Catálogo de publicaciones - revistas

Compartir en
redes sociales


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

Cobertura temática

Tabla de contenidos

Inclusion in human–machine interactions

Tahira Reid; James Gibert

<jats:p>Human–machine interactions research should include diverse subjects and benefit all people</jats:p>

Palabras clave: Multidisciplinary.

Pp. 149-150

An antiquated language, reimagined Kingdom of Characters: The Language Revolution That Made China Modern Jing Tsu Riverhead Books, 2022. 336 pp.

Zuoyue Wang

<jats:p>A new tome traces efforts to unify, reform, and modernize the Chinese language</jats:p>

Palabras clave: Multidisciplinary.

Pp. 151-151

Who gets counted and how Queer Data: Using Gender, Sex and Sexuality Data for Action Kevin Guyan Bloomsbury Academic, 2022. 240 pp.

Nancy Bates

<jats:p>Sexual orientation and gender identity data must be collected and used with thought and with care</jats:p>

Palabras clave: Multidisciplinary.

Pp. 152-152

Pakistan’s markhor population in decline

Shahid Ahmad; Ghulam Nabi

Palabras clave: Multidisciplinary.

Pp. 153-153

Central nervous system weapons dealt a blow

Michael Crowley; Malcolm Dando

Palabras clave: Multidisciplinary.

Pp. 153-154

Transboundary conservation’s rise

Jiajia Liu; Tiantian Zhang; Luke Gibson

Palabras clave: Multidisciplinary.

Pp. 154-154

In Science Journals

Michael Funk (eds.)

<jats:p> Highlights from the <jats:italic>Science</jats:italic> family of journals </jats:p>

Palabras clave: Multidisciplinary.

Pp. 155-157

In Other Journals

Caroline Ash; Jesse Smith (eds.)

<jats:p>Editors’ selections from the current scientific literature</jats:p>

Palabras clave: Multidisciplinary.

Pp. 156-157

4′-Fluorouridine is an oral antiviral that blocks respiratory syncytial virus and SARS-CoV-2 replication

Julien SourimantORCID; Carolin M. Lieber; Megha Aggarwal; Robert M. Cox; Josef D. WolfORCID; Jeong-Joong YoonORCID; Mart Toots; Chengin YeORCID; Zachary SticherORCID; Alexander A. Kolykhalov; Luis Martinez-SobridoORCID; Gregory R. BluemlingORCID; Michael G. Natchus; George R. PainterORCID; Richard K. PlemperORCID

<jats:title>Preparing antiviral defenses</jats:title> <jats:p> Antiviral drugs are an important tool in the battle against COVID-19. Both remdesivir and molnupiravir, which target the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) polymerase, were first developed against other RNA viruses. This highlights the importance of broad-spectrum antivirals that can be rapidly deployed against related emerging pathogens. Sourimant <jats:italic>et al</jats:italic> . used respiratory syncytial virus (RSV) as a primary indication in identifying further drugs that target the polymerase enzyme of RNA viruses. The authors explored derivatives of molnupiravir and identified 4′ fluorouridine (EIDD-2749) as an inhibitor of the polymerase of RSV and SARS-CoV-2. This drug can be delivered orally and was effective against RSV in mice and SARS-CoV-2 in ferrets. —VV </jats:p>

Palabras clave: Multidisciplinary.

Pp. 161-167

Cryo-EM structures of amyloid-β 42 filaments from human brains

Yang YangORCID; Diana ArseniORCID; Wenjuan ZhangORCID; Melissa HuangORCID; Sofia LövestamORCID; Manuel Schweighauser; Abhay KotechaORCID; Alexey G. Murzin; Sew Y. Peak-Chew; Jennifer MacdonaldORCID; Isabelle LavenirORCID; Holly J. GarringerORCID; Ellen GelpiORCID; Kathy L. NewellORCID; Gabor G. KovacsORCID; Ruben VidalORCID; Bernardino GhettiORCID; Benjamin Ryskeldi-FalconORCID; Sjors H. W. ScheresORCID; Michel GoedertORCID

<jats:title>Hi-res view of human Aβ42 filaments</jats:title> <jats:p> Alzheimer’s disease is characterized by a loss of memory and other cognitive functions and the filamentous assembly of Aβ and tau in the brain. The assembly of Aβ peptides into filaments that end at residue 42 is a central event. Yang <jats:italic>et al</jats:italic> . used electron cryo–electron microscopy to determine the structures of Aβ42 filaments from human brain (see the Perspective by Willem and Fändrich). They identified two types of related S-shaped filaments, each consisting of two identical protofilaments. These structures will inform the development of better in vitro and animal models, inhibitors of Aβ42 assembly, and imaging agents with increased specificity and sensitivity. —SMH </jats:p>

Palabras clave: Multidisciplinary.

Pp. 167-172