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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.

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No detectada	desde jul. 2012 / hasta dic. 2023	Nature.com
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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-

Cobertura temática

Ciencias naturales

Ingeniería y tecnología

Ciencias médicas y de la salud

Ciencias agrícolas y veterinarias

Tabla de contenidos

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doi: 10.1038/s41586-021-04262-z

Decoding gene regulation in the fly brain

Jasper Janssens; Sara Aibar; Ibrahim Ihsan Taskiran; Joy N. Ismail; Alicia Estacio Gomez; Gabriel Aughey; Katina I. Spanier; Florian V. De Rop; Carmen Bravo González-Blas; Marc Dionne; Krista Grimes; Xiao Jiang Quan; Dafni Papasokrati; Gert Hulselmans; Samira Makhzami; Maxime De Waegeneer; Valerie Christiaens; Tony Southall; Stein Aerts

Palabras clave: Multidisciplinary.

Pp. 630-636

doi: 10.1038/s41586-021-04295-4

Ageing exacerbates ribosome pausing to disrupt cotranslational proteostasis

Kevin C. Stein; Fabián Morales-Polanco; Joris van der Lienden; T. Kelly Rainbolt; Judith Frydman

Palabras clave: Multidisciplinary.

Pp. 637-642

doi: 10.1038/s41586-021-04274-9

Structural insights into inhibitor regulation of the DNA repair protein DNA-PKcs

Shikang Liang; Sherine E. Thomas; Amanda K. Chaplin; Steven W. Hardwick; Dimitri Y. Chirgadze; Tom L. Blundell

<jats:title>Abstract</jats:title><jats:p>The DNA-dependent protein kinase catalytic subunit (DNA-PKcs) has a central role in non-homologous end joining, one of the two main pathways that detect and repair DNA double-strand breaks (DSBs) in humans<jats:sup>1,2</jats:sup>. DNA-PKcs is of great importance in repairing pathological DSBs, making DNA-PKcs inhibitors attractive therapeuticÂ agents for cancer in combination with DSB-inducing radiotherapy and chemotherapy<jats:sup>3</jats:sup>. Many of the selective inhibitors ofÂ DNA-PKcs that have beenÂ developed exhibit potential as treatment for various cancers<jats:sup>4</jats:sup>. Here we report cryo-electron microscopy (cryo-EM) structures of human DNA-PKcs natively purified from HeLa cell nuclear extracts, in complex with adenosine-5â€²-(Î³-thio)-triphosphate (ATPÎ³S) and four inhibitors (wortmannin, NU7441, AZD7648 and M3814), including drug candidates undergoing clinical trials. The structures reveal molecular details of ATP binding at the active site before catalysis and provide insights into the modes of action and specificities of the competitive inhibitors. Of note, binding of the ligands causes movement of the PIKK regulatory domain (PRD), revealing a connection between the p-loop and PRD conformations. Electrophoretic mobility shift assay and cryo-EM studies on theÂ DNA-dependent protein kinase holoenzyme further show that ligand binding does not have a negative allosteric or inhibitory effect on assembly of the holoenzyme complex and that inhibitors function through direct competition with ATP. Overall, the structures described in this study should greatly assist future efforts in rational drug design targeting DNA-PKcs, demonstrating the potential of cryo-EM in structure-guided drug development for large and challenging targets.</jats:p>

Palabras clave: Multidisciplinary.

Pp. 643-648