Academic literature on the topic 'Fluorescence-based Assays'

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Journal articles on the topic "Fluorescence-based Assays"

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Singh, Rajendra, Shaileja Chopra, Carrie Graham, Melissa Langer, Rainer Ng, Anirudh J. Ullal, and Vamsee K. Pamula. "Emerging Approaches for Fluorescence-Based Newborn Screening of Mucopolysaccharidoses." Diagnostics 10, no. 5 (May 11, 2020): 294. http://dx.doi.org/10.3390/diagnostics10050294.

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Interest in newborn screening for mucopolysaccharidoses (MPS) is growing, due in part to ongoing efforts to develop new therapies for these disorders and new screening assays to identify increased risk for the individual MPSs on the basis of deficiency in the cognate enzyme. Existing tests for MPSs utilize either fluorescence or mass spectrometry detection methods to measure biomarkers of disease (e.g., enzyme function or glycosaminoglycans) using either urine or dried blood spot (DBS) samples. There are currently two approaches to fluorescence-based enzyme function assays from DBS: (1) manual reaction mixing, incubation, and termination followed by detection on a microtiter plate reader; and (2) miniaturized automation of these same assay steps using digital microfluidics technology. This article describes the origins of laboratory assays for enzyme activity measurement, the maturation and clinical application of fluorescent enzyme assays for MPS newborn screening, and considerations for future expansion of the technology.
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Newman, Miki, and Serene Josiah. "Utilization of Fluorescence Polarization and Time Resolved Fluorescence Resonance Energy Transfer Assay Formats for SAR Studies: Src Kinase as a Model System." Journal of Biomolecular Screening 9, no. 6 (September 2004): 525–32. http://dx.doi.org/10.1177/1087057104264597.

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High-throughput screening (HTS), a major component of lead identification, often utilizes fluorescence-based assay technologies. For example, HTS kinase assays are formatted using a variety of fluorescence-based assay technologies including, but not limited to, dissociation enhanced lanthanide fluoroimmunoassay (DELFIA®), time-resolved fluorescence resonance energy transfer (TR-FRET), and fluorescence polarization (FP). These assays offer tremendous advantages such as a nonradioactive format, ease of automation, and excellent reproducibility. Fluorescence-based assays frequently used for lead identification can also be useful for structure activity relationship (SAR) studies during lead optimization. An important issue when assessing an assay to be used for SAR is the ability of the assay to discriminate high-affinity small molecule inhibitors (pM-nM) from low-affinity inhibitors (μM-mM). The purpose of this study was to utilize HTS-friendly assay formats for SAR by developing TR-FRET, FP, and DELFIA® assays measuring Src kinase activity and to define the theoretical lower limit of small molecule inhibitor detection achievable with these assay formats. The authors show that 2 homogeneous assay formats, TR-FRET and FP, allowed for the development of Src kinase assays with a lower limit of detection of Ki = 0.01nM. This study indicates that assay technologies typically used for HTS can be used during lead optimization by providing quantitative measurements of compound activity critical to driving SAR studies.
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Grant, Stephan K., Joseph G. Sklar, and Richard T. Cummings. "Development of Novel Assays for Proteolytic Enzymes Using Rhodamine-Based Fluorogenic Substrates." Journal of Biomolecular Screening 7, no. 6 (December 2002): 531–40. http://dx.doi.org/10.1177/1087057102238627.

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Components within synthetic chemical and natural product extract libraries often interfere with fluorescence-based assays. Fluorescence interference can result when the intrinsic spectral properties of colored compounds overlap with the fluorescent probes. Typically, fluorescence-based protease assays use peptide amidomethylcoumarin derivatives as substrates. However, because many organic compounds absorb in the ultraviolet region, they can interfere with coumarin-based fluorescence assays. Red-shifted fluorescent dyes such as peptidyl rhodamine derivatives are useful because there is generally less interference from organic compounds outside the ultraviolet wavelengths. In this report, rhodamine-based fluorogenic substrates, such as bis-(Leu)2-Rhod110 and bis-(Ala-Pro)2-Rhod110, were developed for leucine aminopeptidase and dipeptidyl aminopeptidase. Novel, tandem rhodamine substrates such as Ala-Pro-Rhod110-Leu were designed with 2 protease cleavage sites and used to assay 2 proteases in a multiplex format. General endpoint high-throughput screening (HTS) assays were also developed for leucine aminopeptidase, dipeptidyl aminopeptidase, and trypsin that incorporated both amidomethylcoumarin and rhodamine-based fluorogenic substrates into a single screening format. These dual-substrate assays allowed for the successful screening of the LOPAC™ collection and natural product extracts despite high levels of fluorescence interference.
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DECIAN, A., L. GUITTAT, M. KAISER, B. SACCA, S. AMRANE, A. BOURDONCLE, P. ALBERTI, M. TEULADEFICHOU, L. LACROIX, and J. MERGNY. "Fluorescence-based melting assays for studying quadruplex ligands." Methods 42, no. 2 (June 2007): 183–95. http://dx.doi.org/10.1016/j.ymeth.2006.10.004.

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Xie, Yonghua, Rui Zhao, Ying Tan, Xin Zhang, Feng Liu, Yuyang Jiang, and Chunyan Tan. "Conjugated Polymer-Based Real-Time Fluorescence Caspase Assays." ACS Applied Materials & Interfaces 4, no. 1 (December 29, 2011): 405–10. http://dx.doi.org/10.1021/am201470a.

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Soukka, Tero, Terhi Rantanen, and Katri Kuningas. "Photon Upconversion in Homogeneous Fluorescence-based Bioanalytical Assays." Annals of the New York Academy of Sciences 1130, no. 1 (May 2008): 188–200. http://dx.doi.org/10.1196/annals.1430.027.

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Zhao, Zijian, Le Wei, Mingfeng Cao, and Meng Lu. "A smartphone-based system for fluorescence polarization assays." Biosensors and Bioelectronics 128 (March 2019): 91–96. http://dx.doi.org/10.1016/j.bios.2018.12.031.

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Prystay, Linda, Annie Gagne, Patricia Kasila, Li-An Yeh, and Peter Banks. "Homogeneous Cell-Based Fluorescence Polarization Assay for the Direct Detection of cAMP." Journal of Biomolecular Screening 6, no. 2 (April 2001): 75–82. http://dx.doi.org/10.1177/108705710100600203.

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A fluorescence polarization-based functional assay for cyclic AMP (cAMP) production in cells has been proven effective for the detection of agonist-stimulated cAMP production in a HEK 293 recombinant cell line expressing the corticotropin-releasing factor subtype 2cr (CRF2a) receptor. Assays were completed in a single well of a 384-well microplate with no transfer, separation, or wash steps incurred. The assay performance is excellent for adaptation to the high throughput screening environment in terms of speed of analysis, magnitude of displaced signal, precision, and detection limits for cAMP quantitation. Relative potencies of agonists and antagonists are maintained with respect to radiometric assays. The assay withstands up to 5% DMSO and up to 10 μM concentrations of highly colored compound. These attributes suggest that accurate assessment of drug binding can be measured using this assay.
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Turek-Etienne, Tammy C., Eliza C. Small, Sharon C. Soh, Tianpei A. Xin, Priti V. Gaitonde, Ellen B. Barrabee, Richard F. Hart, and Robert W. Bryant. "Evaluation of Fluorescent Compound Interference in 4 Fluorescence Polarization Assays: 2 Kinases, 1 Protease, and 1 Phosphatase." Journal of Biomolecular Screening 8, no. 2 (April 2003): 176–84. http://dx.doi.org/10.1177/1087057103252304.

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With the increasing use of fluorescence-based assays in high-throughput screening (HTS), the possibility of interference by fluorescent compounds needs to be considered. To investigate compound interference, a well-defined sample set of biologically active compounds, LOPAC™, was evaluated using 4 fluorescein-based fluorescence polarization (FP) assays. Two kinase assays, a protease assay, and a phosphatase assay were studied. Fluorescent compound interference and light scattering were observed in both mixture- and single-compound testing under certain circumstances. In the kinase assays, which used low levels (1-3 nM) of fluorophore, an increase in total fluorescence, an abnormal decrease in mP readings, and negative inhibition values were attributed to compound fluorescence. Light scattering was observed by an increase in total fluorescence and minimal reduction in mP, leading to false positives. The protease and phosphatase assays, which used a higher concentration of fluorophore (20-1200 nM) than the kinase assays, showed minimal interference from fluorescent compounds, demonstrating that an increase in the concentration of the fluorophore minimized potential fluorescent compound interference. The data also suggests that mixtures containing fluorescent compounds can result in either false negatives that can mask a potential “hit” or false positives, depending on the assay format. Cy™ dyes (e.g., Cy3B™ and Cy5™) excite and emit further into the red region than fluorescein and, when used in place of fluorescein in kinase 1, eliminate fluorescence interference and light scattering by LOPAC™ compounds. This work demonstrates that fluorescent compound and light scattering interferences can be overcome by increasing the fluorophore concentration in an assay or by using longer wavelength dyes. ( Journal of Biomolecular Screening 2003:176-184)
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Boettcher, Andreas, Nathalie Gradoux, Edwige Lorthiois, Trixi Brandl, David Orain, Nikolaus Schiering, Frederic Cumin, Julian Woelcke, and Ulrich Hassiepen. "Fluorescence Lifetime–Based Competitive Binding Assays for Measuring the Binding Potency of Protease Inhibitors In Vitro." Journal of Biomolecular Screening 19, no. 6 (January 31, 2014): 870–77. http://dx.doi.org/10.1177/1087057114521295.

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Fluorescence lifetime (FLT)–based assays have developed to become highly attractive tools in drug discovery. All recently published examples of FLT-based assays essentially describe their use for monitoring enzyme-mediated peptide modifications, such as proteolytic cleavage or phosphorylation/dephosphorylation. Here we report the development of competitive binding assays as novel, inhibitor-centric assays, principally employing the FLT of the acridone dye Puretime 14 (PT14) as the readout parameter. Exemplified with two case studies on human serine proteases, the details of the rationale for both the design and synthesis of probes (i.e., active site–directed low-molecular-weight inhibitors conjugated to PT14) are provided. Data obtained from testing inhibitors with the novel assay format match those obtained with alternative formats such as FLT-based protease activity and time-resolved fluorescence resonance energy transfer–based competitive binding assays.
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Dissertations / Theses on the topic "Fluorescence-based Assays"

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Renberg, Björn. "Fluorescence-based ligand assays for protein detection using affibody affinity proteins." Doctoral thesis, KTH, Skolan för bioteknologi (BIO), 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3936.

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The detection and quantification of biomolecules, and proteins in particular, are of great interest since these molecules are of fundamental importance to our well-being. Body fluids, as for instance human blood, are well suited for sampling of protein levels. However, the complexity of the fluids and the low abundance of many of the interesting biomolecules makes detection and quantification difficult. This has spurred an interest into the development of many protein detection methods, and of these, ligand assays have proven particularly suitable. In this thesis, different types of ligand assays for protein detection have been developed using affibody molecules as ligands. In a first study, a homogeneous competitive detection assay was investigated, based on antiidiotypic affibody molecule pairs and fluorescence resonance energy transfer (FRET) as reporting system. The individual members of two anti-idiotypic affibody pairs, each consisting of a target binding (idiotypic) and an anti-idiotypic affibody ligand, were labeled with a donor fluorophore and an acceptor fluorophore, respectively. Incubation with the two target proteins IgA and Taq DNA polymerase resulted in a concentration dependent decrease in the FRET signal, allowing for target protein detection and quantification. For Taq DNA polymerase, detection in 25% human plasma was also possible in the same concentration span as in buffer. In a second study, a homogeneous, non-competitive detection system was described. Affibody molecules of 58 amino acids directed against IgA and IgG were produced with chemical synthesis, and two fluorophores capable of FRET were site-specifically introduced. Binding of target protein induced a concentration-dependent change in the relative emission of the two fluorophores, which formed the basis for the detection system. In two studies, affibody molecules were evaluated and shown to function well as capture ligands on microarrays. Synthetic affibody molecules directed against Taq DNA polymerase and IgA were modified by the introduction of immobilization tags. Specific immobilization via a C-terminal cysteine or a biotin moiety, or random immobilization via amino groups, were studied in protein microarray experiments and SPR-based biosensor studies. The experiments showed that all immobilization chemistries resulted in functional capture molecules. A short spacer was also introduced, situated between the affibody and the cysteine and biotin moieties, which was shown to improve binding for all constructs. Multidomain affibody constructs of up to four N- to C-terminally linked domains were shown to increase the amount of bound target, compared to monomeric affibody ligands. Six dimeric affibody constructs directed against IgA, IgG, IgE, Taq DNA polymerase, TNF-α and insulin, respectively, showed low limits of detections for their targets and little or no cross-reactivity with the other target proteins. Dimeric affibody molecules directed against IgA and TNF-α were also shown to function in a sandwich format with antibodies for detection of targets in buffer and in human serum and plasma. Successful discrimination between normal and IgA-deficient sera showed that affibody molecules could be used for specific detection of protein in highly complex backgrounds on microarrays.
QC 20100916
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Caputo, Christine A. "Development of fluorescence-based high-throughput assays for diels-alder reactions." Thesis, McGill University, 2004. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=81269.

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The Diels-Alder reaction is one of the most powerful reactions available to synthetic chemists. Novel catalysts for this reaction are constantly being evaluated, thus creating a need for high-throughput assays. In this thesis, three strategies were tested in the design of novel fluorescence-based assays to monitor Diels-Alder reactions. The first strategy relied on intermolecular FRET pairing using fluorescence donors as dienes and fluorescence acceptors as dienophile (or vice versa). The second strategy utilized the dienophile naphthalene fumarate ethyl ester which contains a quenched fluorescent moiety. This dienophile was expected to regain its fluorescence upon Diels-Alder reaction with a diene. The third strategy involved a masked 7-hydroxycoumarin fluorophore linked to a dienophile. The fluorophore was positioned so that after Diels-Alder reaction it could be easily eliminated. The third strategy was the most promising even though several problems had to be overcome.
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Renberg, Björn. "Fluorescence-based ligand assays for protein detection using affibody affinity proteins /." Stockholm, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3936.

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Mileyeva-Biebesheimer, Olga. "An Investigation into Metal Oxide Nanoparticle Toxicity to Bacteria in Environmental Systems Using Fluorescence Based Assays." University of Toledo / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1302125170.

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Galvan, Barbara. "Part I, highly sensitive hybridization assays for prostate-specific antigen mRNA based on time-resolved fluorescence and bioluminescence, Part II, fluorometric and time-resolved immunofluorometric assays for protein-tyrosine phosphatase and kinase activity." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1996. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/NQ30283.pdf.

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Uryga-Polowy, Viviane [Verfasser]. "Development of a labeling strategy for the synthesis of fluorescent libraries of peptides and small molecules and their use in fluorescence-based binding assays for the study of protein-protein interactions / Viviane Uryga-Polowy." Berlin : Freie Universität Berlin, 2009. http://d-nb.info/1023958619/34.

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Pinkert, Thomas. "Entwicklung molekularer Werkzeuge zur Erforschung des Lipidstoffwechsels." Doctoral thesis, Humboldt-Universität zu Berlin, 2017. http://dx.doi.org/10.18452/18034.

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Im Rahmen dieser Arbeit wurden fluoreszierende Sphingomyelin-Analoga zu Studium der sauren Sphingomyelinase (ASM) synthetisiert. Ausgehend von L-Serin wurde ein Sphingosin-Derivat mit natürlicher Stereochemie dargestellt. Anschließend wurde mittels Phosphorodichloridat-Chemie eine Aminoethylphosphat-Gruppe installiert. Zweifache Fluoreszenzmarkierung ergab Sonden mit der Fähigkeit zu Förster-Resonanzenergietransfer (FRET). Diese wurden als Substrate der ASM akzeptiert und erlaubten die Verfolgung der Enzymaktivität in vitro. Durch die Analyse der photophysikalischen Eigenschaften der Fluorophore wurde das allgemeine Konzept der Phasentrennungs-gestützten Signalverstärkung (PS) abgeleitet. Dieses Konzept wurde erfolgreich bestätigt durch die Synthese einer 30-mal leistungsfähigeren zweiten Generation der FRET-Sonde. Ein homogener Assay wurde entwickelt, der die Quantifizierung der ASM-Aktivität erlaubte. Unter Verwendung von gereinigter rekombinanter humaner ASM, HeLa-Zelllysaten oder Lysaten von murinen embryonalen Fibroblasten (MEFs) als Enzymquelle wurde ausschließlich unter den von der ASM bevorzugten Bedingungen eine vollständige und spezifische Hydrolyse der Sonde beobachtet. Des Weiteren erlaubte die Sonde die Detektion relativer Unterschiede der Aktivität der ASM in kultivierten MEFs mittels Fluoreszenzmikroskopie mit Zweiphotonenanregung (2PE).
Fluorescent sphingomyelin analogues have been synthesized to probe the acid sphingomyelinase (ASM). Starting from L-serine, a sphingosine with natural stereochemistry was synthesized. Subsequently, phosphorodichloridate chemistry was used to install an aminoethyl phosphate moiety. Dual fluorescent labeling afforded probes capable of Förster resonance energy transfer (FRET). They were recognized as substrates of ASM and allowed for monitoring of the enzyme’s activity in vitro. Through analysis of the fluorophores’ photophysical properties, the general concept of partition aided amplification of a FRET probe’s signal (PS) was developed. This concept was successfully confirmed by the synthesis of a second-generation probe with 30-fold improved response. A homogenous assay was developed, which allowed for a quantitation of ASM activity. Using either purified recombinant human ASM, or lysates of HeLa cells or mouse embryonic fibroblasts (MEFs) as an enzyme source, complete and specific cleavage was observed exclusively under conditions preferred by ASM. Furthermore, the probe enabled the detection of relative levels of ASM activity in cultivated MEFs using fluorescence microscopy with two-photon excitation (2PE).
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Niu, Sanjun. "A label-free, fluorescence based assay for microarray." Diss., Virginia Tech, 2004. http://hdl.handle.net/10919/11229.

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DNA chip technology has drawn tremendous attention since it emerged in the mid 90 s as a method that expedites gene sequencing by over 100-fold. DNA chip, also called DNA microarray, is a combinatorial technology in which different single-stranded DNA (ssDNA) molecules of known sequences are immobilized at specific spots. The immobilized ssDNA strands are called probes. In application, the chip is exposed to a solution containing ssDNA of unknown sequence, called targets, which are labeled with fluorescent dyes. Due to specific molecular recognition among the base pairs in the DNA, the binding or hybridization occurs only when the probe and target sequences are complementary. The nucleotide sequence of the target is determined by imaging the fluorescence from the spots. The uncertainty of background in signal detection and statistical error in data analysis, primarily due to the error in the DNA amplification process and statistical distribution of the tags in the target DNA, have become the fundamental barriers in bringing the technology into application for clinical diagnostics. Furthermore, the dye and tagging process are expensive, making the cost of DNA chips inhibitive for clinical testing. These limitations and challenges make it difficult to implement DNA chip methods as a diagnostic tool in a pathology laboratory. The objective of this dissertation research is to provide an alternative approach that will address the above challenges.. In this research, a label-free assay is designed and studied. Polystyrene (PS), a commonly used polymeric material, serves as the fluorescence agent. Probe ssDNA is covalently immobilized on polystyrene thin film that is supported by a reflecting substrate. When this chip is exposed to excitation light, fluorescence light intensity from PS is detected as the signal. Since the optical constants and conformations of ssDNA and dsDNA (double stranded DNA) are different, the measured fluorescence from PS changes for the same intensity of excitation light.. The fluorescence contrast is used to quantify the amount of probe-target hybridization. A mathematical model that considers multiple reflections and scattering is developed to explain the mechanism of the fluorescence contrast which depends on the thickness of the PS film. Scattering is the dominant factor that contributes to the contrast. The potential of this assay to detect single nucleotide polymorphism is also tested.
Ph. D.
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Zapka, Carrie A. "Development of a Rapid Fluorescence-Based Adenovirus Inactivation Assay." Youngstown State University / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=ysu1198694566.

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Koutnik, Petr. "First Supramolecular Fluorescence-Based Assay for Carbonic Anhydrase Inhibitors." Bowling Green State University / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1471261858.

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Book chapters on the topic "Fluorescence-based Assays"

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An, W. Frank. "Fluorescence-Based Assays." In Methods in Molecular Biology, 97–107. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-545-3_7.

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Cordero-Sánchez, Celia, Irene Mudarra-Fraguas, and Asia Fernández-Carvajal. "Fluorescence-Based Functional Assays for Ca2+-Permeable ThermoTRP Channels." In Methods in Molecular Biology, 99–110. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9446-5_7.

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Chen, Yu, Xin Liu, Nancy Wu, and Carol A. Fierke. "Fluorescence-Based Real-Time Activity Assays to Identify RNase P Inhibitors." In Methods in Molecular Biology, 201–25. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6634-9_12.

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Spessotto, Paola, Katia Lacrima, Pier Andrea Nicolosi, Eliana Pivetta, Martina Scapolan, and Roberto Perris. "Fluorescence-Based Assays for In Vitro Analysis of Cell Adhesion and Migration." In Methods in Molecular Biology, 221–50. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-413-1_16.

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Antonescu, Costin N., Varinder K. Randhawa, and Amira Klip. "Dissecting GLUT4 Traffic Components in L6 Myocytes by Fluorescence-Based, Single-Cell Assays." In Membrane Trafficking, 367–78. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-261-8_27.

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Davis, J. A., D. M. Fry, and B. W. Wilson. "Field Application of Fluorescence-Based Catalytic Assays for Measuring Cytochrome P450 Induction in Birds." In ACS Symposium Series, 169–79. Washington, DC: American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0643.ch013.

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Abdolvahabi, Alireza, Sanaz Rasouli, Corbin M. Croom, and Devon L. Plewman. "High-Throughput Microplate-Based Fluorescence Assays for Studying Stochastic Aggregation of Superoxide Dismutase-1." In Methods in Molecular Biology, 93–108. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8820-4_6.

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Knapman, Alisa, and Mark Connor. "Fluorescence-Based, High-Throughput Assays for μ-Opioid Receptor Activation Using a Membrane Potential-Sensitive Dye." In Methods in Molecular Biology, 177–85. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1708-2_14.

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Branchini, Bruce. "Firefly Luciferase-Based Sequential Bioluminescence Resonance Energy Transfer (BRET)-Fluorescence Resonance Energy Transfer (FRET) Protease Assays." In Bioluminescence, 101–15. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3813-1_8.

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Ems-McClung, Stephanie C., and Claire E. Walczak. "In Vitro FRET- and Fluorescence-Based Assays to Study Protein Conformation and Protein-Protein Interactions in Mitosis." In Methods in Molecular Biology, 93–122. New York, NY: Springer US, 2019. http://dx.doi.org/10.1007/978-1-0716-0219-5_7.

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Conference papers on the topic "Fluorescence-based Assays"

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Burns, David J., Elisabeth Alder, Yi-Hong Fan, Evelyn McKeegan, Usha Warrior, and Bruce Beutel. "Development of fluorescence-based high-throughput screening assays: choice of appropriate instrumentation." In BiOS '98 International Biomedical Optics Symposium, edited by Gerald E. Cohn. SPIE, 1998. http://dx.doi.org/10.1117/12.307328.

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Choi, Jong-ryul, Jong Hwan Sung, Michael L. Shuler, and Donghyun Kim. "Confocal fluorescence detection of cell-based assays using a digital micromirror device." In MOEMS-MEMS, edited by Michael R. Douglass and Larry J. Hornbeck. SPIE, 2010. http://dx.doi.org/10.1117/12.841738.

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Van Tassell, Roger L., and Mishell Evans. "Monitoring water supplies for weaponized bacteria and bacterial toxins using rapid fluorescence-based viability and affinity assays." In Optical Technologies for Industrial, Environmental, and Biological Sensing, edited by Arthur J. Sedlacek III, Richard Colton, and Tuan Vo-Dinh. SPIE, 2004. http://dx.doi.org/10.1117/12.515093.

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Apfel, Johanna N., and Patricia T. Reischmann. "Abstract 724: New fluorescence-based cell assays for visualizing the Raf - Ras interaction and the Wnt pathway activity." 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.am2013-724.

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Tsurkas, Andrew, and Gang Bao. "Molecular Beacons for Sensitive Gene Detection in Living Cells." In ASME 2003 International Mechanical Engineering Congress and Exposition. ASMEDC, 2003. http://dx.doi.org/10.1115/imece2003-42959.

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Real-time imaging of gene expression in living cells has the potential to significantly impact clinical and laboratory studies of cancer, including cancer diagnosis and analysis. Molecular beacons (MBs) provide a simple and promising tool for the detection of target mRNA as tumor markers due to their high signal-to-background ratio, and their improved specificity in detecting point mutations. However, the harsh intracellular environment does limit the sensitivity of MB-based gene detection. Specifically, MBs bound to target mRNAs cannot be distinguished from those degraded by nucleases, or opened due to non-specific interactions. To overcome this difficulty, we have developed a novel dual FRET molecular beacons approach in which a pair of molecular beacons, one with a donor fluorophore and a second with an acceptor fluorophore, hybridize to adjacent regions on the same target resulting in fluorescence resonance energy transfer (FRET). The detection of a FRET signal leads to a substantially increased signal-to-background ratio compared with that in single molecular beacon assays and enables discrimination between fluorescence due to specific probe/target hybridization and a variety of false-positive events. We have performed systematic in-solution and cellular studies of dual FRET molecular beacon and demonstrated that this new approach allows for real-time imaging of gene expression in living cells.
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Cummins, Brian M., and Gerard L. Coté. "A fluorescence polarization based assay for glucose sensing." In SPIE BiOS, edited by Robert J. Nordstrom and Gerard L. Coté. SPIE, 2012. http://dx.doi.org/10.1117/12.908630.

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Sharma, Ashutosh, and Nigel S. M. Quantrill. "Novel L-glutamate assay based on fluorescence quenching." In OE/LASE '94, edited by James A. Harrington, David M. Harris, Abraham Katzir, and Fred P. Milanovich. SPIE, 1994. http://dx.doi.org/10.1117/12.180765.

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Sumner, James J., Robert U. Mmerole, Dimitra N. Stratis-Cullum, Hyunmin Yi, William E. Bentley, and James B. Gillespie. "Hybridization assay based on evanescent fluorescence excitation and collection." In AeroSense 2003, edited by Patrick J. Gardner. SPIE, 2003. http://dx.doi.org/10.1117/12.486963.

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9

Hou, Ching-Wen, Meilin Zhu, Karen S. Anderson, Uwadiae Obahiagbon, and Jennifer Blain Christen. "Assay Development and Storage for Fluorescence-Based Lateral Flow Immunoassay." In 2018 IEEE Life Sciences Conference (LSC). IEEE, 2018. http://dx.doi.org/10.1109/lsc.2018.8572244.

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Wang, Fengyang, Renzhi Hu, Hao Chen, Pinhua Xie, Yihui Wang, Zhiyan Li, and Huawei Jin. "OH radical field observation based on Fluorescence Assay by Gas Expansion technique." In Fourier Transform Spectroscopy. Washington, D.C.: OSA, 2018. http://dx.doi.org/10.1364/fts.2018.jt2a.17.

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