Notable

The Faculty of 1000 is aWeb-based literature awareness tool published by BioMed Central. For more information visit www.facultyof1000.com. ACTIVATING PK B/AKT 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

Chris Bahls
Jul 21, 2002
The Faculty of 1000 is a
Web-based literature awareness tool published by BioMed Central. For more information visit www.facultyof1000.com.

ACTIVATING PK B/AKT
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


ASSEMBLING POROUS SOLIDS
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...

Interested in reading more?

Become a Member of

Receive full access to digital editions of The Scientist, as well as TS Digest, feature stories, more than 35 years of archives, and much more!
Already a member?