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Elizabeth A. Gordon

Researcher at University of California, Irvine

Publications -  8
Citations -  287

Elizabeth A. Gordon is an academic researcher from University of California, Irvine. The author has contributed to research in topics: Docking (molecular) & Mitogen-activated protein kinase. The author has an hindex of 6, co-authored 7 publications receiving 243 citations. Previous affiliations of Elizabeth A. Gordon include Massachusetts Institute of Technology.

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Computational prediction and experimental verification of new MAP kinase docking sites and substrates including Gli transcription factors.

TL;DR: A hybrid computational search algorithm is developed that combines machine learning and expert knowledge to identify kinase docking sites, and this algorithm is used to search the human genome for novel MAP kinase substrates and regulators focused on the JNK family of MAP kinases.
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On-demand dissolution of modular, synthetic extracellular matrix reveals local epithelial-stromal communication networks

TL;DR: A modular, synthetic, and dissolvable extracellular matrix (MSD-ECM) hydrogel that fosters functional 3D epithelial-stromal co-culture, and that can be dissolved on-demand to recover cells and paracrine signaling proteins intact for subsequent analysis, has potential as a tool in identifying and validating therapeutic targets in complex diseases.
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The Grainyhead transcription factor Grhl3/Get1 suppresses miR-21 expression and tumorigenesis in skin: modulation of the miR-21 target MSH2 by RNA-binding protein DND1

TL;DR: Findings indicate that decreased Grhl3 expression contributes to tumor progression and upregulation of the oncomir miR-21 in squamous cell carcinoma of the skin.
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Combining docking site and phosphosite predictions to find new substrates: identification of smoothelin-like-2 (SMTNL2) as a c-Jun N-terminal kinase (JNK) substrate.

TL;DR: A novel JNK substrate that emerged from this analysis is described, the functionally uncharacterized protein smoothelin-like 2 (SMTNL2), which bound with high-affinity to multiple MAPKs including JNK1-3 and ERK2 and was expressed in many mammalian tissues.
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CK2 activates kinesin via induction of a conformational change

TL;DR: Kinesin inactivation results from a conformational change that causes the neck linker to be positioned closer to the motor domain and treatment of kinesin with CK2 prevents and reverses this repositioning, and CK2 treatment facilitates ADP dissociation from the motor, resulting in a nucleotide-free state that promotes microtubule binding.