8A Chemical Reviews, 2001, Vol. 101, No. 8
In Color on the Front Cover (Top) CI-1033 bound into the active site of the epidermal growth factor receptor tyrosine kinase. See “Chemical Inhibitors of Protein Kinases” by Alexander J. Bridges, p 2541. (Bottom left) Structural overlay of the dual-specificity protein phosphatase VHR with the phospholipid phosphatase PTEN. See “Molecular Reactions of Protein Phosphatases−Insights from Structure and Chemistry” by Michael D. Jackson and John M. Denu, p 2313. (Bottom right) Phospho-CDK2/KAP complex. See “Structural Basis for Control by Phosphorylation” by Louise N. Johnson and Richard J. Lewis, p 2209. In Color on the Inside Front Cover (Middle left) Modular design of protein kinases (catalytic domains in dark green) regulated by calcium/calmodulin (binding domains in yellow). See “Structure and Regulation of Calcium/Calmodulin-Dependent Protein Kinases” by Thomas R. Soderling and James T. Stull, p 2341. (Bottom left) c-Src phosphorylation of the EGF receptor, p190RhoGAP, or focal adhesion kinase leads to a variety of cellular responses including proliferation, adhesion/migration, and actin rearrangements. See “c-Src Tyrosine Phosphorylation of Epidermal Growth Factor Receptor, P190 RhoGAP, and Focal Adhesion Kinase Regulates Diverse Cellular Processes” by Michelle D. Haskell, Jill K. Slack, J. Thomas Parsons, and Sarah J. Parsons, p 2425. In Color on the Inside Back Cover (Bottom left) Structural model of the wedge−PTP domain 1 interaction in a CD45 dimer resulting in inhibition. See “Regulatory Mechanisms for Receptor Protein Tyrosine Phosphatases” by Ravindra Majeti and Arthur Weiss, p 2441. In Color on the Back Cover (Top left) Structural model of a MAP kinase. See “MAP Kinases” by Zhu Chen, Tara Beers Gibson, Fred Robinson, Loraine Silvestro, Gray Pearson, Bing-e Xu, Angelique Wright, Colleen Vanderbilt, and Melanie H. Cobb, p 2449. (Top right) Regulation of β-catenin by the CSK-3 mediated destruction complex. See “Glycogen Synthase Kinase-3: Properties, Functions, and Regulation” by Adnan Ali, Klaus P. Hoeflich, and James R. Woodgett, p 2527. (Middle left) Mechanism of activation of PKB due to PI 3 kinase activation. See “Phosphoinositide-Regulated Kinases and Phosphoinositide Phosphatases” by Nick R. Leslie, Ricardo M. Biondi, and Dario R. Alessi, p 2365. (Middle right) Structure of a Cdk2/cyclin A complex bound to a peptide substrate (in green). The Cdk2/cyclin A structure is depicted via a surface representation of the electrostatic potential with acidic regions in red and basic regions in blue. See “Cyclin-Dependent Kinases” by J. W. Harper and P. D. Adams, p 2511. (Bottom left) Model for the regulation of protein kinase C by phosphorylation and cofactors. See “Protein Kinase C: Structural and Spatial Regulation by Phosphorylation, Cofactors, and Macromolecular Interactions” by Alexandra C. Newton, p 2353. (Bottom right) Structural organization of the regulatory subunit of the cAMP-dependent protein kinase (cAPK), a highly dynamic and multifunctional protein with two stable, protein-interacting domains joined by a flexible and disordered linker. See “Dynamics of cAMP-Dependent Protein Kinase” by David A. Johnson, Pearl Akamine, Elzbieta RadzioAndzelm, Madhusudan, and Susan S. Taylor, p 2243.
