Catálogo de publicaciones - revistas

Compartir en
redes sociales


Science

Resumen/Descripción – provisto por la editorial

No disponible.

Palabras clave – provistas por la editorial

No disponibles.

Disponibilidad
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

Binding of ISRIB reveals a regulatory site in the nucleotide exchange factor eIF2B

Alisa F. ZyryanovaORCID; Félix WeisORCID; Alexandre Faille; Akeel Abo AlardORCID; Ana Crespillo-CasadoORCID; Yusuke Sekine; Heather P. HardingORCID; Felicity AllenORCID; Leopold Parts; Christophe FromontORCID; Peter M. FischerORCID; Alan J. WarrenORCID; David RonORCID

<jats:title>ISRIB mechanism of action</jats:title> <jats:p> In rodents, a druglike small molecule named ISRIB enhances cognition and reverses cognitive deficits after traumatic brain injury. ISRIB activates a protein complex called eIF2B that is required for the synthesis of new proteins. Tsai <jats:italic>et al.</jats:italic> report the visualization of eIF2B bound to ISRIB at near-atomic resolution by cryo–electron microscopy. Biochemical studies revealed that ISRIB is a “molecular staple” that promotes assembly of the fully active form of eIF2B. Zyryanova <jats:italic>et al.</jats:italic> report similar structures together with information on the binding of ISRIB analogs and their effects on protein translation. </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.aaq0939">eaaq0939</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6383" page="1533" related-article-type="in-this-issue" vol="359" xlink:href="10.1126/science.aar5129">1533</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 1533-1536

Antibody-mediated inhibition of MICA and MICB shedding promotes NK cell–driven tumor immunity

Lucas Ferrari de AndradeORCID; Rong En TayORCID; Deng PanORCID; Adrienne M. Luoma; Yoshinaga ItoORCID; Soumya Badrinath; Daphne Tsoucas; Bettina Franz; Kenneth F. MayORCID; Christopher J. Harvey; Sebastian KoboldORCID; Jason W. PyrdolORCID; Charles Yoon; Guo-Cheng Yuan; F. Stephen HodiORCID; Glenn DranoffORCID; Kai W. WucherpfennigORCID

<jats:title>Helping NK cells find their way</jats:title> <jats:p> MICA and MICB proteins can be expressed on tumors and act as “kill me” signals to the immune system. But tumors often disguise themselves by shedding these proteins, which prevents specialized natural killer (NK) cells from recognizing and destroying the cancer. Ferrari de Andrade <jats:italic>et al.</jats:italic> engineered antibodies directed against the site responsible for the proteolytic shedding of MICA and MICB (see the Perspective by Cerwenka and Lanier). The approach effectively locked MICA and MICB onto tumors so that NK cells could spot them for elimination. The antibodies exhibited preclinical efficacy in multiple tumor models, including humanized melanoma. Furthermore, the strategy reduced lung cancer metastasis after NK cell–mediated tumor lysis. </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="6383" page="1537" related-article-type="in-this-issue" vol="359" xlink:href="10.1126/science.aao0505">1537</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6383" page="1460" related-article-type="in-this-issue" vol="359" xlink:href="10.1126/science.aat2184">1460</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 1537-1542

Destabilizing mutations encode nongenetic variation that drives evolutionary innovation

Katherine L. PetrieORCID; Nathan D. PalmerORCID; Daniel T. Johnson; Sarah J. Medina; Stephanie J. YanORCID; Victor LiORCID; Alita R. BurmeisterORCID; Justin R. MeyerORCID

<jats:title>Nongenetic variation drives viral evolution</jats:title> <jats:p> Bacteriophage λ is a virus that infects bacteria by exploiting various membrane proteins in a well-characterized manner. Petrie <jats:italic>et al.</jats:italic> show how the evolution of variable folding conformations of isogenic proteins, which do not differ in their genetic sequences, contributed to λ's ability to exploit an additional host receptor for infection. Because the protein can take on two shapes, this genotype can have two phenotypes. Natural selection may thus be able to act on this nongenetic heterogeneity to connect phenotypic heterogeneity, evolvability, and protein stability. </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="6383" page="1542" related-article-type="in-this-issue" vol="359" xlink:href="10.1126/science.aar1954">1542</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 1542-1545

Technology Feature | Live-cell imaging: Deeper, faster, wider

Amber Dance

<jats:p> The latest in live-cell microscopy—multiphoton imaging, light-sheet techniques, and technology borrowed from Raman spectroscopy—allow researchers to study living cells in more detail with less effort. <jats:list list-type="bullet"> <jats:list-item> <jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="uri" xlink:href="http://www.sciencemag.org/features/2018/03/live-cell-imaging-deeper-faster-wider">Read the Feature (Full-Text HTML)</jats:ext-link> </jats:p> </jats:list-item> <jats:list-item> <jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="uri" xlink:href="http://www.sciencemag.org/sites/default/files/30MarchMicrobioticsFeature.pdf">Read the Feature (PDF)</jats:ext-link> </jats:p> </jats:list-item> <jats:list-item> <jats:p> <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="uri" xlink:href="http://www.sciencemag.org/sites/default/files/documents/30MarchNewProducts.pdf">Read New Products (PDF)</jats:ext-link> </jats:p> </jats:list-item> </jats:list> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 1549-1549

New Products

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

Palabras clave: Multidisciplinary.

Pp. 1549-1549

Figuring out how I belong

Malin L. Nording

Palabras clave: Multidisciplinary.

Pp. 1558-1558

Our tree-climbing human ancestors could walk upright like us, study of chimps and other primates shows

Ann Gibbons

Palabras clave: Multidisciplinary.

Pp. No disponible

A four-eyed lizard walked the earth 49 million years ago

Katie Langin

Palabras clave: Multidisciplinary.

Pp. No disponible

Our growing taste for shrimp is bad news for climate change

Erik Stokstad

Palabras clave: Multidisciplinary.

Pp. No disponible

U.S. leprosy budget cut closes clinics, threatens research

Jon Cohen

Palabras clave: Multidisciplinary.

Pp. No disponible