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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
Biosynthesis of monoterpene scent compounds in roses
Jean-Louis Magnard; Aymeric Roccia; Jean-Claude Caissard; Philippe Vergne; Pulu Sun; Romain Hecquet; Annick Dubois; Laurence Hibrand-Saint Oyant; Frédéric Jullien; Florence Nicolè; Olivier Raymond; Stéphanie Huguet; Raymonde Baltenweck; Sophie Meyer; Patricia Claudel; Julien Jeauffre; Michel Rohmer; Fabrice Foucher; Philippe Hugueney; Mohammed Bendahmane; Sylvie Baudino
<jats:title>Stop to smell the roses</jats:title> <jats:p> Some roses smell beautiful, yet others only look beautiful. Magnard <jats:italic>et al.</jats:italic> leveraged this distinction to study the biosynthesis of geraniol, a monoterpene alcohol in rose scent (see the Perspective by Tholl and Gershenzon). Enzymes known for geraniol synthesis in other plants, such as basil, did not seem to provide that function for roses. Instead, a diphosphohydrolase, which functions in the cytoplasm of cells in rose petals, generates the geraniol emitted by fragrant roses. Identification of the enzyme and its gene enables marker-assisted breeding to put the perfume back into beauty. </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="6243" page="81" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aab0696">81</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6243" page="28" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aac6509">28</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 81-83
Genetic assignment of large seizures of elephant ivory reveals Africa’s major poaching hotspots
S. K. Wasser; L. Brown; C. Mailand; S. Mondol; W. Clark; C. Laurie; B. S. Weir
<jats:title>Focused on protecting a few</jats:title> <jats:p> The illegal ivory trade threatens the persistence of stable wild elephant populations. The underground and covert nature of poaching makes it difficult to police. Wasser <jats:italic>et al.</jats:italic> used genetic tools to identify the origins of elephant tusks seized during transit (see the Perspective by Hoelzel). The majority of source animals were part of just a few wild elephant populations in Africa—and just two areas since 2006. Increased focus on enforcement in a few such areas could help interrupt poaching activities and restore wild elephant populations. </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="6243" page="84" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aaa2457">84</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6243" page="34" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aac6301">34</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 84-87
Cryo-EM structure of an antibody that neutralizes dengue virus type 2 by locking E protein dimers
Guntur Fibriansah; Kristie D. Ibarra; Thiam-Seng Ng; Scott A. Smith; Joanne L. Tan; Xin-Ni Lim; Justin S. G. Ooi; Victor A. Kostyuchenko; Jiaqi Wang; Aravinda M. de Silva; Eva Harris; James E. Crowe; Shee-Mei Lok
<jats:title>An antibody to lock dengue virus out</jats:title> <jats:p> Mosquito-borne dengue virus (DENV) is a growing public health threat. Nearly 400 million people are infected annually, and no vaccine is currently available. Fibriansah <jats:italic>et al.</jats:italic> report that a human antibody (2D22) specific for DENV serotype 2, when given therapeutically, can protect mice from a lethal form of this virus. Structural analysis revealed that 2D22 binds across multiple DENV envelope proteins, which probably blocks the ability of these proteins to assemble into the orientation necessary for viral entry. The epitope where 2D22 binds to the virus may therefore represent a potential vaccine target. </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="6243" page="88" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aaa8651">88</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 88-91
CRL2 aids elimination of truncated selenoproteins produced by failed UGA/Sec decoding
Hsiu-Chuan Lin; Szu-Chi Ho; Yi-Yun Chen; Kay-Hooi Khoo; Pang-Hung Hsu; Hsueh-Chi S. Yen
<jats:title>Clearing out selenoprotein garbage</jats:title> <jats:p> Our DNA consists of codons that code for 20 different amino acids. Another amino acid, selenocysteine, is also found in several human selenoproteins. Selenocysteine is incorporated through the recoding of a stop codon, but failures in this process result in premature termination of protein synthesis. Lin <jats:italic>et al.</jats:italic> showed that the potentially dangerous truncated proteins formed in such cases are specifically degraded by a protein quality surveillance system. The surveillance system can specifically recognize the truncated ends of the various prematurely terminated selenoproteins and target their destruction. </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="6243" page="91" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aab0515">91</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 91-95
Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography
G. Obal; F. Trajtenberg; F. Carrión; L. Tomé; N. Larrieux; X. Zhang; O. Pritsch; A. Buschiazzo
<jats:title>Retroviral capsids in their native form</jats:title> <jats:p> Capsid proteins of retroviruses form protective lattices around viral RNA molecules. The precise molecular details of how individual, full-length capsid proteins assemble to shield the viral genome; however, are not well understood. Obal <jats:italic>et al.</jats:italic> and Gres <jats:italic>et al.</jats:italic> now report high resolution crystal structures of the full length capsid proteins from Bovine Leukemia Virus and HIV-1, respectively. The two studies complement each other to reveal the dynamic nature of capsid protein assembly and of how individual capsid proteins interact in the lattice. The findings may have relevance for drug design. </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="6243" page="95" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aaa5182">95</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6243" page="99" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aaa5936">99</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 95-98
X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability
Anna T. Gres; Karen A. Kirby; Vineet N. KewalRamani; John J. Tanner; Owen Pornillos; Stefan G. Sarafianos
<jats:title>Retroviral capsids in their native form</jats:title> <jats:p> Capsid proteins of retroviruses form protective lattices around viral RNA molecules. The precise molecular details of how individual, full-length capsid proteins assemble to shield the viral genome; however, are not well understood. Obal <jats:italic>et al.</jats:italic> and Gres <jats:italic>et al.</jats:italic> now report high resolution crystal structures of the full length capsid proteins from Bovine Leukemia Virus and HIV-1, respectively. The two studies complement each other to reveal the dynamic nature of capsid protein assembly and of how individual capsid proteins interact in the lattice. The findings may have relevance for drug design. </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="6243" page="95" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aaa5182">95</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6243" page="99" related-article-type="in-this-issue" vol="349" xlink:href="10.1126/science.aaa5936">99</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 99-103
Science Podcast: 3 July Show
<jats:p>On this week's show: Behind the scent of a rose and a roundup of daily news stories.</jats:p>
Palabras clave: Multidisciplinary.
Pp. 104-104
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. 104-104
Improving tissue-sample profiling: The optimization and application of immunohistochemistry
Nissi M. Varki; Kevin D. Long
<jats:p>Though it has been used for more than 70 years, immunohistochemistry (IHC) is still an essential research and diagnostic tool in many scientific laboratories. Understanding the basic principles underlying IHC and how to address the technical aspects of experimental design are key to producing high-quality, reproducible data. IHC is used in a variety of fields—from cancer diagnostics to neuroscience research—but some common advice can be applied across-the-board. Many variables are vital for generating valuable results and require optimization when designing IHC experiments, such as fixing tissue, choosing the proper antibodies, and defining the proper controls. In this webinar, we will hear from experts who will share their insights into the key aspects of assay design.</jats:p>
Palabras clave: Multidisciplinary.
Pp. 104-104
Find your most interesting question
Nicola Spaldin
Palabras clave: Multidisciplinary.
Pp. 110-110