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Michael Sundström

Researcher at Karolinska University Hospital

Publications -  86
Citations -  3530

Michael Sundström is an academic researcher from Karolinska University Hospital. The author has contributed to research in topics: Crystal structure & Drug discovery. The author has an hindex of 18, co-authored 85 publications receiving 3144 citations. Previous affiliations of Michael Sundström include Karolinska Institutet & University of Copenhagen.

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The promise and peril of chemical probes.

Cheryl H. Arrowsmith, +53 more
TL;DR: A community-driven wiki resource to improve quality and convey current best practice on chemical probes, and to help address shortcomings of poor quality or that are used incorrectly generate misleading results.
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Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination.

TL;DR: Two screening platforms are implemented, based on either fluorimetry or static light scattering, to measure the increase in protein thermal stability upon binding of a ligand without the need to monitor enzyme activity, and a small molecule was identified that stabilized the proteins and promoted structure determination.
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A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases

TL;DR: This analysis evaluated the specificity of 156 validated kinase inhibitors, including inhibitors used in clinical trials, against 60 human Ser/Thr kinases using a thermal stability shift assay and revealed many unexpected cross-reactivities for inhibitors thought to be specific for certain targets.
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Structural Basis for Protein-Protein Interactions in the 14-3-3 Protein Family.

TL;DR: Structural detail for five 14-3-3 isoforms bound to ligands is provided, providing structural coverage for all isoforms of a human protein family, and shows that the 14- 3-3 proteins are adaptable structures in which internal flexibility is likely to facilitate recognition and binding of their interaction partners.
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Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.

TL;DR: How human JMJD2A (jumonji domain containing 2A), which is selective towards tri- and dimethylated histone H3 lysyl residues 9 and 36, discriminates between methylation states and achieves sequence selectivity for H3K9 is revealed.