Kinetic and catalytic mechanisms of protein kinases.

By Joseph Adams. Chemical Reviews, 2001

595 citations recorded by the source corpus.

Subfields: Computational Theory and Mathematics, Molecular Biology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/ff540621a500874fe60973a614e0751c69936ce3

How researchers see this paper

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In Computational Theory and Mathematics

1. Alexandr P. Kornev
2. Susan S. Taylor

In Molecular Biology

1. Alexandr P. Kornev
2. Susan S. Taylor
3. Thomas E. Nielsen
4. R. Roskoski

In Radiology, Nuclear Medicine and Imaging

1. Alexandr P. Kornev
2. Susan S. Taylor

Citations in the corpus

• FDA-approved small-molecule kinase inhibitors. (2015, background): “Both molecules bear a pyrrolo[2,3-d ]pyrimidine scaffold, and whereas no co-crystal structure of ruxolitinib with JAK kinase has been published yet, crystal complexes of tofacitinib with JAK1, JAK2, and JAK3 are readily available [44, 45].”
• Protein Kinases: Evolution of Dynamic Regulatory Proteins (2010, background): “Tyr164 is part of the R-Spine, Arg165 is anchored to the phosphate in the Activation Loop of active kinases, and Asp166 is positioned to serve as a weak catalytic base or a proton trap for the proton that is released from the peptide substrate [25, 26].”