Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment

Intracellular antibodies can inhibit disease-relevant protein interactions, but inefficient cellular uptake limits their utility. Using a RAS-targeting intracellular antibody as a screening tool, the authors here identify small molecules that inhibit RAS-effector interactions and readily penetrate c...

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Autores principales: Camilo E. Quevedo, Abimael Cruz-Migoni, Nicolas Bery, Ami Miller, Tomoyuki Tanaka, Donna Petch, Carole J. R. Bataille, Lydia Y. W. Lee, Phillip S. Fallon, Hanna Tulmin, Matthias T. Ehebauer, Narcis Fernandez-Fuentes, Angela J. Russell, Stephen B. Carr, Simon E. V. Phillips, Terence H. Rabbitts
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Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/67c80be1d0a14b3aa0feecf6b7e3b832
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spelling oai:doaj.org-article:67c80be1d0a14b3aa0feecf6b7e3b8322021-12-02T17:32:45ZSmall molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment10.1038/s41467-018-05707-22041-1723https://doaj.org/article/67c80be1d0a14b3aa0feecf6b7e3b8322018-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05707-2https://doaj.org/toc/2041-1723Intracellular antibodies can inhibit disease-relevant protein interactions, but inefficient cellular uptake limits their utility. Using a RAS-targeting intracellular antibody as a screening tool, the authors here identify small molecules that inhibit RAS-effector interactions and readily penetrate cells.Camilo E. QuevedoAbimael Cruz-MigoniNicolas BeryAmi MillerTomoyuki TanakaDonna PetchCarole J. R. BatailleLydia Y. W. LeePhillip S. FallonHanna TulminMatthias T. EhebauerNarcis Fernandez-FuentesAngela J. RussellStephen B. CarrSimon E. V. PhillipsTerence H. RabbittsNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Camilo E. Quevedo
Abimael Cruz-Migoni
Nicolas Bery
Ami Miller
Tomoyuki Tanaka
Donna Petch
Carole J. R. Bataille
Lydia Y. W. Lee
Phillip S. Fallon
Hanna Tulmin
Matthias T. Ehebauer
Narcis Fernandez-Fuentes
Angela J. Russell
Stephen B. Carr
Simon E. V. Phillips
Terence H. Rabbitts
Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment
description Intracellular antibodies can inhibit disease-relevant protein interactions, but inefficient cellular uptake limits their utility. Using a RAS-targeting intracellular antibody as a screening tool, the authors here identify small molecules that inhibit RAS-effector interactions and readily penetrate cells.
format article
author Camilo E. Quevedo
Abimael Cruz-Migoni
Nicolas Bery
Ami Miller
Tomoyuki Tanaka
Donna Petch
Carole J. R. Bataille
Lydia Y. W. Lee
Phillip S. Fallon
Hanna Tulmin
Matthias T. Ehebauer
Narcis Fernandez-Fuentes
Angela J. Russell
Stephen B. Carr
Simon E. V. Phillips
Terence H. Rabbitts
author_facet Camilo E. Quevedo
Abimael Cruz-Migoni
Nicolas Bery
Ami Miller
Tomoyuki Tanaka
Donna Petch
Carole J. R. Bataille
Lydia Y. W. Lee
Phillip S. Fallon
Hanna Tulmin
Matthias T. Ehebauer
Narcis Fernandez-Fuentes
Angela J. Russell
Stephen B. Carr
Simon E. V. Phillips
Terence H. Rabbitts
author_sort Camilo E. Quevedo
title Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment
title_short Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment
title_full Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment
title_fullStr Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment
title_full_unstemmed Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment
title_sort small molecule inhibitors of ras-effector protein interactions derived using an intracellular antibody fragment
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/67c80be1d0a14b3aa0feecf6b7e3b832
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