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Yuliya Skorobogatko

Researcher at University of California, San Diego

Publications -  17
Citations -  1349

Yuliya Skorobogatko is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Imatinib mesylate & Glucose transporter. The author has an hindex of 11, co-authored 16 publications receiving 1127 citations. Previous affiliations of Yuliya Skorobogatko include Fox Chase Cancer Center & Drexel University.

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Increasing O -GlcNAc slows neurodegeneration and stabilizes tau against aggregation

TL;DR: Using in vitro biochemical aggregation studies, it is found that O-GlcNAc modification, on its own, hinders tau oligomerization and inhibits thermally induced aggregation of an unrelated protein, TAK-1 binding protein, suggesting that a basic biochemical function of O- GladiatorNAc may be to prevent protein aggregation.
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TBK1 at the Crossroads of Inflammation and Energy Homeostasis in Adipose Tissue.

TL;DR: It is reported that the kinase uniquely controls energy metabolism, and a unique role for TBK1 in mediating bidirectional crosstalk between energy sensing and inflammatory signaling pathways in both over- and undernutrition.
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In Vivo Modulation of O-GlcNAc Levels Regulates Hippocampal Synaptic Plasticity through Interplay with Phosphorylation *

TL;DR: O-GlcNAc is a novel regulatory signaling component of excitatory synapses, with specific roles in synaptic plasticity that involve interplay with phosphorylation.
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Analysis of KIT mutations in sporadic and familial gastrointestinal stromal tumors: therapeutic implications through protein modeling.

TL;DR: Why patients with GIST tumors containing exon 11 mutations are the most responsive to imatinib mesylate treatment is clarified, and a novel germ-line mutation in KIT was identified that is associated with an autosomal dominant predisposition to the development of GIST.
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Mapping O -GlcNAc modification sites on tau and generation of a site-specific O -GlcNAc tau antibody

TL;DR: A method for the production of recombinant O-GlcNAc modified tau is described and, using this tau, sites of O- GlcNAC on tau are mapped using mass spectrometry and detected in rat brain, which confirms the validity of this in vitro mapping approach.