M
Michael S. Kilberg
Researcher at University of Florida
Publications - 175
Citations - 12412
Michael S. Kilberg is an academic researcher from University of Florida. The author has contributed to research in topics: Amino acid & Asparagine synthetase. The author has an hindex of 57, co-authored 170 publications receiving 11313 citations. Previous affiliations of Michael S. Kilberg include Louisiana State University & University of Michigan.
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Journal ArticleDOI
ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
Jaeseok Han,Sung Hoon Back,Junguk Hur,Yu Hsuan Lin,Robert D. Gildersleeve,Jixiu Shan,Celvie L. Yuan,Dawid Krokowski,Shiyu Wang,Maria Hatzoglou,Michael S. Kilberg,Maureen A. Sartor,Randal J. Kaufman +12 more
TL;DR: It is shown that eIF2α-phosphorylation-attenuated protein synthesis, and not Atf4 mRNA translation, promotes cell survival, and suggesting that limiting protein synthesis will be therapeutic for diseases caused by protein misfolding in the ER.
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ATF4-dependent transcription mediates signaling of amino acid limitation.
TL;DR: This review outlines the ATF4-dependent transcriptional mechanisms associated with the AAR, focusing on progress during the past 5 years, and describes the transcriptional programs initiated by amino acid limitation.
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A Caveolar Complex between the Cationic Amino Acid Transporter 1 and Endothelial Nitric-oxide Synthase May Explain the “Arginine Paradox”
TL;DR: Direct transfer of extracellular arginine to membrane-bound eNOS accounts for the “arginine paradox” and explains why caveolar localization of eNos is required for optimal nitric oxide production by endothelial cells.
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The regulation of neutral amino acid transport in mammalian cells.
TL;DR: I.II1.
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Characteristics of an amino acid transport system in rat liver for glutamine, asparagine, histidine, and closely related analogs.
TL;DR: Especially significant in view of the importance of glutamine metabolism are an insensitivity of the new system to stimulation by either insulin or glucagon, and its distinct enhancement on starvation of the cells with respect to amino acids, suggesting a second system has been found to show adaptive regulation.