Catálogo de publicaciones - revistas

<jats:title>How farming protects against allergies</jats:title> <jats:p> People who grow up on dairy farms only rarely develop asthma or allergies. This is probably because as children, they breathe air containing bacterial components, which reduce the overall reactivity of the immune system. Schuijs <jats:italic>et al.</jats:italic> chronically exposed mice to bacterial endotoxin before they received an allergic stimulus. The protocol indeed protected them from developing an allergic response. Protection relied on a particular enzyme: A20. In humans, a variant of A20 correlates with increased susceptibility to asthma and allergy in children growing up on farms. </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="6252" page="1106" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aac6623">1106</jats:related-article> </jats:p>

<jats:title>Unravelling the SM-SNARE conundrum</jats:title> <jats:p> So-called SNARE proteins mediate and lend specificity to the fusion between different intracellular membranes. The SM proteins are universally required for intracellular vesicle fusion, yet their mechanism of action has long been enigmatic. Baker <jats:italic>et al.</jats:italic> have solved a piece of the puzzle by “capturing” SNAREs in the process of assembling into fusogenic complexes on the surface of an SM protein. The findings suggest exactly how and why SM proteins help vesicular fusion during intracellular membrane trafficking. </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="6252" page="1111" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aac7906">1111</jats:related-article> </jats:p>

<jats:title>RNA editing helps identify cellular RNAs</jats:title> <jats:p> Adenosine bases in messenger RNA (mRNAs) can be enzymatically modified and changed into inosine bases. This RNA “editing” is mediated by adenosine deaminase acting on RNA (ADAR) enzymes. Liddicoat <jats:italic>et al.</jats:italic> show that the in vivo targets of the principal editing enzyme, ADAR1, are long double-stranded RNA (dsRNA) structures in noncoding portions of cellular mRNAs. ADAR1-directed editing of these cellular targets is critical to avoid activation of an immune response to dsRNA in the cytoplasm, because dsRNA is also a marker of viral infection. </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="6252" page="1115" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aac7049">1115</jats:related-article> </jats:p>

<jats:title>Plasmid partitioning superstructure system</jats:title> <jats:p> Partitioning and sharing DNA between dividing cells is critical for all domains of life. Prokaryotes must share certain plasmids as well as their genomic DNA to survive. Schumacher <jats:italic>et al.</jats:italic> studied the partition system that segregates a conjugative plasmid in the prokaryote Sulfolobus. The system consists of three proteins. AspA spreads along the plasmid DNA to create a protein-DNA superhelix. The ParA motor protein is linked to the protein-DNA superhelix through the ParB protein, which has structural similarities to eukaryotic centromere segregating proteins. </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="6252" page="1120" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aaa9046">1120</jats:related-article> </jats:p>

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