https://scholar.dgist.ac.kr/handle/20.500.11750/265 2026-05-26T21:44:37Z https://scholar.dgist.ac.kr/handle/20.500.11750/60358 Title: Juvenile-to-adult refinement of thalamic reticular circuits via LRRTM3 enables high-resolution sensory encoding Author(s): Lee, Dongsu; Han, Kyung Ah; Jeong, Hyeonyeong; Ha, Go Eun; Lee, Hyeongjin; Kim, Beom Soo; Park, Chanmi; Piao, Yao; Lee, Haeun; Kim, Joon; Yoon, Taek Han; Kim, Seungjoon; Kim, Byeongchan; Shin, Jungsu; Cho, Yujin; Kang, Sunghyun; Park, Han-Eol; Um, Ji Won; Sohn, Chang Ho; Huguenard, John R.; Ko, Jaewon; Cheong, Eunji Abstract: Sensory processing enables adaptive behavior by accurately encoding dynamic environmental stimuli. Within thalamocortical (TC) circuits, the thalamic reticular nucleus (TRN) functions as a key inhibitory gate that regulates cortical access to sensory input. While classical models posit that sensory circuits stabilize after early critical periods, we uncover a previously unrecognized phase of synaptic refinement in TRN circuitry extending from the juvenile period into adulthood. This late-stage remodeling is driven by a progressive reduction in corticothalamic (CT) excitatory input and is essential for enhancing sensory gain, response linearity, and stimulus discriminability. We identify LRRTM3, a TRN-enriched synaptic adhesion molecule, as a molecular gatekeeper of this process. TRN-specific deletion of LRRTM3 disrupts CT–TRN refinement, elevates TRN-mediated inhibition, and impairs fine tactile discrimination. These findings revise canonical views of sensory circuit maturation, revealing that LRRTM3-mediated juvenile-to-adult TRN plasticity is essential for the emergence of high-resolution sensory encoding in the adult brain. 2026-03-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/60353 Title: MLPH-mediated activation of dermal papilla IGF-1 signaling drives human hair shaft elongation and anagen induction Author(s): Kwack, Mi Hee; Kang, Eunho; Kim, Jewoo; Ji, Youngheum; Ju, Hyeonchang; Lee, Chang-Hun; Sung, Young Kwan; Kim, So Yeon; Moon, Cheil Abstract: Introduction Hair loss (alopecia) is a multifactorial disorder that often causes distress. Approved therapies such as minoxidil and finasteride act indirectly and do not specifically target hair follicle (HF) cells. Erythropoietin (EPO), however, has been shown to activate dermal papilla (DP) cells via the erythropoietin receptor (EPOR), suggesting a potential role in hair follicle regeneration and hair growth. Objectives This study aimed to develop and validate Helix C-1–based EPO-derived peptides that activate DP cells and increase IGF-1 expression, while not inducing overt systemic erythropoietic effects (e.g., increases in red blood cell counts, reticulocytes, hemoglobin, or hematocrit) under the tested experimental conditions. Methods Peptides derived from the Helix C-1 region of EPO were synthesized and characterized by EPOR-binding affinity, CD spectroscopy, and ERK/AKT activation. In vitro, DP-cell metabolic activity, proliferation, and IGF-1 secretion were assessed. Ex vivo efficacy was evaluated by hair shaft elongation in hair follicle organ culture, and in vivo efficacy was tested in a murine depilation-induced anagen model with concurrent hematologic assessment to exclude erythropoiesis-related effects. Results The peptides increased DP-cell metabolic activity and proliferation, reduced oxidative stress, and enhanced IGF-1 production via EPOR-mediated ERK/AKT activation. They promoted hair shaft elongation ex vivo and promoted anagen entry in mice without significant changes in standard hematologic parameters under the tested dosing regimen. Conclusion These findings support the conclusion that MLPH promotes hair growth via an EPOR-linked, IGF-1–dependent mechanism in DP cells. Future pharmacokinetic and disease-model studies are warranted to evaluate its translational potential. © 2026 The Authors. 2026-02-28T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/60291 Title: Accurate conformational ensembles of intrinsically disordered proteins using reweighting based on NMR chemical shifts Author(s): Jeon, Juhyeong; Yang, Wonjin; Park, Sangmin; Kim, Jin Hae; Lee, Young-Ho; Yu, Wookyung Abstract: Intrinsically disordered proteins and protein regions (IDRs) underpin a wide range of vital biological processes but exhibit dynamic and heterogeneous conformations. Currently, many computational efforts seek to elucidate the conformational ensembles of these disordered proteins, yet most methods still struggle to fully capture their structural diversity. Here, we integrate structural libraries of various IDRs—derived from coarse-grained molecular dynamics (MD) simulations and machine learning models—with experimental chemical shifts obtained from NMR spectroscopy. Through a maximum entropy reweighting approach, we obtain reliable ensembles that more accurately reflect observed chemical shifts and reveal transient states. Our results highlight the importance of comprehensive sampling strategies for capturing diverse conformational states. Furthermore, we show that these weighted ensembles faithfully track conformational rearrangements under various conditions such as temperature, mutational effects, and environment, which are not fully captured by experiments alone. This approach provides a dataset encompassing each IDR’s specific structures along with their weights, offering a foundation for systematically exploring IDR structural landscapes, refining our understanding of their functional roles, and shedding light on processes related to misfolding and aggregation. Copyright © 2026 the Author(s). 2026-01-31T15:00:00Z https://scholar.dgist.ac.kr/handle/20.500.11750/60241 Title: RITA 또는 이의 유도체를 포함하는 뇌신경계 질환 예방 또는 치료용 조성물 Author(s): 정성희; 유성운