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Lila Kim

Researcher at Korea Research Institute of Bioscience and Biotechnology

Publications -  11
Citations -  793

Lila Kim is an academic researcher from Korea Research Institute of Bioscience and Biotechnology. The author has contributed to research in topics: Schizosaccharomyces pombe & Downregulation and upregulation. The author has an hindex of 7, co-authored 9 publications receiving 702 citations. Previous affiliations of Lila Kim include Chungnam National University.

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Journal ArticleDOI

The Fission Yeast GATA Factor, Gaf1, Modulates Sexual Development via Direct Down-Regulation of ste11+ Expression in Response to Nitrogen Starvation

TL;DR: Gaf1 provides the prime example for negative regulation of ste11+ transcription through direct binding to a cis-acting motif of its promoter, and binds to the canonical GATA motif spanning from −371 to −366 in Ste11+ promoter.
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PPARγ activation abolishes LDL-induced proliferation of human aortic smooth muscle cells via SOD-mediated down-regulation of superoxide

TL;DR: The first report of PPARgamma activation by troglitazone (TG) exerting its inhibitory effects on LDL-induced cell proliferation via generation not of H(2)O(2), but of O2(.-), and the subsequent activation of Erk1/2 in hAoSMCs suggests that the regulation of O 2(.-) is located at the crossroads between LDL signaling and cell proliferation.
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PPARα activation abolishes LDL-stimulated IL-8 production via AP-1 deactivation in human aortic smooth muscle cells

TL;DR: It is shown, for the first time, that the peroxisome proliferator-activated receptor (PPARα) agonist, fenofibrate, completely abolishes the LDL-induced IL-8 up-regulation at the transcriptional level.
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Activation of PKCβII and PKCθ is essential for LDL-induced cell proliferation of human aortic smooth muscle cells via Gi-mediated Erk1/2 activation and Egr-1 upregulation

TL;DR: It is reported that LDL translocated PKCbeta(II) and PKCtheta from cytosol to plasma membrane, and inhibition of PKC beta(II), PKC theta, and GPCR decreased LDL effects via the deactivation of Erk1/2, suggesting that Gi protein plays a role in LDL effects.