Catálogo de publicaciones - revistas
Science
Resumen/Descripción – provisto por la editorial
No disponible.
Palabras clave – provistas por la editorial
No disponibles.
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
Editors' Choice
Caroline Ash; Jesse Smith (eds.)
Palabras clave: Multidisciplinary.
Pp. 1228-1229
Speaking in parts
Caroline Ash; Jesse Smith (eds.)
Palabras clave: Multidisciplinary.
Pp. 1228.1-1229
Predicting fecal transplant success
Caroline Ash; Jesse Smith (eds.)
Palabras clave: Multidisciplinary.
Pp. 1228.2-1228
Secrets of CRISPR enzymes revealed
Caroline Ash; Jesse Smith (eds.)
Palabras clave: Multidisciplinary.
Pp. 1228.3-1229
Tracking expanding dimensions of words
Caroline Ash; Jesse Smith (eds.)
Palabras clave: Multidisciplinary.
Pp. 1228.4-1229
Tumor sensing by the immune system
Caroline Ash; Jesse Smith (eds.)
Palabras clave: Multidisciplinary.
Pp. 1228.5-1229
Plant puzzle patterns
Caroline Ash; Jesse Smith (eds.)
Palabras clave: Multidisciplinary.
Pp. 1228.6-1229
Seeing the human hand
Caroline Ash; Jesse Smith (eds.)
Palabras clave: Multidisciplinary.
Pp. 1228.7-1229
Phenotype risk scores identify patients with unrecognized Mendelian disease patterns
Lisa Bastarache
; Jacob J. Hughey
; Scott Hebbring; Joy Marlo
; Wanke Zhao; Wanting T. Ho; Sara L. Van Driest
; Tracy L. McGregor; Jonathan D. Mosley
; Quinn S. Wells
; Michael Temple; Andrea H. Ramirez
; Robert Carroll
; Travis Osterman; Todd Edwards
; Douglas Ruderfer
; Digna R. Velez Edwards
; Rizwan Hamid; Joy Cogan
; Andrew Glazer
; Wei-Qi Wei
; QiPing Feng
; Murray Brilliant; Zhizhuang J. Zhao; Nancy J. Cox
; Dan M. Roden
; Joshua C. Denny
<jats:title>Hidden effects of Mendelian inheritance</jats:title> <jats:p> Identifying the determinate factors of genetic disease has been quite successful for Mendelian inheritance of large-effect pathogenic variants. In these cases, two non- or low-functioning genes contribute to disease. However, Mendelian effects of lesser strength have generally been ignored when looking at genomic consequences in human health. Bastarache <jats:italic>et al.</jats:italic> used electronic records to identify the phenotypic effects of previously unidentified Mendelian variations. Their analysis suggests that individuals with undiagnosed Mendelian diseases may be more prevalent in the general population than assumed. Because of this, genetic analysis may be able to assist clinicians in arriving at a diagnosis. </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="6381" page="1233" related-article-type="in-this-issue" vol="359" xlink:href="10.1126/science.aal4043">1233</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 1233-1239
Random heteropolymers preserve protein function in foreign environments
Brian Panganiban
; Baofu Qiao
; Tao Jiang
; Christopher DelRe
; Mona M. Obadia
; Trung Dac Nguyen
; Anton A. A. Smith
; Aaron Hall
; Izaac Sit
; Marquise G. Crosby
; Patrick B. Dennis
; Eric Drockenmuller
; Monica Olvera de la Cruz; Ting Xu
<jats:title>Mimicking the designs found in proteins</jats:title> <jats:p> Natural proteins combine a range of useful features, including chemical diversity, the ability to rapidly switch between preprogrammed shapes, and a hierarchy of structures. Panganiban <jats:italic>et al.</jats:italic> designed random copolymers with polar and nonpolar groups, using many of the features found in proteins (see the Perspective by Alexander-Katz and Van Lehn). Their structures could serve as “broad spectrum” surfactants, able to promote the solubilization of proteins in organic solvents and help preserve the functionality of proteins in aqueous environments. </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="6381" page="1239" related-article-type="in-this-issue" vol="359" xlink:href="10.1126/science.aao0335">1239</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6381" page="1216" related-article-type="in-this-issue" vol="359" xlink:href="10.1126/science.aat0155">1216</jats:related-article> </jats:p>
Palabras clave: Multidisciplinary.
Pp. 1239-1243