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Irina Tchernyshyov

Researcher at Cedars-Sinai Medical Center

Publications -  16
Citations -  6247

Irina Tchernyshyov is an academic researcher from Cedars-Sinai Medical Center. The author has contributed to research in topics: Cancer cell & Proteome. The author has an hindex of 10, co-authored 15 publications receiving 5499 citations. Previous affiliations of Irina Tchernyshyov include Johns Hopkins University & Johns Hopkins University School of Medicine.

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HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia

TL;DR: A hypoxia-induced metabolic switch that shunts glucose metabolites from the mitochondria to glycolysis to maintain ATP production and to prevent toxic ROS production is revealed.
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c-Myc suppression of miR-23a/b enhances mitochondrial glutaminase expression and glutamine metabolism.

TL;DR: In this paper, the c-Myc (hereafter referred to as Myc) oncogenic transcription factor, which is known to regulate microRNAs and stimulate cell proliferation, transcriptionally represses miR-23a and miR23b, resulting in greater expression of their target protein, mitochondrial glutaminase, in human P-493 B lymphoma cells and PC3 prostate cancer cells.
Journal Article

Abstract #LB-186: c-Myc suppression of miR-23 enhances mitochondrial glutaminase and glutamine metabolism

TL;DR: The c-Myc oncogenic transcription factor, which is known to regulate microRNAs and stimulate cell proliferation, transcriptionally represses miR-23a and miB-23b, resulting in greater expression of their target protein, mitochondrial glutaminase, in human P-493 B lymphoma cells and PC3 prostate cancer cells, which leads to upregulation of glutamine catabolism.
Journal Article

Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) Is Pyruvylated during 3-Bromopyruvate Mediated Cancer Cell Death

TL;DR: GAPDH pyruvylation by 3BrPA affects its enzymatic function and is the primary intracellular target in 2D gel electrophoretic autoradiography, mass spectrometry and immunoprecipitation.
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The Mouse C2C12 Myoblast Cell Surface N-Linked Glycoproteome IDENTIFICATION, GLYCOSITE OCCUPANCY, AND MEMBRANE ORIENTATION

TL;DR: The strategy and data presented shed new light on the complexity of the myoblast cell surface subproteome and reveal new targets for the clinically important characterization of cell intermediates during myOBlast differentiation into myotubes.