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Christian Grütter

Researcher at Technical University of Dortmund

Publications -  25
Citations -  2952

Christian Grütter is an academic researcher from Technical University of Dortmund. The author has contributed to research in topics: Kinase & MAP2K7. The author has an hindex of 21, co-authored 25 publications receiving 2610 citations. Previous affiliations of Christian Grütter include Max Planck Society & Vanderbilt University.

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Integrative genome analyses identify key somatic driver mutations of small-cell lung cancer

Martin Peifer, +94 more
- 01 Oct 2012 - 
TL;DR: This study implicates histone modification as a major feature of SCLC, reveals potentially therapeutically tractable genomic alterations and provides a generalizable framework for the identification of biologically relevant genes in the context of high mutational background.
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Natural-product-derived fragments for fragment-based ligand discovery.

TL;DR: A library of 2,000 natural-product-derived fragments with high structural diversity, which resemble the properties of the natural products themselves and give access to novel inhibitor chemotypes are produced.
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ALK Mutations Conferring Differential Resistance to Structurally Diverse ALK Inhibitors

TL;DR: The results show that different ALK resistance mutations as well as different AlK inhibitors impact the therapeutic efficacy in the setting of EML4–ALK fusions and ALK mutations.
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Strategies for the Selective Regulation of Kinases with Allosteric Modulators: Exploiting Exclusive Structural Features

TL;DR: This review highlights various strategies that have been developed to utilizing exclusive structural features of kinases and thereby modulating their activity allosterically and thought to provide various advantages such as higher selectivity and extended drug target residence times.
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Development of a fluorescent-tagged kinase assay system for the detection and characterization of allosteric kinase inhibitors.

TL;DR: A fluorescence-based kinase binding assay for identifying and characterizing ligands which stabilize the inactive kinase conformation is developed and validation of this assay using the serine/threonine kinase p38alpha is presented.