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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

Cobertura temática

Tabla de contenidos

NASA's Busload of Science

Dan Charles

<jats:p>For 30 years, the shuttle has been the main ticket into space for NASA astronauts. But it has also delivered—and fixed—massive observatories and served as an orbiting laboratory. As the program ends, what is its scientific legacy?</jats:p>

Palabras clave: Multidisciplinary.

Pp. 28-29

The Highs and Lows of Shuttle Science

Dan Charles

<jats:p> The contributions of the shuttle to science have come in many flavors and at an irregular pace. <jats:italic>Science</jats:italic> has created a timeline of shuttle science missions. </jats:p>

Palabras clave: Multidisciplinary.

Pp. 30-33

Editorial Expression of Concern

Bruce Alberts

Palabras clave: Multidisciplinary.

Pp. 35-35

Not-So-Sunny Outlook for Organic Photovoltaics

Edwin A. Chandross

Palabras clave: Multidisciplinary.

Pp. 35-36

An Unorthodox Approach to Forest Restoration

Chris J. Kettle; David F. R. P. Burslem; Jaboury Ghazoul

Palabras clave: Multidisciplinary.

Pp. 36-36

An Unorthodox Approach to Forest Restoration—Response

David J. Merritt; Kingsley W. Dixon

Palabras clave: Multidisciplinary.

Pp. 36-37

Response to Comment on “The Mechanism for Activation of GTP Hydrolysis on the Ribosome”

Rebecca M. Voorhees; T. Martin Schmeing; Ann C. Kelley; V. Ramakrishnan

<jats:p> Our report of the crystal structure of elongation factor Tu (EF-Tu) and aminoacyl–transfer RNA bound to the ribosome with a guanosine triphosphate (GTP) analog included a proposed mechanism of GTP hydrolysis by EF-Tu involving histidine-84. Liljas <jats:italic>et al</jats:italic> . summarize experimental evidence against this mechanism and propose a substrate-assisted catalytic model. However, these experiments and the model are also problematic. Further study is required to definitively determine the mechanism of GTP hydrolysis by EF-Tu. </jats:p>

Palabras clave: Multidisciplinary.

Pp. 37-37

Comment on “The Mechanism for Activation of GTP Hydrolysis on the Ribosome”

Anders Liljas; Måns Ehrenberg; Johan Åqvist

<jats:p> Voorhees <jats:italic>et al</jats:italic> . (Reports, 5 November 2010, p. 835) determined the structure of elongation factor Tu (EF-Tu) and aminoacyl–transfer RNA bound to the ribosome with a guanosine triphosphate (GTP) analog. However, their identification of histidine-84 of EF-Tu as deprotonating the catalytic water molecule is problematic in relation to their atomic structure; the terminal phosphate of GTP is more likely to be the proper proton acceptor. </jats:p>

Palabras clave: Multidisciplinary.

Pp. 37-37

Books Received

<jats:p> A <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="uri" xlink:href="http://www.sciencemag.org/site/feature/data/books/brl6038.xhtml">listing of books received</jats:ext-link> at <jats:italic>Science</jats:italic> during the week ending 24 June 2011. </jats:p>

Palabras clave: Multidisciplinary.

Pp. 38-38

Books Received

<jats:p> A <jats:ext-link xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="uri" xlink:href="http://www.sciencemag.org/site/feature/data/books/brl6038.xhtml">listing of books received</jats:ext-link> at <jats:italic>Science</jats:italic> during the week ending 24 June 2011. </jats:p>

Palabras clave: Multidisciplinary.

Pp. 38-38