Catálogo de publicaciones - revistas
Science
Resumen/Descripción – provisto por la editorial
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Palabras clave – provistas por la editorial
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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
Softening up your target
Stella M. Hurtley
Palabras clave: Multidisciplinary.
Pp. 1170-1171
Remote sensing for analyzing smallholder farm yields
Pamela J. Hines
Palabras clave: Multidisciplinary.
Pp. 1170.1-1170
Sand-driven magnetic field
Brent Grocholski
Palabras clave: Multidisciplinary.
Pp. 1170.2-1170
Microaggression actions outpace evidence
Brad Wible
Palabras clave: Multidisciplinary.
Pp. 1170.3-1170
Softening up your target
Stella M. Hurtley
Palabras clave: Multidisciplinary.
Pp. 1170.4-1171
Restacking the deck
Phil Szuromi
Palabras clave: Multidisciplinary.
Pp. 1170.5-1171
Love hormones and mental health
Megan Eldred
Palabras clave: Multidisciplinary.
Pp. 1170.6-1171
Fine-scale structure in higher brain areas
Peter Stern
Palabras clave: Multidisciplinary.
Pp. 1170.7-1171
Structural basis of the day-night transition in a bacterial circadian clock
Roger Tseng
; Nicolette F. Goularte; Archana Chavan; Jansen Luu; Susan E. Cohen; Yong-Gang Chang; Joel Heisler; Sheng Li; Alicia K. Michael; Sarvind Tripathi; Susan S. Golden; Andy LiWang; Carrie L. Partch
<jats:title>Molecular clockwork from cyanobacteria</jats:title> <jats:p> The cyanobacterial circadian clock oscillator can be reconstituted in a test tube from just three proteins—KaiA, KaiB, and KaiC—and adenosine triphosphate (ATP). Tseng <jats:italic>et al.</jats:italic> studied crystal and nuclear magnetic resonance structures of complexes of the oscillator proteins and their signaling output proteins and tested the in vivo effects of structure-based mutants. Large conformational changes in KaiB and ATP hydrolysis by KaiC are coordinated with binding to output protein, which couples signaling and the day-night transitions of the clock. Snijder <jats:italic>et al.</jats:italic> provide complementary analysis of the oscillator proteins by mass spectrometry and cryo–electron microscopy. Their results help to explain the structural basis for the dynamic assembly of the oscillator complexes. </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="6330" page="1174" related-article-type="in-this-issue" vol="355" xlink:href="10.1126/science.aag2516">1174</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6330" page="1181" related-article-type="in-this-issue" vol="355" xlink:href="10.1126/science.aag3218">1181</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 1174-1180
Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state
Joost Snijder; Jan M. Schuller; Anika Wiegard; Philip Lössl; Nicolas Schmelling; Ilka M. Axmann; Jürgen M. Plitzko; Friedrich Förster; Albert J. R. Heck
<jats:title>Molecular clockwork from cyanobacteria</jats:title> <jats:p> The cyanobacterial circadian clock oscillator can be reconstituted in a test tube from just three proteins—KaiA, KaiB, and KaiC—and adenosine triphosphate (ATP). Tseng <jats:italic>et al.</jats:italic> studied crystal and nuclear magnetic resonance structures of complexes of the oscillator proteins and their signaling output proteins and tested the in vivo effects of structure-based mutants. Large conformational changes in KaiB and ATP hydrolysis by KaiC are coordinated with binding to output protein, which couples signaling and the day-night transitions of the clock. Snijder <jats:italic>et al.</jats:italic> provide complementary analysis of the oscillator proteins by mass spectrometry and cryo–electron microscopy. Their results help to explain the structural basis for the dynamic assembly of the oscillator complexes. </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="6330" page="1174" related-article-type="in-this-issue" vol="355" xlink:href="10.1126/science.aag2516">1174</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6330" page="1181" related-article-type="in-this-issue" vol="355" xlink:href="10.1126/science.aag3218">1181</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 1181-1184