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Kotb Abdelmohsen

Researcher at National Institutes of Health

Publications -  163
Citations -  21231

Kotb Abdelmohsen is an academic researcher from National Institutes of Health. The author has contributed to research in topics: RNA-binding protein & Gene silencing. The author has an hindex of 63, co-authored 145 publications receiving 17825 citations. Previous affiliations of Kotb Abdelmohsen include Catalan Institution for Research and Advanced Studies & University of Maryland, Baltimore.

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miR-519 suppresses tumor growth by reducing HuR levels.

TL;DR: Evidence that the miR-519-elicited reduction of HuR was critical for its tumor suppressor influence was obtained by reducing HuR, as HuR-silenced cells formed markedly smaller tumors and were unable to form large tumors even after lowering miR -519 abundance.
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Emerging roles and context of circular RNAs.

TL;DR: The emerging functions of circRNAs, including RNA transcription, splicing, turnover, and translation are discussed, including circRNA abundance, subcellular localization, interacting partners, dynamic changes in interactions following stimulation, and potential circRNA translation.
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High-purity circular RNA isolation method (RPAD) reveals vast collection of intronic circRNAs.

TL;DR: A novel method for the isolation of highly pure circRNA populations involving RNase R treatment followed by Polyadenylation and poly(A)+ RNA Depletion (RPAD), which removes linear RNA to near completion is described.
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Enhanced translation by Nucleolin via G-rich elements in coding and non-coding regions of target mRNAs

TL;DR: Nucleolin binds G-rich sequences in the CR and UTRs of target mRNAs, many of which encode cancer proteins, and enhances their translation, particularly in the coding region (CR) and 5′-UTR.
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Epidermal Growth Factor Receptor Is a Common Mediator of Quinone-induced Signaling Leading to Phosphorylation of Connexin-43: ROLE OF GLUTATHIONE AND TYROSINE PHOSPHATASES *

TL;DR: Rat liver epithelial cells were exposed to three quinones with different properties, and EGFR-dependent signaling was mediated by protein-tyrosine phosphatase inactivation, GSH depletion (BQ), and redox-cycling (DMNQ), funneling into the same signaling pathway.