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  <channel rdf:about="https://scholar.dgist.ac.kr/handle/20.500.11750/305">
    <title>Repository Community: null</title>
    <link>https://scholar.dgist.ac.kr/handle/20.500.11750/305</link>
    <description />
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        <rdf:li rdf:resource="https://scholar.dgist.ac.kr/handle/20.500.11750/61151" />
        <rdf:li rdf:resource="https://scholar.dgist.ac.kr/handle/20.500.11750/60947" />
        <rdf:li rdf:resource="https://scholar.dgist.ac.kr/handle/20.500.11750/58901" />
        <rdf:li rdf:resource="https://scholar.dgist.ac.kr/handle/20.500.11750/58220" />
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    <dc:date>2026-11-11T11:05:17Z</dc:date>
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  <item rdf:about="https://scholar.dgist.ac.kr/handle/20.500.11750/61151">
    <title>Why behavior lasts while neurons drift</title>
    <link>https://scholar.dgist.ac.kr/handle/20.500.11750/61151</link>
    <description>Title: Why behavior lasts while neurons drift
Author(s): Kim, Kyuhyung
Abstract: Traditional dogmas assume that executing a stable behavior requires neural circuits to remain in a fixed, steady state. However, recent population imaging reveals “representational drift”, a continuous, unprompted shifting of neural activity over time despite invariant behavioral outputs. This introduces a profound paradox where behavioral permanence must emerge from a volatile physical substrate. Here, I review how nervous systems maintain dynamic stability across diverse biological scales. In Caenorhabditis elegans, a structurally fixed connectome achieves functional invariance amid intrinsic whole-brain drift by dynamically reweighting sensory-to-motor paths via acute neuromodulation, metabolic gates, and intergenerational RNA cascades. In mammals, behavioral constancy emerges through collective population dynamics constrained within low-dimensional neural manifolds and stabilized by homeostatic compensation. Far from a biological flaw, representational drift acts as an active computational feature to explore degenerate solution spaces. Together, these multiscale insights demonstrate that behavioral permanence is anchored not in structural rigidity, but in the regulated preservation of network-level dynamics.</description>
    <dc:date>2026-11-30T15:00:00Z</dc:date>
  </item>
  <item rdf:about="https://scholar.dgist.ac.kr/handle/20.500.11750/60947">
    <title>Caenorhabditis elegans avoids epigallocatechin gallate (EGCG) through SRXA-7 G-protein coupled receptor</title>
    <link>https://scholar.dgist.ac.kr/handle/20.500.11750/60947</link>
    <description>Title: Caenorhabditis elegans avoids epigallocatechin gallate (EGCG) through SRXA-7 G-protein coupled receptor
Author(s): Cheon, YongJin; Hwang, Hyeonjeong; Kim, Kyuhyung
Abstract: Flavonoids are plant-derived polyphenols that influence nematode behavior, yet their neuronal and molecular targets remain poorly understood. Here, we show that the free-living nematode Caenorhabditis elegans detects and avoids a green tea catechin epigallocatechin gallate (EGCG) via the SRXA-7 Gprotein coupled receptor (GPCR) in the ASH nociceptive neurons. EGCG and epicatechin gallate (ECG), both containing a galloyl group, trigger strong avoidance, unlike other green tea catechins lacking this moiety. EGCG avoidance behavior displays species-and strain-specific differences among Caenorhabditis species and wild C. elegans isolates. Moreover, it is dynamically modulated by prior experience and feeding state. The ASH chemosensory neurons are required for EGCG detection, with avoidance mediated through canonical GPCR signaling components including GRK-2, GPA-3, ODR-3, and TRPV channels OCR-2 and OSM-9. A targeted GPCR screen revealed that srxa-7 mutants exhibited specific defects in EGCG avoidance. EGCG-evoked calcium responses in ASH are reduced in srxa-7 mutants and restored by ASH-specific expression of srxa-7 cDNA. These findings indicate that SRXA-7 is a sensory receptor for galloylated polyphenols, uncovering the neuronal and molecular basis of adaptive aversive responses to dietary plant compounds in nematodes. [BMB Reports 2026; 59(8): 384-390]</description>
    <dc:date>2025-12-31T15:00:00Z</dc:date>
  </item>
  <item rdf:about="https://scholar.dgist.ac.kr/handle/20.500.11750/58901">
    <title>A practical guide to ordering C. elegans strains for biological research</title>
    <link>https://scholar.dgist.ac.kr/handle/20.500.11750/58901</link>
    <description>Title: A practical guide to ordering C. elegans strains for biological research
Author(s): Park, Yeon-Ji; Moon, Kyeong Min; Kim, Kyuhyung
Abstract: Caenorhabditis elegans (C. elegans) is a widely used model organism in biological research, contributing to our understanding of fundamental processes in areas such as development, neurobiology, and aging. Accessing the appropriate C. elegans strains is crucial for conducting experiments and advancing scientific knowledge. This work provides a comprehensive overview of the process of ordering C. elegans.</description>
    <dc:date>2025-08-31T15:00:00Z</dc:date>
  </item>
  <item rdf:about="https://scholar.dgist.ac.kr/handle/20.500.11750/58220">
    <title>Cryo-EM structures of mouse bestrophin 1 channel in closed and partially open conformations</title>
    <link>https://scholar.dgist.ac.kr/handle/20.500.11750/58220</link>
    <description>Title: Cryo-EM structures of mouse bestrophin 1 channel in closed and partially open conformations
Author(s): Kim, Kwon-Woo; Lee, Euna; Ko, Ara; Hwang, Junmo; Park, Kunwoong; Lee, Byoung-Cheol; Kim, Ki Woo; Oh, Won-Jong; Kim, Kyuhyung; Lim, Hyun-Ho
Abstract: Bestrophin 1 (BEST1) channels are calcium-activated Cl- channels involved in diverse physiological processes, including gliotransmitter release in astrocytes. Although human and chicken BEST1 orthologs have been extensively studied, the structural and functional properties of mouse BEST1 (mBEST1) remain poorly understood. In this study, we characterized the structure-function of mBEST1-BF, a C-terminally tagged variant, using whole-cell patch-clamp recordings, surface biotinylation assays, and single-particle cryo-electron microscopy. Cryo-electron microscopy structural analysis of mBEST1-BF revealed closed and partially open conformations. Comparative analysis with human and chicken BEST1 orthologs highlighted conserved calcium-binding and gating mechanisms, with distinct features in mBEST1, including a wider aperture sufficient to accommodate dehydrated Cl- ions and potential anion-binding sites near Val205 and Gln208 residues. The disordered C-terminal region of mBEST1 remains unresolved, suggesting it may require stabilizing factors for structural determination. Additionally, the autoinhibitory domain, which includes Ser354, likely plays a key role in regulating gating, with Ser354 potentially serving as a phosphorylation site that modulates channel activity. Our findings provide structural and functional insights into mBEST1 and suggest mechanisms underlying its unique gating and ion (c) 2025 The Author(s). Published by Elsevier Inc. on behalf of Korean Society for Molecular and Cellular Biology. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).</description>
    <dc:date>2025-04-30T15:00:00Z</dc:date>
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