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Science
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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
1880-
Cobertura temática
Tabla de contenidos
Binding of ISRIB reveals a regulatory site in the nucleotide exchange factor eIF2B
Alisa F. Zyryanova
; Félix Weis
; Alexandre Faille; Akeel Abo Alard
; Ana Crespillo-Casado
; Yusuke Sekine; Heather P. Harding
; Felicity Allen
; Leopold Parts; Christophe Fromont
; Peter M. Fischer
; Alan J. Warren
; David Ron
<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 Andrade
; Rong En Tay
; Deng Pan
; Adrienne M. Luoma; Yoshinaga Ito
; Soumya Badrinath; Daphne Tsoucas; Bettina Franz; Kenneth F. May
; Christopher J. Harvey; Sebastian Kobold
; Jason W. Pyrdol
; Charles Yoon; Guo-Cheng Yuan; F. Stephen Hodi
; Glenn Dranoff
; Kai W. Wucherpfennig
<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. Petrie
; Nathan D. Palmer
; Daniel T. Johnson; Sarah J. Medina; Stephanie J. Yan
; Victor Li
; Alita R. Burmeister
; Justin R. Meyer
<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