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Avital Eisenberg-Lerner
Researcher at Weizmann Institute of Science
Publications - 25
Citations - 7184
Avital Eisenberg-Lerner is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Medicine & Autophagy. The author has an hindex of 12, co-authored 20 publications receiving 6523 citations.
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Metabolic alterations in the tumor microenvironment and their role in oncogenesis.
TL;DR: The association between the reprogramming of glucose metabolism in the TME and oncogenic signaling and its reflection in the non-canonical functions of metabolic enzymes is discussed and special emphasis is given in this regard to lysophosphatidic acid (LPA) and adenosine, two powerful metabolites, the concentrations of which rise in theTME due to altered metabolism of the tumor and its surrounding cells.
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Post-translational modification profiling – A novel tool for mapping the protein modification landscape in cancer
TL;DR: This mini-review discusses common proteomic methodologies applied to studying the ubiquitome, and focuses on the recently developed post-translational modification (PTM) profiling approach, which is a functional assay, amenable to biochemical manipulation, which allows the detection of protein modifications in a high-throughput manner.
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PKD at the crossroads of necrosis and autophagy.
TL;DR: DAPK and PKD are identified by demonstrating their role in the process of autophagy in general, and specifically during oxidative stress, by associating with and phosphorylating VPS34, leading to its activation.
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DAPk silencing by DNA methylation conveys resistance to anti EGFR drugs in lung cancer cells.
TL;DR: This data indicates that T-cell reprograming may be a viable alternative to conventional “spatially aggregating” chemotherapy for wound healing and may also have important implications for regenerative medicine.
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Histone degradation by the proteasome regulates chromatin and cellular plasticity
TL;DR: In this paper, the authors discuss proteasome-dependent degradation of histones and the protein modifications associated with it, and highlight specific cellular and physiological states that are associated with altered histone degradation by cellular proteasomes.