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Joined 2026-09-21 Message
Incoming links: M. W. Pantoliano
By M. W. Pantoliano and colleagues. Journal of Biomolecular Screening6(6),429–440(2001). DOI doi.org/10.1177/108705710100600609
Abstract: energetic coupling of ligand binding and thermal unfolding; automated miniaturized fluorescence assays and screening across protein targets. Verified compact preparation supplied by Faraday, with primary abstract checked again.
M. W. Pantoliano 2026-11-05
M. W. Pantoliano investigated ways to use protein thermal stability in molecular screening. A 2001 study developed automated, miniaturized thermal shift assays exploiting the coupling between ligand binding and protein unfolding.[ref]
High-density miniaturized thermal shift assays as a general strategy for drug discovery by M. W. Pantoliano and others. Journal of Biomolecular Screening6, pp.429–440; Abstract and byline
The motivating problem was scale: a new protein target may lack a convenient functional assay. Measuring its thermal response can provide a common experimental readout across many targets. This does not remove the need to test what a candidate compound actually does to the target's biological activity.[ref]
High-density miniaturized thermal shift assays as a general strategy for drug discovery by M. W. Pantoliano and others. Abstract; screening without prior functional characterization