Philip LoGrasso
Scripps Research Institute
94 Papers
1.2K Citations
Philip LoGrasso is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Kinase & Rho-associated protein kinase. The author has an hindex of 38, co-authored 94 publications. Previous affiliations of Philip LoGrasso include Lawrence Berkeley National Laboratory & United States Military Academy.
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Papers
Discovery of Potent and Selective Covalent Inhibitors of JNK
Tinghu Zhang,Francisco Inesta-Vaquera,Mario Niepel,Jianming Zhang,Scott B. Ficarro,Thomas Machleidt,Ting Xie,Jarrod A. Marto,Namdoo Kim,Taebo Sim,John D. Laughlin,HaJeung Park,Philip LoGrasso,Matthew P. Patricelli,Tyzoon K. Nomanbhoy,Peter K. Sorger,Dario R. Alessi,Nathanael S. Gray +17 more
TL;DR: JNK-IN-8 is a selective JNK inhibitor that inhibits phosphorylation of c-Jun, a direct substrate of JNK, in cells exposed to submicromolar drug in a manner that depends on covalent modification of the conserved cysteine residue.
358
Rho Kinase (ROCK) Inhibitors and Their Therapeutic Potential
TL;DR: A comprehensive review of the physiological and biological functions for ROCK, the properties and development of over 170 ROCK inhibitors as well as their therapeutic potential, the current status, and future considerations are presented.
337
Signalling for survival and death in neurones: the role of stress-activated kinases, JNK and p38.
Sarah J. Harper,Philip LoGrasso +1 more
TL;DR: The evidence that these pathways are important in neuronal cell death is examined and the evidence that inhibitors of these pathways have a neuroprotective effect both in vitro and in vivo is reviewed.
318
Mitochondrial c-Jun N-terminal Kinase (JNK) Signaling Initiates Physiological Changes Resulting in Amplification of Reactive Oxygen Species Generation
TL;DR: It is demonstrated that a sequence of events exist for JNK mitochondrial signaling whereby ROS activates JNK, thereby affecting mitochondrial physiology, which can have effects on cell survival and death.
185
The structure of JNK3 in complex with small molecule inhibitors: structural basis for potency and selectivity
TL;DR: Four crystal structures of JNK3 in complex with three different classes of inhibitors provide a clear picture of the interactions that each class of compound made with the kinase provides for structure-guided modification of these compounds.
128