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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

Ciencias naturales

Tabla de contenidos

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doi: 10.1126/science.aam9712

Moving in the Anthropocene: Global reductions in terrestrial mammalian movements

Marlee A. Tucker; Katrin Böhning-Gaese; William F. Fagan; John M. Fryxell; Bram Van Moorter; Susan C. Alberts; Abdullahi H. Ali; Andrew M. Allen; Nina Attias; Tal Avgar; Hattie Bartlam-Brooks; Buuveibaatar Bayarbaatar; Jerrold L. Belant; Alessandra Bertassoni; Dean Beyer; Laura Bidner; Floris M. van Beest; Stephen Blake; Niels Blaum; Chloe Bracis; Danielle Brown; P. J. Nico de Bruyn; Francesca Cagnacci; Justin M. Calabrese; Constança Camilo-Alves; Simon Chamaillé-Jammes; Andre Chiaradia; Sarah C. Davidson; Todd Dennis; Stephen DeStefano; Duane Diefenbach; Iain Douglas-Hamilton; Julian Fennessy; Claudia Fichtel; Wolfgang Fiedler; Christina Fischer; Ilya Fischhoff; Christen H. Fleming; Adam T. Ford; Susanne A. Fritz; Benedikt Gehr; Jacob R. Goheen; Eliezer Gurarie; Mark Hebblewhite; Marco Heurich; A. J. Mark Hewison; Christian Hof; Edward Hurme; Lynne A. Isbell; René Janssen; Florian Jeltsch; Petra Kaczensky; Adam Kane; Peter M. Kappeler; Matthew Kauffman; Roland Kays; Duncan Kimuyu; Flavia Koch; Bart Kranstauber; Scott LaPoint; Peter Leimgruber; John D. C. Linnell; Pascual López-López; A. Catherine Markham; Jenny Mattisson; Emilia Patricia Medici; Ugo Mellone; Evelyn Merrill; Guilherme de Miranda Mourão; Ronaldo G. Morato; Nicolas Morellet; Thomas A. Morrison; Samuel L. Díaz-Muñoz; Atle Mysterud; Dejid Nandintsetseg; Ran Nathan; Aidin Niamir; John Odden; Robert B. O’Hara; Luiz Gustavo R. Oliveira-Santos; Kirk A. Olson; Bruce D. Patterson; Rogerio Cunha de Paula; Luca Pedrotti; Björn Reineking; Martin Rimmler; Tracey L. Rogers; Christer Moe Rolandsen; Christopher S. Rosenberry; Daniel I. Rubenstein; Kamran Safi; Sonia Saïd; Nir Sapir; Hall Sawyer; Niels Martin Schmidt; Nuria Selva; Agnieszka Sergiel; Enkhtuvshin Shiilegdamba; João Paulo Silva; Navinder Singh; Erling J. Solberg; Orr Spiegel; Olav Strand; Siva Sundaresan; Wiebke Ullmann; Ulrich Voigt; Jake Wall; David Wattles; Martin Wikelski; Christopher C. Wilmers; John W. Wilson; George Wittemyer; Filip Zięba; Tomasz Zwijacz-Kozica; Thomas Mueller

<jats:title>Restrictions on roaming</jats:title> <jats:p> Until the past century or so, the movement of wild animals was relatively unrestricted, and their travels contributed substantially to ecological processes. As humans have increasingly altered natural habitats, natural animal movements have been restricted. Tucker <jats:italic>et al.</jats:italic> examined GPS locations for more than 50 species. In general, animal movements were shorter in areas with high human impact, likely owing to changed behaviors and physical limitations. Besides affecting the species themselves, such changes could have wider effects by limiting the movement of nutrients and altering ecological interactions. </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="6374" page="466" related-article-type="in-this-issue" vol="359" xlink:href="10.1126/science.aam9712">466</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 466-469

doi: 10.1126/science.aao3099

The ER membrane protein complex is a transmembrane domain insertase

Alina Guna; Norbert Volkmar; John C. Christianson; Ramanujan S. Hegde

<jats:title>A new way into the ER</jats:title> <jats:p> Membrane-embedded proteins are highly diverse in topology, physical characteristics, and location. This diversity necessitates multiple pathways for their effective membrane insertion. Guna <jats:italic>et al.</jats:italic> found that a widely conserved protein complex is responsible for inserting a subset of membrane proteins into the endoplasmic reticulum (ER) membrane (see the Perspective by Fry and Clemons Jr.). This ER membrane protein complex (EMC) inserts transmembrane domains whose topology and hydrophobicity preclude effective recognition by other insertion factors. This finding helps explain why the loss of EMC causes ER stress and altered protein trafficking. </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="6374" page="470" related-article-type="in-this-issue" vol="359" xlink:href="10.1126/science.aao3099">470</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6374" page="390" related-article-type="in-this-issue" vol="359" xlink:href="10.1126/science.aar5992">390</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 470-473

doi: 10.1126/science.359.6374.474

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. 474-474

doi: 10.1126/science.359.6374.486