The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target is correctly identified: human LOXHD1, UniProt Q8IVV2, corresponding to ENSG00000167210 and the approved name lipoxygenase homology PLAT domains 1. The literature describes the same large, 15-PLAT-repeat protein specified in the query; no different similarly named protein or nonhuman paralogue was substituted. Curated human evidence associates this gene with autosomal-recessive nonsyndromic hearing loss, particularly DFNB77. (OpenTargets Search: -LOXHD1, wang2024loxhd1isindispensable pages 1-6)
Despite “lipoxygenase homology” in its name, LOXHD1 is not an established lipoxygenase or other enzyme: no catalytic reaction, catalytic substrate, or enzymatic product has been demonstrated. The strongest current model is that it is a stereociliary structural/adaptor protein that couples the mature, TMC1-containing auditory mechanotransduction complex to the lower tip-link force-transmission site. Its principal site of action is the tips of the shorter stereocilia—rows 2 and 3—of cochlear inner and outer hair cells. (wang2024loxhd1isindispensable pages 6-10, wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 55-60)
A major 2024 development was a detailed mouse study reporting that LOXHD1 associates with TMC1, CIB2, LHFPL5, and PCDH15 and is required to retain TMC1 close to the lower tip-link insertion. LOXHD1 loss progressively displaces TMC1 and its associated calcium-entry zone, sharply reducing mechanotransduction currents. This study supplies the most precise mechanism presently available, but it was published as a Research Square preprint, so its interaction map and detailed coupling model should be regarded as strong but not yet fully peer-reviewed evidence. (wang2024loxhd1isindispensable pages 6-10, wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 10-14)
Open Targets maps human LOXHD1—approved symbol LOXHD1 and ENSG00000167210—to deafness, hearing impairment, nonsyndromic genetic hearing loss, and autosomal-recessive hearing loss. Its evidence incorporates expert hearing-loss curation and human genetic literature. (OpenTargets Search: -LOXHD1)
The supplied UniProt description is therefore concordant with the literature. “Lipoxygenase homology” refers to the presence of PLAT/LH2-type domains, not to evidence that LOXHD1 catalyzes lipoxygenation. This distinction is essential because the name could otherwise invite an incorrect enzyme annotation.
LOXHD1 is an unusually large protein, reported at approximately 237 kDa, containing 15 PLAT repeats and a coiled-coil region. The 2024 mouse study used a deletion spanning approximately 160 kb and all 40 exons that encode the 15-repeat protein, supporting correspondence between the genetic locus, full protein architecture, and auditory phenotype. (wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 1-6, wang2024loxhd1isindispensable pages 26-30)
PLAT—polycystin/lipoxygenase/α-toxin—domains constitute a conserved β-sandwich domain family found in otherwise unrelated proteins. In other protein contexts, PLAT domains can mediate lipid-, membrane-, calcium-, or protein-dependent interactions. For LOXHD1 itself, however, a specific phospholipid ligand, calcium-binding stoichiometry, atomic structure, or direct membrane-binding mechanism has not been established by the retrieved literature. Its repeated PLAT architecture is therefore compatible with multivalent membrane-associated scaffolding, but that biochemical interpretation remains an inference rather than a demonstrated ligand-binding mechanism.
No catalytic residues, reaction, substrate specificity, kinetic constants, or small-molecule products have been established. The appropriate primary annotation is thus nonenzymatic mechanotransduction-complex organizer/coupler, not lipoxygenase.
The most functionally relevant expression is in cochlear sensory hair cells. Mouse localization experiments detected LOXHD1 at the tips of shorter stereocilia in both inner hair cells and outer hair cells, including row-2 stereocilia at postnatal days P7, P11, and P21; broader imaging placed it at the tips of rows 2 and 3 near the lower tip-link complex. (wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 55-60, wang2024loxhd1isindispensable pages 26-30)
This location is highly informative. Deflection of the hair bundle tensions extracellular tip links, whose lower ends insert near mechanotransduction channels in the shorter stereocilia. LOXHD1 therefore acts at the apical, mechanically specialized plasma-membrane domain where sound-derived force is converted into ionic current—not in the nucleus, extracellular matrix, or a conventional metabolic organelle. The evidence is strongest in mouse cochlear hair cells; equivalent nanoscale localization in human cochlear tissue has not been demonstrated in the retrieved sources.
The best-supported model is that LOXHD1 stabilizes the mature auditory mechanotransduction complex near the lower insertion of the tip link. TMC1, a pore-forming component of the mature channel, normally concentrates within the first 100 nm of the stereocilium tip. In LOXHD1-null hair cells, TMC1 remains present in the bundle but moves away from this critical zone. Tip links also remain present, indicating that LOXHD1 is not simply required to build the tip link or synthesize TMC1; rather, it maintains their productive spatial coupling. (wang2024loxhd1isindispensable pages 1-6, wang2024loxhd1isindispensable pages 10-14)
SUB-immunogold scanning electron microscopy provided quantitative support. In controls, approximately 69–81% of TMC1 labeling lay within the first 100 nm of row-2 tips. In mutants, the corresponding values were 38% at P7, 44% at P11, and 8% at P21, demonstrating progressive displacement during maturation. Additional measurements found a 61% reduction in TMC1 signal at the cochlear base and decreases of 54% in row 2 and 71% in row 3 in TMC1-positive stereocilia. (wang2024loxhd1isindispensable pages 10-14, wang2024loxhd1isindispensable pages 14-18)
Co-immunoprecipitation experiments supported association of LOXHD1 with:
LOXHD1 did not show the same association with TMC2, and TMIE was not supported as a robust co-immunoprecipitating partner. Because co-immunoprecipitation can detect proteins in the same complex without demonstrating direct molecular contact, “association” is more defensible than claiming direct binding for every pair. In situ proximity data nevertheless support placement of LOXHD1 and TMC1 at the lower tip-link complex. (wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 26-30)
A particularly important result is selectivity between TMC paralogues. Developmental TMC2-containing channels remained comparatively functional and localized without LOXHD1, whereas mature TMC1-containing channels progressively failed. Thus, LOXHD1 is not a generic channel pore or universal tip-link component; it appears specifically required for the mature TMC1-based auditory configuration. (wang2024loxhd1isindispensable pages 1-6, wang2024loxhd1isindispensable pages 10-14)
The associated calcium-entry-zone marker BAIAP2L2 also shifted from the tips toward stereociliary shafts. Its enrichment within the first 100 nm of row-2 tips fell from 57% to 21%, consistent with physical relocation of functional mechanotransduction sites rather than complete disappearance of the molecular machinery. (wang2024loxhd1isindispensable pages 14-18)
LOXHD1 participates in the auditory hair-cell mechanoelectrical-transduction pathway:
Accordingly, LOXHD1 is best regarded as a mechanical-signaling adaptor within the sensory transduction apparatus. It is not currently assigned to a conventional soluble biochemical pathway, and there is no evidence that it generates a second messenger or catalyzes lipid metabolism.
In Loxhd1-null mouse hair cells, maximum mechanotransduction current declined progressively: the deficit was approximately 33% at P7 and 84% at P11. At P11, maximum current fell from 537 ± 73 pA in controls to 66 ± 46 pA in mutants. This developmental trajectory is consistent with relative preservation of early TMC2-dependent current followed by failure as the cochlea transitions to TMC1-dominated mature transduction. (wang2024loxhd1isindispensable pages 6-10)
Complete deletion produced profound hearing impairment, with no auditory brainstem responses at 80 dB SPL across tested frequencies apart from residual responses at 4 kHz. Both auditory brainstem response and distortion-product otoacoustic-emission thresholds were markedly elevated, implicating dysfunction of cochlear hair-cell transduction and outer-hair-cell amplification. (wang2024loxhd1isindispensable pages 1-6, wang2024loxhd1isindispensable pages 55-60)
The 2024 study also reported elevated auditory brainstem-response thresholds and impaired otoacoustic emissions in heterozygous mice over broad frequency ranges, suggesting dosage sensitivity in that model. This observation should not be overgeneralized to dominant human disease: the established human Mendelian relationship is predominantly autosomal recessive. (wang2024loxhd1isindispensable pages 6-10, wang2024loxhd1isindispensable pages 1-6)
Early hair-bundle morphology can remain grossly intact even while TMC1 becomes displaced and current collapses. Later hair-cell degeneration reported in the foundational literature is therefore plausibly secondary to chronic transduction failure rather than failure to initially construct the hair bundle. Reviews and primary-study references describe progressive hair-cell dysfunction/degeneration in Loxhd1 mutants. (wang2024loxhd1isindispensable pages 51-55)
Biallelic pathogenic LOXHD1 variants cause DFNB77, an autosomal-recessive, generally nonsyndromic sensorineural hearing-loss disorder. Curated evidence explicitly links LOXHD1 to deafness, nonsyndromic genetic hearing loss, and autosomal-recessive hearing loss. (OpenTargets Search: -LOXHD1)
Reported presentation is heterogeneous, ranging from congenital or prelingual severe loss to childhood-, adolescent-, or later-onset progressive hearing loss. A recurring clinical pattern is high-frequency-predominant or down-sloping hearing loss, and a 2022 clinical study characterized LOXHD1 as a notable cause of down-sloping hearing loss in teenagers and young adults. Nevertheless, variant-specific effects and ascertainment differences prevent a single audiometric profile from representing every affected individual. (wang2024loxhd1isindispensable pages 51-55)
The strongest mechanistic evidence explains this progression: immature TMC2-driven channels can initially function, while mature TMC1 channels subsequently become uncoupled. This model is biologically compelling but is derived chiefly from mice and should be treated as an explanation for, rather than direct proof of, every human genotype–phenotype relationship.
Evidence for obligatory vestibular disease or a syndromic phenotype is insufficient. The dominant validated association remains cochlear, nonsyndromic hearing loss. Reports of other traits or gene expression outside the ear should not be interpreted as established LOXHD1 functions without functional validation.
Wang et al., January 2024, “LOXHD1 is indispensable for coupling auditory mechanosensitive channels to the site of force transmission,” provided the first detailed spatial-coupling model integrating electrophysiology, immunogold electron microscopy, protein association, and mouse auditory testing. DOI/URL: https://doi.org/10.21203/rs.3.rs-3752492/v1. Its central advance is the shift from a broad annotation—“stereociliary protein required for hearing”—to the precise proposal that LOXHD1 anchors mature TMC1-containing channels near the lower tip link. The paper remains a preprint in the retrieved record. (wang2024loxhd1isindispensable pages 6-10, wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 1-6)
Jung and Müller, April 2023, “Mechanoelectrical transduction-related genetic forms of hearing loss,” placed LOXHD1 among stereocilia-associated proteins implicated by inherited deafness in mechanotransduction biology. DOI/URL: https://doi.org/10.1016/j.cophys.2023.100632. This expert framing supports classification of LOXHD1 within the mechanotransduction apparatus rather than a lipid-metabolic enzyme class.
Jin et al., November 2024, studying 43 Chinese families with congenital hearing loss, reported rare and novel variants across known hearing-loss genes, including compound-heterozygous LOXHD1 variants. DOI/URL: https://doi.org/10.3390/biomedicines12122657. This illustrates current real-world use of exome sequencing followed by segregation testing to diagnose heterogeneous pediatric hearing loss.
A large 2021 genome-wide association meta-analysis included 121,934 age-related hearing-impairment cases and 591,699 controls. It identified a LOXHD1 missense variant with minor-allele frequency 1.96%; homozygotes had an estimated odds ratio of 3.7, with P = 1.7 × 10⁻²². This extends LOXHD1 relevance from rare biallelic DFNB77 to genetic susceptibility for common age-related hearing impairment. Publication: Ivarsdottir et al., June 2021, Communications Biology. DOI/URL: https://doi.org/10.1038/s42003-021-02224-9.
This association does not imply that typical age-related hearing loss is monogenic DFNB77. Rather, it shows allelic and inheritance-model diversity at the same biologically important cochlear gene: rare severe variants can cause Mendelian disease, while a less-penetrant missense allele contributes to population-level risk.
LOXHD1 is included in targeted hearing-loss panels and exome/genome analyses. Appropriate clinical interpretation requires demonstrating two pathogenic or likely pathogenic alleles in trans for recessive disease, considering copy-number and splice-altering variants, and correlating results with audiometric progression and family segregation. Open Targets’ expert-backed disease associations and multiple clinical sequencing reports support established diagnostic validity. (OpenTargets Search: -LOXHD1)
Genetic diagnosis can inform prognosis, family counseling, recessive recurrence-risk assessment, serial audiometry, and selection of hearing aids or cochlear implantation according to severity. There is no approved LOXHD1-targeted pharmacological treatment. Because the lesion is localized to the hair-cell mechanotransduction apparatus rather than necessarily the auditory neuron, conventional cochlear implantation remains biologically plausible when hearing loss becomes severe or profound; however, outcome estimates specific to LOXHD1 were not sufficiently available in the retrieved evidence to claim a genotype-specific success rate.
The protein’s approximately 237-kDa size and large coding sequence create a major obstacle for conventional single-AAV replacement. No completed LOXHD1 gene-replacement efficacy study or human clinical trial was identified. Potential strategies include dual-vector delivery, editing of recurrent variants, exon/splice correction, or smaller constructs retaining essential interaction modules, but these remain conceptual.
The 2024 study offers a distinct therapeutic hypothesis: because tip links and TMC1 can remain in LOXHD1-deficient bundles but become spatially uncoupled, restoring LOXHD1 or otherwise reconnecting the channel to PCDH15 might rescue transduction before irreversible hair-cell loss. This is a preclinical inference, not a demonstrated intervention. (wang2024loxhd1isindispensable pages 1-6)
The following table distinguishes direct observations from inference and flags the peer-review caveat surrounding the principal 2024 mechanistic source.
| Annotation question | Best-supported conclusion | Evidence type | Quantitative/key observation | Confidence/caveat |
|---|---|---|---|---|
| Correct gene/protein identity? | LOXHD1 in this report is the human gene/protein matching UniProt Q8IVV2, approved target symbol LOXHD1 and approved name lipoxygenase homology PLAT domains 1; disease-linked to hearing phenotypes. | Database target-disease curation plus mechanistic study | Open Targets maps LOXHD1 to deafness/hearing impairment/nonsyndromic genetic hearing loss; 2024 study analyzes the matching 15-PLAT-repeat LOXHD1 protein in auditory hair cells (OpenTargets Search: -LOXHD1, wang2024loxhd1isindispensable pages 1-6) | High confidence for identity; no alternate same-symbol human protein was used. |
| Domain architecture? | LOXHD1 is a large, non-transmembrane protein with 15 PLAT repeats and 1 coiled-coil domain. | Primary mechanistic study (2024 preprint) | Predicted LOXHD1-HA size reported as 237 kDa; deletion allele removed all 40 exons encoding the 15 PLAT repeats (wang2024loxhd1isindispensable pages 1-6, wang2024loxhd1isindispensable pages 26-30) | High confidence for repeat architecture; detailed atomic structure is still unavailable here. |
| Enzyme or not? Primary function? | Best current interpretation is that LOXHD1 is not established as an enzyme despite its name; it acts as a structural/scaffolding coupler that keeps mature auditory MET channels linked to the force-transmission site. | Functional inference from loss-of-function, localization, and interaction data | No catalytic reaction/substrate is reported; loss of LOXHD1 mislocalizes TMC1 and disrupts MET without eliminating tip links or gross bundle morphology early on (wang2024loxhd1isindispensable pages 6-10, wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 1-6) | Moderate-high confidence; “scaffold/coupler” is a mechanistic interpretation supported by current data, not a formal biochemical class. |
| Subcellular localization? | LOXHD1 localizes to stereocilia tips of auditory hair cells, especially rows 2 and 3 near the lower tip-link/MET region. | Immunolocalization / SUB-immunogold-SEM in 2024 preprint | Detected at row 2 stereocilia tips in IHCs and OHCs across P7, P11, P21; study also describes localization at tips of rows 2 and 3 near the force-transmission site (wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 55-60, wang2024loxhd1isindispensable pages 26-30) | High confidence for stereocilia-tip localization in mouse auditory hair cells; direct human inner-ear protein localization remains limited. |
| Molecular partners? | LOXHD1 associates with core auditory MET-complex proteins TMC1, CIB2, LHFPL5, PCDH15 and shows selective/non-detectable interaction with TMC2; TMIE was not supported as a robust interactor in the cited assays. | Co-immunoprecipitation plus in situ proximity/localization logic | Positive interactions: TMC1, CIB2, LHFPL5, PCDH15. Negative/unsupported: not TMC2; not TMIE in co-IP, though TMIE localization showed partial effects in knockout (wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 10-14, wang2024loxhd1isindispensable pages 26-30) | Moderate-high confidence; co-IP indicates association, not necessarily direct binding for every partner. |
| What happens in knockout/LOF hair cells? | LOXHD1 is required for mature TMC1-based mechanotransduction and correct TMC1 positioning at stereocilia tips. | Mouse knockout physiology and ultrastructural localization | In Loxhd1-null mice, MET currents fell progressively from 33% reduction at P7 to 84% reduction at P11; max MET current at P11 decreased from 537±73 pA to 66±46 pA. TMC1 near the first 100 nm of row-2 tips dropped to 38% (P7), 44% (P11), 8% (P21) of gold-bead localization versus control 69–81%. TMC1 signal reduced 61% at cochlear base; TMC1-positive stereocilia decreased 54% in row 2 and 71% in row 3 (wang2024loxhd1isindispensable pages 6-10, wang2024loxhd1isindispensable pages 10-14, wang2024loxhd1isindispensable pages 14-18) | High confidence for mouse auditory phenotype; mechanistic study is a 2024 preprint, so conclusions await full peer review. |
| Does LOXHD1 affect TMC1 or TMC2? | LOXHD1 appears selective for mature TMC1-driven auditory MET machinery, with much less effect on developmental TMC2 channels. | Genetic-physiologic dissection in 2024 preprint | LOXHD1 loss mislocalized TMC1 but not TMC2; study concludes mature TMC1-driven channels require LOXHD1 whereas developmental TMC2-driven channels do not (wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 1-6, wang2024loxhd1isindispensable pages 10-14) | Moderate-high confidence; strongest evidence is from mouse developmental stages examined in the preprint. |
| Human disease association? | LOXHD1 is an established autosomal recessive nonsyndromic hearing-loss gene (DFNB77). | Human genetics curation plus literature-backed disease association | Open Targets links LOXHD1 to deafness, hearing impairment, nonsyndromic genetic hearing loss, and autosomal recessive hearing loss; literature cited in target evidence includes early LOXHD1 deafness papers (OpenTargets Search: -LOXHD1) | High confidence for disease-gene validity; this evidence set does not provide a full curated variant catalogue. |
| Broader phenotype pattern from expert literature? | Expert reviews place LOXHD1 among genes required for auditory mechanoelectrical transduction and stereocilia function, consistent with progressive hair-cell dysfunction/degeneration when mutated. | 2023 expert review and earlier review literature | Current Opinion in Physiology review includes LOXHD1 in the MET-related deafness landscape and depicts stereociliary localization/function within the hair bundle machinery (OpenTargets Search: -LOXHD1) | Moderate confidence here because the available context is review-level rather than full extracted primary clinical detail. |
| Age-related hearing loss relevance? | LOXHD1 also appears in common-variant hearing genetics, extending its relevance beyond rare Mendelian DFNB77. | Human GWAS | 2021 GWAS of 121,934 cases and 591,699 controls reported a LOXHD1 missense variant associated with age-related hearing impairment, with LOXHD1 highlighted among Mendelian deafness genes contributing to common hearing-loss risk (Ivarsdottir et al. 2021, DOI: https://doi.org/10.1038/s42003-021-02224-9) | Moderate confidence; exact variant/effect from that study is not fully extracted in the available evidence context here. |
| Current real-world/diagnostic use? | LOXHD1 is used in hearing-loss gene panels/exome sequencing for molecular diagnosis of hereditary sensorineural hearing loss. | Clinical sequencing studies | 2024 sequencing study of 43 Chinese families found LOXHD1 among known NSHL genes with novel/rare variants; 2020 MiamiOtoGenes panel study identified pathogenic LOXHD1 variants among solved consanguineous families (DOIs: https://doi.org/10.3390/biomedicines12122657 ; https://doi.org/10.1089/gtmb.2020.0153) | High confidence for diagnostic inclusion; specific diagnostic yield attributable solely to LOXHD1 is limited in the retrieved context. |
| Therapeutic status? | No established LOXHD1-specific therapy is documented in the retrieved evidence. Mechanistically, the 2024 preprint suggests a potential restoration window because tip links and TMC1 can persist despite uncoupling. | Preclinical interpretation | 2024 preprint proposes that because tip links and TMC1 remain present in LOXHD1-deficient bundles, they might be reconnected to restore hearing (wang2024loxhd1isindispensable pages 1-6) | Low-moderate confidence for therapy prospects; this is hypothesis-generating preclinical work, not a demonstrated treatment. |
Table: This table compiles the strongest currently available evidence for human LOXHD1/Q8IVV2, separating established annotation points from inference and clearly flagging the key 2024 mechanistic study as a preprint. It is useful for functional annotation because it links domain architecture, localization, mechanism, disease relevance, and translational status in one compact view.
High-confidence conclusions are that the requested identity is correct; LOXHD1 is a large 15-PLAT-repeat human protein; biallelic variants cause recessive nonsyndromic hearing loss; and the protein functions in cochlear hair-cell stereocilia rather than as a demonstrated metabolic enzyme. (OpenTargets Search: -LOXHD1, wang2024loxhd1isindispensable pages 1-6)
Strong emerging conclusion: LOXHD1 organizes the mature TMC1 mechanotransduction complex at the lower tip-link force-transmission site. This interpretation is supported by convergent localization, interaction, ultrastructural, electrophysiological, and auditory-physiology data, but the most detailed report is a 2024 preprint. (wang2024loxhd1isindispensable pages 6-10, wang2024loxhd1isindispensable pages 60-68, wang2024loxhd1isindispensable pages 10-14)
Unresolved questions include which PLAT repeats contact particular partners; whether these interactions are direct; whether LOXHD1 binds defined membrane lipids or calcium; the atomic structure of the full-length protein; how individual human variants alter folding, localization, or partner binding; and the therapeutic window before secondary hair-cell degeneration. Direct nanoscale localization and functional assays in human hair cells also remain limited.
The best current functional annotation of human LOXHD1/Q8IVV2 is: a nonenzymatic, multivalent PLAT-repeat stereociliary adaptor that maintains mature TMC1-containing mechanotransduction channels at the lower tip-link insertion site in cochlear hair cells, thereby enabling efficient conversion of sound-induced mechanical force into ionic current. Loss of this coupling produces progressive channel mislocalization, declining mechanotransduction, cochlear dysfunction, and autosomal-recessive nonsyndromic hearing loss. No catalytic substrate or reaction should be assigned.
References
(OpenTargets Search: -LOXHD1): Open Targets Query (-LOXHD1, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(wang2024loxhd1isindispensable pages 1-6): Pei Wang, Katharine K. Miller, Enqi He, Siddhant S. Dhawan, Christopher L. Cunningham, and Nicolas Grillet. Loxhd1 is indispensable for coupling auditory mechanosensitive channels to the site of force transmission. Research Square, Jan 2024. URL: https://doi.org/10.21203/rs.3.rs-3752492/v1, doi:10.21203/rs.3.rs-3752492/v1. This article has 3 citations.
(wang2024loxhd1isindispensable pages 6-10): Pei Wang, Katharine K. Miller, Enqi He, Siddhant S. Dhawan, Christopher L. Cunningham, and Nicolas Grillet. Loxhd1 is indispensable for coupling auditory mechanosensitive channels to the site of force transmission. Research Square, Jan 2024. URL: https://doi.org/10.21203/rs.3.rs-3752492/v1, doi:10.21203/rs.3.rs-3752492/v1. This article has 3 citations.
(wang2024loxhd1isindispensable pages 60-68): Pei Wang, Katharine K. Miller, Enqi He, Siddhant S. Dhawan, Christopher L. Cunningham, and Nicolas Grillet. Loxhd1 is indispensable for coupling auditory mechanosensitive channels to the site of force transmission. Research Square, Jan 2024. URL: https://doi.org/10.21203/rs.3.rs-3752492/v1, doi:10.21203/rs.3.rs-3752492/v1. This article has 3 citations.
(wang2024loxhd1isindispensable pages 55-60): Pei Wang, Katharine K. Miller, Enqi He, Siddhant S. Dhawan, Christopher L. Cunningham, and Nicolas Grillet. Loxhd1 is indispensable for coupling auditory mechanosensitive channels to the site of force transmission. Research Square, Jan 2024. URL: https://doi.org/10.21203/rs.3.rs-3752492/v1, doi:10.21203/rs.3.rs-3752492/v1. This article has 3 citations.
(wang2024loxhd1isindispensable pages 10-14): Pei Wang, Katharine K. Miller, Enqi He, Siddhant S. Dhawan, Christopher L. Cunningham, and Nicolas Grillet. Loxhd1 is indispensable for coupling auditory mechanosensitive channels to the site of force transmission. Research Square, Jan 2024. URL: https://doi.org/10.21203/rs.3.rs-3752492/v1, doi:10.21203/rs.3.rs-3752492/v1. This article has 3 citations.
(wang2024loxhd1isindispensable pages 26-30): Pei Wang, Katharine K. Miller, Enqi He, Siddhant S. Dhawan, Christopher L. Cunningham, and Nicolas Grillet. Loxhd1 is indispensable for coupling auditory mechanosensitive channels to the site of force transmission. Research Square, Jan 2024. URL: https://doi.org/10.21203/rs.3.rs-3752492/v1, doi:10.21203/rs.3.rs-3752492/v1. This article has 3 citations.
(wang2024loxhd1isindispensable pages 14-18): Pei Wang, Katharine K. Miller, Enqi He, Siddhant S. Dhawan, Christopher L. Cunningham, and Nicolas Grillet. Loxhd1 is indispensable for coupling auditory mechanosensitive channels to the site of force transmission. Research Square, Jan 2024. URL: https://doi.org/10.21203/rs.3.rs-3752492/v1, doi:10.21203/rs.3.rs-3752492/v1. This article has 3 citations.
(wang2024loxhd1isindispensable pages 51-55): Pei Wang, Katharine K. Miller, Enqi He, Siddhant S. Dhawan, Christopher L. Cunningham, and Nicolas Grillet. Loxhd1 is indispensable for coupling auditory mechanosensitive channels to the site of force transmission. Research Square, Jan 2024. URL: https://doi.org/10.21203/rs.3.rs-3752492/v1, doi:10.21203/rs.3.rs-3752492/v1. This article has 3 citations.