Progress towards a public chemogenomic set for protein kinases and a call for contributions.

Protein kinases are highly tractable targets for drug discovery. However, the biological function and therapeutic potential of the majority of the 500+ human protein kinases remains unknown. We have developed physical and virtual collections of small molecule inhibitors, which we call chemogenomic s...

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Main Authors: David H Drewry, Carrow I Wells, David M Andrews, Richard Angell, Hassan Al-Ali, Alison D Axtman, Stephen J Capuzzi, Jonathan M Elkins, Peter Ettmayer, Mathias Frederiksen, Opher Gileadi, Nathanael Gray, Alice Hooper, Stefan Knapp, Stefan Laufer, Ulrich Luecking, Michael Michaelides, Susanne Müller, Eugene Muratov, R Aldrin Denny, Kumar S Saikatendu, Daniel K Treiber, William J Zuercher, Timothy M Willson
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2017-01-01
Series:PLoS ONE
Online Access:https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0181585&type=printable
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author David H Drewry
Carrow I Wells
David M Andrews
Richard Angell
Hassan Al-Ali
Alison D Axtman
Stephen J Capuzzi
Jonathan M Elkins
Peter Ettmayer
Mathias Frederiksen
Opher Gileadi
Nathanael Gray
Alice Hooper
Stefan Knapp
Stefan Laufer
Ulrich Luecking
Michael Michaelides
Susanne Müller
Eugene Muratov
R Aldrin Denny
Kumar S Saikatendu
Daniel K Treiber
William J Zuercher
Timothy M Willson
author_facet David H Drewry
Carrow I Wells
David M Andrews
Richard Angell
Hassan Al-Ali
Alison D Axtman
Stephen J Capuzzi
Jonathan M Elkins
Peter Ettmayer
Mathias Frederiksen
Opher Gileadi
Nathanael Gray
Alice Hooper
Stefan Knapp
Stefan Laufer
Ulrich Luecking
Michael Michaelides
Susanne Müller
Eugene Muratov
R Aldrin Denny
Kumar S Saikatendu
Daniel K Treiber
William J Zuercher
Timothy M Willson
author_sort David H Drewry
collection DOAJ
description Protein kinases are highly tractable targets for drug discovery. However, the biological function and therapeutic potential of the majority of the 500+ human protein kinases remains unknown. We have developed physical and virtual collections of small molecule inhibitors, which we call chemogenomic sets, that are designed to inhibit the catalytic function of almost half the human protein kinases. In this manuscript we share our progress towards generation of a comprehensive kinase chemogenomic set (KCGS), release kinome profiling data of a large inhibitor set (Published Kinase Inhibitor Set 2 (PKIS2)), and outline a process through which the community can openly collaborate to create a KCGS that probes the full complement of human protein kinases.
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issn 1932-6203
language English
publishDate 2017-01-01
publisher Public Library of Science (PLoS)
record_format Article
series PLoS ONE
spelling doaj-art-ca1842e46c3c4d9282fcf8bc425a50a82025-08-20T02:45:24ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01128e018158510.1371/journal.pone.0181585Progress towards a public chemogenomic set for protein kinases and a call for contributions.David H DrewryCarrow I WellsDavid M AndrewsRichard AngellHassan Al-AliAlison D AxtmanStephen J CapuzziJonathan M ElkinsPeter EttmayerMathias FrederiksenOpher GileadiNathanael GrayAlice HooperStefan KnappStefan LauferUlrich LueckingMichael MichaelidesSusanne MüllerEugene MuratovR Aldrin DennyKumar S SaikatenduDaniel K TreiberWilliam J ZuercherTimothy M WillsonProtein kinases are highly tractable targets for drug discovery. However, the biological function and therapeutic potential of the majority of the 500+ human protein kinases remains unknown. We have developed physical and virtual collections of small molecule inhibitors, which we call chemogenomic sets, that are designed to inhibit the catalytic function of almost half the human protein kinases. In this manuscript we share our progress towards generation of a comprehensive kinase chemogenomic set (KCGS), release kinome profiling data of a large inhibitor set (Published Kinase Inhibitor Set 2 (PKIS2)), and outline a process through which the community can openly collaborate to create a KCGS that probes the full complement of human protein kinases.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0181585&type=printable
spellingShingle David H Drewry
Carrow I Wells
David M Andrews
Richard Angell
Hassan Al-Ali
Alison D Axtman
Stephen J Capuzzi
Jonathan M Elkins
Peter Ettmayer
Mathias Frederiksen
Opher Gileadi
Nathanael Gray
Alice Hooper
Stefan Knapp
Stefan Laufer
Ulrich Luecking
Michael Michaelides
Susanne Müller
Eugene Muratov
R Aldrin Denny
Kumar S Saikatendu
Daniel K Treiber
William J Zuercher
Timothy M Willson
Progress towards a public chemogenomic set for protein kinases and a call for contributions.
PLoS ONE
title Progress towards a public chemogenomic set for protein kinases and a call for contributions.
title_full Progress towards a public chemogenomic set for protein kinases and a call for contributions.
title_fullStr Progress towards a public chemogenomic set for protein kinases and a call for contributions.
title_full_unstemmed Progress towards a public chemogenomic set for protein kinases and a call for contributions.
title_short Progress towards a public chemogenomic set for protein kinases and a call for contributions.
title_sort progress towards a public chemogenomic set for protein kinases and a call for contributions
url https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0181585&type=printable
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