Catálogo de publicaciones - revistas
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
1880-
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