Catálogo de publicaciones - revistas

<jats:title>Maximal efficiency from enzyme cascades</jats:title> <jats:p> Enzymes are highly selective catalysts that can be useful for specific transformations in organic synthesis. Huffman <jats:italic>et al.</jats:italic> combined designer enzymes in a multistep cascade reaction (see the Perspective by O'Reilly and Ryan). The approach eliminates purification steps, recycles expensive cofactors, and couples favorable and unfavorable reactions. With the target molecule islatravir, an experimental HIV drug, they optimized five enzymes by directed evolution to be compatible with unnatural substrates and stable in the reaction conditions. Stereochemical purity was amplified at every enzymatic step, and the final synthesis was both atom economical and efficient. </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="6470" page="1255" related-article-type="in-this-issue" vol="366" xlink:href="10.1126/science.aay8484">1255</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6470" page="1199" related-article-type="in-this-issue" vol="366" xlink:href="10.1126/science.aaz7376">1199</jats:related-article> </jats:p>

<jats:title>Regulating synaptic signals</jats:title> <jats:p>In the brain, AMPA-type glutamate receptors (AMPARs) are ion channels that play key roles in synaptic plasticity, cognition, learning, and memory. Two classes of subunits, the claudin family and the cornichon family, regulate AMPAR gating and trafficking. Previous structures have been presented of AMPAR bound to claudin homologs. Now, Nakagawa reports a high-resolution structure of AMPAR bound to the cornichon homolog CNIH3, determined by cryo–electron microscopy (see the Perspective by Schwenk and Fakler). In contrast to a predicted topology of three transmembrane helices and an intracellular amino terminus, CNIH3 has four transmembrane helices, and both the amino and carboxyl termini are extracellular. The structure reveals the architecture of the interaction interface between AMPAR and CNIH3 and suggests a role for lipids in regulating the assembly and function of the AMPAR-CNIH3 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="6470" page="1259" related-article-type="in-this-issue" vol="366" xlink:href="10.1126/science.aay2783">1259</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6470" page="1194" related-article-type="in-this-issue" vol="366" xlink:href="10.1126/science.aaz8642">1194</jats:related-article> </jats:p>

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