Cellular model system to dissect the isoform-selectivity of Akt inhibitors

Elucidating specific effects of protein kinase Akt isoforms remains challenging. Here, the authors establish an Akt isoform-dependent cellular model system and use it, together with X-ray crystallography and structure-based ligand design, to develop isoform-selective covalent-allosteric Akt inhibito...

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Autores principales:	Lena Quambusch, Laura Depta, Ina Landel, Melissa Lubeck, Tonia Kirschner, Jonas Nabert, Niklas Uhlenbrock, Jörn Weisner, Michael Kostka, Laura M. Levy, Carsten Schultz-Fademrecht, Franziska Glanemann, Kristina Althoff, Matthias P. Müller, Jens T. Siveke, Daniel Rauh
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e9d5b9b56b6e4d8f9a3489c70c876e8e
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spelling	oai:doaj.org-article:e9d5b9b56b6e4d8f9a3489c70c876e8e2021-12-02T17:41:19ZCellular model system to dissect the isoform-selectivity of Akt inhibitors10.1038/s41467-021-25512-82041-1723https://doaj.org/article/e9d5b9b56b6e4d8f9a3489c70c876e8e2021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25512-8https://doaj.org/toc/2041-1723Elucidating specific effects of protein kinase Akt isoforms remains challenging. Here, the authors establish an Akt isoform-dependent cellular model system and use it, together with X-ray crystallography and structure-based ligand design, to develop isoform-selective covalent-allosteric Akt inhibitorsLena QuambuschLaura DeptaIna LandelMelissa LubeckTonia KirschnerJonas NabertNiklas UhlenbrockJörn WeisnerMichael KostkaLaura M. LevyCarsten Schultz-FademrechtFranziska GlanemannKristina AlthoffMatthias P. MüllerJens T. SivekeDaniel RauhNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Lena Quambusch Laura Depta Ina Landel Melissa Lubeck Tonia Kirschner Jonas Nabert Niklas Uhlenbrock Jörn Weisner Michael Kostka Laura M. Levy Carsten Schultz-Fademrecht Franziska Glanemann Kristina Althoff Matthias P. Müller Jens T. Siveke Daniel Rauh Cellular model system to dissect the isoform-selectivity of Akt inhibitors
description	Elucidating specific effects of protein kinase Akt isoforms remains challenging. Here, the authors establish an Akt isoform-dependent cellular model system and use it, together with X-ray crystallography and structure-based ligand design, to develop isoform-selective covalent-allosteric Akt inhibitors
format	article
author	Lena Quambusch Laura Depta Ina Landel Melissa Lubeck Tonia Kirschner Jonas Nabert Niklas Uhlenbrock Jörn Weisner Michael Kostka Laura M. Levy Carsten Schultz-Fademrecht Franziska Glanemann Kristina Althoff Matthias P. Müller Jens T. Siveke Daniel Rauh
author_facet	Lena Quambusch Laura Depta Ina Landel Melissa Lubeck Tonia Kirschner Jonas Nabert Niklas Uhlenbrock Jörn Weisner Michael Kostka Laura M. Levy Carsten Schultz-Fademrecht Franziska Glanemann Kristina Althoff Matthias P. Müller Jens T. Siveke Daniel Rauh
author_sort	Lena Quambusch
title	Cellular model system to dissect the isoform-selectivity of Akt inhibitors
title_short	Cellular model system to dissect the isoform-selectivity of Akt inhibitors
title_full	Cellular model system to dissect the isoform-selectivity of Akt inhibitors
title_fullStr	Cellular model system to dissect the isoform-selectivity of Akt inhibitors
title_full_unstemmed	Cellular model system to dissect the isoform-selectivity of Akt inhibitors
title_sort	cellular model system to dissect the isoform-selectivity of akt inhibitors
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/e9d5b9b56b6e4d8f9a3489c70c876e8e
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Cellular model system to dissect the isoform-selectivity of Akt inhibitors

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