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Jane E. Ishmael

Researcher at Oregon State University

Publications -  49
Citations -  7143

Jane E. Ishmael is an academic researcher from Oregon State University. The author has contributed to research in topics: Myosin & Myosin light-chain kinase. The author has an hindex of 20, co-authored 44 publications receiving 6521 citations. Previous affiliations of Jane E. Ishmael include University of Maryland, Baltimore & Oregon Health & Science University.

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Depsipeptide Companeramides from a Panamanian Marine Cyanobacterium Associated with the Coibamide Producer

TL;DR: Two new cyclic depsipeptides, companeramides A (1) and B (2) showed high nanomolar in vitro antiplasmodial activity but were not overtly cytotoxic to four human cancer cell lines at the doses tested.
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Direct interaction of myosin regulatory light chain with the NMDA receptor.

TL;DR: Myosin RLC–NMDA receptor interactions may contribute to the contractile and motile forces that are placed upon NMDA receptor subunits during changes associated with synaptic plasticity and neural morphogenesis.
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Coibamide A, a natural lariat depsipeptide, inhibits VEGFA/VEGFR2 expression and suppresses tumor growth in glioblastoma xenografts

TL;DR: Comparisons between coibamide A- and apratoxin A-induced changes in cell morphology, decreases in VEGFR2 expression and macroautophagy signaling in HUVECs raise the possibility that both cyanobacterial natural products share a common mechanism of action.
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Coibamide A Targets Sec61 to Prevent Biogenesis of Secretory and Membrane Proteins

TL;DR: This work connecting CbA activity with selective prevention of secretory and membrane protein biogenesis by inhibition of Sec61 opens up possibilities for developing new Sec61 inhibitors with improved drug-like properties that are based on the coibamide pharmacophore.
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Heterodimeric Interactions between Chicken Ovalbumin Upstream Promoter-Transcription Factor Family Members ARP1 and Ear2

TL;DR: It is demonstrated that ARP1 and Ear2 form heterodimers in solution and on directly repeated response elements with high efficiency and a specificity differing from that of homodimeric complexes composed of either receptor.