Catálogo de publicaciones - revistas

<jats:p>Women engage in less commercial patenting and invention than do men, which may affect what is invented. Using text analysis of all U.S. biomedical patents filed from 1976 through 2010, we found that patents with all-female inventor teams are 35% more likely than all-male teams to focus on women’s health. This effect holds over decades and across research areas. We also found that female researchers are more likely to discover female-focused ideas. These findings suggest that the inventor gender gap is partially responsible for thousands of missing female-focused inventions since 1976. More generally, our findings suggest that who benefits from innovation depends on who gets to invent.</jats:p>

<jats:title>Timing cues epigenomic reprogramming</jats:title> <jats:p> Different temporal dynamics of activation of the transcription factor nuclear factor κB (NF-κB) can influence the inflammatory response of activated macrophages. Cheng <jats:italic>et al.</jats:italic> report a mechanism by which oscillatory and sustained NF-κB signaling may produce distinct transcriptional responses (see the Perspective by Nandagopal <jats:italic>et al.</jats:italic> ). Oscillatory activation of NF-κB activated poised enhancers to transcribe inflammatory genes in mouse macrophages. However, sustained activation of NF-κB produced in cells activated by other stimuli acted on the epigenome. These stimuli relieved chromatin silencing at enhancers and enabled regulation of additional genes. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , abc0269, this issue p. <jats:related-article issue="6548" page="1349" related-article-type="in-this-issue" vol="372">1349</jats:related-article> ; see also abj2040, p. <jats:related-article issue="6548" page="1263" related-article-type="in-this-issue" vol="372">1263</jats:related-article> </jats:p>

<jats:title>Tailoring stress responses</jats:title> <jats:p> When faced with environmental stress, cells respond by shutting down cellular processes such as translation and nucleocytoplasmic transport. At the same time, cells preserve cytoplasmic messenger RNAs in structures known as stress granules, and many cellular proteins are modified by the covalent addition of ubiquitin, which has long been presumed to reflect degradation of stress-damaged proteins (see the Perspective by Dormann). Maxwell <jats:italic>et al.</jats:italic> show that cells generate distinct patterns of ubiquitination in response to different stressors. Rather than reflecting the degradation of stress-damaged proteins, this ubiquitination primes cells to dismantle stress granules and reinitiate normal cellular activities once the stress is removed. Gwon <jats:italic>et al.</jats:italic> show that persistent stress granules are degraded by autophagy, whereas short-lived granules undergo a process of disassembly that is autophagy independent. The mechanism of this disassembly depends on the initiating stress. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , abc3593 and abf6548, 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.abc3593">eabc3593</jats:related-article> and 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.abf6548">eabf6548</jats:related-article> ; see also abj2400, p. <jats:related-article issue="6549" page="1393" related-article-type="in-this-issue" vol="372">1393</jats:related-article> </jats:p>

<jats:title>Adapting to the new normal</jats:title> <jats:p>Successfully responding to the impacts of climate change will be a challenge for many communities, especially cities. Considering the situation in the United States, Shi and Moser examine how stakeholders can help to build urban resilience even in the absence of federal leadership. They discuss how local and state governments, private industry, and civil society can engage to adapt to the extreme weather events and other consequences of changing climate that are expected in the future. Preparing for these looming issues requires coherent, cohesive, and collective responses across all scales and sectors of society.</jats:p> <jats:p> <jats:italic>Science</jats:italic> , abc8054, 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.abc8054">eabc8054</jats:related-article> </jats:p>

<jats:title>Tailoring stress responses</jats:title> <jats:p> When faced with environmental stress, cells respond by shutting down cellular processes such as translation and nucleocytoplasmic transport. At the same time, cells preserve cytoplasmic messenger RNAs in structures known as stress granules, and many cellular proteins are modified by the covalent addition of ubiquitin, which has long been presumed to reflect degradation of stress-damaged proteins (see the Perspective by Dormann). Maxwell <jats:italic>et al.</jats:italic> show that cells generate distinct patterns of ubiquitination in response to different stressors. Rather than reflecting the degradation of stress-damaged proteins, this ubiquitination primes cells to dismantle stress granules and reinitiate normal cellular activities once the stress is removed. Gwon <jats:italic>et al.</jats:italic> show that persistent stress granules are degraded by autophagy, whereas short-lived granules undergo a process of disassembly that is autophagy independent. The mechanism of this disassembly depends on the initiating stress. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , abc3593 and abf6548, 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.abc3593">eabc3593</jats:related-article> and 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.abf6548">eabf6548</jats:related-article> ; see also abj2400, p. <jats:related-article issue="6549" page="1393" related-article-type="in-this-issue" vol="372">1393</jats:related-article> </jats:p>

<jats:title>Cell death limits pathogens</jats:title> <jats:p> During infection, <jats:italic>Yersinia</jats:italic> inhibition of the protein kinase TAK1 triggers cleavage of the pore-forming protein gasdermin D (GSDMD), which leads to a kind of inflammatory cell death called pyroptosis. In a genome-wide screen, Zheng <jats:italic>et al.</jats:italic> identified a lysosome-tethered regulatory supercomplex as being a critical driver of <jats:italic>Yersinia</jats:italic> -induced pyroptosis. The activity of the GTPase Rag and lysosomal tethering of Rag-Ragulator were required to recruit and activate the kinase RIPK1 and protease caspase-8 to cleave GSDMD, which causes cell death and limits infection. By contrast, Rag-Ragulator was not required for inflammasome-mediated pyroptosis. Thus, metabolic signaling on lysosomes can regulate cell death during pathogenic bacterial infection. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , abg0269, 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.abg0269">eabg0269</jats:related-article> </jats:p>

<jats:title>MeCP2 binds hydroxymethylated CA repeats</jats:title> <jats:p> Despites of decades of research on the Rett syndrome protein MeCP2, its function remains unclear. Ibrahim <jats:italic>et al.</jats:italic> show that MeCP2 is a hydroxymethylated cytosine-adenosine (CA) repeat-binding protein that modulates chromatin architecture at a distance from the transcription start site (see the Perspective by Zhou and Zoghbi). MeCP2 accumulates and spreads around modified CA repeats and competes for nucleosome occupancy. Loss of MeCP2 results in a widespread increase in nucleosome density inside lamina-associated domains and transcriptional dysregulation of genes enriched in CA repeats. These results shed light on the underlying molecular mechanism of Rett syndrome, a severe disease associated with mutations in MeCP2. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , abd5581, 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.abd5581">eabd5581</jats:related-article> ; see also abj5027, p. <jats:related-article issue="6549" page="1390" related-article-type="in-this-issue" vol="372">1390</jats:related-article> </jats:p>

<jats:p>This month marks a somber anniversary—40 years since the first reported cases in the United States of what would later become known as AIDS. There have been tremendous basic, clinical, and prevention advances in HIV science over the past four decades. Yet, despite widespread messaging that the United States is on track to “end AIDS,” the latest trends in infection tell a different story. One fundamental reality underlies the country's failure to achieve control of the HIV epidemic and could undermine efforts to end AIDS—the lack of access to health care for all Americans.</jats:p>

<jats:p>Alzheimer's disease (AD) afflicts some 6 million Americans with progressive cognitive impairment and personal anguish while imposing a huge economic burden on society. Everyone wants to find a way to help slow or even halt this disease. But there will be no quick fix. Responding to mounting pressure, the United States Food and Drug Administration (FDA) jumped the gun by granting accelerated approval this month to Biogen's pricey, questionably effective, and possibly harmful new drug aducanumab—a decision supported by not one of the 11 members of the agency's Expert Advisory Committee. Even worse, the approval may divert funding into a therapeutic dead end and away from approaches that might actually work.</jats:p>