen, and phosphorus. Soil carbon and nitrogen were measured in July 2015 only, since these soil variables are not expected to change monthly.
Enzymes from the BRENDA and CAZy databases annotated with organism growth temperatures and predicted Topt
<p>This repo is an updated version of repo <strong>Gang Li, & Martin KM Engqvist. (2019). Enzymes from the BRENDA database annotated with organism growth temperatures and predicted <em>T</em><sub>opt</sub> (Version 1.0) [Data set]. Zenodo. http://doi.org/10.5281/zenodo.2539114. </strong></p> <p>Experimental as well as predicted organism growth temperatures were used to annotate enzymes from the BRENDA database (doi: 10.1093/nar/gky1048, https://www.brenda-enzymes.org) version 2018.2 (July 2018) and CAZy database (http://www.cazy.org/). </p> <p>An updated machine learning model was applied to predict the optimal functional temperature of enzymes from BRENDA and CAZy. </p> <p>There are four files in this repo:</p> <p>1. 'annotated_brenda.tsv' is a tab-seperated file that contains the annotated enzymes from BRENDA. There are 9 columns in the file: index column; "ec", EC number; "uniprot_id", protein id in Uniprot database; "domain", the domain of life (superkingdom), either Archaea, Bacteria, or Eukarya; "organism", species name; "ogt", optimal growth temperature of the organism; "ogt_note", whether the experimental or predicted ogt is used; "topt", the optimal functional temperature of the enzyme; "topt_note", whether the experimental or predicted topt is used.</p> <p>2. 'annotated_cazy.tsv' is a tab-seperated file that contains the annotated enzymes from CAZy. There are 12 columns in the file: index column; "family", CAZy family id; "genbank", genbank id; "Protein Name", the protein name from CAZy database; "ec", EC number; "organism", strain name; "uniprot_id", protein id in Uniprot database; "PDB/3D", structure id in PDB database; "ogt", optimal growth temperature of the organism; "ogt_note", whether the experimental or predicted ogt is used; "topt", the optimal functional temperature of the enzyme; "topt_note", whether the experimental or predicted topt is used.</p> <p>3. 'brenda.sql', which is a SQLite3 database version of 'annotated_brenda.tsv', with an additional column of enzyme sequences.</p> <p>4. 'cazy.sql', which is a SQLite3 database version of 'annotated_cazy.tsv'', with an additional column of enzyme sequences.</p> <p>The SQLite3 databases are for the Tome tool (<a href="https://github.com/EngqvistLab/Tome">https://github.com/EngqvistLab/Tome</a>), version 2.0.</p>
Three-Enzyme Phosphorylase Cascade Immobilized on Solid Support for Biocatalytic Synthesis of Cello-oligosaccharides
<p>We provide here the underlying data of the scientific publication "Three-Enzyme Phosphorylase Cascade Immobilized on Solid Support for Biocatalytic Synthesis of Cello-oligosaccharides". Please find the abstract below:</p> <p>Enzyme cascades are promising for multistep biocatalytic synthesis, but their effective use beyond the proof-of-concept stage is challenging. Strategies to recycle the individual enzymes are critical for the applicability of such cascades. Immobilization on solid support is well developed for single enzymes but remains difficult for enzyme ensembles. Here, we show a controlled co-immobilization of three glycoside phosphorylases to establish a highly active and recyclable biocatalyst for the conversion of sucrose and glucose into soluble (short-chain) cello-oligosaccharides. We use protein fusion with the binding module Z<sub>basic2 </sub>to enable non-covalent surface tethering of all enzymes according to a uniform principle and in a programmable fashion. We thus achieve loading of the phosphorylases in an activity ratio optimal for the overall conversion rate and for controlling the cello-oligosaccharide chain length (≤ 6), hence the solubility, in the reaction. We demonstrate efficient production of ~12 g/L cello-oligosaccharides in 5 reaction cycles with integrated enzyme re-use. This study presents a major advance toward the practical use of systems bio-catalysis on solid support.</p>
Supplementary data for "Machine learning-based prediction of activity and substrate specificity for OleA enzymes in the thiolase superfamily"
<p>Supplementary data for "Machine learning-based prediction of activity and substrate specificity for OleA enzymes in the thiolase superfamily"</p>
TERMINUS WP4: Enzyme immobilization, protection, and triggering. TASK 4.2: Experimental data
<p>A. E. Delorme, J.-M. Andanson and V. Verney: Improving Laccase Thermostability with aqueous Natural Deep Eutectic Solvents, <em>Int. J. Biol. Macromol.</em>, (2020), <a href="https://doi.org/10.1016/j.ijbiomac.2020.07.022">doi.org/10.1016/j.ijbiomac.2020.07.022</a></p> <p><strong>Abstract</strong></p> <p>The wide-spread use of laccases in industry is often limited due to the enzyme inactivation over time at conditions which exceeds the operating conditions of the enzymes, which are neutral pH and ambient temperatures (30-40 °C). Today, the most common strategies used to improve enzyme stability are chemical modifications and immobilization of enzymes on solid supports. Although, these techniques have shown promise in improving enzyme stability, they are often synthetically demanding and unsustainable in terms of costs and synthesis route. Deep Eutectic Solvents (DESs) have attracted considerable attention as reaction media in biocatalysis due to their promising compatibility with enzymes and sustainable derivation. In this contribution we demonstrate the possibility of applying DESs as incubation media to inhibit thermal inactivation of laccase T. Versicolor. For example we show that by incubating laccase in 25 wt% of a betaine-xylitol based DES at 70 °C for 15 minutes, the measured residual activity of laccase is a near 10 fold greater than the measured residual activity of laccase when incubated without the DES. The drastic enhancement of the enzyme thermostability by pre-incubation of laccase in DES media showcases a facile, cheap and green method of boosting the stability laccase.</p> <p> </p> <p><strong>Dataset</strong></p> <p>This dataset contains all the UV-kinetic raw data used to calculate the laccase activity in the article “Improving Laccase Thermostability with aqueous Natural Deep Eutectic Solvents”. Data are available in a compressed .zip file with 1 folder (Laccase-thermostability-DES_v1.0_TER_WP4_D4-2) containing 3 files:</p> <p> </p> <ul> <li>one tabular file saved in .xlsx format containing all UV-kinetic raw data used to calculate the relative and residual laccase activities for figure 1-6 in the article (<a href="https://doi.org/10.1016/j.ijbiomac.2020.07.022">doi.org/10.1016/j.ijbiomac.2020.07.022</a>). The Laccase-thermostability-DES_v1.0_TER_WP4_D4-2.xlsx file contains the UV kinetic absorption spectra (at wavelength 417 nm) and each row in represent one spectrum. The spectra are grouped under laccase incubation temperature and length of time of incubation. For each incubation time, three solutions were prepared which signifies the three trials under each incubation times. Each sheet in the .xlsx file represent the data set collected for each laccase incubation medium</li> <li>The Materials_and_experimental_method-D4-2-Laccase-Thermostability-DES.pdf file details the experimental method and conditions for the data acquisition presented in the Laccase-thermostability-DES_v1.0_TER_WP4_D4-2.xlsx. Guidance is also provided on how to use the data to calculate the laccase activity and thermostability.</li> <li>The_metadata_information-D4-2-Laccase-Thermostability-DES.pdf includes more detailed metadata information for the dataset represented in the excel file Laccase-thermostability-DES_v1.0_TER_WP4_D4-2.xlsx.</li> </ul>
Evolutionary coupling range varies widely among enzymes: data and code
<p>Data and code needed to reproduce result of the paper "Evolutionary coupling range varies widely among enzymes", by J. Echave.</p> <p>biorxiv: https://doi.org/10.1101/2020.12.19.423588</p>
TERMINUS WP4 Enzyme immobilization, protection, and triggering. TASK 4.1 TASK 4.2 Experimental data – Hydrolytic enzyme immobilization and triggering
<p>The use of polymer-degrading enzymes is an attractive and effective method for the management of plastic waste. Synthetic polyesters such as poly(ethylene terephthalate) (PET) or polyurethane (PUR) have been shown to be susceptible to enzymatic degradation by microbial polyester hydrolases, as well as biopolyesters such as poly(lactic acid) (PLA), poly(butylene succinate) (PBS), and polycaprolactone (PCL). However, raw enzymes are not used in polymer formulations because the high processing temperatures would deteriorate the proteins (whose enzymes are made of), by destroying their macromolecular structure and catalytic center. The possibility of a direct use of enzyme in a polymer formulation thorough an opportune protective system, able to preserve the activity of the enzyme and increase its thermal stability, could open to new materials degradable “on-demand” at the end-of life. Therefore, significant progresses could be possible for example in the field of plastic packaging, which currently represents 40% of the total production of plastic in EU and requires the consumption of more than 19 million tons of oil and gas.</p> <p>This dataset includes some of the experimental raw data presented by UNIBO in deliverable D4.1 and D4.3, namely FT-IR analysis, X-ray diffraction analysis, TGA analysis, UV-Vis spectrophotometer. Data are available in a compressed .zip file with 1 folder (Hydrolytic enzyme immobilization and triggering_v1.0_TER_WP4_D4.1_D4.3) containing 6 files, 4 .xlsx files containing the FT-IR, XRD, TGA, Enzyme release kinetics and Thermostability raw data, 1 .pdf file describing the experimental methods and materials and a second .pdf file outlining the metadata and information.</p> <p>1_Hydrolytic enzyme immobilization and triggering _FTIR.xlsx contains all the FTIR raw data and curves of the Immobilized enzyme systems prepared.</p> <p>2_Hydrolytic enzyme immobilization and triggering _XRD.xlsx contains all the XRD raw data and profiles of the Immobilized enzyme systems prepared.</p> <p>3_Hydrolytic enzyme immobilization and triggering _TGA.xlsx contains all the TGA raw data and curves of the Immobilized enzyme systems prepared.</p> <p>4_Hydrolytic enzyme immobilization and triggering release activity and thermal resistance.xlsx contains all the raw data and graphs related to the protein content, activity of the Immobilized enzyme systems prepared after release and the thermal stress experiment data.</p> <p>Materials and experimental method_D4.1_D4.3_Hydrolytic enzyme immobilization and triggering.pdf contains the details of the experimental method and conditions for the data acquisition presented in the data set.</p> <p>Metadata information for WP4 dataset_D4.1_D4.3_Hydrolytic enzyme immobilization and triggering.pdf includes more detailed metadata information for the dataset presented.</p>
Biotransamination of Furan-Based Aldehydes with Isopropylamine: Enzyme Screening and pH Influence
<p>Furan-based amines are highly valuable compounds which can be directly obtained via reductive amination from easily accessible furfural, 5-(hydroxymethyl)furfural (HMF) and 2,5-diformylfuran (DFF). Herein the biocatalytic amination of these carbonyl derivatives is disclosed using amine transaminases (ATAs) and isopropylamine (IPA) as amine donors. Among the different biocatalysts tested, the ones from <i>Chromobacterium violaceum</i> (Cv-TA), <i>Arthrobacter citreus</i> (ArS-TA), and variants from <i>Arthrobacter</i> sp. (ArRmut11-TA) and <i>Vibrio fluvialis</i> (Vf-mut-TA), afforded high levels of product formation (>80 %) at 100–200 mM aldehyde concentration. The transformations were studied in terms of enzyme and IPA loading. The pH influence was found as a key factor and attributed to the imine/aldehyde equilibrium that can arise from the high reactivity of the carbonyl substrates with a nucleophilic amine such as IPA.</p>
Dataset for the Endothelin-converting enzyme 1 antibody screening study
<p>This project contains the following underlying data included in a study aimed at characterizing six antibodies agaisnt Endothelin-converting enzyme 1 (ECE1). The study is available on Zenodo (DOI: 10.5281/zenodo.7459248).</p>
Alpha-Galactosaminidase family GH191 protein from Environmental sample (99.2% identity to Myxococcus fulvus enzyme): X-ray diffraction images
<p><span>This submission includes a zip archive of diffraction images recorded with the Dectris EIGER X 9M detector at the DIAMOND beamline I04-1. The model of the crystal structure and associated information can be found in the Protein Data Bank entry 9EP5. This is a case of crystal pathology – partial disorder. The model has C 2 2 21 symmetry and two molecules per asymmetric unit with occupancies 1 and 1/3. The molecule with partial occupancy overlaps with a symmetry related molecule.</span></p>
Activity of antioxidant enzymes and lipid peroxidation of soybean plants treated with five Diaporthe species
<p>Absorbance data from spectrophotometric measurements of catalase, reduced glutathion, lipid peroxidation and superoxide-dismutase of soybean cv. Sava plants infected with five <em>Diaporthe</em> species (i.e. <em>D. aspalathi</em>, <em>D. caulivora</em>, <em>D. eres</em>, <em>D. gulyae</em>, <em>D. longicolla</em>).</p> <p>Supplementary data to the publication Petrovic et al. (2023) The biochemical response of soybean cultivars infected by <em>Diaporthe</em> species complex. Plants 12, 2896. https://doi.org/10.3390/plants12162896</p>
Molecular Models and Wave Function Definitions for Models A-G of the [2Fe]F Cluster in FeFe-hydrogenase Maturase Enzyme HydF
<p>The dataset contains all relevant atomic positional coordinates for 2Fe-cluster models, and electronic wave function data (using formatted Gaussian checkpoint files) as described in the related publication (see citation below).</p> <p>The version 2.0 contains additional models for [2Fe-2S] cluster linked [2Fe]F constructs.</p> <p>The top folder contains "analysis.xlsx" electronic spreadsheet that summarizes all the numerical results for absolute and relative electronic energy values, internal coordinates, calculated and scaled vibrational frequencies for diatomic stretching modes. The details of developing scaled quantum forcefields as a function of level of theory and model composition are also given.<br> The schematic structural definitions are given in the "models.pdf" file and keys for abbreviations are provided in "symbols.txt" file.<br> </p>
Three-Enzyme Phosphorylase Cascade for Integrated Production of Short-chain Cellodextrins
<p>Cellodextrins are linear β-1,4-gluco-oligosaccharides that are well soluble in water up to a degree of polymerization (DP) of ~6. Soluble cellodextrins have promising applications as nutritional ingredients. A DP-controlled, bottom-up synthesis from expedient substrates is desired for their bulk production. Here, we developed a three-enzyme glycoside phosphorylase cascade for the conversion of sucrose and glucose into the short-chain cellodextrins (DP range 3 – 6). The cascade reaction involves iterative β-1,4-glucosylation of glucose from α-glucose 1-phosphate (αGlc1-P) donor that is formed in situ from sucrose and phosphate. With final concentration and yield of soluble cellodextrins set as targets for the biocatalytic synthesis, we identified, and partly optimized, three major factors of reaction efficiency: the ratio of enzyme activities; the ratio of sucrose and glucose; and the phosphate concentration used. We demonstrate efficient use of the phosphate/αGlc1-P shuttle for cellodextrins production and obtain the soluble product at 40 g/L under near complete utilization of the donor substrate offered (88 mol.% from 200 mM sucrose). The productivity was 16 g/(L h). Through a simple two-step route, the soluble cellodextrins were recovered from the reaction mixtures in ≥ 95% purity and ~92% yield. Overall, this study provides the basis for their integrated production. </p>
Plasmid Maps for a Nuclear Transformation Vector in Chlamydomonas reinhardtii for the Expression and Secretion of the Plastic-Degrading Enzyme (PHL7)
<p><strong>pJP32PHL7 Vector:</strong></p> <ul> <li> <p><strong>Size:</strong> 5692 bp</p> </li> <li> <p><strong>Key Features:</strong></p> <ul> <li><strong>HSP70 Promoter:</strong> A heat shock protein promoter fused with the <em>rbcS2</em> promoter to drive expression of downstream genes.</li> <li><strong>Ble Resistance Gene:</strong> Confers resistance to bleomycin, useful for selection in <em>Chlamydomonas reinhardtii</em>.</li> <li><strong>PHL7 Gene:</strong> Encodes the plastic-degrading enzyme PHL7, inserted downstream of the <em>F2A</em> site for expression in the host.</li> <li><strong>Intron Sequences:</strong> Contains multiple <em>rbcS2</em> introns for enhancing expression in <em>Chlamydomonas</em>.</li> <li><strong>Selectable Marker (AmpR):</strong> Confers ampicillin resistance for selection in <em>E. coli</em>.</li> <li><strong>Replication Origin:</strong> Includes <em>ori</em> and <em>F1 ori</em> for replication in <em>E. coli</em>.</li> </ul> <p> </p> </li> <li> <p><strong>Applications:</strong> This vector is designed for nuclear transformation in <em>Chlamydomonas reinhardtii</em>, enabling the expression and secretion of the plastic-degrading enzyme (PHL7) under the control of a hybrid <em>HSP70</em>rbcS2 promoter.</p> </li> </ul> <p><strong>pJP32PHL7dg Vector:</strong></p> <ul> <li> <p><strong>Size:</strong> 5692 bp</p> </li> <li> <p><strong>Key Features:</strong></p> <ul> <li><strong>HSP70 Promoter:</strong> Retains the HSP70 and <em>rbcS2</em> fusion promoter for gene expression.</li> <li><strong>LacZ Alpha Fragment:</strong> Includes a LacZ alpha fragment for blue/white screening.</li> <li><strong>PHL7 Gene:</strong> Encodes the plastic-degrading enzyme PHL7, linked downstream of the <em>F2A</em> site, allowing for expression in the host.</li> <li><strong>Ble Resistance Gene:</strong> Also confers bleomycin resistance for selection in <em>Chlamydomonas</em>.</li> <li><strong>Selectable Marker (AmpR):</strong> Confers ampicillin resistance for selection in <em>E. coli</em>.</li> <li><strong>Intron Sequences:</strong> Contains <em>rbcS2</em> introns for optimizing gene expression in the host organism.</li> </ul> <p> </p> </li> <li> <p><strong>Applications:</strong> The pJP32PHL7dg vector is similarly designed for nuclear transformation in <em>Chlamydomonas reinhardtii.</em> It also facilitates the expression and secretion of the plastic-degrading enzyme PHL7, driven by the hybrid <em>HSP70</em>rbcS2 promoter, but without glycosilation sites.</p> </li> </ul>
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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.