Catálogo de publicaciones - revistas

<jats:title>How a toxin makes epithelial sheets leaky</jats:title> <jats:p> The entire human body and its many compartments are shielded from their external environments by the barrier function of epithelial cell sheets. The paracellular barrier function of tight junctions (TJs) is critical for maintaining homeostasis in any multicellular organism, especially in the skin and internal organs and at the blood-brain barrier. One of the major components of TJs is a family of adhesive membrane proteins known as claudins. Several members of the claudin family are receptors for the bacterial toxin <jats:italic>Clostridium perfringens</jats:italic> enterotoxin. This toxin often causes food-borne illness both in humans and animals. Saitoh <jats:italic>et al.</jats:italic> crystallized a complex between the toxin and a claudin that reveals just how the toxin damages epithelial barriers (see the Perspective by Artursson and Knight). </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="6223" page="775" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.1261833">775</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6223" page="716" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.aaa6124">716</jats:related-article> </jats:p>

<jats:title>Toward drugging the undruggable in cancer</jats:title> <jats:p> Many human cancers are characterized by inappropriate activity of transcription factors. These proteins are attractive drug targets in principle, but normalizing their function requires drugs that modulate specific protein-protein interactions, a goal that has been challenging. In acute myeloid leukemia, a chromosomal translocation creates an aberrant form of the transcription factor CBF-beta, which outcompetes “normal” CBF-beta for binding to another transcription factor called RUNX1, thereby deregulating its activity. Illendula <jats:italic>et al.</jats:italic> identified and chemically optimized a small molecule that selectively disrupts the interaction between the aberrant CBF-beta and RUNX1 (see the Perspective by Koehler and Chen). This molecule restored normal gene expression patterns and delayed leukemia progression in mice. Thus, transcription factors may not be as undruggable as once thought. </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="6223" page="779" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.aaa0314">779</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6223" page="713" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.aaa6119">713</jats:related-article> </jats:p>

<jats:title>For a single B cell, many roads to take</jats:title> <jats:p> To successfully fight a pathogen, immunological B cells must wage a multipronged attack: They can differentiate into antibody-secreting plasma cells or become T cell–helping germinal center cells, or even long-lived memory cells. But can a single B cell acquire all of these different fates? To find out, Taylor <jats:italic>et al.</jats:italic> tracked the responses of single B cells in mice. Although some B cells acquired only one fate, others differentiated into all three. The authors linked the ability of B cells to differentiate into multiple subsets to their ability to proliferate and resist cell death, and the affinity of their antigen receptor. </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="6223" page="784" related-article-type="in-this-issue" vol="347" xlink:href="10.1126/science.aaa1342">784</jats:related-article> </jats:p>

<jats:p>Lipids have traditionally been among the hardest biomolecules to study, but new technologies and techniques are gradually revealing more of the lipidome.</jats:p>

<jats:p>A weekly roundup of information on newly offered instrumentation, apparatus, and laboratory materials of potential interest to researchers.</jats:p>

<jats:p>On this week's show: Updating the planetary boundaries framework, an accounting of ocean plastics, and a roundup of daily news stories.</jats:p>