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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
Protein structure determination using metagenome sequence data
Sergey Ovchinnikov; Hahnbeom Park; Neha Varghese; Po-Ssu Huang; Georgios A. Pavlopoulos; David E. Kim; Hetunandan Kamisetty; Nikos C. Kyrpides; David Baker
<jats:title>Filling in the protein fold picture</jats:title> <jats:p> Fewer than a third of the 14,849 known protein families have at least one member with an experimentally determined structure. This leaves more than 5000 protein families with no structural information. Protein modeling using residue-residue contacts inferred from evolutionary data has been successful in modeling unknown structures, but it requires large numbers of aligned sequences. Ovchinnikov <jats:italic>et al.</jats:italic> augmented such sequence alignments with metagenome sequence data (see the Perspective by Söding). They determined the number of sequences required to allow modeling, developed criteria for model quality, and, where possible, improved modeling by matching predicted contacts to known structures. Their method predicted quality structural models for 614 protein families, of which about 140 represent newly discovered protein folds. </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="6322" page="294" related-article-type="in-this-issue" vol="355" xlink:href="10.1126/science.aah4043">294</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6322" page="248" related-article-type="in-this-issue" vol="355" xlink:href="10.1126/science.aal4512">248</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 294-298
Mechanistic basis for a molecular triage reaction
Sichen Shao; Monica C. Rodrigo-Brenni; Maryann H. Kivlen; Ramanujan S. Hegde
<jats:title>Deciding a protein's fate</jats:title> <jats:p> Protein synthesis inside cells is finely balanced with protein degradation to maintain homeostasis. Shao <jats:italic>et al.</jats:italic> show how differential affinities and binding kinetics of three chaperones regulate the fate of tail-anchored (TA) membrane proteins. The chaperone SGTA binds to TA proteins and quickly transfers them to the targeting factor TRC40 through the C-terminal domain of the quality-control module BAG6. Proteins that dissociate from SGTA can either rebind or, at a slower rate, be bound by the C-terminal domain of BAG6. The latter puts them on a path to degradation. This hierarchy means that biosynthesis has the higher priority, but excess free TA proteins are degraded. </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="6322" page="298" related-article-type="in-this-issue" vol="355" xlink:href="10.1126/science.aah6130">298</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 298-302
AAAS 2017 Annual Meeting Program
<jats:p> This issue of <jats:italic>Science</jats:italic> includes the program of the 2017 AAAS Annual Meeting. The theme of the AAAS Annual Meeting in Boston, 16 to 20 February 2017, is <jats:italic>Serving Society Through Science Policy</jats:italic> . </jats:p> <jats:p> A <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="uri" xlink:href="http://www.sciencemag.org/cgi/reprint/355/6322/303.pdf">PDF</jats:ext-link> of the program as it appears in this issue is available here; for more information on the meeting (including registration forms and information on accommodations), please visit <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="uri" xlink:href="www.aaas.org/meetings/">www.aaas.org/meetings/</jats:ext-link> . </jats:p>
Palabras clave: Multidisciplinary.
Pp. 303-312
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. 313-313
The transcontinental scientist
Wim Delva
Palabras clave: Multidisciplinary.
Pp. 318-318
Jet lag puts baseball players off their game
Rachael Lallensack
Palabras clave: Multidisciplinary.
Pp. No disponible
Wanted: A leader for the toughest job in global health
Kai Kupferschmidt
Palabras clave: Multidisciplinary.
Pp. No disponible
Facing ‘doomsday’ scenario, scientists consider fleeing Brazil
Herton Escobar
Palabras clave: Multidisciplinary.
Pp. No disponible
Amsterdam to host Europe's first 'forensic cemetery'
Martin Enserink
Palabras clave: Multidisciplinary.
Pp. No disponible
How to handle grad school doubts
Maggie Kuo
Palabras clave: Multidisciplinary.
Pp. No disponible