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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
And Science’s Breakthrough of the Year is …
Science Staff
Palabras clave: Multidisciplinary.
Pp. No disponible
NAS panel tackles—and is tackled by—genome editing in animals
Elizabeth Pennisi
Palabras clave: Multidisciplinary.
Pp. No disponible
Volcanoes sound like jet planes—and that could help calculate how hard they blow
Kerry Klein
Palabras clave: Multidisciplinary.
Pp. No disponible
Top stories: Saturn’s helium ‘rain,’ autism and antidepressants, and U.S. science’s budget boost
Catherine Matacic
Palabras clave: Multidisciplinary.
Pp. No disponible
Structure of the voltage-gated calcium channel Ca v 1.1 complex
Jianping Wu; Zhen Yan; Zhangqiang Li; Chuangye Yan; Shan Lu; Mengqiu Dong; Nieng Yan
<jats:title>A complex channel comes into focus</jats:title> <jats:p> Voltage-gated calcium (Cav) channels are activated in response to membrane potential to initiate calcium-mediated signaling pathways and are associated with diseases such as cardiac arrhythmia and epilepsy. Cav1.1 couples changes in membrane potential to cardiac muscle contraction. It comprises a core subunit and three auxiliary subunits. Wu <jats:italic>et al.</jats:italic> isolated the Cav1.1 complex from rabbit skeletal muscle and determined its structure by single-particle electron cryomicroscopy using direct electron detection and advanced image processing. The detailed architecture of the pseudotetrameric eukaryotic Cav channel in complex with its auxiliary subunits provides an important framework for understanding the function and disease mechanisms of related channels. </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.aad2395">10.1126/science.aad2395</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. No disponible
Structural basis of Nav1.7 inhibition by an isoform-selective small-molecule antagonist
Shivani Ahuja; Susmith Mukund; Lunbin Deng; Kuldip Khakh; Elaine Chang; Hoangdung Ho; Stephanie Shriver; Clint Young; Sophia Lin; J. P. Johnson; Ping Wu; Jun Li; Mary Coons; Christine Tam; Bobby Brillantes; Honorio Sampang; Kyle Mortara; Krista K. Bowman; Kevin R. Clark; Alberto Estevez; Zhiwei Xie; Henry Verschoof; Michael Grimwood; Christoph Dehnhardt; Jean-Christophe Andrez; Thilo Focken; Daniel P. Sutherlin; Brian S. Safina; Melissa A. Starovasnik; Daniel F. Ortwine; Yvonne Franke; Charles J. Cohen; David H. Hackos; Christopher M. Koth; Jian Payandeh
<jats:title>A channel involved in pain perception</jats:title> <jats:p> Voltage-gated sodium (Nav) channels propagate electrical signals in muscle cells and neurons. In humans, Nav1.7 plays a key role in pain perception. It is challenging to target a particular Nav isoform; however, arylsulfonamide antagonists selective for Nav1.7 have been reported recently. Ahuja <jats:italic>et al.</jats:italic> characterized the binding of these small molecules to human Nav channels. To further investigate the mechanism, they engineered a bacterial Nav channel to contain features of the Nav1.7 voltage-sensing domain that is targeted by the antagonist and determined the crystal structure of the chimera bound to an inhibitor. The structure gives insight into the mechanism of voltage sensing and will enable the design of more-selective Nav channel antagonists. </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.aac5464">10.1126/science.aac5464</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. No disponible
Opportunities and challenges in liquid cell electron microscopy
Frances M. Ross
<jats:title>Advances in seeing small things</jats:title> <jats:p>Electron microscopes, particularly those with aberration correction, can view materials at the subnanometer scale. Additional improvements make it possible to obtain images at lower electron doses, thus minimizing the damage to the sample. However, for a number of materials, particularly those of biological origin, samples need to be imaged in solution. Ross reviews recent advances that have made it possible to do liquid cell electron microscopy, which opens up the possibility of studying problems such as the changes inside a battery during operation, the growth of crystals from solution, or biological molecules in their native state.</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.aaa9886">10.1126/science.aaa9886</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. No disponible
ESCRTs work in two very different ways
S. M. Hurtley
Palabras clave: Multidisciplinary.
Pp. i-1488
Breakthrough to genome editing
Marcia McNutt
<jats:p> A, T, G, C: the alphabet code for the nucleotides that are the building blocks of life. Minor, but consequential, changes in this DNA coding can change gene function. Researchers have long sought better ways to edit the genetic code in cultured cells and laboratory organisms to silence, activate, or change targeted genes to gain a better understanding of their roles. This, in turn, could open the door to beneficial applications, from ecological to agricultural to biomedical. Over the years, several editing methods have been developed, but they have suffered from a lack of specificity, difficulty in assembling the molecular constituents, or concerns about off-target effects. Recently, accomplishments in genome editing across biological disciplines have been so remarkable that the method known as clustered regularly interspaced short palindromic repeats—or CRISPR—is <jats:italic>Science</jats:italic> 's 2015 Breakthrough of the Year (see p. 1456). </jats:p>
Palabras clave: Multidisciplinary.
Pp. 1445-1445
News at a glance
<jats:p>A roundup of weekly science policy and related news.</jats:p>
Palabras clave: Multidisciplinary.
Pp. 1446-1448