MCC950 directly targets the NLRP3 ATP-hydrolysis motif for inflammasome inhibition

By Rebecca C. Coll, James R. Hill, C. Day, A. Zamoshnikova, D. Boucher, Nicholas L. Massey, Jessica L. Chitty, J. Fraser, M. Jennings, A. Robertson and 1 more. Nature Chemical Biology, 2019

882 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Surgery

View Paper: https://www.semanticscholar.org/paper/5971f6c79b6f6e8f88f87715fff871e157af8f2b

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. J. K. Kim
2. C. Sasakawa
3. E. Jo

Citations in the corpus

• An update on the regulatory mechanisms of NLRP3 inflammasome activation (2021, background): “The NACHT domain of NLRP3 is the molecular target of diarylsulfonylurea inhibitors, including MCC950/CRID3,(243) which is a potent and selective inhibitor of the NLRP3 inflammasome pathway through its interaction with the Walker B motif within the NACHT domain of NLRP3 by which ATP hydrolysis is blo”