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Institución detectada Período Navegá Descargá Solicitá
No detectada desde mar. 1997 / hasta dic. 2023 Science Journals

Información

Tipo de recurso:

revistas

ISSN impreso

0036-8075

ISSN electrónico

1095-9203

Editor responsable

American Association for the Advancement of Science (AAAS)

País de edición

Estados Unidos

Fecha de publicación

Cobertura temática

Tabla de contenidos

Determining structural and chemical heterogeneities of surface species at the single-bond limit

Jiayu XuORCID; Xiang ZhuORCID; Shijing TanORCID; Yao ZhangORCID; Bin Li; Yunzhe TianORCID; Huan ShanORCID; Xuefeng CuiORCID; Aidi Zhao; Zhenchao DongORCID; Jinlong YangORCID; Yi LuoORCID; Bing WangORCID; J. G. HouORCID

<jats:title>Joint strategy for surface chemistry</jats:title> <jats:p> Recent advances in the development of tip-based microscopy have led to angstrom-scale spatial resolution, but no technique provides univocal characterization of the structural and chemical heterogeneities of surface species. Using a model system of pentacene derivatives on the Ag(110) surface, Xu <jats:italic>et al.</jats:italic> show that the combination of scanning tunneling microscopy, atomic force microscopy, and tip-enhanced Raman scattering provides the electronic, structural, and chemical information sufficiently correlated for an unambiguous characterization of the different—but structurally similar—chemical species and their interaction with the metal surface with single-bond resolution. The proposed multitechnique approach could find wide application in fundamental studies of heterogeneous catalysis and surface chemistry in general. </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="6531" page="818" related-article-type="in-this-issue" vol="371" xlink:href="10.1126/science.abd1827">818</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 818-822

Broad and potent activity against SARS-like viruses by an engineered human monoclonal antibody

C. Garrett RappazzoORCID; Longping V. TseORCID; Chengzi I. KakuORCID; Daniel WrappORCID; Mrunal Sakharkar; Deli HuangORCID; Laura M. DeveauORCID; Thomas J. YockachonisORCID; Andrew S. HerbertORCID; Michael B. BattlesORCID; Cecilia M. O’BrienORCID; Michael E. BrownORCID; James C. Geoghegan; Jonathan Belk; Linghang Peng; Linlin YangORCID; Yixuan HouORCID; Trevor D. Scobey; Dennis R. BurtonORCID; David NemazeeORCID; John M. DyeORCID; James E. VossORCID; Bronwyn M. GunnORCID; Jason S. McLellanORCID; Ralph S. BaricORCID; Lisa E. GralinskiORCID; Laura M. WalkerORCID

<jats:title>Targeting sarbecoviruses</jats:title> <jats:p> As we continue to battle the COVID-19 pandemic, we must confront the possibility of new pathogenic coronaviruses emerging in humans in the future. With this in mind, Rappazzo <jats:italic>et al.</jats:italic> isolated antibodies from a survivor of the 2003 severe acute respiratory syndrome coronavirus (SARS-CoV), used yeast display libraries to introduce diversity into these antibodies, and then screened for binding to SARS-CoV-2. One of the affinity-matured progeny strongly neutralized SARS-CoV-2, SARS-CoV, and two SARS-related viruses from bats. In addition, this antibody bound to the receptor-binding domains from a panel of sarbecoviruses, suggesting broader activity, and provided protection against SARS-CoV and SARS-CoV-2 in mouse models. </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="6531" page="823" related-article-type="in-this-issue" vol="371" xlink:href="10.1126/science.abf4830">823</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 823-829

High-entropy-stabilized chalcogenides with high thermoelectric performance

Binbin JiangORCID; Yong YuORCID; Juan CuiORCID; Xixi Liu; Lin Xie; Jincheng Liao; Qihao Zhang; Yi Huang; Shoucong Ning; Baohai Jia; Bin ZhuORCID; Shengqiang BaiORCID; Lidong ChenORCID; Stephen J. PennycookORCID; Jiaqing HeORCID

<jats:title>Distorted thermal properties</jats:title> <jats:p> Thermoelectric devices can convert waste heat into electricity, providing one path for improving energy efficiency. Jiang <jats:italic>et al.</jats:italic> leveraged entropy engineering to synthesize a single-phase high-entropy alloy with attractive thermoelectric properties. By increasing the number of elements in the alloy, the resulting disorder helps to stabilize against breakdown into multiple phases. The disordered and distorted crystal lattice suppresses thermal transport while maintaining the electrical properties, which boosts the heat-conversion efficiency of the material. </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="6531" page="830" related-article-type="in-this-issue" vol="371" xlink:href="10.1126/science.abe1292">830</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 830-834

Human impacts on global freshwater fish biodiversity

Guohuan SuORCID; Maxime LogezORCID; Jun Xu; Shengli TaoORCID; Sébastien VillégerORCID; Sébastien BrosseORCID

<jats:p>Freshwater fish represent one-fourth of the world’s vertebrates and provide irreplaceable goods and services but are increasingly affected by human activities. A new index, Cumulative Change in Biodiversity Facets, revealed marked changes in biodiversity in &gt;50% of the world’s rivers covering &gt;40% of the world’s continental surface and &gt;37% of the world’s river length, whereas &lt;14% of the world’s surface and river length remain least impacted. Present-day rivers are more similar to each other and have more fish species with more diverse morphologies and longer evolutionary legacies. In temperate rivers, where the impact has been greatest, biodiversity changes were primarily due to river fragmentation and introduction of non-native species.</jats:p>

Palabras clave: Multidisciplinary.

Pp. 835-838

Cholangiocyte organoids can repair bile ducts after transplantation in the human liver

Fotios SampaziotisORCID; Daniele MuraroORCID; Olivia C. TysoeORCID; Stephen SawiakORCID; Timothy E. Beach; Edmund M. Godfrey; Sara S. Upponi; Teresa BreviniORCID; Brandon T. WesleyORCID; Jose Garcia-BernardoORCID; Krishnaa MahbubaniORCID; Giovanni CanuORCID; Richard Gieseck; Natalie L. BerntsenORCID; Victoria L. MulcahyORCID; Keziah Crick; Corrina Fear; Sharayne RobinsonORCID; Lisa SwiftORCID; Laure GambardellaORCID; Johannes BargehrORCID; Daniel Ortmann; Stephanie E. Brown; Anna OsnatoORCID; Michael P. MurphyORCID; Gareth Corbett; William T. H. Gelson; George F. Mells; Peter Humphreys; Susan E. Davies; Irum Amin; Paul GibbsORCID; Sanjay SinhaORCID; Sarah A. TeichmannORCID; Andrew J. Butler; Teik Choon See; Espen MelumORCID; Christopher J. E. Watson; Kourosh Saeb-ParsyORCID; Ludovic VallierORCID

<jats:title>Organoids regenerate human bile ducts</jats:title> <jats:p> Bile ducts carry bile from the liver and gall bladder to the small intestine, where it aids digestion. Cholangiocytes are epithelial cells that line bile ducts and modify bile as its transported through the biliary tree. Chronic liver diseases involving cholangiocytes account for a large fraction of liver failure and the need for liver transplantation. Because liver donors are in short supply, Sampaziotis <jats:italic>et al.</jats:italic> used organoid technology to develop a cell-based therapy using human tissue (see the Perspective by Kurial and Willenbring). Cholangiocyte organoids were transplanted into the intrahepatic ducts of deceased human donor livers undergoing ex vivo normothermic perfusion. The livers could be maintained for up to 100 hours, and the transplanted organoids engrafted, exhibited function, and could repair bile ducts. </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="6531" page="839" related-article-type="in-this-issue" vol="371" xlink:href="10.1126/science.aaz6964">839</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6531" page="786" related-article-type="in-this-issue" vol="371" xlink:href="10.1126/science.abg3179">786</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 839-846

Mechanism of membrane-tethered mitochondrial protein synthesis

Yuzuru ItohORCID; Juni AndréllORCID; Austin ChoiORCID; Uwe RichterORCID; Priyanka MaitiORCID; Robert B. BestORCID; Antoni BarrientosORCID; Brendan J. BattersbyORCID; Alexey AmuntsORCID

<jats:title>Making the energy makers</jats:title> <jats:p> Within a mitochondrion, the powerhouse of eukaryotic cells, synthesis of the specialized transmembrane proteins of the electron transport chain is performed by dedicated mitoribosomes. The mechanism by which mitoribosomes couple protein synthesis with membrane insertion is poorly understood. Itoh <jats:italic>et al.</jats:italic> determined structures of the human mitoribosome during nascent chain synthesis while bound to its membrane insertase. These structures revealed a series of coordinated conformational changes within the polypeptide exit tunnel. The gating mechanism offers a fundamental molecular insight into how membrane proteins are synthesized in human mitochondria. </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="6531" page="846" related-article-type="in-this-issue" vol="371" xlink:href="10.1126/science.abe0763">846</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 846-849

Prospective mapping of viral mutations that escape antibodies used to treat COVID-19

Tyler N. StarrORCID; Allison J. GreaneyORCID; Amin AddetiaORCID; William W. HannonORCID; Manish C. ChoudharyORCID; Adam S. Dingens; Jonathan Z. LiORCID; Jesse D. BloomORCID

<jats:title>Mapping antibody escape in SARS-CoV-2</jats:title> <jats:p> Several antibodies are in use or under development as therapies to treat COVID-19. As new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants emerge, it is important to predict whether they will remain susceptible to antibody treatment. Starr <jats:italic>et al.</jats:italic> used a yeast library that covers all mutations to the SARS-CoV-2 receptor-binding domain that do not strongly disrupt binding to the host receptor (ACE2) and mapped how these mutations affect binding to three leading anti–SARS-CoV-2 antibodies. The maps identify mutations that escape antibody binding, including a single mutation that escapes both antibodies in the Regeneron antibody cocktail. Many of the mutations that escape single antibodies are circulating in the human population. </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="6531" page="850" related-article-type="in-this-issue" vol="371" xlink:href="10.1126/science.abf9302">850</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 850-854

Mentor as you'd want to be mentored

Eric Wengert

Palabras clave: Multidisciplinary.

Pp. 858-858

Brain cell clusters, grown in lab for more than a year, mirror changes in a newborn’s brain

Kelly Servick

Palabras clave: Multidisciplinary.

Pp. No disponible

U.S. National Science Foundation could get $600 million in pandemic relief bill

Jeffrey Mervis

Palabras clave: Multidisciplinary.

Pp. No disponible