ArticleAngewandte Chemie (International ed. in English)2023
Good Things Take Time: Tiwary-Seeliger Collaboration for Predictive Pharmacodynamics.
Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Abstract
This invited Team Profile was created by the Tiwary group, University of Maryland, College Park (USA) and the Seeliger group, Stony Brook University, New York (USA). They recently published an article on the previously made observation through in-cell screening that the blockbuster cancer drug Gleevec has the same binding affinity, yet different dissociation kinetics against wild-type and N368S-mutated Abl kinase. Through all-atom enhanced molecular dynamics simulations guided by statistical mechanics and information theory, they were able to explain the mechanistic basis of this perplexing observation. Their work has ramifications for how pharmaceutical drugs might experience kinetic resistance due to mutations. "Protein Flexibility and Dissociation Pathway Differentiation Can Explain Onset of Resistance Mutations in Kinases", M. Shekhar, Z. Smith, M. A. Seeliger, P. Tiwary, Angew. Chem. Int. Ed. 2022, e202200983; Angew. Chem. 2022, e202200983.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.