Research datakeyboard_double_arrow_right Bioentity 30 Sep 2013Funded by:WT | Open access research to p..., WT | Identification of atypica..., NIH | Molecular and functional ... +1 projects

Authors: 2 c. H. Arrowsmith; A. M. Edwards; C. Bountra; A. Bullock;

structure of the kinase domain of human ripk2 in complex with ponatinib

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6 Research products, page 1 of 1

Regulatory spine RS3 residue of protein kinases: a lipophilic bystander or a decisive element in the small-molecule kinase inhibitor binding?
2022IsRelatedTo
Inflammatory Signaling by NOD-RIPK2 Is Inhibited by Clinically Relevant Type II Kinase Inhibitors
2015IsSupplementedBy
Inflammatory Signaling by NOD-RIPK2 Is Inhibited by Clinically Relevant Type II Kinase Inhibitors
2015IsRelatedTo
Discovery of a cooperative mode of inhibiting RIPK1 kinase
2021IsRelatedTo
Structure of LRRK2 in Parkinson’s disease and model for microtubule interaction
2020IsRelatedTo
Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor–associated kinase 4 (IRAK4)
2019IsRelatedTo

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structure of the kinase domain of human ripk2 in complex with ponatinib

structure of the kinase domain of human ripk2 in complex with ponatinib

6 Research products, page 1 of 1

Regulatory spine RS3 residue of protein kinases: a lipophilic bystander or a decisive element in the small-molecule kinase inhibitor binding?

Inflammatory Signaling by NOD-RIPK2 Is Inhibited by Clinically Relevant Type II Kinase Inhibitors

Inflammatory Signaling by NOD-RIPK2 Is Inhibited by Clinically Relevant Type II Kinase Inhibitors

Discovery of a cooperative mode of inhibiting RIPK1 kinase

Structure of LRRK2 in Parkinson’s disease and model for microtubule interaction

Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor–associated kinase 4 (IRAK4)