Готові списки джерел за темами / High-throughput screening assay

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Добірка наукової літератури з теми "High-throughput screening assay"

Автор: Grafiati

Опубліковано: 4 червня 2021

Оновлено: 6 лютого 2022

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Статті в журналах з теми "High-throughput screening assay"

ARAI, Koshi. "Assay in high throughput screening." Folia Pharmacologica Japonica 118, no. 2 (2001): 81–88. http://dx.doi.org/10.1254/fpj.118.81.

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Kolb, Alfred J., and Kenneth Neumann. "Luciferase Measurements in High Throughput Screening." Journal of Biomolecular Screening 1, no. 2 (March 1996): 85–88. http://dx.doi.org/10.1177/108705719600100207.

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Luminescence assays are becoming more popular in high throughput screening (HTS) laboratories with the luciferase reporter gene being the most common. As with other assays that are adapted to HTS, improvements have been made to the luciferase assay to make it better suited to the requirements of HTS. For the luciferase reporter gene, these improvements included stabilization of the enzyme, increasing the half-life of the luminescence signal to 5 h, and eliminating separation steps (centrifugation and aliquot transfer) after cell lysis. The improved assay, LucLite, is homogeneous and is measured directly in the cell culture media. In addition to reagent improvements, a temperature-controlled, multidetector microplate counter, TopCount, can quickly and accurately measure luminescence signals.

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Shumate, Chris, Scott Beckey, Peter Coassin, and Harry Stylli. "Ultra-High Throughput Screening." Laboratory Automation News 2, no. 4 (September 1997): 24–29. http://dx.doi.org/10.1177/221106829700200406.

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Aurora Biosciences Corporation designs and develops proprietary drug discovery systems, services and technologies to accelerate and enhance the discovery of new pharmaceuticals. Aurora is developing an integrated technology platform centered around two technologies; 1) a portfolio of proprietary fluorescent assay technologies and, 2) an ultra-high throughput screening (“UHTS”) system designed to allow assay miniaturization and to overcome many of the limitations associated with the traditional drug discovery process. This approach takes advantage of the opportunities created by recent advances in genomics and combinatorial chemistry that have generated many new therapeutic targets and an abundance of new small molecule compounds. Aurora believes its integrated platform will accelerate the drug discovery process by shortening the time required to identify high quality lead compounds and to optimize those compounds into drug development candidates.

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Sittampalam, G. Sitta, Steven D. Kahl, and William P. Janzen. "High-throughput screening: advances in assay technologies." Current Opinion in Chemical Biology 1, no. 3 (October 1997): 384–91. http://dx.doi.org/10.1016/s1367-5931(97)80078-6.

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Silverman, Lauren, Robert Campbell, and James R. Broach. "New assay technologies for high-throughput screening." Current Opinion in Chemical Biology 2, no. 3 (June 1998): 397–403. http://dx.doi.org/10.1016/s1367-5931(98)80015-x.

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Sivaraja, M., H. Giordano, and M. G. Peterson. "High-Throughput Screening Assay for Helicase Enzymes." Analytical Biochemistry 265, no. 1 (December 1998): 22–27. http://dx.doi.org/10.1006/abio.1998.2875.

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Parham, Fred, Chris Austin, Noel Southall, Ruili Huang, Raymond Tice, and Christopher Portier. "Dose-Response Modeling of High-Throughput Screening Data." Journal of Biomolecular Screening 14, no. 10 (October 14, 2009): 1216–27. http://dx.doi.org/10.1177/1087057109349355.

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The National Toxicology Program is developing a high-throughput screening (HTS) program to set testing priorities for compounds of interest, to identify mechanisms of action, and potentially to develop predictive models for human toxicity. This program will generate extensive data on the activity of large numbers of chemicals in a wide variety of biochemical- and cell-based assays. The first step in relating patterns of response among batteries of HTS assays to in vivo toxicity is to distinguish between positive and negative compounds in individual assays. Here, the authors report on a statistical approach developed to identify compounds positive or negative in an HTS cytotoxicity assay based on data collected from screening 1353 compounds for concentration-response effects in 9 human and 4 rodent cell types. In this approach, the authors develop methods to normalize the data (removing bias due to the location of the compound on the 1536-well plates used in the assay) and to analyze for concentration-response relationships. Various statistical tests for identifying significant concentration-response relationships and for addressing reproducibility are developed and presented.

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Poul, Emmanuel Le, Sunao Hisada, Yoshinori Mizuguchi, Vincent J. Dupriez, Emmanuel Burgeon, and Michel Detheux. "Adaptation of Aequorin Functional Assay to High Throughput Screening." Journal of Biomolecular Screening 7, no. 1 (February 2002): 57–65. http://dx.doi.org/10.1177/108705710200700108.

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AequoScreen™, a cellular aequorin-based functional assay, has been optimized for luminescent high-throughput screening (HTS) of G protein-coupled receptor (GPCRs). AequoScreen is a homogeneous assay in which the cells are loaded with the apoaequorin cofactor coelenterazine, diluted in assay buffer, and injected into plates containing the samples to be tested. A flash of light is emitted following the calcium increase resulting from the activation of the GPCR by the sample. Here we have validated a new plate reader, the Hamamatsu Photonics FDSS6000, for HTS in 96- and 384-well plates with CHO-K1 cells stably coexpressing mitochondrial apoaequorin and different GPCRs (AequoScreen cell lines). The acquisition time, plate type, and cell number per well have been optimized to obtain concentration-response curves with 4000 cells/well in 384-well plates and a high signal: background ratio. The FDSS6000 and AequoScreen cell lines allow reading of twenty 96- or 384-well plates in 1 h with Z’ values of 0.71 and 0.78, respectively. These results bring new insights to functional assays, and therefore reinforce the interest in aequorin-based assays in a HTS environment.

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Zander Balderud, Linda, David Murray, Niklas Larsson, Uma Vempati, Stephan C. Schürer, Marcus Bjäreland, and Ola Engkvist. "Using the BioAssay Ontology for Analyzing High-Throughput Screening Data." Journal of Biomolecular Screening 20, no. 3 (December 15, 2014): 402–15. http://dx.doi.org/10.1177/1087057114563493.

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High-throughput screening (HTS) is the main starting point for hit identification in drug discovery programs. This has led to a rapid increase of available screening data both within pharmaceutical companies and the public domain. We have used the BioAssay Ontology (BAO) 2.0 for assay annotation within AstraZeneca to enable comparison with external HTS methods. The annotated assays have been analyzed to identify technology gaps, evaluate new methods, verify active hits, and compare compound activity between in-house and PubChem assays. As an example, the binding of a fluorescent ligand to formyl peptide receptor 1 (FPR1, involved in inflammation, for example) in an in-house HTS was measured by fluorescence intensity. In total, 155 active compounds were also tested in an external ligand binding flow cytometry assay, a method not used for in-house HTS detection. Twelve percent of the 155 compounds were found active in both assays. By the annotation of assay protocols using BAO terms, internal and external assays can easily be identified and method comparison facilitated. They can be used to evaluate the effectiveness of different assay methods, design appropriate confirmatory and counterassays, and analyze the activity of compounds for identification of technology artifacts.

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Skehan, Philip. "Dealing with the data deluge in high throughput screening." Journal of Automated Methods and Management in Chemistry 22, no. 5 (2000): 145–48. http://dx.doi.org/10.1155/s1463924600000237.

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Numerical taxonomy and pattern recognition analysis offer powerful tools that can greatly reduce the information burden of multiple-assay screening programs. These methods can be used to rationally design prescreens, identify assays that have similar chemical response patterns, select reporter assays for chemical response groups, evaluate drug selectivity, and predict a drug's likely mechanism of action. When combined with assays designed to identify lead compounds that have characteristics likely to cause failure at a later and more expensive stage of development, a simple three-stage primary discovery process consisting of a rational prescreen, reporters, and clinical failure assay can reduce the number of required culture wells by more than 20-fold and can eliminate all but 1–2 drugs per 1000 tested as leads for further evaluation and development.

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Дисертації з теми "High-throughput screening assay"

Cardno, Tony Stuart, and n/a. "Development of a high throughput fluorescent screening assay for genetic recoding." University of Otago. Department of Biochemistry, 2007. http://adt.otago.ac.nz./public/adt-NZDU20071218.145806.

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The development of new drug therapies traditionally requires mass screening of thousands if not millions of substances to identify lead compounds. They are then further optimised to increase potency. The screening of the large pharmaceutical compound libraries can be incredibly expensive, with the industry responding by miniaturising the assays to smaller formats, enabling the compound screening to be automated and, importantly, eliminating assay reagents that are a major contributing cost for running large screens. A potential target for such an approach is the genetic recoding site of viruses like HIV-1 and SARS. They use programmed recoding of the genetic code to regulate the translation of necessary proteins required for viable virus production. For example HIV-1 uses a -1 frameshift mechanism to regulate the ratio of the Gag to the Pol proteins, crucial for viable virus formation. The study of recoding, including readthrough of premature termination codons have most recently used bicistronic reporters with different combinations of enzymes. The most widely used plasmid bicistronic reporter utilises a dual luciferase arrangement comprised of firefly luciferase and Renilla luciferase reporters flanking the DNA being studied. Both of the luciferase enzymatic reporters emit light in response to their respective substrates. The cost of these substrates is the major issue to using luciferase reporters for high throughput screening. My study aimed at designing and developing a bicistronic assay suitable for genetic recoding that was amenable to high throughput screening. The luciferase reporters were replaced with Green Fluorescent Protein (GFP) reporters that do not require the addition of substrates. The development of a dual GFP assay required the appropriate selection of GFP fluorophores, the best arrangement of the GFPs to maximise the ratio of relative fluorescence intensity signal to background, the optimisation of the cells and growth conditions, DNA transfection, plate reader selection, and optical filter sets. Cassettes encoding protein linkers were also incorporated into the design of the constructs to separate the fluorescent proteins spatially to facilitate unimpaired folding into their functional units within the fusion protein. The assay was further improved by moving from transient transfection to stably expressing cell lines. A viable assay was almost achieved for 96 (and 384) well plates with a Z� factor compatible with the assay being suitable for high throughput screening. The assay was used to test a small collection of compounds known to interact with the ribosome and compounds known in the literature to affect frameshifting. This proof of concept was important, since it showed that the assay, with the various modifications, optimisations and miniaturisation steps, still retained the capability of correctly measuring the -1 frameshifting efficiency at the HIV-1 recoding site, and recording compound-induced modulations to the frameshifting efficiency. The compounds cycloheximide and anisomycin, for example, were shown to decrease -1 frameshifting albeit at some expense to overall protein synthesis. The dual GFP assay was also shown to be able to measure accurately changes in the frameshift efficiency brought about by mutations to the frameshift element, and additionally, it would be suitable for the detection and study of compounds, like the recently reported PTC-124 (currently undergoing phase II clinical trial for Duchenne Muscular Dystrophy and cystic fibrosis) that increases readthrough of a UGA premature stop codon mutation. The dual GFP assay developed in this study is at most only 1/10th of the cost of a comparable dual luciferase assay, largely due to removal of assay substrates and transfection reagents. The assay has a robust Z� factor comparable to that of the dual luciferase assay, and would substantially decrease the costs of high throughput screening in situations where a bicistronic reporter is required. The HIV-1 frameshift element is such a site.

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Ravindranath, Padma Priya. "PROCESS OPTIMIZATION AND VALIDATION OF AN ASSAY FOR HIGH-THROUGHPUT SCREENING." UKnowledge, 2006. http://uknowledge.uky.edu/gradschool_theses/375.

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A biological assay is designed to set up a rapid and robust drug-screening system on a small scale. An assay is considered as a single unit of a platform to screen various compounds for aiding in drug discovery. Each assay is carried out in a 96-well plate, each of whose wells consists of the biological component called the Spheroids. The value of each assay lies in it facilitating for versatile screening applications. The spheroid is considered as a micro-structural product. And the addition of various compounds for testing is performed in each well (consisting of the spheroids). The focus has been to put forth the production principles and validation strategies to run the biological assay and test its efficacy to be used for screening in high volumes. The assay development illustrates processing and validation techniques. The goal is to develop optimized standards to process the assay, addressing various quality control issues, from the raw material to the end-product stage. Such an approach also brings interesting analogies of biological process in a manufacturing scenario. The developed system incorporates a value stream approach, by pulling the product from the customer end. The process involves simply encapsulating HUVECs (Human Umbelical Vein Endothelial cells) from the raw material stage, culturing to form the spheroid and transferring the component to assemblage in a 96-well format undergoing stages of heat treatments. The small scale screening system allows the use of small amounts of drug, which is especially essential for new drug synthesis or in rapid decision making to find out any unknown potent compounds. The design of optimal processes in product development of the spheroid assay is illustrated. Thus in light of the value of this assay, developing the production system has been pivotal so as to produce quality spheroids in the 96-well plate formats. The quantification of the stimulatory and inhibitory effects of the different agents is required to help understand the complex biological behavior involved. The goal is to validate the data using image analysis software. The image analysis helps determine the quantification to be accurate, objective, and consistent. The quality of the product is tested by the reproducibility and robustness of the assay.

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Morgan, Jemma. "Development of a novel high-throughput screening assay and its application to racemases." Thesis, University of Edinburgh, 2008. http://hdl.handle.net/1842/11188.

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A high-throughput hydrogen peroxide-based colorimetric screen used to detect oxidase activity was extended to detect racemase activity through the production of the specific substrate for an enantioselective oxidase enzyme. A two-plasmid system (encoding the racemase and oxidase) was shown to be successful and could have possible applications for many different classes of enzymes that produce an oxidase substrate. In order to validate the screening technology, three amino acid racemase genes were cloned from genomic DNA and placed into expression vectors. The screen was used to confirm the substrate specificities of each racemase. The amino acid racemases were then subjected to random mutagenesis using the mutator strain method and error-prone polymerase chain reaction. Libraries of the variant racemase enzymes were screened for novel activities towards substrates not accepted by the wild type enzymes: L-arginine; L-lysine and L-leucine. Novel activity was discovered in selected Streptomyces coelicolor alanine racemase variants. Sequencing revealed that the best variant had three point mutations I195T, N223D and I374N. Computer modelling suggested that the I374N mutation was a key mutation and so the variant containing the double mutation (I195T and N223D) was prepared. Partial purification of the wild type enzyme, the variants containing the double and the triple mutations was carried out to compare the substrate specificities. The I195T/N223D variant was shown to be ten times more active towards L-arginine that the wild type enzyme, and the variant containing all three mutations was shown to be 100 times more active towards L-arginine than the wild type enzyme. Both variants displayed novel activity towards L-arginine only.

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Xin, Xin. "Development of 3D Cell-Based Assay for High Throughput Screening of Cancer Drugs." The Ohio State University, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=osu1492700405342723.

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Schuster, Sascha. "Ein GFP-basierter in vivo Assay für das Hochdurchsatz-Screening nach Hydrolaseaktivität." [S.l. : s.n.], 2005. http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-24718.

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Zhou, Rui. "FITSelect: An Invention to Select Microbial Strains Maximizing Product Formation from a Single Culture Without High-Throughput Screening." Thesis, Virginia Tech, 2011. http://hdl.handle.net/10919/76843.

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In metabolic engineering of prokaryotes, combinatorial approaches have developed recently that induce random genetic perturbations to achieve a desired cell phenotype. A screening strategy follows the randomized genetic manipulations to select strain(s) with the more optimal phenotype of interest. This screening strategy is often divided into two categories: (i) a growth competition assay and (ii) selection by high-throughput screening. The growth competition assay involves culturing strains together. The strain with the highest growth rate will ultimately dominate the culture. This strategy is ideal for selecting strain with cellular fitness (e.g., solvent tolerance), but it does not work for selecting a strain that can over-produce a product (e.g., an amino acid). For the case of selecting highly productive phenotypes, high-throughput screening is used. This method analyzes strains individually and is costly and time-consuming. In this research, a synthetic genetic circuit was developed to select highly productive phenotypes using a growth competition assay rather than high-throughput screening. This novel system is called Feed-back Inhibition of Transcription for Growth Selection (FITSelect), and it uses a natural feedback inhibition mechanism in the L-arginine production pathway to select strains (transformed with a random genomic library) that can over-produce L-arginine in E. coli DH10B. With FITSelect, the cell can thrive in the growth competition assay when L-arginine is over-produced (i.e., growth is tied to L-arginine production). Cell death or reduced growth results if L-arginine is not over-produced by the cell. This system was created by including an L-arginine concentration responsive argF promoter to control a ccdB cell death gene in the FITSelect system. The effects of ccdB were modulated by the antidote ccdA gene under control of an L-tryptophan responsive trp promoter. Several insights and construction strategies were required to build a system that ties the growth rate of the cell to L-arginine concentrations.
Master of Science

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He, Shanshan. "Neglected Tropical Disease Chemotherapy: Mechanistic Characterization of Antitrypanosomal Dihydroquinolines and Development of a High Throughput Antileishmanial Screening Assay." The Ohio State University, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=osu1337980540.

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Fraley, Brian J. "High-Throughput 3-D Cellular Assays Using Destabilized Green Fluorescence Protein." The Ohio State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=osu1250689920.

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Ashman, Stephen M. "An examination of novel fluorescent assay methodologies for proteases, compatible with miniaturised high throughput screening and drug discovery : caspase-3, a case study." Thesis, University of Bristol, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.288311.

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Pow, Andrew James. "Protein complementation assay as a display system for screening protein libraries in the intracellular environment." Queensland University of Technology, 2008. http://eprints.qut.edu.au/30392/.

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A wide range of screening strategies have been employed to isolate antibodies and other proteins with specific attributes, including binding affinity, specificity, stability and improved expression. However, there remains no high-throughput system to screen for target-binding proteins in a mammalian, intracellular environment. Such a system would allow binding reagents to be isolated against intracellular clinical targets such as cell signalling proteins associated with tumour formation (p53, ras, cyclin E), proteins associated with neurodegenerative disorders (huntingtin, betaamyloid precursor protein), and various proteins crucial to viral replication (e.g. HIV-1 proteins such as Tat, Rev and Vif-1), which are difficult to screen by phage, ribosome or cell-surface display. This study used the â-lactamase protein complementation assay (PCA) as the display and selection component of a system for screening a protein library in the cytoplasm of HEK 293T cells. The colicin E7 (ColE7) and Immunity protein 7 (Imm7) Escherichia coli proteins were used as model interaction partners for developing the system. These proteins drove effective â-lactamase complementation, resulting in a signal-to-noise ratio (9:1 – 13:1) comparable to that of other â-lactamase PCAs described in the literature. The model Imm7-ColE7 interaction was then used to validate protocols for library screening. Single positive cells that harboured the Imm7 and ColE7 binding partners were identified and isolated using flow cytometric cell sorting in combination with the fluorescent â-lactamase substrate, CCF2/AM. A single-cell PCR was then used to amplify the Imm7 coding sequence directly from each sorted cell. With the screening system validated, it was then used to screen a protein library based the Imm7 scaffold against a proof-of-principle target. The wildtype Imm7 sequence, as well as mutants with wild-type residues in the ColE7- binding loop were enriched from the library after a single round of selection, which is consistent with other eukaryotic screening systems such as yeast and mammalian cell-surface display. In summary, this thesis describes a new technology for screening protein libraries in a mammalian, intracellular environment. This system has the potential to complement existing screening technologies by allowing access to intracellular proteins and expanding the range of targets available to the pharmaceutical industry.

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Книги з теми "High-throughput screening assay"

Chen, Taosheng. A practical guide to assay development and high-throughput screening in drug discovery. Boca Raton: Taylor & Francis, 2010.

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Zhu, Hao, and Menghang Xia, eds. High-Throughput Screening Assays in Toxicology. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6346-1.

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Clemons, Paul A., Nicola J. Tolliday, and Bridget K. Wagner, eds. Cell-Based Assays for High-Throughput Screening. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-545-3.

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Virtual screening: Principles, challenges, and practical guidelines. Weinheim, Germany: Wiley-VCH, 2011.

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Prazeres, Duarte Miguel F., and Sofia Aires M. Martins. G protein-coupled receptor screening assays: Methods and protocols. New York: Humana Press, 2015.

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Structural genomics and drug discovery: Methods and protocols. New York: Humana Press, 2014.

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Mylonakis, Eleftherios, and George Tegos. Antimicrobial drug discovery: Emerging strategies. Wallingford, Oxfordshire: CABI, 2012.

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Bikker, J. A., and Matthew M. Hayward. Lead-seeking approaches. Heidelberg: Springer, 2010.

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Cell-based assays for high-throughput screening: Methods and protocols. New York: Humana, 2008.

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Cell-based assays for high-throughput screening: Methods and protocols. New York: Humana, 2008.

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Частини книг з теми "High-throughput screening assay"

An, Frank W., and Jose R. Perez. "Assay Design for High-Throughput Screening." In Plant Chemical Biology, 73–91. Hoboken, NJ: John Wiley & Sons, Inc, 2013. http://dx.doi.org/10.1002/9781118742921.ch3.1.

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Natsch, Andreas. "The Keratinosens Assay: A High-Throughput Screening Assay to Assess Chemical Skin Sensitization." In High-Throughput Screening Methods in Toxicity Testing, 159–75. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118538203.ch8.

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Blümel, Jörg, and Nadine Krause. "High-Throughput Genotoxicity Testing: The Greenscreen Assay." In High-Throughput Screening Methods in Toxicity Testing, 271–84. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118538203.ch13.

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Witte, Irene, and André Stang. "High-Throughput Versions of the Comet Assay." In High-Throughput Screening Methods in Toxicity Testing, 295–308. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118538203.ch15.

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Williams, Kevin P., and John E. Scott. "Enzyme Assay Design for High-Throughput Screening." In Methods in Molecular Biology, 107–26. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-258-2_5.

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Verschaeve, Luc. "High-Throughput Bacterial Mutagenicity Testing: Vitotox™ Assay." In High-Throughput Screening Methods in Toxicity Testing, 213–32. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118538203.ch11.

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Leesnitzer, M. Anthony, D. Mark Bickett, Marcia L. Moss, and J. David Becherer. "A high throughput assay for the TNF converting enzyme." In High Throughput Screening for Novel Anti-Inflammatories, 87–100. Basel: Birkhäuser Basel, 2000. http://dx.doi.org/10.1007/978-3-0348-8462-4_5.

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Sergienko, Eduard A. "Phosphatase High-Throughput Screening Assay Design and Selection." In Methods in Molecular Biology, 7–25. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-562-0_2.

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Steinberg, Pablo. "Automated Soft Agar Colony Formation Assay for the High-Throughput Screening of Malignant Cell Transformation." In High-Throughput Screening Methods in Toxicity Testing, 309–16. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118538203.ch16.

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Uibel, Frederik, and Michael Schwarz. "ReProGlo: A New Stem-Cell-Based High-Throughput Assay to Predict the Embryotoxic Potential of Chemicals." In High-Throughput Screening Methods in Toxicity Testing, 341–55. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118538203.ch18.

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Тези доповідей конференцій з теми "High-throughput screening assay"

Frederick, Barbara, Nathan Gomes, and Tin Tin Su. "Abstract 3055: Clonogenic high-throughput assay for screening radiation modulators." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-3055.

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Frederick, Barbara, Nathan Gomes, and Tin Tin Su. "Abstract PO-080: Clonogenic high-throughput assay for screening radiation modulators." In Abstracts: AACR Virtual Special Conference on Radiation Science and Medicine; March 2-3, 2021. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1557-3265.radsci21-po-080.

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de Pril, Remko, Carla Oerlemans-Bergs, Edo Elstak, Ilhem Maghrani, and Richard Janssen. "Abstract C227: High-throughput anchorage independence assay for screening inhibitors of cancer metastasis." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Oct 19-23, 2013; Boston, MA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1535-7163.targ-13-c227.

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Arai, Kazuya, Ruriko Sakamoto, Manabu Itoh, Hiromi Miura, Manami Shimomura, and Tetsuya Nakatsura. "Abstract 5525: Development of novel high-throughput screening assay system for exploring EMT inhibitors." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5525.

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Arslan, Ahmet Dirim, Xiaolong He, Minxiu Wang, Emily Rumschlag-Booms, Lijun Rong, and William T. Beck. "Abstract A180: Development of a high-throughput screening (HTS) assay to detect splicing inhibitors." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-a180.

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Wilder, Paul T., Kira Gianni, Deborah L. Green, and David J. Weber. "Abstract 1372: A cell based high throughput screening assay for inhibitors of melanoma with high S100B." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1372.

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Huang, Alice H., Nuzhat A. Motlekar, Ashley Stein, Eileen M. Shore, Scott L. Diamond, and Robert L. Mauck. "High-Throughput Screening of Chemical Libraries for Modulators of Mesenchymal Stem Cell Chondrogenesis." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-193118.

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Анотація:

Mesenchymal stem cells (MSCs) are a multi-potential cell type that can be induced to differentiate to a variety of tissue-specific cell phenotypes, including cartilage (chondrogenesis) and bone (osteogenesis). Given this multi-potentiality, MSCs are a promising cell source for exploring developmental paradigms and for tissue engineering (TE) applications. For cartilage formation assays, MSCs are collected in high-density pellets and treated with specific biofactors, including TGF-β superfamily members and dexamethasone in a chemically defined medium (CM) [1]. During chondrogenesis, extracellular matrix (ECM) rich in glycosaminoglycan (GAG) and type II collagen is synthesized. While MSC chondrogenesis is well-characterized using existing protocols, the effect of alternative biofactors, their doses and combinations requires laborious combinatorial studies [2]. High-throughput screening (HTS) overcomes this limitation through the simultaneous layout and query of a large number of conditions within a single plate. HTS depends on the use of precise robotic liquid handling systems and on the development of sensitive, validated, and readily quantifiable assays. In a recent study, we optimized cell culture and assay procedures for HTS by minimizing cell number, handling and culture duration [3]. We successfully reduced the time scale from 21 to 7 days and the number of cells required from 225K to 30K cells per pellet. Further, we developed a novel in-well digestion protocol to enable high-throughput analysis and minimize handling. In this study, we have further streamlined these assays for HTS by providing a rapid and robotic approach for layout, culture, and analysis of ECM deposition using ‘micro’ MSC pellets (10K cells per pellet) in a 384-well format. Furthermore, we have carried out an initial screen of the NINDS small molecule library and demonstrated the feasibility of this technology for use in HTS of chondrogenesis.

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Park, Sun Hee, JiYeon Kim, Yu Kyung Tak, and Joon Myong Song. "On chip superoxide dismutase assay for high-throughput screening of radioprotective activity of herbal plants." In 2010 IEEE 4th International Conference on Nano/Molecular Medicine and Engineering (NANOMED). IEEE, 2010. http://dx.doi.org/10.1109/nanomed.2010.5749838.

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Tseng, H., LG Sabino, WL Haisler, JA Gage, SK Neeley, and GR Souza. "Abstract P4-01-15: A high-throughput three-dimensional cell migration assay (BiO assay) for toxicity screening for breast cancer applications." In Abstracts: Thirty-Sixth Annual CTRC-AACR San Antonio Breast Cancer Symposium - Dec 10-14, 2013; San Antonio, TX. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/0008-5472.sabcs13-p4-01-15.

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Grobben, Yvonne, Joost C. Uitdehaag, Nicole Willemsen-Seegers, Werner W. Tabak, Martine B. Prinsen, Suzanne J. van Gerwen, Jan van Groningen, et al. "Abstract 1944: High-throughput fluorescence-based assay for screening of Arginase I inhibitors for cancer immunotherapy." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1944.

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