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

Microtubule sliding during Drosophila development

V. Vinson

Palabras clave: Multidisciplinary.

Pp. 883-883

Editors' Choice

Valda Vinson; Andrew M. Sugden; Phil Szuromi; Brent Grocholski; Guy Riddihough; Ian S. Osborne

Palabras clave: Multidisciplinary.

Pp. 883-884

Making vibration sensors noble

B. Grocholski

Palabras clave: Multidisciplinary.

Pp. 883-884

An integrated route to frequency combs

I. S. Osborne

Palabras clave: Multidisciplinary.

Pp. 883-884

Climate change and megafaunal extinction

A. M. Sugden

Palabras clave: Multidisciplinary.

Pp. 883-884

A framework for drug delivery

P. Szuromi

Palabras clave: Multidisciplinary.

Pp. 883-884

Slow-motion state of mind

G. Riddihough

Palabras clave: Multidisciplinary.

Pp. 883-884

Targeting health subsidies through a nonprice mechanism: A randomized controlled trial in Kenya

Pascaline Dupas; Vivian Hoffmann; Michael Kremer; Alix Peterson Zwane

<jats:title>Delivering chlorine to those who use it</jats:title> <jats:p> In developed countries, a consumer's valuation of a health product can be measured by his or her willingness to pay for it. But poorer individuals, especially those in developing countries, might want and need a product yet be unable to pay for it with money. Dupas <jats:italic>et al.</jats:italic> demonstrate that a nonprice voucher mechanism can be used to deliver chlorine for water treatment to people in Kenya who are too poor to pay for it, but who use it when they get it (see the Perspective by Olken). Having to redeem the vouchers screens out people who would accept the free chlorine solution but not use it. </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="6302" page="889" related-article-type="in-this-issue" vol="353" xlink:href="10.1126/science.aaf6288">889</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6302" page="864" related-article-type="in-this-issue" vol="353" xlink:href="10.1126/science.aah5055">864</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 889-895

Structure of a yeast catalytic step I spliceosome at 3.4 Å resolution

Ruixue Wan; Chuangye Yan; Rui Bai; Gaoxingyu Huang; Yigong Shi

<jats:title>How spliceosomes make the first cut</jats:title> <jats:p> In eukaryotes, transcribed precursor mRNA includes noncoding sequences that must be spliced out. This is done by the spliceosome, a dynamic complex in which five small nuclear RNAs and several proteins go through a series of ordered interactions and conformational rearrangements to achieve splicing. Two protein structures provide a look at the first catalytic step in the pathway. Yan <jats:italic>et al.</jats:italic> report the structure of the activated spliceosome (the B <jats:sup>act</jats:sup> complex) at 3.5 Å resolution, revealing how latency is maintained even though the complex is mostly primed for catalysis. Wan <jats:italic>et al.</jats:italic> report the structure of the catalytic step 1 spliceosome (the C complex) at 3.4 Å resolution; this complex forms after the first step of the splicing reaction. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue pp. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6302" page="904" related-article-type="in-this-issue" vol="353" xlink:href="10.1126/science.aag0291">904</jats:related-article> and <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6302" page="895" related-article-type="in-this-issue" vol="353" xlink:href="10.1126/science.aag2235">895</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 895-904

Structure of a yeast activated spliceosome at 3.5 Å resolution

Chuangye Yan; Ruixue Wan; Rui Bai; Gaoxingyu Huang; Yigong Shi

<jats:title>How spliceosomes make the first cut</jats:title> <jats:p> In eukaryotes, transcribed precursor mRNA includes noncoding sequences that must be spliced out. This is done by the spliceosome, a dynamic complex in which five small nuclear RNAs and several proteins go through a series of ordered interactions and conformational rearrangements to achieve splicing. Two protein structures provide a look at the first catalytic step in the pathway. Yan <jats:italic>et al.</jats:italic> report the structure of the activated spliceosome (the B <jats:sup>act</jats:sup> complex) at 3.5 Å resolution, revealing how latency is maintained even though the complex is mostly primed for catalysis. Wan <jats:italic>et al.</jats:italic> report the structure of the catalytic step 1 spliceosome (the C complex) at 3.4 Å resolution; this complex forms after the first step of the splicing reaction. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue pp. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6302" page="904" related-article-type="in-this-issue" vol="353" xlink:href="10.1126/science.aag0291">904</jats:related-article> and <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6302" page="895" related-article-type="in-this-issue" vol="353" xlink:href="10.1126/science.aag2235">895</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 904-911