In This Issue - pv

doi:10.1038/nchembio0905-v

Full Text - In This Issue | PDF (335 KB) - In This Issue

Back to school - p175

doi:10.1038/nchembio0905-175

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Teaching undergraduates at the interface of chemistry and biology: challenges and opportunities - pp176 - 179

Hilary Arnold Godwin & Benjamin Lee Davis

doi:10.1038/nchembio0905-176

The growth of research at the chemistry-biology interface provides a unique opportunity to inspire undergraduate students to pursue careers in science and to educate science and nonscience students broadly in both chemical and biological sciences.

Full Text - Teaching undergraduates at the interface of chemistry and biology: challenges and opportunities | PDF (498 KB) - Teaching undergraduates at the interface of chemistry and biology: challenges and opportunities | Supplementary information

Putting small molecules in the lead - pp180 - 183

Stefan Jaroch & Hilmar Weinmann

doi:10.1038/nchembio0905-180

Chemical genomic approaches offer an alternative to traditional high-throughput screening for drug discovery and provide an emerging approach to probing cellular biology. The 58^th Ernst Schering Foundation Workshop on "Chemical Genomics: Small Molecule Probes to Study Cellular Function," held April 6–8, 2005, in Berlin, Germany, captured recent chemical genomics advances and highlighted the power of a tight integration of chemistry and biology.

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Imaging G protein–coupled receptor islands - pp184 - 185

Paul S-H Park & Krzysztof Palczewski

doi:10.1038/nchembio0905-184

Near-field scanning optical microscopy has been used to study the organization of ₁- and ₂-adrenergic receptors in cardiac cells. The fluorescently labeled receptors organize into distinct clusters, which may represent localization in microdomains such as lipid rafts and caveolae.

Full Text - Imaging G protein–coupled receptor islands | PDF (187 KB) - Imaging G protein–coupled receptor islands

See also: Letter by Ianoul et al.

Antigene leaps forward through an open door - pp185 - 186

Bruce A Armitage

doi:10.1038/nchembio0905-185

Blocking gene expression by interfering with translation of mRNA can be accomplished by means of antisense or short interfering RNA strategies, but more potent inhibitors would act by inhibiting transcription of genomic DNA. Two new studies show efficient inhibition of transcription using single-stranded peptide nucleic acid or double-stranded RNA targeted to the open complex formed at the transcription start site.

Full Text - Antigene leaps forward through an open door | PDF (191 KB) - Antigene leaps forward through an open door

See also: Article by Janowski et al. | Article by Janowski et al.

Watching proteases in action - pp186 - 187

Klaudia Brix & Silvia Jordans

doi:10.1038/nchembio0905-186

Activity-based probes can be used for monitoring enzyme activity based on their covalent reactions with active-site residues. A quenched activity-based probe has now been developed that becomes fluorescent only after labeling active proteases. The specificity of the fluorescent signal and cell permeability of the small molecule make this probe effective for monitoring protease activity in living cells.

Full Text - Watching proteases in action | PDF (368 KB) - Watching proteases in action

See also: Letter by Blum et al.

Cardiolipin oxidation sets cytochrome c free - pp188 - 189

Sten Orrenius & Boris Zhivotovsky

doi:10.1038/nchembio0905-188

Cytochrome c release from the mitochondria is a critical component of the apoptotic cell-death program. Cytochrome c–catalyzed peroxidation of cardiolipin, a mitochondrial phospholipid, has now been shown to lessen the binding of cytochrome c to the mitochondrial inner membrane and facilitate permeabilization of the outer membrane. These results describe a new and earlier pro-apoptotic role for cytochrome c.

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See also: Article by Kagan et al.

A glimpse at the grail - pp189 - 191

Dirk Trauner

doi:10.1038/nchembio0905-189

Voltage-gated ion channels respond to alterations in membrane potential and mediate action potential in neurons. A recent study provides new insights into the structure and gating of the Shaker potassium channel.

Full Text - A glimpse at the grail | PDF (317 KB) - A glimpse at the grail

The econometrics of evolution - pp191 - 192

Stephen S Fong, Andrew R Joyce & Bernhard Ø Palsson

doi:10.1038/nchembio0905-191

Examples abound in nature in which organisms adapt and optimize their fitness in a given environment. A new study demonstrates that a cellular cost-benefit analysis drives growth optimization over the course of evolution by attenuation of protein expression levels.

Full Text - The econometrics of evolution | PDF (151 KB) - The econometrics of evolution

Linking physiological functions of iron - pp193 - 194

Tracey A Rouault

doi:10.1038/nchembio0905-193

Iron-sulfur clusters and hemes are two iron-containing prosthetic groups involved in important physiological functions. Identification of the gene responsible for anemia in a mutant zebrafish has revealed an unexpected link between iron-sulfur cluster assembly and heme synthesis in red blood cells.

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Research Highlights - p195

doi:10.1038/nchembio0905-195

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Corrigendum: Assignment of protein function in the postgenomic era - p233

Alan Saghatelian & Benjamin F Cravatt

doi:10.1038/nchembio0905-233

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Corrigendum: Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury - p234

Alexei Degterev, Zhihong Huang, Michael Boyce, Yaqiao Li, Prakash Jagtap, Noboru Mizushima, Gregory D Cuny, Timothy J Mitchison, Michael A Moskowitz & Junying Yuan

doi:10.1038/nchembio0905-234a

Full Text - Corrigendum: Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury | PDF (47 KB) - Corrigendum: Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury

Erratum: Small-molecule interaction with a five-guanine-tract G-quadruplex structure from the human MYC promoter - p234

Anh Tuân Phan, Vitaly Kuryavyi, Hai Yan Gaw & Dinshaw J Patel

doi:10.1038/nchembio0905-234b

Full Text - Erratum: Small-molecule interaction with a five-guanine-tract G-quadruplex structure from the human MYC promoter | PDF (47 KB) - Erratum: Small-molecule interaction with a five-guanine-tract G-quadruplex structure from the human MYC promoter