Catálogo de publicaciones - revistas

<jats:title>Getting rid of faulty mRNA</jats:title> <jats:p> The cell monitors the health of its mRNAs, destroying those that are faulty or damaged. Destruction by the exosome complex prevents them from being used to synthesize deranged and potentially dangerous proteins. Schmidt <jats:italic>et al.</jats:italic> determined the structure of the Ski helicase complex, which guides RNAs to the exosome complex destruction machinery in association with a mRNAbound ribosome. The end of the mRNA is threaded from the ribosome into the heart of the helicase, whence the message would be channeled into the maw of the exosome complex. </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="6318" page="1431" related-article-type="in-this-issue" vol="354" xlink:href="10.1126/science.aaf7520">1431</jats:related-article> </jats:p>

<jats:title>Structural insights into capsid flexibility</jats:title> <jats:p> Viral capsids are protein structures that enclose the genetic material of viruses. Previous structural studies of the HIV-1 capsid have relied on recombinant, cross-linked, or mutant capsid proteins. Mattei <jats:italic>et al.</jats:italic> now report subnanometer-resolution cryo–electron tomography structures of the HIV-1 capsid from intact virions. These structures confirm the hollow cone shape of the capsid and allow for the specific placement of each individual capsid hexamer and pentamer within the lattice structure. The structures also reveal the flexible nature of the capsid, which likely helps it to accommodate interactions with host cell factors. </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="6318" page="1434" related-article-type="in-this-issue" vol="354" xlink:href="10.1126/science.aah4972">1434</jats:related-article> </jats:p>

<jats:title>Rescuing stalled ribosomes</jats:title> <jats:p> A small percentage of bacterial mRNAs lack a stop codon. Ribosomes stall at the end of such mRNAs, and the buildup of stalled ribosomes can be lethal. The primary rescue mechanism, in which translation continues on a piece of RNA that contains a stop codon, is a drug target. However, bacteria have another backup plan. James <jats:italic>et al.</jats:italic> present structures that show that ArfA (alternative rescue factor A) substitutes for a stop codon by binding in the ribosomal mRNA channel and recruiting RF2 (release factor 2). It mediates conformational changes required for RF2 to catalyze peptide release. </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="6318" page="1437" related-article-type="in-this-issue" vol="354" xlink:href="10.1126/science.aai9127">1437</jats:related-article> </jats:p>

<jats:title>Engineering control of cellular proteins</jats:title> <jats:p> The ability to switch proteins between active and inactive conformations can give insight into their function. Dagliyan <jats:italic>et al.</jats:italic> present a method to insert domains that control protein activity. They computationally identified protein loops that are coupled to the active site. Sensory domains inserted into these loops could modulate protein activity when their conformation was changed by light or ligand binding. The authors engineered domains into three different classes of proteins involved in cell signaling and found that switching the proteins between active and inactive states could control the shape and movement of living cells. </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="6318" page="1441" related-article-type="in-this-issue" vol="354" xlink:href="10.1126/science.aah3404">1441</jats:related-article> </jats:p>

<jats:p>Robotics is not just fodder for fiction, despite the word being coined by Russian-born American sci-fi writer Isaac Asimov in his 1942 short story "Runaround." The field has become multidisciplinary, borrowing from engineering, mathematics, computer science, and more recently, neuroscience. Researchers from these fields are trying to build better robots and also to better humanity through their use. In this supplement, researchers from across China and around the world discuss the latest challenges and advancements in their field. For many functions, such as grasping, vision, and memory, researchers are turning to neurobiology for inspiration. Building humanoid or anthropomorphic robots remains the ultimate goal, but since the robots’ memory and learning algorithms are patterned after the human brain, there is still much to learn about neurobiology before that goal is attained.</jats:p> <jats:p> This special supplement brought to you by the <jats:bold>Science</jats:bold> /AAAS Custom Publishing Office. </jats:p>

<jats:p>Robotics is not just fodder for fiction, despite the word being coined by Russian-born American sci-fi writer Isaac Asimov in his 1942 short story "Runaround." The field has become multidisciplinary, borrowing from engineering, mathematics, computer science, and more recently, neuroscience. Researchers from these fields are trying to build better robots and also to better humanity through their use. In this supplement, researchers from across China and around the world discuss the latest challenges and advancements in their field. For many functions, such as grasping, vision, and memory, researchers are turning to neurobiology for inspiration. Building humanoid or anthropomorphic robots remains the ultimate goal, but since the robots’ memory and learning algorithms are patterned after the human brain, there is still much to learn about neurobiology before that goal is attained.</jats:p> <jats:p> This special supplement brought to you by the <jats:bold>Science</jats:bold> /AAAS Custom Publishing Office. </jats:p>

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