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

Editors' Choice

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1297-1298

Leadership from behind

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1297.1-1297

Naked droplets for culturing cells

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1297.2-1298

Turtles and tortoises in decline

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1297.3-1298

A core-shell silver cluster

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1297.4-1298

Careers in STEM start early

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1297.5-1298

Lysosome repositioning

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1297.6-1298

Reproducible instability

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1297.7-1298

Structures of human Na v 1.7 channel in complex with auxiliary subunits and animal toxins

Huaizong ShenORCID; Dongliang LiuORCID; Kun WuORCID; Jianlin LeiORCID; Nieng YanORCID

<jats:title>Targeting sodium channels</jats:title> <jats:p> Voltage-gated sodium (Na <jats:sub>v</jats:sub> ) channels have been implicated in cardiac and neurological disorders. There are many subtypes of these channels, making it challenging to develop specific therapeutics. A core α subunit is sufficient for voltage sensing and ion conductance, but function is modulated by β subunits and by natural toxins that can either act as pore blockers or gating modifiers (see the Perspective by Chowdhury and Chanda). Shen <jats:italic>et al.</jats:italic> present the structures of Na <jats:sub>v</jats:sub> 1.7 in complex with both β1 and β2 subunits and with animal toxins. Pan <jats:italic>et al.</jats:italic> present the structure of Na <jats:sub>v</jats:sub> 1.2 bound to β2 and a toxic peptide, the µ-conotoxin KIIIA. The structure shows why KIIIA is specific for Na <jats:sub>v</jats:sub> 1.2. These and other recently determined Na <jats:sub>v</jats:sub> structures provide a framework for targeted drug development. </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="6433" page="1303" related-article-type="in-this-issue" vol="363" xlink:href="10.1126/science.aaw2493">1303</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6433" page="1309" related-article-type="in-this-issue" vol="363" xlink:href="10.1126/science.aaw2999">1309</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6433" page="1278" related-article-type="in-this-issue" vol="363" xlink:href="10.1126/science.aaw8645">1278</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 1303-1308

Molecular basis for pore blockade of human Na + channel Na v 1.2 by the μ-conotoxin KIIIA

Xiaojing PanORCID; Zhangqiang LiORCID; Xiaoshuang HuangORCID; Gaoxingyu Huang; Shuai GaoORCID; Huaizong ShenORCID; Lei LiuORCID; Jianlin LeiORCID; Nieng YanORCID

<jats:title>Targeting sodium channels</jats:title> <jats:p> Voltage-gated sodium (Na <jats:sub>v</jats:sub> ) channels have been implicated in cardiac and neurological disorders. There are many subtypes of these channels, making it challenging to develop specific therapeutics. A core α subunit is sufficient for voltage sensing and ion conductance, but function is modulated by β subunits and by natural toxins that can either act as pore blockers or gating modifiers (see the Perspective by Chowdhury and Chanda). Shen <jats:italic>et al.</jats:italic> present the structures of Na <jats:sub>v</jats:sub> 1.7 in complex with both β1 and β2 subunits and with animal toxins. Pan <jats:italic>et al.</jats:italic> present the structure of Na <jats:sub>v</jats:sub> 1.2 bound to β2 and a toxic peptide, the µ-conotoxin KIIIA. The structure shows why KIIIA is specific for Na <jats:sub>v</jats:sub> 1.2. These and other recently determined Na <jats:sub>v</jats:sub> structures provide a framework for targeted drug development. </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="6433" page="1303" related-article-type="in-this-issue" vol="363" xlink:href="10.1126/science.aaw2493">1303</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6433" page="1309" related-article-type="in-this-issue" vol="363" xlink:href="10.1126/science.aaw2999">1309</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6433" page="1278" related-article-type="in-this-issue" vol="363" xlink:href="10.1126/science.aaw8645">1278</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 1309-1313