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Relevant bibliographies by topics / Thermal shift assay

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Journal articles

Academic literature on the topic 'Thermal shift assay'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 March 2023

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Journal articles on the topic "Thermal shift assay"

1

McMahon, Róisín M., Martin J. Scanlon, and Jennifer L. Martin. "Interrogating Fragments Using a Protein Thermal Shift Assay." Australian Journal of Chemistry 66, no. 12 (2013): 1502. http://dx.doi.org/10.1071/ch13279.

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Protein thermal shift is a relatively rapid and inexpensive technique for the identification of low molecular weight compound interactions with protein targets. An increase in the melting temperature of the target protein in the presence of a test ligand is indicative of a promising ligand–protein interaction. Due to its simplicity, protein thermal shift is an attractive method for screening libraries and validating hits in drug discovery programs. The methodology has been used successfully in high throughput screens of small molecule libraries, and its application has been extended to report

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2

DeLeeuw, Lynn W., Robert C. Monsen, Vytautas Petrauskas, et al. "POT1 stability and binding measured by fluorescence thermal shift assays." PLOS ONE 16, no. 3 (2021): e0245675. http://dx.doi.org/10.1371/journal.pone.0245675.

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The protein POT1 (Protection of Telomeres 1) is an integral part of the shelterin complex that protects the ends of human chromosomes from degradation or end fusions. It is the only component of shelterin that binds single-stranded DNA. We describe here the application of two separate fluorescent thermal shift assays (FTSA) that provide quantitative biophysical characterization of POT1 stability and its interactions. The first assay uses Sypro Orange™ and monitors the thermal stability of POT1 and its binding under a variety of conditions. This assay is useful for the quality control of POT1 p

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3

Dart, Melanie L., Thomas Machleidt, Emily Jost, et al. "Homogeneous Assay for Target Engagement Utilizing Bioluminescent Thermal Shift." ACS Medicinal Chemistry Letters 9, no. 6 (2018): 546–51. http://dx.doi.org/10.1021/acsmedchemlett.8b00081.

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4

Andreotti, Giuseppina, Maria Monticelli, and Maria Vittoria Cubellis. "Looking for protein stabilizing drugs with thermal shift assay." Drug Testing and Analysis 7, no. 9 (2015): 831–34. http://dx.doi.org/10.1002/dta.1798.

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5

YATA, YUYA, TAKAYUKI ISHIDA, MITSUTOSHI KUBOTA, TARO MASUDA, and HARUHIKO TOYOHARA. "Studies on the thermal denaturation of fish actomyosin by thermal shift assay." NIPPON SUISAN GAKKAISHI 80, no. 4 (2014): 594–600. http://dx.doi.org/10.2331/suisan.80.594.

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6

Fleischhauer, Lutz, Christoph Niemietz, Sara Reinartz Groba, et al. "Thermal shift assay for evaluation of transthyretin stability in plasma." Amyloid 24, sup1 (2017): 34–35. http://dx.doi.org/10.1080/13506129.2017.1281121.

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7

Kelm, Melanie, and Martin Knoll. "Real-Time-Erfassung der Proteinstabilität mit dem thermal shift assay." BIOspektrum 21, no. 1 (2015): 76–77. http://dx.doi.org/10.1007/s12268-015-0543-5.

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8

McMahon, Roisin M., Martin J. Scanlon, and Jennifer L. Martin. "ChemInform Abstract: Interrogating Fragments Using a Protein Thermal Shift Assay." ChemInform 45, no. 8 (2014): no. http://dx.doi.org/10.1002/chin.201408278.

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9

Pantoliano, Michael W., Eugene C. Petrella, Joseph D. Kwasnoski, et al. "High-Density Miniaturized Thermal Shift Assays as a General Strategy for Drug Discovery." Journal of Biomolecular Screening 6, no. 6 (2001): 429–40. http://dx.doi.org/10.1177/108705710100600609.

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More general and universally applicable drug discovery assay technologies are needed in order to keep pace with the recent advances in combinatorial chemistry and genomics-based target generation. Ligand-induced conformational stabilization of proteins is a well-understood phenomenon in which substrates, inhibitors, cofactors, and even other proteins provide enhanced stability to proteins on binding. This phenomenon is based on the energetic coupling of the ligand-binding and protein-melting reactions. In an attempt to harness these biophysical properties for drug discovery, fully automated in

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10

Kopra, Kari, Salla Valtonen, Randa Mahran, et al. "Thermal Shift Assay for Small GTPase Stability Screening: Evaluation and Suitability." International Journal of Molecular Sciences 23, no. 13 (2022): 7095. http://dx.doi.org/10.3390/ijms23137095.

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Thermal unfolding methods are commonly used as a predictive technique by tracking the protein’s physical properties. Inherent protein thermal stability and unfolding profiles of biotherapeutics can help to screen or study potential drugs and to find stabilizing or destabilizing conditions. Differential scanning calorimetry (DSC) is a ‘Gold Standard’ for thermal stability assays (TSA), but there are also a multitude of other methodologies, such as differential scanning fluorimetry (DSF). The use of an external probe increases the assay throughput, making it more suitable for screening studies,

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