Catálogo de publicaciones - revistas

<jats:title>Even more like birds</jats:title> <jats:p> Ecological convergence between pterosaurs and birds is often invoked, but to what degree the two groups share behavior is debated. Wang <jats:italic>et al.</jats:italic> describe a site with more than 100 fossilized pterosaur eggs that reveals that hatchling pterosaurs were likely not as precocial as previously thought (see the Perspective by Deeming). Furthermore, the overlaying of multiple clutches suggests that the pterosaurs may have exhibited breeding site fidelity, similar to rookery-breeding seabirds. Thus, the similarity between these two groups goes beyond wings. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6367" page="1197" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aan2329">1197</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6367" page="1124" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aao6493">1124</jats:related-article> </jats:p>

<jats:title>Blood DNases hack the NET</jats:title> <jats:p> Neutrophil extracellular traps (NETs) are lattices of processed chromatin decorated with select secreted and cytoplasmic proteins that trap and neutralize microbes. However, their inappropriate release may do more harm than good by promoting inflammation and thrombosis. Jiménez-Alcázar <jats:italic>et al.</jats:italic> report that two deoxyribonucleases (DNases), DNASE1 and DNASE1L3, have partially redundant roles in degrading NETs in the circulation (see the Perspective by Gunzer). Knockout mice lacking these enzymes were unable to tolerate chronic neutrophilia, quickly dying after blood vessels were occluded by NET clots. Furthermore, the damage unleashed by clots during septicemia was enhanced when these DNases were absent. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6367" page="1202" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aam8897">1202</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6367" page="1126" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aar2428">1126</jats:related-article> </jats:p>

<jats:title>Holding a master regulator in check</jats:title> <jats:p> A family of eukaryotic protein kinases, the phosphatidylinositol 3-kinase-related kinases (PIKKs), has key functions in DNA repair and nutrient sensing. In humans, ATR kinase locates DNA damage through its partner, ATRIP. Once activated, ATR initiates a cell-cycle cascade that culminates in cell-cycle arrest. Wang <jats:italic>et al.</jats:italic> determined the high-resolution structure of Mec1-Ddc2 (the yeast homolog of ATR-ATRIP) by electron microscopy. The structure shows the detailed architecture of the multidomain complex that overall forms a dimer of heterodimers. The detailed analysis of the structure reveals how an allosteric mechanism may activate the kinase. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6367" page="1206" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aan8414">1206</jats:related-article> </jats:p>

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