E
Eidarus Salah
Researcher at University of Oxford
Publications - 58
Citations - 1783
Eidarus Salah is an academic researcher from University of Oxford. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 12, co-authored 48 publications receiving 1412 citations. Previous affiliations of Eidarus Salah include Mansfield University of Pennsylvania & Structural Genomics Consortium.
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Journal ArticleDOI
Stereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategy
Kilian Huber,Eidarus Salah,Branka Radic,Manuela Gridling,Jonathan M. Elkins,Alexey Stukalov,Ann-Sofie Jemth,Camilla Göktürk,Kumar Sanjiv,Kia Strömberg,Therese Pham,Ulrika Warpman Berglund,Jacques Colinge,Keiryn L. Bennett,Joanna I. Loizou,Thomas Helleday,Stefan Knapp,Giulio Superti-Furga +17 more
TL;DR: Disruption of nucleotide pool homeostasis via MTH1 inhibition by (S)-crizotinib induced an increase in DNA single-strand breaks, activated DNA repair in human colon carcinoma cells, and effectively suppressed tumour growth in animal models.
Journal ArticleDOI
Comprehensive characterization of the Published Kinase Inhibitor Set
Jonathan M. Elkins,Vita Fedele,M. Szklarz,Kamal R. Abdul Azeez,Eidarus Salah,Jowita Mikolajczyk,Sergei Romanov,Nikolai Sepetov,Xi Ping Huang,Bryan L. Roth,Ayman Al Haj Zen,Denis Fourches,Eugene N. Muratov,Alexander Tropsha,Joel Morris,Beverly A. Teicher,Mark Kunkel,Eric C. Polley,Karen Lackey,Francis Atkinson,John P. Overington,John P. Overington,Paul Bamborough,Susanne Müller,Daniel J. Price,Timothy M. Willson,Timothy M. Willson,David H. Drewry,David H. Drewry,Stefan Knapp,Stefan Knapp,William J. Zuercher,William J. Zuercher +32 more
TL;DR: A thorough characterization of the Published Kinase Inhibitor Set is provided and chemical starting points for designing new chemical probes of orphan kinases are identified and the utility of these leads are illustrated by developing a selective inhibitor for the previously untargeted kinases LOK and SLK.
Journal ArticleDOI
Structure of the Camkiidelta/Calmodulin Complex Reveals the Molecular Mechanism of Camkii Kinase Activation.
P. Rellos,Ashley C. W. Pike,Frank H. Niesen,Eidarus Salah,Wen Hwa Lee,Frank von Delft,Stefan Knapp +6 more
TL;DR: Structural and biophysical studies reveal how CaMKII kinases, which are important for cellular learning and memory, are switched on by binding of Ca2+/calmodulin.
Journal ArticleDOI
Structural Coupling of SH2-Kinase Domains Links Fes and Abl Substrate Recognition and Kinase Activation
Panagis Filippakopoulos,Michael Kofler,Oliver Hantschel,Gerald D. Gish,Florian Grebien,Eidarus Salah,Philipp Neudecker,Lewis E. Kay,Benjamin E. Turk,Giulio Superti-Furga,Tony Pawson,Tony Pawson,Stefan Knapp,Stefan Knapp +13 more
TL;DR: The structure of the prototypic SH2-kinase unit of the human Fes tyrosine kinase, which appears specialized for positive signaling, is solved and it is found that the SH2 domain of the active Abl kinase stimulates catalytic activity and substrate phosphorylation through a distinct SH2 -kinase interface.
Journal ArticleDOI
Salt-Inducible Kinase 2 Couples Ovarian Cancer Cell Metabolism with Survival at the Adipocyte-Rich Metastatic Niche.
Fabrizio Miranda,David Mannion,Shujuan Liu,Yiyan Zheng,Lingegowda S. Mangala,Clara Redondo,Sandra Herrero-Gonzalez,Ruoyan Xu,Charlotte Taylor,Donatien Fotso Chedom,Mohammad KaramiNejadRanjbar,Ashwag Albukhari,Ashwag Albukhari,Dahai Jiang,Sunila Pradeep,Cristian Rodriguez-Aguayo,Gabriel Lopez-Berestein,Eidarus Salah,Kamal R. Abdul Azeez,Jonathan M. Elkins,Leticia Campo,Kevin A. Myers,Daniel Klotz,Serena Bivona,Sunanda Dhar,Robert C. Bast,Hideyuki Saya,Hwan Geun Choi,Nathanael S. Gray,Roman Fischer,Benedikt M. Kessler,Christopher Yau,Anil K. Sood,Takeshi Motohara,Stefan Knapp,Stefan Knapp,Ahmed Ashour Ahmed +36 more
TL;DR: This work shows that salt-inducible kinase 2 (SIK2) is overexpressed in adipocyte-rich metastatic deposits compared with ovarian primary lesions, and identifies SIK2 at the apex of the adipocytes-induced signaling cascades in cancer cells and makes a compelling case for targeting Sik2 for therapy in ovarian cancer.