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Small-molecule activation switches on apoptosis. Putt et al. (p 543) identify the first small molecule (PAC-1) that directly causes cleavage of procaspase-3 to generate the active executioner enzyme caspase-3. Thus, PAC-1 bypasses the normal apoptosis circuitry in causing cell death - an effect that may be especially important in cancer cells, in which these signal cascades are often interrupted by faulty wiring (see also News & Views by Porter, p 509). Cover art by Erin Boyle, based on a transmission electron microscope image of lymphocytes provided by Paul Hergenrother, courtesy of Carolyn Bertozzi.
Successful science education requires a knowledgeable teacher, a challenging curriculum, and teaching methods that actively engage students in a learning process that evokes the scientific method.
Bioinorganic chemistry remains a vibrant discipline at the interface of chemistry and the biological sciences. Metal ions function in numerous metalloenzymes, are incorporated into pharmaceuticals and imaging agents, and inspire the synthesis of catalysts used to achieve many chemical transformations.
Caspase-3 is a central player in the orchestration of apoptotic cell death. A newly identified compound selectively activates caspase-3, has proapoptotic activity against transformed cells and retards the growth of procaspase-3–rich tumors.
Enzymatic cyclization of the linear polyketide chain to form a macrolactone is a key step in the biosynthesis of type I polyketide natural products. Structural biology and inhibitor design were used to gain insight into the mechanism and specificity of this enzymatic process.
A histone deacetylase inhibitor seems to restore the transcriptional activity of a silenced gene by overcoming heterochromatin effects, thereby offering a potential treatment for the neurodegenerative disease Friedreich's ataxia.
D-Amino acids can be useful building blocks for pharmaceuticals, but synthesizing them at a low cost remains challenging. A good catalyst for generating unnatural D-amino acids has been created by expanding the substrate range of a highly specific dehydrogenase.
New advances in mass spectrometry allow researchers to determine the way multiple protein subunits are assembled spatially. This approach can reveal topology and provide information on the interacting proteins of the 19S proteasome.