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37 results for “Luciferase”
Assessing protein refolding by molecular chaperones using smFRET and luciferase refolding assays
<p>Dataset contains (predominantly) pre-processed data for single-molecule FRET (smFRET) and luciferase refolding assays. For smFRET experiments, the conformation of individual luciferase (FlucIDS) proteins was monitored in real-time and incubated either in the presence of chemical denaturant or in the presence of various combinations and concentrations of molecular chaperones from the bacterial Hsp70 system (i.e., DnaJ, DnaK and GrpE). Similarly, the ability of this chaperone system to refold FlucIDS to an enzymatically active state was assessed using luciferase refolding assays. Owing to the size of the raw .TIF images generated during smFRET experiments, only a subset of these representative raw images are provided (see figure 1C, 2M GdHCl treatment) that can be used to perform the analysis from its earliest starting point.</p> <p>Note: data required for Figures S4, S5 and S6 are provided in Figure 2, 3 and 4, respectively.</p> <p>Note 2: Within each figure is a txt document that outlines the format and meaning of each dataset.</p>
Let There Be Light: Genome-reduction Enables Bacillus subtilis to Produce Disulfide-bonded Gaussia Luciferase
<p>Supplemental Material:</p> <ul> <li>Plasmid Maps in PNG format</li> <li>Plasmid Sequences in GB format</li> <li>Plasmid Sequences in DNA format (SnapGene)</li> </ul>
Illuminating the mechanism and allosteric behavior of NanoLuc luciferase
<p>NanoLuc, a superior β-barrel fold luciferase, was engineered 10 years ago but the nature of its catalysis<br> remains puzzling. Here experimental and computational techniques were combined, revealing that<br> imidazopyrazinone luciferins bind to an intra-barrel catalytic site but also to an allosteric site shaped on<br> the enzyme surface. Binding to the allosteric site prevents simultaneous binding to the catalytic site, and<br> vice versa, through concerted conformational changes. We demonstrate that restructuration of the<br> allosteric site can boost the luminescent reaction in the remote active site. Mechanistically, an intra-barrel<br> arginine coordinates the imidazopyrazinone component of luciferin which then react with O 2 via a radical<br> charge-transfer mechanism, and it also protonates the resulting excited amide product to form a light-<br> emitting neutral species. Concomitantly, an aspartate, supported by two tyrosines, is fine-tuning the blue<br> color emitter to secure a high emission intensity. This information is critical to engineering the next-<br> generation of ultrasensitive bioluminescent reporters.</p>
Catalytic mechanism for Renilla-type luciferases
<p>The widely used coelenterazine-powered Renilla luciferase was discovered over 40 years ago but the oxidative mechanism by which it generates blue photons remains unclear. Here we decipher Renilla-type catalysis through crystallographic, spectroscopic, and computational experiments. Structures of ancestral and extant luciferases complexed with the substrate-like analogue azacoelenterazine or a reaction product were obtained, providing unprecedented snapshots of coelenterazine-to-coelenteramide oxidation. Bound coelenterazine adopts a Y-shaped conformation, enabling the deprotonated imidazopyrazinone component to attack O2 via a radical charge-transfer mechanism. A high emission intensity is secured by an aspartate from a conserved proton-relay system, which protonates the excited coelenteramide product. Another aspartate on the rim of the catalytic pocket fine-tunes the electronic state of coelenteramide and promotes the formation of the blue light-emitting phenolate anion. The results obtained also reveal structural features distinguishing flash-type from glow-type bioluminescence, providing insights that will guide the engineering of next-generation luciferase‒luciferin pairs for ultrasensitive optical bioassays.</p>
Determining the suitability of C2C12 and HEK293 in dual luciferase assay (DLA) for ACVR1 (ALK2) and TGFBR1 (ALK5)
<p>Aside from having high potency towards ACVR1/ALK2, inhibitor compounds ideally should be highly selective and not target other members of the Transforming Growth Factor beta (TGFb) superfamily. TGFBR1/ALK5 is selected for off-target screening because of its potential role in cardiac functions.</p>
Determining the dual luciferase ALK5 IC50 values of 30 legacy ACVR1/ALK2 inhibitors
<p>A large number of ACVR1/ALK2 inhibitors were previously synthesised by Paul Brenner’s team (Target Discovery Center, University of Oxford) for the purpose of treating Fibrodysplasia Ossificans Progressiva (FOP). Although these compounds were not designed with blood-brain-barrier permeability in mind, they can serve as good bench-marks for my cellular assays. Therefore, 30 of these legacy compounds were chosen to be tested before other new bespoke Diffused Intrinsic Pontine Glioma (DIPG) compounds from Ontario Institute for Cancer Research (OICR) and Charles River Laboratories (CRL). Inhibition of TGFBR1/ALK5 leads to cardiac toxicity. Since I have not yet been able to establish a robust nanoBRET target engagement assay for TGFBR1/ALK5, I will have to resort to dual luciferase promoter assay (orthologous assay) for the time being.</p> <p>For my corresponding opennotebook post, please visit the following page:</p> <p>https://openlabnotebooks.org/determining-the-dual-luciferase-alk5-ic50-values-of-30-legacy-acvr1-alk2-inhibitors/</p>
FT TFL1 bimolecular luciferase complementation assays
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Functional characterization of luciferase in a brittle star indicates parallel evolution influenced by genomic availability of haloalkane dehalogenase
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Inhibition of firefly luciferase activity by a HIF prolyl hydroxylase inhibitor
<p>The three hypoxia-inducible factor (HIF) prolyl-4-hydroxylase domain (PHD) 1–3 enzymes confer oxygen sen-sitivity to the HIF pathway and are novel therapeutic targets for treatment of renal anemia. Inhibition of thePHDs may further be beneficial in other hypoxia-associated diseases, including ischemia and chronic in-flammation. Several pharmacologic PHD inhibitors (PHIs) are available, but our understanding of their selectivity and its chemical basis is limited.We here report that the PHI JNJ-42041935 (JNJ-1935) is structurally similar to the firefly luciferase substrate D-luciferin. Our results demonstrate that JNJ-1935 is a novel inhibitor of firefly luciferase enzymatic activity. In contrast, the PHIs FG-4592 (roxadustat) and FG-2216 (ICA,BIQ,IOX3,YM311) did not affect firefly luciferase. The JNJ-1935 mode of inhibition is competitive with a Ki of 1.36 μM. D-luciferin did not inhibit the PHDs, despite its structural similarity to JNJ-1935. This study provides insights into a previously unknown JNJ-1935 off-target effect as well as into the chemical requirements for firefly luciferase and PHD inhibitors and may inform the development of novel compounds targeting these enzymes.</p>
Dataset related to article "Optimization of a Luciferase-Expressing Non-Invasive Intrapleural Model of Malignant Mesothelioma in Immunocompetent Mice"
<p>This record contains data related to article "Optimization of a Luciferase-Expressing Non-Invasive Intrapleural Model of Malignant Mesothelioma in Immunocompetent Mice"</p> <p>Malignant Pleural Mesothelioma (MPM) is an aggressive tumor of the pleural lining that is usually identified at advanced stages and resistant to current therapies. Appropriate pre-clinical mouse tumor models are of pivotal importance to study its biology. Usually, tumor cells have been injected intraperitoneally or subcutaneously. Using three available murine mesothelioma cell lines with different histotypes (sarcomatoid, biphasic, epithelioid), we have set up a simplified model of in vivo growth orthotopically by inoculating tumor cells directly in the thorax with a minimally invasive procedure. Mesothelioma tumors grew along the pleura and spread on the superficial areas of the lungs, but no masses were found outside the thoracic cavity. As observed in human MPM, tumors were highly infiltrated by macrophages and T cells. The luciferase-expressing cells can be visualized in vivo by bioluminescent optical imaging to precisely quantify tumor growth over time. Notably, the bioluminescence signal detected in vivo correctly matched the tumor burden quantified with classical histology. In contrast, the subcutaneous or intraperitoneal growth of these mesothelioma cells was considered either non-representative of the human disease or unreliable to precisely quantify tumor load. Our non-invasive in vivo model of mesothelioma is simple and reproducible, and it reliably recapitulates the human disease.</p>
Luciferase readout: Raw neutralization results for neutralization assays from pseudoparticles containing the SARS-CoV-2 receptor binding domain from a cryptic lineage
<div> <div> <div> <p>Deep sequencing of wastewater to detect SARS-CoV-2 has been used during the COVID- 19 pandemic to monitor viral variants as they appear and circulate in communities. SARS- CoV-2 lineages of an unknown source that have not been detected in clinical samples, referred to as cryptic lineages, are sometimes repeatedly detected from specific locations. We have continued to detect one such lineage previously seen in a Missouri site. This cryptic lineage has continued to evolve, indicating continued selective pressure similar to that observed in Omicron lineages.</p> </div> </div> </div> <p>This file contains the raw neutralization data using pseudoparticles containing a SARS-CoV-2 Spike protein with the RBD from the cryptic lineage detected in Missouri wastewater.</p>
Supplemental Material S2 for "Development of a highly sensitive luciferase-based reporter system to study two-step protein secretion in cyanobacteria"
<p>Table S1. Densitometric analysis of NLuc immunoblot in Fig. 2A.</p> <p>Figure S1. PilA1 quantification in the sheared pili fractions of WT, Δ<em>hfq</em> and Δ<em>pilT1</em> <em>Synechocystis</em> mutants.</p>
Luciferase readout: Raw neutralization results for neutralization assays from pseudoparticles containing the SARS-CoV-2 receptor binding domain from a cryptic lineage
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Inhibition of firefly luciferase activity by a HIF prolyl hydroxylase inhibitor
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Next-generation interaction screening to discover luciferase (construct #2) related protein-protein interactions regulating barley powdery mildew disease immunity and susceptibility
GEO Series GSE164762. Hordeum vulgare; Blumeria hordei. 4 samples. Type: Other.
IPTG-induced CRISPRi repression of firefly luciferase in Streptococcus pneumoniae
GEO Series GSE89763. Streptococcus pneumoniae. 6 samples. Type: Expression profiling by high throughput sequencing.
Expression data from HeLa cells after hnRNP L knockdown (versus luciferase control), including cycloheximide treatment
GEO Series GSE37561. Homo sapiens. 6 samples. Type: Expression profiling by array.
Human Breast Cancer Cell Lines: Control vs. Fn14 or Luciferase siRNA Treated
GEO Series GSE8871. Homo sapiens. 8 samples. Type: Expression profiling by array.
Comparative analysis of mouse oropharyngeal cells expressing HPV16 E6/E7, hRas, and luciferase (mEERL) with mEERL lung metastasis cell lines (MLM)
GEO Series GSE68935. Mus musculus. 16 samples. Type: Expression profiling by array.
Effect of depletion of USF1 or USF2 on Jurkat Tat mHIV-Luciferase T cell gene expression.
GEO Series GSE227850. Homo sapiens. 18 samples. Type: Expression profiling by high throughput sequencing.
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Allen Brain Atlas
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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.