Publications by authors named "Hyun Ho Lim"

Clinical biomarkers are crucial for diagnosing and predicting outcomes in patients with traumatic brain injury (TBI). In this study, we performed an unbiased analysis of plasma proteins in acute TBI patients using bead-based multiplex assays and identified a strong positive correlation between LCN2 and IL-6 levels. Based on these findings, we hypothesized that LCN2 and IL-6 are closely related circulating biomarkers for TBI.

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  • Proton-activated chloride (PAC) channels play a crucial role in regulating chloride levels and cell death during acidosis, but their modulation mechanisms are not well understood.
  • Research shows that the phosphatidylinositol 4,5-bisphosphate (PI(4,5)P) found in the plasma membrane is crucial for activating these channels, as its depletion significantly reduces PAC currents.
  • Structural simulations indicate that the binding site for PI(4,5)P shifts from the cytosol to the membrane upon activation, revealing a complex interaction that influences PAC channel activity.
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Axon guidance molecules are critical for neuronal pathfinding because they regulate directionality and growth pace during nervous system development. However, the molecular mechanisms coordinating proper axonal extension and turning are poorly understood. Here, metastasis suppressor 1 (Mtss1), a membrane protrusion protein, ensured axonal extension while sensitizing axons to the Semaphorin 3E (Sema3E)-Plexin-D1 repulsive cue.

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Work-related musculoskeletal disorders represent a major occupational disability issue, and 53.4% of these disorders occur in the back or shoulders. Various types of passive shoulder exoskeletons have been introduced to support the weight of the upper arm and work tools during overhead work, thereby preventing injuries and improving the work environment.

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The anion channel SLAC1 functions as a crucial effector in the ABA signaling, leading to stomata closure. SLAC1 is activated by phosphorylation in its intracellular domains. Both a binding-activation model and an inhibition-release model for activation have been proposed based on only the closed structures of SLAC1, rendering the structure-based activation mechanism controversial.

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  • SHLP2 is a mitochondrial peptide linked to aging and oxidative stress, but its role in energy balance and receptor remains unspecified.
  • Administering SHLP2 to mice on a high-fat diet reduces obesity and enhances insulin sensitivity by activating POMC neurons in the hypothalamus, which helps control food intake and increase thermogenesis.
  • The study identifies CXCR7 as the receptor for SHLP2, highlighting its potential as a therapeutic agent for metabolic disorders and providing insights into its functioning in energy regulation.
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Living cells efflux intracellular ions for maintaining cellular life, so intravital measurements of specific ion signals are of significant importance for studying cellular functions and pharmacokinetics. In this work, de novo synthesis of artificial K -selective membrane and its integration with polyelectrolyte hydrogel-based open-junction ionic diode (OJID) is demonstrated, achieving a real-time K -selective ion-to-ion current amplification in complex bioenvironments. By mimicking biological K channels and nerve impulse transmitters, in-line K -binding G-quartets are introduced across freestanding lipid bilayers by G-specific hexylation of monolithic G-quadruplex, and the pre-filtered K flow is directly converted to amplified ionic currents by the OJID with a fast response time at 100 ms intervals.

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BEST family is a class of Ca-activated Cl- channels evolutionary well conserved from bacteria to human. The human BEST paralogs (BEST1-BEST4) share significant amino acid sequence homology in the N-terminal region, which forms the transmembrane helicases and contains the direct calcium-binding site, Ca-clasp. But the cytosolic C-terminal region is less conserved in the paralogs.

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  • * This study focused on understanding the structure and behavior of the MLC1 protein, revealing it has eight transmembrane (TM) domains with both ends facing the cytoplasm.
  • * The researchers discovered that MLC1 can form oligomers, specifically trimeric complexes, and the findings set the stage for detailed structural and functional studies of the protein.
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CLC-ec1 is a Cl/H antiporter that forms stable homodimers in lipid bilayers, with a free energy of -10.9 kcal/mol in 2:1 POPE/POPG lipid bilayers. The dimerization interface is formed by four transmembrane helices: H, I, P and Q, that are lined by non-polar side-chains that come in close contact, yet it is unclear as to whether their interactions drive dimerization.

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Connexin family proteins assemble into hexameric channels called hemichannels/connexons, which function as transmembrane channels or dock together to form gap junction intercellular channels (GJIChs). We determined the cryo-electron microscopy structures of human connexin 31.3 (Cx31.

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Background: Megalencephalic leukoencephalopathy with subcortical cysts (MLC) is a rare form of infantile-onset leukodystrophy. The disorder is caused primarily by mutations of MLC1 that leads to a series of phenotypic outcomes including vacuolation of myelin and astrocytes, subcortical cysts, brain edema, and macrocephaly. Recent studies have indicated that functional interactions among MLC1, GlialCAM, and ClC-2 channels play key roles in the regulation of neuronal, glial and vascular homeostasis.

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The CLC family of proteins are involved in a variety of physiological processes to control cellular chloride concentration. Two distinct classes of CLC proteins, Cl channels and Cl/H antiporters, have been functionally and structurally investigated over the last several decades. Previous studies have suggested that the conformational heterogeneity of the critical glutamate residue, Glu, could explain the transport cycle of CLC-type Cl/H antiporters.

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Animal locomotion is mediated by a sensory system referred to as proprioception. Defects in the proprioceptive coordination of locomotion result in uncontrolled and inefficient movements. However, the molecular mechanisms underlying proprioception are not fully understood.

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The chloride channel (CLC) family of proteins consists of channels and transporters that share similarities in architecture and play essential roles in physiological functions. Among the CLC family, CLC-1 channels have the representative homodimeric double-barreled structure carrying two gating processes. One is protopore gating that acts on each pore independently by glutamate residue (E).

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This article introduces the history and the long-term goals of the Korea Brain Initiative, which is centered on deciphering the brain functions and mechanisms that mediate the integration and control of brain functions that underlie decision-making. The goal of this initiative is the mapping of a functional connectome with searchable, multi-dimensional, and information-integrated features. The project also includes the development of novel technologies and neuro-tools for integrated brain mapping.

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Preclinical Research Emerging evidence suggests that Dalbergia odorifera T. Chen (Leguminosae), an indigenous medicinal herb, has therapeutic potential. This study examined the antiwrinkle effects of ethanol extracts of D.

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Dalbergia odorifera T. Chen (Leguminosae), an indigenous medicinal herb, has been widely used in northern and eastern Asia to treat diverse diseases. Here, we investigated the anti-senescent effects of ethanolic extracts of Dalbergia odorifera (EEDO) in ultraviolet (UV) B-irradiated skin cells.

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Cl(-)/H(+) antiporters of the CLC superfamily transport anions across biological membranes in varied physiological contexts. These proteins are weakly selective among anions commonly studied, including Cl(-), Br(-), I(-), NO3(-) and SCN(-), but they seem to be very selective against F(-). The recent discovery of a new CLC clade of F(-)/H(+) antiporters, which are highly selective for F(-) over Cl(-), led us to investigate the mechanism of Cl(-)-over-F(-) selectivity by a CLC Cl(-)/H(+) antiporter, CLC-ec1.

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Chloride-transporting membrane proteins of the CLC family appear in two distinct mechanistic flavors: H(+)-gated Cl(-) channels and Cl(-)/H(+) antiporters. Transmembrane H(+) movement is an essential feature of both types of CLC. X-ray crystal structures of CLC antiporters show the Cl(-) ion pathway through these proteins, but the H(+) pathway is known only inferentially by two conserved glutamate residues that act as way-stations for H(+) in its path through the protein.

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Article Synopsis
  • The chloride channel (CLC) family includes both Cl(-) ion channels and Cl(-)/H(+) antiporters, but the exact mechanism for H(+) and Cl(-) transport in antiporters is still not understood.
  • Research on the novel bacterial protein CLC-ck2 shows it can transport Cl(-), even without key amino acids typically required, and its ion selectivity differs from another CLC protein, CLC-ec1, particularly regarding SO4(2-) interference.
  • Interestingly, CLC-ck2 operates as a Cl(-)/H(+) antiporter despite having a nonpolar residue at a position thought to be essential for H(+) movement, indicating that the
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A subclass of bacterial CLC anion-transporting proteins, phylogenetically distant from long-studied CLCs, was recently shown to be specifically up-regulated by F(-). We establish here that a set of randomly selected representatives from this "CLC(F)" clade protect Escherichia coli from F(-) toxicity, and that the purified proteins catalyze transport of F(-) in liposomes. Sequence alignments and membrane transport experiments using (19)F NMR, osmotic response assays, and planar lipid bilayer recordings reveal four mechanistic traits that set CLC(F) proteins apart from all other known CLCs.

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As previously reported, the activity of the large-conductance calcium (Ca(2+))-activated potassium (K(+)) (BK(Ca)) channel is strongly potentiated from the extracellular side of the cell membrane by certain benzofuroindole derivatives. Here, the mechanism of action of one of the most potent activators, 4-chloro-7-(trifluoromethyl)-10H-benzofuro[3,2-b]indole-1-carboxylic acid (CTBIC), is characterized. This compound, Compound 22 in the previous report (Chembiochem 6:1745-1748, 2005), potentiated the activity of the channel by shifting its conductance-voltage relationship toward the more negative direction.

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