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1. Çмú»ó (KSMCB Academic Research Awards)

 
Á¦22ȸ ¼ö»óÀÚ (2023³â) Á¦21ȸ ¼ö»óÀÚ (2022³â) Á¦20ȸ ¼ö»óÀÚ (2021³â)
Á¦19ȸ ¼ö»óÀÚ (2020³â) Á¦18ȸ ¼ö»óÀÚ (2019³â) Á¦17ȸ ¼ö»óÀÚ (2018³â) Á¦16ȸ ¼ö»óÀÚ (2017³â)
Á¦15ȸ ¼ö»óÀÚ (2016³â) Á¦14ȸ ¼ö»óÀÚ (2015³â) Á¦13ȸ ¼ö»óÀÚ (2014³â) Á¦12ȸ ¼ö»óÀÚ (2013³â)
Á¦11ȸ ¼ö»óÀÚ (2012³â) Á¦10ȸ ¼ö»óÀÚ (2011³â) Á¦9ȸ ¼ö»óÀÚ (2010³â) Á¦8ȸ ¼ö»óÀÚ (2009³â)
Á¦7ȸ ¼ö»óÀÚ (2008³â) Á¦6ȸ ¼ö»óÀÚ (2007³â) Á¦5ȸ ¼ö»óÀÚ (2006³â) Á¦4ȸ ¼ö»óÀÚ (2005³â)
Á¦3ȸ ¼ö»óÀÚ (2004³â) Á¦2ȸ ¼ö»óÀÚ (2003³â) Á¦1ȸ ¼ö»óÀÚ (2002³â) ¸ñ¾Ï»ý¸í°úÇлó
(1994³â-2000³â)
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Dr. Dae-Sik Lim is a professor in the Department of Biological Sciences at KAIST. He received his bachelor's degree and master's degree in Seoul National University, and a Ph.D. degree in the Genes and Developmental Program at U.T & M. D. Anderson Cancer Center in 1996. During his graduate studies in the laboratory of Dr. Paul Hasty, he investigated the function of two proteins, Rad51 and Ku80, in the repair of DNA damage in mice. During his postdoctoral training under the guidance of Dr. Michael Kastan at Johns Hopkins and St. Jude Children's Research Hospital, he characterized functions of the ATM kinase and identified many substrates for ATM kinases in DNA damage response pathway. He joined Korea University as an assistant Professor in 2000 and moved to KAIST in 2002. Since then, he has been interested in understanding the regulatory mechanisms underlying control of cell proliferation and tumor suppression. His initial studies characterized the roles of the tumor suppressor protein RASSF1A and identified its associated proteins which were key molecules (MST1/2, SAV1/WW45, LATS1/2 and YAP) of the "Hippo signaling pathway". Thereafter, he has focused on understanding the roles and mechanism of action of Hippo signaling pathway, which is a key player both in the control of cell proliferation, and organ development as well as tumor suppression. He was one of the pioneers to reveal the functions of mammalian hippo signaling pathway by generating various tissue-specific knockout mice (Mst1/2, Sav1, Lats1/2 etc) and analyzing their phenotypes. His group demonstrated that Hippo signaling pathway controls stem/progenitor cell proliferation, cell fate determination and differentiation by inhibiting YAP/TAZ activity in epithelial organs. His group also revealed that the actin cytoskeletal changes regulate the Hippo-YAP pathway via cAMP/PKA and SRF-IL6 functions as a critical mediator of YAP-induced stem cell properties in mammary epithelial cells. His current studies are attempting to shed light on the roles of the Hippo signaling pathway in the regulation of adult stem/progenitor cell properties, organ development and tissue regeneration.

Representative papers
- Lats-Yap/Taz controls lineage specification by regulating Tgf¥â signaling and Hnf4¥á expression during liver development. (2016). Nature Communications. 10.1038/ncomms11961
- A basal-like breast cancer-specific role for SRF-IL6 in YAP-induced cancer stemness. (2015) Nature Communications. 10.1038/NCOMMS10186
- cAMP/PKA signaling reinforces the LATS-YAP pathway to fully suppress YAP in response to actin cytoskeletal changes. (2013) The EMBO Journal. 32, 1543-1555
- ER71 acts downstream of BMP, Notch, and Wnt signaling in blood and vessel progenitor specification. (2008) Cell Stem Cell. 2(5):497-507.
- The tumour suppressor RASSF1A regulates mitosis by inhibiting the APC-Cdc20 complex. (2004) Nature Cell Biology. 6(2):129-37

   

Çѱ¹ºÐÀÚ·¼¼Æ÷»ý¹°ÇÐȸ Çмú»ó Molecules and Cells (M&C) ¿ì¼ö³í¹®»ó ¼ö»óÀÚ

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MicroRNA-26a Regulates RANKL-Induced Osteoclast Formation (2015). Mol. Cells 38(1), 75-80.

Osteoclasts are unique cells responsible for the resorption of bone matrix. MicroRNAs (miRNAs) are involved in the regulation of a wide range of physiological processes. In this study, we examined the role of miR-26a in RANKL-induced osteoclastogenesis. The expression of miR-26a was up-regulated by RANKL during osteoclastogenesis. Ectopic expression of miR-26a mimic in osteoclast precursor cells attenuated osteoclast formation, actin-ring formation, and bone resorption by suppressing the expression of CTGF, which can promote osteoclast formation via up-regulation of DC-STAMP. On the other hand, overexpression of miR-26a inhibitor enhanced RANKL-induced osteoclast formation and function as well as CTGF expression. In addition, the inhibitory effect of miR-26a on osteoclast formation and function was prevented by treatment with recombinant CTGF. Collectively, our results suggest that miR-26a modulates osteoclast formation and function through the regulation of CTGF.

   

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