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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

Mobile elements' joyride

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 494.7-495

Editors' Choice

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 494-495

Temperate forest dynamics and climate

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 494.1-495

Potent peptidic fusion inhibitors of influenza virus

Rameshwar U. KadamORCID; Jarek JuraszekORCID; Boerries BrandenburgORCID; Christophe BuyckORCID; Wim B. G. SchepensORCID; Bart KesteleynORCID; Bart StoopsORCID; Rob J. VreekenORCID; Jan VermondORCID; Wouter GoutierORCID; Chan TangORCID; Ronald Vogels; Robert H. E. Friesen; Jaap Goudsmit; Maria J. P. van DongenORCID; Ian A. WilsonORCID

<jats:title>Broadly reactive drugs for flu</jats:title> <jats:p> Drugs for influenza are limited. For those available, viral resistance is rife. Part of the problem is that the virus is constantly mutating. Kadam <jats:italic>et al.</jats:italic> tested the cell entry stage of the virus life cycle as a drug target (see the Perspective by Whitehead). Cell entry is mediated by the major surface glycoprotein hemagglutinin (HA). This stage can be blocked by broadly neutralizing antibodies binding to HA. The authors generated small cyclic peptides that bind to the same sites on HA as the antibodies and mimic their activity. The peptides are cheap and easy to synthesize, are nontoxic to mice, and prevented infection of cells by many types of influenza virus. </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="6362" page="496" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aan0516">496</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6362" page="450" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aap9608">450</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 496-502

Toughening elastomers using mussel-inspired iron-catechol complexes

Emmanouela FilippidiORCID; Thomas R. CristianiORCID; Claus D. EisenbachORCID; J. Herbert WaiteORCID; Jacob N. IsraelachviliORCID; B. Kollbe AhnORCID; Megan T. ValentineORCID

<jats:title>Combining stiffness and stretchiness</jats:title> <jats:p> There is usually a trade-off between making a material stretchy, so that it can absorb energy on deformation, and making a material stiff, so that it does not extend very much when stretched. Mussels have long been an inspiration for developing adhesives that work when wet. Filippidi <jats:italic>et al.</jats:italic> produced an extensible polymeric material containing catechol groups whose mechanical properties were augmented when dry through the addition of iron ions (see the Perspective by Winey). The iron ions lead to sacrificial metal coordination bonds, creating a reversible load-bearing network that does not trade extensibility for stiffness. </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="6362" page="502" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aao0350">502</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6362" page="449" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aap8114">449</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 502-505

Atomic structure of sensitive battery materials and interfaces revealed by cryo–electron microscopy

Yuzhang LiORCID; Yanbin LiORCID; Allen PeiORCID; Kai Yan; Yongming SunORCID; Chun-Lan WuORCID; Lydia-Marie JoubertORCID; Richard Chin; Ai Leen KohORCID; Yi Yu; John PerrinoORCID; Benjamin ButzORCID; Steven ChuORCID; Yi CuiORCID

<jats:title>Frozen in time</jats:title> <jats:p> The electrochemical processes occurring in a battery are highly dynamic. To understand the complexities of the charge and discharge cycles, you need to be able to watch the processes in situ or to freeze the battery rapidly for ex situ analysis. Li <jats:italic>et al.</jats:italic> applied cryo–electron microscopy techniques commonly used for studying biological samples to examine batteries. They identified the solid electrolyte interphase that forms, observed the interactions of Li with the interphase, and captured the formation of dendrites that can be detrimental to the lifetime of a battery. </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="6362" page="506" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aam6014">506</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 506-510

Size effect in ion transport through angstrom-scale slits

A. EsfandiarORCID; B. RadhaORCID; F. C. WangORCID; Q. YangORCID; S. HuORCID; S. GarajORCID; R. R. NairORCID; A. K. GeimORCID; K. GopinadhanORCID

<jats:title>Squeezing through a hole</jats:title> <jats:p> Transport of an ion is usually directly related to its hydrated radius and assumed to be nonflexible. Either a hydrated ion fits through an aperture or it does not, and shape should play a dominant role rather than charge. Esfandiar <jats:italic>et al.</jats:italic> created nanofluidic devices by stacking structured bulk materials, including graphite, boron nitride, and molybdenum disulfide. They investigated the transport of ions in aqueous solutions through the nanochannels in the devices. Unexpectedly, they observed different behavior for ions of similar hydrated size but opposite charge. </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="6362" page="511" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aan5275">511</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 511-513

Tunable porous nanoallotropes prepared by post-assembly etching of binary nanoparticle superlattices

Thumu UdayabhaskararaoORCID; Thomas AltantzisORCID; Lothar HoubenORCID; Marc Coronado-PuchauORCID; Judith LangerORCID; Ronit Popovitz-Biro; Luis M. Liz-MarzánORCID; Lela VukovićORCID; Petr Král; Sara BalsORCID; Rafal KlajnORCID

<jats:title>Non–close-packed nanoparticle arrays</jats:title> <jats:p> Films of colloidal nanoparticles usually form dense, close-packed lattices. If binary lattices could be made and one component removed, then a more open array could form, as long as the remaining nanoparticles could be stabilized. Udayabhaskararao <jats:italic>et al.</jats:italic> formed binary superlattices of gold and magnetite nanoparticles at an air-liquid interface that could then be transferred to carbon-coated surfaces (see the Perspective by Kotov). Selective etching of either of the nanoparticles created non–close-packed arrays with vacancies stabilized by the carbon surface. </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="6362" page="514" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aan6046">514</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6362" page="448" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aap8994">448</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 514-518

Plasmepsins IX and X are essential and druggable mediators of malaria parasite egress and invasion

Armiyaw S. NasamuORCID; Svetlana GlushakovaORCID; Ilaria RussoORCID; Barbara Vaupel; Anna Oksman; Arthur S. KimORCID; Daved H. Fremont; Niraj Tolia; Josh R. Beck; Marvin J. MeyersORCID; Jacquin C. NilesORCID; Joshua ZimmerbergORCID; Daniel E. GoldbergORCID

<jats:title> <jats:italic>Plasmodium</jats:italic> parasite entrance and exit </jats:title> <jats:p> Sweats and fever are the hallmarks of malaria. Red blood cells are the replication factories for malaria parasites. Fever occurs when the parasites' merozoite stages burst en masse from red blood cells into the circulation. Nasamu <jats:italic>et al.</jats:italic> and Pino <jats:italic>et al.</jats:italic> discovered that two parasite proteases, plasmepsin IX and X, are essential for mass cell exit (see the Perspective by Boddey). Plasmepsin X is also used by the merozoites to enter a fresh red blood cell to continue the replicative cycle. These two plasmepsins act by regulating the maturation of enzymes required to disrupt host cell membranes. Because these functions are essential for the parasite, the authors used protease inhibitors to show that plasmepsins provide potential drug targets. </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="6362" page="518" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aan1478">518</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6362" page="522" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aaf8675">522</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6362" page="445" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aaq0002">445</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 518-522

A multistage antimalarial targets the plasmepsins IX and X essential for invasion and egress

Paco PinoORCID; Reto Caldelari; Budhaditya MukherjeeORCID; Juha Vahokoski; Natacha Klages; Bohumil MacoORCID; Christine R. CollinsORCID; Michael J. BlackmanORCID; Inari Kursula; Volker HeusslerORCID; Mathieu BrochetORCID; Dominique Soldati-FavreORCID

<jats:title> <jats:italic>Plasmodium</jats:italic> parasite entrance and exit </jats:title> <jats:p> Sweats and fever are the hallmarks of malaria. Red blood cells are the replication factories for malaria parasites. Fever occurs when the parasites' merozoite stages burst en masse from red blood cells into the circulation. Nasamu <jats:italic>et al.</jats:italic> and Pino <jats:italic>et al.</jats:italic> discovered that two parasite proteases, plasmepsin IX and X, are essential for mass cell exit (see the Perspective by Boddey). Plasmepsin X is also used by the merozoites to enter a fresh red blood cell to continue the replicative cycle. These two plasmepsins act by regulating the maturation of enzymes required to disrupt host cell membranes. Because these functions are essential for the parasite, the authors used protease inhibitors to show that plasmepsins provide potential drug targets. </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="6362" page="518" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aan1478">518</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6362" page="522" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aaf8675">522</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6362" page="445" related-article-type="in-this-issue" vol="358" xlink:href="10.1126/science.aaq0002">445</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 522-528