Affinage

LRRC8C

Volume-regulated anion channel subunit LRRC8C · UniProt Q8TDW0

Length
803 aa
Mass
92.5 kDa
Annotated
2026-06-10
38 papers in source corpus 22 papers cited in narrative 23 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

LRRC8C is a non-obligatory, accessory subunit of heteromeric volume-regulated anion channels (VRACs), assembling with the essential LRRC8A subunit and additional LRRC8 paralogs into hexameric complexes that mediate swelling-activated anion and osmolyte transport (PMID:27579940, PMID:28833202, PMID:36522427). Cryo-EM of murine LRRC8A/C channels shows a hexamer with a predominant 4:2 LRRC8A:LRRC8C stoichiometry, in which the more flexible LRRC8C subunits destabilize the tightly packed LRRC8A pairs to favor channel activation (PMID:36522427). LRRC8C contributes subunit-specific functional properties: residues at the C-terminus of its first extracellular loop govern inactivation kinetics and anion selectivity (PMID:27325695, PMID:29853476), and LRRC8A/C channels display strong DCPIB sensitivity that recapitulates native VRAC pharmacology (PMID:33356947). The channel's substrate scope extends beyond inorganic anions to charged osmolytes such as D-aspartate and glutamate (PMID:28833202, PMID:41740631) and to the cyclic dinucleotide 2'3'-cGAMP, which LRRC8A/C complexes import and export down the electrochemical gradient to drive STING signaling (PMID:33171122). LRRC8C also confers oxidant modulation: oxidation of its start methionine, with a contribution from the LRR domain, inhibits LRRC8A/C channels, while its extracellular loops render these channels comparatively oxidant-resistant relative to LRRC8A/D (PMID:33932953, PMID:35861288). These properties underpin distinct physiological roles—abolishing VRAC currents, regulatory volume decrease, and cGAMP-driven STING/p53-mediated immune suppression in T cells (PMID:35105987); supporting Nox1-dependent superoxide signaling in vascular smooth muscle (PMID:33932953); and enabling AKT-eNOS signaling and vasodilation in endothelium where LRRC8C partners with LRRC8A and LRRC8B (PMID:41636028). De novo gain-of-function variants at the LRRC8C pore/cytoplasmic domain boundary cause constitutive channel activation and a dominant human multisystem disorder affecting blood vessels, brain, eyes, and bones (PMID:39623139).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2004 Low

    Before any functional assay, LRRC8C needed to be placed within a protein family and given a candidate architecture, establishing it as a leucine-rich repeat membrane protein linked to immune cell activation.

    Evidence Homology-based sequence and predicted structural analysis

    PMID:15094057

    Open questions at the time
    • Computational prediction only with no direct functional experiment
    • No evidence of channel activity or VRAC role at this stage
    • Predicted topology not experimentally validated
  2. 2014 Medium

    Establishing whether LRRC8 proteins act alone or in complex was needed to define the molecular unit of transport; co-IP showed LRRC8C physically associates with other LRRC8 paralogs in heteromeric assemblies.

    Evidence Co-immunoprecipitation of LRRC8C with LRRC8A/B/D

    PMID:24782309

    Open questions at the time
    • Stoichiometry and architecture of complexes not resolved
    • Functional consequence of each interaction not defined
  3. 2015 High

    Resolving which subunits drive channel cargo specificity, knockout work showed LRRC8C is a VRAC subunit but, unlike LRRC8A/D, does not contribute to platinum-drug uptake, establishing subunit-specific substrate roles.

    Evidence CRISPR knockout with drug uptake and viability assays

    PMID:26530471

    Open questions at the time
    • Which substrates LRRC8C does favor was not yet defined
    • Did not address electrophysiological contribution
  4. 2016 High

    To map which protein regions set channel behavior, chimera and mutagenesis studies localized inactivation kinetics and anion selectivity to the C-terminus of the LRRC8C first extracellular loop, and showed EL1 is essential for VRAC activity.

    Evidence LRRC8C/E chimeras, point mutagenesis, patch-clamp; combinatorial RNAi electrophysiology

    PMID:27325695 PMID:27579940 PMID:29853476

    Open questions at the time
    • Atomic structure of the gating element not yet available
    • Contribution of cytoplasmic domains incompletely defined
  5. 2017 High

    Defining the physiological cargo, subunit-resolved knockdown and oxidant assays showed LRRC8C-containing channels preferentially conduct charged osmolytes and are inhibited by intracellular oxidation, distinguishing them from other heteromers.

    Evidence RNAi knockdown with radiotracer efflux assays; patch-clamp with oxidants on defined heteromers

    PMID:28833202 PMID:28841766

    Open questions at the time
    • Molecular identity of the oxidation target not yet pinpointed
    • Whether substrate preference holds across cell types untested at this point
  6. 2018 Medium

    Identifying upstream regulation, MLC1 was shown to alter the phosphorylation state of LRRC8C in astrocytes, indicating LRRC8C is subject to post-translational control via ERK signaling.

    Evidence Western blot phosphorylation analysis with MLC1 manipulation and electrophysiology

    PMID:30076890

    Open questions at the time
    • Phosphorylation sites on LRRC8C not mapped
    • Direct functional consequence of phosphorylation on channel gating not established
  7. 2020 High

    Extending VRAC cargo to signaling molecules, screens and transport assays established LRRC8A/C channels as bidirectional conduits for 2'3'-cGAMP and other cyclic dinucleotides, linking the channel to STING-based immune signaling; pharmacology confirmed LRRC8A/C channels mimic native VRAC.

    Evidence Genome-wide screens, radiotracer/STING reporter transport assays, pharmacology; DCPIB electrophysiology with R103F mutagenesis

    PMID:33171122 PMID:33356947

    Open questions at the time
    • Directionality control and regulation in vivo not fully defined
    • Whether cGAMP transport competes with osmolyte conduction unresolved
  8. 2021 High

    Connecting the channel to vascular redox signaling, LRRC8C was shown to co-IP with Nox1 and to support TNFα-induced superoxide production and proliferation in smooth muscle, while domain swaps localized oxidant resistance to LRRC8C extracellular loops.

    Evidence siRNA knockdown, reciprocal co-IP, functional assays; chimeric channel electrophysiology with oxidants

    PMID:33932953

    Open questions at the time
    • Stoichiometry of LRRC8C-Nox1 interaction unknown
    • Whether interaction is direct not established
  9. 2022 High

    A convergence of structure, genetics, and cell biology defined the channel's architecture and a major physiological role: cryo-EM revealed a 4:2 LRRC8A:LRRC8C hexamer with LRRC8C promoting activation; the oxidation site was mapped to the LRRC8C start methionine; and T cell knockout linked LRRC8C-mediated cGAMP transport to STING-p53 immune suppression.

    Evidence Cryo-EM; chimeric/concatemeric mutagenesis electrophysiology; Lrrc8c-/- mice with electrophysiology, transport assays, and in vivo immune models; epitope-tag knock-in immunolocalization

    PMID:35105987 PMID:35777784 PMID:35861288 PMID:36522427

    Open questions at the time
    • Gating transition between closed and open states not fully captured
    • Tissue distribution beyond kidney endothelium and T cells incompletely mapped
  10. 2024 High

    Disease relevance and physiological regulation were established: de novo gain-of-function variants at the pore/cytoplasmic boundary cause constitutive activation and a human multisystem disorder, while HSV-1 UL56 degrades LRRC8C to block cGAMP uptake and tumor-derived cGAMP enters endothelium via LRRC8C to drive STING-mediated vascular normalization.

    Evidence Cryo-EM and electrophysiology of mutants; viral infection and proteasome assays; preclinical liver cancer cGAS/STING mouse models

    PMID:38177099 PMID:38652659 PMID:39623139

    Open questions at the time
    • Genotype-phenotype correlation across affected organs not detailed
    • Whether other viral or endogenous regulators target LRRC8C unknown
  11. 2025 High

    Cell-type-specific assembly and pharmacology were refined: in endothelium LRRC8C partners with LRRC8A and LRRC8B to sustain AKT-eNOS-dependent vasodilation; LRRC8A/C channels are inhibited by leukotriene-receptor antagonists binding the N-terminal/fenestrae region; and LRRC8A and LRRC8C mutually stabilize each other post-translationally in glutamate-permeable astrocytic VRACs.

    Evidence Co-IP in knock-in mice, siRNA in HUVECs, pressure myography, in vivo hypertension model; MD simulation and mutagenesis electrophysiology; RNAi with radiotracer efflux and Western blot in astrocytes

    PMID:41053296 PMID:41636028 PMID:41740631

    Open questions at the time
    • Mechanism coupling AKT-eNOS to VRAC activity not fully resolved
    • How partner subunit identity is selected per tissue unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How LRRC8C dynamically switches between conducting inorganic anions, charged osmolytes, and immune second messengers, and how its assembly partner choice is determined across tissues, remains unresolved.
  • No open-state structure capturing substrate translocation
  • Rules governing tissue-specific LRRC8 paralog pairing unknown
  • Physiological signals that gate cGAMP versus osmolyte permeation undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005215 transporter activity 4 GO:0140299 molecular sensor activity 2
Localization
GO:0005886 plasma membrane 2
Pathway
R-HSA-168256 Immune System 3 R-HSA-382551 Transport of small molecules 3 R-HSA-162582 Signal Transduction 2
Partners
LRRC8ALRRC8BLRRC8DNOX1
Complex memberships
VRAC (volume-regulated anion channel)

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2004 LRRC8C (alias AD158) was identified as a member of the LRRC8 family of leucine-rich repeat proteins with predicted structure consisting of 16 extracellular LRRs and four transmembrane regions, implicated in proliferation and activation of lymphocytes and monocytes. Homology-based sequence analysis and predicted structural characterization FEBS letters Low 15094057
2014 LRRC8D interacts with LRRC8A, LRRC8B, and LRRC8C, as determined by co-immunoprecipitation, supporting a model where LRRC8 proteins form heteromeric complexes that mediate solute transport. Co-immunoprecipitation The Journal of biological chemistry Medium 24782309
2015 LRRC8C is a subunit of heteromeric volume-regulated anion channels (VRACs) but does not contribute to cisplatin/carboplatin uptake under isotonic or hypotonic conditions; loss of LRRC8C did not increase resistance to platinum-based drugs, in contrast to LRRC8A and LRRC8D. CRISPR/genetic knockout with drug uptake and cell viability assays The EMBO journal High 26530471
2016 The C-terminal residues of the first extracellular loop (EL1) of LRRC8C, specifically equivalent residues to Lys-98 and Asp-100 in LRRC8A, are major determinants of VRAC inactivation kinetics and anion selectivity, as determined using LRRC8C/LRRC8E chimeras and point mutations. Chimeric channel construction, point mutagenesis, patch-clamp electrophysiology The Journal of biological chemistry High 27325695
2016 Combinatory expression of LRRC8A with LRRC8D and LRRC8C is essential for VSOR (VRAC) activity in HeLa cells, as demonstrated by double, triple, and quadruple gene-silencing studies. RNA silencing (multiple gene combinations), electrophysiology Channels (Austin, Tex.) Medium 27579940
2017 In primary rat astrocytes, LRRC8A/C/E-containing (and LRRC8D-containing) heteromeric VRACs preferentially conduct charged osmolytes (d-aspartate), while LRRC8A/D-containing VRACs dominate release of uncharged osmolytes (taurine, myo-inositol); LRRC8C+LRRC8E knockdown strongly reduced charged osmolyte efflux but not uncharged osmolyte release. RNAi knockdown combined with radiotracer efflux assays The Journal of physiology High 28833202
2017 LRRC8A-LRRC8C heteromeric channels are directly inhibited by oxidation of intracellular cysteine residues (e.g., by chloramine-T or tert-butyl hydroperoxide), in contrast to LRRC8A-LRRC8E heteromers which are potentiated, demonstrating subunit-dependent oxidative modulation. Patch-clamp electrophysiology with oxidant treatment on heterologously expressed fluorescently tagged LRRC8 heteromers The Journal of physiology High 28841766
2018 The intracellular loop (IL) of LRRC8A connecting TM2 and TM3 and the first extracellular loop (EL1) of LRRC8C are both essential for VRAC activity; replacing EL1 of LRRC8A with that of LRRC8C generates a functional homomeric VRAC with normal volume regulation, and LRRC8A IL sequences determine anion permeability, rectification, and voltage sensitivity. Chimeric channel construction, electrophysiology, cell volume regulation assays The Journal of general physiology High 29853476
2018 MLC1 modulates VRAC currents indirectly in astrocytes; absence of MLC1 leads to changes in the phosphorylation state of the VRAC subunit LRRC8C, suggesting LRRC8C is subject to post-translational regulation via MLC1-dependent signal transduction pathways (ERK phosphorylation). Western blot (phosphorylation state), RNAi knockdown and overexpression of MLC1, electrophysiology Neurobiology of disease Medium 30076890
2020 LRRC8A forms heteromeric complexes with LRRC8C and/or LRRC8E to transport 2'3'-cGAMP and other cyclic dinucleotides; LRRC8A/C channels mediate cGAMP import and export driven by the electrochemical gradient, and LRRC8D inhibits cGAMP transport. Sphingosine 1-phosphate activates and DCPIB inhibits channel-mediated cGAMP transport. Genetic knockout/knockdown screens, radiotracer and STING reporter assays for cGAMP transport, pharmacological manipulation Molecular cell High 33171122
2020 LRRC8A homohexamers poorly recapitulate VRAC function; coexpression of LRRC8A and LRRC8C generates heteromeric channels with strong, voltage-independent DCPIB inhibition under normal intracellular ionic strength, more closely mimicking native VRAC pharmacology than LRRC8A alone. Electrophysiology in HCT116 Lrrc8c cells, pharmacological analysis with DCPIB, mutagenesis (R103F) American journal of physiology. Cell physiology High 33356947
2021 LRRC8C co-immunoprecipitates with NADPH oxidase 1 (Nox1) in vascular smooth muscle cells; LRRC8C knockdown inhibits TNFα-induced superoxide production, receptor endocytosis, NF-κB activation, and proliferation, positioning LRRC8A/C channels as key supporters of Nox1 activity. siRNA knockdown, co-immunoprecipitation, functional assays (O2·- production, NF-κB, proliferation) The Journal of physiology High 33932953
2021 LRRC8A/C channels are resistant to oxidant-mediated inhibition compared to LRRC8A/D channels; the extracellular loop domains (EL1, EL2) of LRRC8C confer oxidant resistance, as substitution of 8D extracellular loops into 8C conferred stronger chloramine-T-dependent inhibition. Chimeric channel construction, patch-clamp electrophysiology with oxidant treatment The Journal of physiology High 33932953
2022 LRRC8C is a critical component of VRAC in T cells; its deletion abolishes VRAC currents and regulatory volume decrease (RVD). LRRC8C mediates transport of 2'3'-cGAMP in T cells, leading to STING and p53 activation, which inhibits T cell proliferation, survival, and cytokine production. Genetic KO (Lrrc8c-/- mice), electrophysiology, volume regulation assays, radiotracer cGAMP transport, STING/p53 pathway analysis, in vivo immune challenge models Nature immunology High 35105987
2022 Cryo-EM structure of murine LRRC8A/C heteromeric channels reveals hexameric assembly with a predominant A:C ratio of 2:1 (four LRRC8A and two LRRC8C subunits). LRRC8A subunits cluster in pairs stabilizing a closed state, while LRRC8C subunits show larger flexibility and destabilize tightly packed LRRC8A subunits to enhance channel activation. Cryo-electron microscopy structure determination Nature structural & molecular biology High 36522427
2022 Oxidation of the start methionine of LRRC8C, with additional contribution from the LRR domain, mediates inhibition of LRRC8A-LRRC8C heteromeric channels by oxidants, as identified by chimeric and concatemeric channel analysis. Chimeric/concatemeric channel construction, mutagenesis, patch-clamp electrophysiology with oxidant treatment The Journal of physiology High 35861288
2022 In kidney, LRRC8C is exclusively localized to vascular endothelium (not nephron epithelia), as determined by immunolocalization in mice expressing epitope-tagged LRRC8 subunits. Immunolocalization using epitope-tagged knock-in mice Journal of the American Society of Nephrology : JASN Medium 35777784
2024 HSV-1 protein UL56 targets LRRC8A and LRRC8C for degradation (at least partially via proteasomal turnover), thereby inhibiting cGAMP uptake via VRAC channels and reducing intercellular cGAMP-mediated innate immune signaling. Viral infection assays, proteasome inhibition, protein degradation quantification, cGAMP transport functional assays Cell reports Medium 38652659
2024 cGAMP produced by tumor cGAS is transported via LRRC8C channels into endothelial cells, where it activates STING signaling to enhance lymphocyte recruitment and transendothelial migration, contributing to vascular normalization in liver cancer. Preclinical liver cancer models with cGAS/STING-deficient mice, in vivo functional studies Nature communications Medium 38177099
2024 De novo gain-of-function variants in LRRC8C at the pore/cytoplasmic domain boundary cause constitutive channel activation (activity even at isotonic conditions) due to increased structural flexibility of the mutant proteins, resulting in a dominant multisystem human disorder affecting blood vessels, brain, eyes, and bones. Cryo-EM structural analysis of mutant proteins, electrophysiology of co-expressed LRRC8A + mutant LRRC8C The EMBO journal High 39623139
2025 In endothelial cells, LRRC8C forms heteromeric complexes with LRRC8A and LRRC8B (not LRRC8D); LRRC8C depletion reduces endothelial VRAC currents, inhibits AKT-eNOS phosphorylation, increases myogenic tone, impairs eNOS-dependent vasodilation, and exacerbates angiotensin-induced hypertension in vivo. Co-immunoprecipitation with epitope-tagged knock-in mice, siRNA knockdown in HUVECs, electrophysiology, pressure myography, in vivo hypertension model Hypertension (Dallas, Tex. : 1979) High 41636028
2025 Zafirlukast and pranlukast inhibit LRRC8A/C heteromeric channels by binding to the N-terminal domain and inter-subunit fenestrae between TM1 and TM2; mutations in NTD, TM1, and TM2 alter sensitivity to both drugs, and inhibition involves destabilization of pore-lipid interactions promoting channel inactivation. Molecular dynamics simulation, mutagenesis, patch-clamp electrophysiology with chimeric homomeric 8C-8A(IL125) and heteromeric 8A/8C channels Communications biology High 41053296
2025 In brain astrocytes, LRRC8A and LRRC8C are key components of glutamate-permeable VRACs; LRRC8C knockdown reduces swelling-activated glutamate (D-aspartate) release by ~56%; knockdown of LRRC8A or LRRC8C reciprocally reduces the protein stability of the partner subunit without affecting mRNA levels, indicating mutual post-translational stabilization. RNAi knockdown in primary astrocytes, radiotracer efflux assays, Western blot for protein stability, qRT-PCR American journal of physiology. Cell physiology High 41740631

Source papers

Stage 0 corpus · 38 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2015 Subunit composition of VRAC channels determines substrate specificity and cellular resistance to Pt-based anti-cancer drugs. The EMBO journal 225 26530471
2020 LRRC8A:C/E Heteromeric Channels Are Ubiquitous Transporters of cGAMP. Molecular cell 155 33171122
2022 The volume-regulated anion channel LRRC8C suppresses T cell function by regulating cyclic dinucleotide transport and STING-p53 signaling. Nature immunology 98 35105987
2017 Molecular composition and heterogeneity of the LRRC8-containing swelling-activated osmolyte channels in primary rat astrocytes. The Journal of physiology 85 28833202
2024 TET2-mediated tumor cGAS triggers endothelial STING activation to regulate vasculature remodeling and anti-tumor immunity in liver cancer. Nature communications 80 38177099
2014 The protein synthesis inhibitor blasticidin s enters mammalian cells via leucine-rich repeat-containing protein 8D. The Journal of biological chemistry 67 24782309
2016 Inactivation and Anion Selectivity of Volume-regulated Anion Channels (VRACs) Depend on C-terminal Residues of the First Extracellular Loop. The Journal of biological chemistry 50 27325695
2017 Subunit-dependent oxidative stress sensitivity of LRRC8 volume-regulated anion channels. The Journal of physiology 48 28841766
2004 LRRC8 involved in B cell development belongs to a novel family of leucine-rich repeat proteins. FEBS letters 47 15094057
2017 DNA and RNA-sequence based GWAS highlights membrane-transport genes as key modulators of milk lactose content. BMC genomics 44 29246110
2018 Intracellular and extracellular loops of LRRC8 are essential for volume-regulated anion channel function. The Journal of general physiology 39 29853476
2018 GlialCAM/MLC1 modulates LRRC8/VRAC currents in an indirect manner: Implications for megalencephalic leukoencephalopathy. Neurobiology of disease 35 30076890
2022 Structure of a volume-regulated heteromeric LRRC8A/C channel. Nature structural & molecular biology 33 36522427
2016 Leucine-rich repeat containing protein LRRC8A is essential for swelling-activated Cl- currents and embryonic development in zebrafish. Physiological reports 27 27688432
2017 Leucine-rich repeat-containing 8B protein is associated with the endoplasmic reticulum Ca2+ leak in HEK293 cells. Journal of cell science 25 28972132
2020 LRRC8A homohexameric channels poorly recapitulate VRAC regulation and pharmacology. American journal of physiology. Cell physiology 23 33356947
2021 Oxidant-resistant LRRC8A/C anion channels support superoxide production by NADPH oxidase 1. The Journal of physiology 22 33932953
2022 Renal Deletion of LRRC8/VRAC Channels Induces Proximal Tubulopathy. Journal of the American Society of Nephrology : JASN 20 35777784
2022 Molecular determinants underlying volume-regulated anion channel subunit-dependent oxidation sensitivity. The Journal of physiology 18 35861288
2021 LncRNA CTD-2528L19.6 prevents the progression of IPF by alleviating fibroblast activation. Cell death & disease 18 34112765
2016 Distinct contributions of LRRC8A and its paralogs to the VSOR anion channel from those of the ASOR anion channel. Channels (Austin, Tex.) 17 27579940
2024 HSV-1 employs UL56 to antagonize expression and function of cGAMP channels. Cell reports 15 38652659
2024 De novo variants in LRRC8C resulting in constitutive channel activation cause a human multisystem disorder. The EMBO journal 12 39623139
2021 Identification and Construction of a Predictive Immune-Related lncRNA Signature Model for Melanoma. International journal of general medicine 12 34880662
2020 Ca2+ Dependence of Volume-Regulated VRAC/LRRC8 and TMEM16A Cl- Channels. Frontiers in cell and developmental biology 12 33335902
2021 Properties, Structures, and Physiological Roles of Three Types of Anion Channels Molecularly Identified in the 2010's. Frontiers in physiology 6 35002778
2025 Recent advances in structural characterization of volume-regulated anion channels (VRACs). The Journal of physiology 5 39977537
2026 Endothelial LRRC8C Associates With LRRC8A and LRRC8B to Regulate Vascular Reactivity and Blood Pressure. Hypertension (Dallas, Tex. : 1979) 2 41636028
2025 Endothelial LRRC8C associates with LRRC8A and LRRC8B to regulate vascular reactivity and blood pressure. bioRxiv : the preprint server for biology 2 40894750
2025 A conserved mechanism of LRRC8 channel inhibition by two structurally distinct drugs. Communications biology 2 41053296
2025 Subunit-specific roles of LRRC8 proteins in determining glutamate permeability of astrocytic volume-regulated anion channels. bioRxiv : the preprint server for biology 1 40766626
2024 Genetic variants of LRRC8C, OAS2, and CCL25 in the T cell exhaustion-related genes are associated with non-small cell lung cancer survival. Frontiers in immunology 1 39416786
2022 The LRRC8C-STING-p53 axis in T cells: A Ca2+ affair. Cell calcium 1 35596964
2020 Society of General Physiologists Symposium on "Ion Channels and Transporters in Immunity, Inflammation and Antitumor Immunity" (held online on September 11, 2020). Bioelectricity 1 34476372
2026 Subunit-specific roles of LRRC8 proteins in determining glutamate permeability of astrocytic volume-regulated anion channels. American journal of physiology. Cell physiology 0 41740631
2026 Mechanism of action of two potent LRRC8/VRAC channel inhibitors. Research square 0 41756460
2026 Structural patterns and transcriptional effects of integrated Epstein-Barr Virus revealed by long-read sequencing and RNA-sequencing in nasopharyngeal carcinoma. Virology journal 0 42115903
2024 Identification of ion channel-related genes as diagnostic markers and potential therapeutic targets for osteoarthritis through bioinformatics and machine learning-based approaches. Biomarkers : biochemical indicators of exposure, response, and susceptibility to chemicals 0 38767974

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