Catálogo de publicaciones - revistas

<jats:title>Thrifty thermoelectric cooling</jats:title> <jats:p> Currently available thermoelectric devices for cooling rely on expensive bismuth telluride. Mao <jats:italic>et al.</jats:italic> systematically developed a far less expensive n-type magnesium-bismuth–based material with good thermoelectric properties. They built a device that could generate a temperature difference of up to 90 kelvin when coupled with a commercially available p-type material. Such materials should provide an excellent basis for cost-effective thermoelectric cooling technology. </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="6452" page="495" related-article-type="in-this-issue" vol="365" xlink:href="10.1126/science.aax7792">495</jats:related-article> </jats:p>

<jats:title>Spontaneous degradation in hormone synthesis</jats:title> <jats:p> The phytohormone salicylic acid (SA) helps plants respond to biological and physical stresses. Rekhter <jats:italic>et al.</jats:italic> identified the biosynthetic pathway that produces SA in response to pathogens. A precursor, isochorismic acid, is formed in the chloroplast and then exported to the cytosol. There, enzymatically produced isochorismate-9-glutamate spontaneously decomposes to release SA plus a by-product. The results clarify key steps in the mechanisms involved in synthesizing this important regulator of plant immunity. </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="6452" page="498" related-article-type="in-this-issue" vol="365" xlink:href="10.1126/science.aaw1720">498</jats:related-article> </jats:p>

<jats:title>Protein unfolding, one substrate at a time</jats:title> <jats:p> Ubiquitin marks proteins for degradation by the proteasome. However, many substrates cannot be directly degraded because they are well folded or are located in cell membranes or in multimeric complexes. These proteins are first unfolded by the Cdc48 adenosine triphosphatase (ATPase), which forms a hexameric assembly that pulls polypeptides through its central pore. Twomey <jats:italic>et al.</jats:italic> determined structures of Cdc48 at an initiation stage of substrate processing. Surprisingly, a ubiquitin molecule in the substrate-linked polyubiquitin chain could be unfolded simply by binding to the Cdc48 complex. A segment of the unfolded ubiquitin inserts into the ATPase ring and initiates substrate unfolding. This explains why Cdc48 can deal with a broad range of substrates—even ones that are folded. Cooney <jats:italic>et al.</jats:italic> report the cryo–electron microscopy structure of Cdc48 in complex with an authentic substrate. In contrast to previously reported Cdc48 structures, an asymmetric spiraling assembly wraps around the extended substrate polypeptide. Thus, Cdc48 uses a hand-over-hand mechanism of translocation, which supports a common mechanism for protein substrate unfolding for AAA+ ATPases. </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" related-article-type="in-this-issue" xlink:href="10.1126/science.aax1033">eaax1033</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6452" page="502" related-article-type="in-this-issue" vol="365" xlink:href="10.1126/science.aax0486">502</jats:related-article> </jats:p>

<jats:title>Building a better RSV vaccine</jats:title> <jats:p> Respiratory syncytial virus (RSV) causes severe respiratory disease, especially in infants and the elderly. However, attempts to produce effective human vaccines have largely been unsuccessful. Structure-based design has been used to generate an RSV fusion glycoprotein stabilized in its prefusion conformation (DS-Cav1). This immunogen is highly effective in mice and macaques. Crank <jats:italic>et al.</jats:italic> now report the results of a phase I vaccine clinical trial using the stabilized prefusion DS-Cav1 molecule. Four weeks after immunization, these vaccines elicited substantially more high-quality antibody titers than those typically generated using earlier RSV immunogens. The findings provide a proof of concept for how structural biology can contribute to precision vaccine design. </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="6452" page="505" related-article-type="in-this-issue" vol="365" xlink:href="10.1126/science.aav9033">505</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>