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In This Issue

In This Issue pv

doi:10.1038/nchembio0706-v


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Editorial

Walking the walk p347

doi:10.1038/nchembio0706-347


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News and Views

One-electron oxidation of DNA and inflammation processes pp348 - 349

Jean Cadet, Thierry Douki & Jean-Luc Ravanat

doi:10.1038/nchembio0706-348

Nitrosoperoxycarbonate anion, a reactive species generated in inflammation processes, is able to specifically oxidize guanine bases with a sequence selectivity that is almost opposite from that usually observed for one-electron oxidants.

See also: Brief Communication by Margolin et al.


NO place to hide pp349 - 350

Nathaniel Finney

doi:10.1038/nchembio0706-349

Nitric oxide (NO) regulates a broad range of biological processes, yet many intracellular details of NO-mediated processes remain hidden. A new fluorescein derivative capable of direct detection provides a key advance in determining NO function in vivo.

See also: Article by Lim et al.


Significance of one-bead-one-compound combinational chemistry pp351 - 352

Xiaoyuan Chen & Sanjiv S Gambhir

doi:10.1038/nchembio0706-351

One-bead-one-compound combinatorial peptidomimetic libraries, in conjunction with a high-stringency screening method, are a powerful tool for screening peptide and peptidomimetic ligands for target proteins. Picomolar-affinity peptidomimetics for the integrin alpha4beta1 have now been developed and have been successfully used to image alpha4beta1-expressing tumors in living mice.

See also: Article by Peng et al.


Visualizing tricoordinate copper transfer pp352 - 353

Paul A Cobine & Dennis R Winge

doi:10.1038/nchembio0706-352

Copper is a requisite cofactor in myriad cellular enzymes and is shuttled to different cellular sites for the assembly of copper-containing enzymes by Cu(I)-binding metallochaperones. NMR structural studies now reveal a key step in copper ion trafficking to sites of use.

See also: Brief Communication by Banci et al.


Slip sliding away: new insights into DNA-protein recognition pp353 - 354

Frederick W Dahlquist

doi:10.1038/nchembio0706-353

DNA-binding proteins accomplish the remarkable feat of finding their correct target sequences within a sea of genomic DNA. A new study uses NMR spectroscopy to show the mechanism by which proteins may hop between and slide along DNA as they search for their target binding sites.


Discovery of a new 'dynasore' pp355 - 356

Heather M Thompson & Mark A McNiven

doi:10.1038/nchembio0706-355

Dynamin is a large GTPase that participates in the severing of membrane-bound vesicles. A small-molecule inhibitor specific for the dynamin family of GTPases has been identified and reveals new aspects of membrane dynamics.


Research Highlights p357

doi:10.1038/nchembio0706-357


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Brief Communications

Paradoxical hotspots for guanine oxidation by a chemical mediator of inflammation pp365 - 366

Yelena Margolin, Jean-Francois Cloutier, Vladimir Shafirovich, Nicholas E Geacintov & Peter C Dedon

doi:10.1038/nchembio796

no alt info

See also: News and Views by Cadet et al.


The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction pp367 - 368

Lucia Banci, Ivano Bertini, Francesca Cantini, Isabella C Felli, Leonardo Gonnelli, Nick Hadjiliadis, Roberta Pierattelli, Antonio Rosato & Petros Voulgaris

doi:10.1038/nchembio797

no alt info

See also: News and Views by Cobine & Winge


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Letter

Small molecule–based reversible reprogramming of cellular lifespan pp369 - 374

Jaejoon Won, Mina Kim, Nuri Kim, Jin Hee Ahn, Woo Gil Lee, Sung Soo Kim, Ki-Young Chang, Yong-Weon Yi & Tae Kook Kim

doi:10.1038/nchembio800

no alt info

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Erratum

Erratum: The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography p390

Georg Wille, Danilo Meyer, Andrea Steinmetz, Erik Hinze, Ralph Golbik & Kai Tittmann

doi:10.1038/nchembio0706-390


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