X. Zhang et al., "An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor," Cell, 125:1137-49, June 16, 2006.
This structural/biochemical study provides compelling evidence that the epidermal growth factor (EGF) receptor kinase domain is activated through formation of an asymmetric dimer, in which the C-lobe of one kinase domain impinges on the N-lobe of the other kinase domain, activating the latter.
Stevan Hubbard
New York University School of Medicine, USA
J. Wang et al., "Platensimycin is a selective FabF inhibitor with potent antibiotic properties," Nature, 441:358-61, May 18, 2006.
This paper reports the discovery and characterization of a new compound, platensimycin, that seems to have broad-spectrum, Gram-positive antibiotic activity by binding to the catalytic apparatus of a known antibacterial target FabF.
Xiayang Qiu
Pfizer Inc., USA
S. Wang et al., "Venular basement membranes contain specific matrix protein low expression regions that act as exit points ...
