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J. Yang et al., "Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation," Molecular Cell, 9:1227-40, 2002.

"This contribution is important because it presents the crystal structure of the catalytic domain of Akt/protein kinase B and presents a molecular explanation for why phosphorylation of the hydrophobic motif stabilizes the conformation of AGC kinases. Specifically, the authors propose that phosphorylation of the hydrophobic motif orders the C helix to more favorably align residues for catalysis."

--Alexandra Newton,
University of California, San Diego, US

C.J. Kuehl et al., "Coordination-driven self assembly: solids with bidirectional porosity," Journal of the American Chemical Society, 124:7266-7, June 26, 2002.

"The authors show that a very large dipyridyl macrocycle self-assembles...

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