Catálogo de publicaciones - revistas
Nature
Resumen/Descripción – provisto por la editorial en inglés
Nature is a weekly international journal publishing the finest peer-reviewed research in all fields of science and technology on the basis of its originality, importance, interdisciplinary interest, timeliness, accessibility, elegance and surprising conclusions. Nature also provides rapid, authoritative, insightful and arresting news and interpretation of topical and coming trends affecting science, scientists and the wider public.Palabras clave – provistas por la editorial
No disponibles.
Disponibilidad
| Institución detectada | Período | Navegá | Descargá | Solicitá |
|---|---|---|---|---|
| No detectada | desde jul. 2012 / hasta dic. 2023 | Nature.com | ||
| No detectada | desde jul. 2006 / hasta ago. 2012 | Ovid |
Información
Tipo de recurso:
revistas
ISSN impreso
0028-0836
ISSN electrónico
1476-4687
Editor responsable
Springer Nature
País de edición
Reino Unido
Fecha de publicación
1869-
Tabla de contenidos
Oestrogen engages brain MC4R signalling to drive physical activity in female mice
William C. Krause; Ruben Rodriguez
; Bruno Gegenhuber; Navneet Matharu; Andreas N. Rodriguez; Adriana M. Padilla-Roger; Kenichi Toma; Candice B. Herber; Stephanie M. Correa; Xin Duan; Nadav Ahituv; Jessica Tollkuhn; Holly A. Ingraham
Palabras clave: Multidisciplinary.
Pp. 131-135
SLC25A39 is necessary for mitochondrial glutathione import in mammalian cells
Ying Wang; Frederick S. Yen; Xiphias Ge Zhu; Rebecca C. Timson; Ross Weber; Changrui Xing; Yuyang Liu; Benjamin Allwein; Hanzhi Luo; Hsi-Wen Yeh; Søren Heissel; Gokhan Unlu; Eric R. Gamazon; Michael G. Kharas; Richard Hite; Kıvanç Birsoy
Palabras clave: Multidisciplinary.
Pp. 136-140
Whole-cell organelle segmentation in volume electron microscopy
Larissa Heinrich; Davis Bennett; David Ackerman; Woohyun Park; John Bogovic; Nils Eckstein; Alyson Petruncio; Jody Clements; Song Pang; C. Shan Xu; Jan Funke; Wyatt Korff; Harald F. Hess; Jennifer Lippincott-Schwartz; Stephan Saalfeld; Aubrey V. Weigel; Riasat Ali; Rebecca Arruda; Rohit Bahtra; Destiny Nguyen;
Palabras clave: Multidisciplinary.
Pp. 141-146
An open-access volume electron microscopy atlas of whole cells and tissues
C. Shan Xu; Song Pang; Gleb Shtengel; Andreas Müller; Alex T. Ritter; Huxley K. Hoffman; Shin-ya Takemura; Zhiyuan Lu; H. Amalia Pasolli; Nirmala Iyer; Jeeyun Chung; Davis Bennett; Aubrey V. Weigel; Melanie Freeman; Schuyler B. van Engelenburg; Tobias C. Walther; Robert V. Farese; Jennifer Lippincott-Schwartz; Ira Mellman; Michele Solimena; Harald F. Hess
Palabras clave: Multidisciplinary.
Pp. 147-151
Systems-level effects of allosteric perturbations to a model molecular switch
Tina Perica; Christopher J. P. Mathy; Jiewei Xu; Gwendolyn Μ. Jang; Yang Zhang; Robyn Kaake; Noah Ollikainen; Hannes Braberg; Danielle L. Swaney; David G. Lambright; Mark J. S. Kelly; Nevan J. Krogan; Tanja Kortemme
Palabras clave: Multidisciplinary.
Pp. 152-157
Structural basis of gating modulation of Kv4 channel complexes
Yoshiaki Kise; Go Kasuya; Hiroyuki H. Okamoto; Daichi Yamanouchi; Kan Kobayashi; Tsukasa Kusakizako; Tomohiro Nishizawa; Koichi Nakajo; Osamu Nureki
<jats:title>Abstract</jats:title><jats:p>Modulation of voltage-gated potassium (Kv) channels by auxiliary subunits is central to the physiological function of channels in the brain and heart<jats:sup>1,2</jats:sup>. Native Kv4 tetrameric channels form macromolecular ternary complexes with two auxiliary β-subunits—intracellular Kv channel-interacting proteins (KChIPs) and transmembrane dipeptidyl peptidase-related proteins (DPPs)—to evoke rapidly activating and inactivating A-type currents, which prevent the backpropagation of action potentials<jats:sup>1–5</jats:sup>. However, the modulatory mechanisms of Kv4 channel complexes remain largely unknown. Here we report cryo-electron microscopy structures of the Kv4.2–DPP6S–KChIP1 dodecamer complex, the Kv4.2–KChIP1 and Kv4.2–DPP6S octamer complexes, and Kv4.2 alone. The structure of the Kv4.2–KChIP1 complex reveals that the intracellular N terminus of Kv4.2 interacts with its C terminus that extends from the S6 gating helix of the neighbouring Kv4.2 subunit. KChIP1 captures both the N and the C terminus of Kv4.2. In consequence, KChIP1 would prevent N-type inactivation and stabilize the S6 conformation to modulate gating of the S6 helices within the tetramer. By contrast, unlike the reported auxiliary subunits of voltage-gated channel complexes, DPP6S interacts with the S1 and S2 helices of the Kv4.2 voltage-sensing domain, which suggests that DPP6S stabilizes the conformation of the S1–S2 helices. DPP6S may therefore accelerate the voltage-dependent movement of the S4 helices. KChIP1 and DPP6S do not directly interact with each other in the Kv4.2–KChIP1–DPP6S ternary complex. Thus, our data suggest that two distinct modes of modulation contribute in an additive manner to evoke A-type currents from the native Kv4 macromolecular complex.</jats:p>
Palabras clave: Multidisciplinary.
Pp. 158-164
Tips for managing an industry move without your academic supervisor’s support
Amy DePaul
Palabras clave: Multidisciplinary.
Pp. 165-167
Refining the toolkit for sugar analysis
Amber Dance
Palabras clave: Multidisciplinary.
Pp. 168-169
Virus detective: searching for Zika, dengue and SARS-CoV-2
Patrícia Maia Noronha
Palabras clave: Multidisciplinary.
Pp. 172-172
My first pet
Robert Blasiak
Palabras clave: Multidisciplinary.
Pp. No disponible