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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 as human MYO7A, alias USH1B, encoding unconventional myosin-VIIa (UniProt Q13402). The literature matches the supplied identity, organism, motor family and FERM-containing architecture; no evidence concerning a different similarly named gene was used. MYO7A is primarily a slow, actin-activated ATPase motor and mechanical tether. It converts ATP hydrolysis into directed movement or sustained force on F-actin, while its long tail binds membrane-associated cargo and multiprotein complexes. Its best-established physiological functions are: (1) anchoring and tensioning the mechanotransduction apparatus in inner-ear hair-cell stereocilia and (2) transporting or retaining melanosomes and phagosomes in retinal pigment epithelium (RPE). A proposed photoreceptor-ciliary transport role is supported by animal and localization data but is less settled than its RPE function. (coluccio2020myosinsanddisease. pages 280-282, radhakrishnan2022theroleof pages 19-21, radhakrishnan2022theroleof pages 9-11, miyoshi2024pathophysiologyofhuman pages 11-12)
Biallelic loss-of-function variants cause Usher syndrome type 1B, classically combining congenital profound sensorineural deafness, vestibular dysfunction and progressive retinitis pigmentosa. Some alleles cause nonsyndromic recessive or dominant hearing loss or isolated retinal disease, indicating substantial allele- and residual-function dependence. (miyoshi2024pathophysiologyofhuman pages 17-18, miyoshi2024pathophysiologyofhuman pages 11-12)
Independent reviews identify MYO7A as the myosin-VIIa protein associated with USH1B and describe expression in cochlea and retina. The architecture reported in the literature—motor head, five IQ motifs, single-α-helix segment and tandem MyTH4–FERM modules separated by SH3—is consistent with the supplied UniProt FERM/Band-4.1-domain annotations. (coluccio2020myosinsanddisease. pages 280-282, radhakrishnan2022theroleof pages 19-21, miyoshi2024pathophysiologyofhuman pages 11-12)
The supplied InterPro Band_41_domain, FERM_domain, FERM_central, FERM_2 and FERM/acyl-CoA-binding-protein superfamily calls therefore describe parts or structural classifications of the tandem FERM-containing cargo-binding tail; MYO7A is not primarily an acyl-CoA enzyme.
| Topic/system | Precise molecular role or finding | Key quantitative evidence | Evidence type | Source/date/URL |
|---|---|---|---|---|
| Identity and architecture | Human MYO7A/USH1B encodes unconventional myosin-VIIa, an actin-based ATPase motor. Its architecture comprises an N-terminal motor, a neck with five IQ motifs, a single-α-helix region, and an approximately 1,200-residue cargo-binding tail containing two MyTH4–FERM modules separated by an SH3 domain. (coluccio2020myosinsanddisease. pages 280-282, miyoshi2024pathophysiologyofhuman pages 11-12) | Five IQ motifs; two MyTH4–FERM modules; one SH3 domain | Curated protein annotation supported by biochemical and structural reviews | Coluccio, 2020, DOI; Miyoshi et al., March 2024, DOI |
| Motor kinetics and regulation | The long human isoform has greater actin-activated ATPase and gliding activity than the short isoform. Purified full-length MYO7A is predominantly monomeric and folded/autoinhibited; artificial dimerization or binding to the cargo adaptor MyRIP produces processive actin movement. (hollo2024molecularregulatorymechanism pages 6-8, hollo2024molecularregulatorymechanism pages 5-6) | Long versus short isoform: Vmax 0.83 ± 0.14 versus 0.13 ± 0.06 s⁻¹; Km 27 ± 5 versus 8 ± 1.1 μM actin; gliding 5.4 ± 0.9 versus 3.0 ± 0.9 nm/s. Zipper dimer: 4.3 ± 1.5 nm/s, 378-nm run length. MYO7A–MyRIP: 7.8 ± 4.2 nm/s, 552-nm run length, 113-s attachment. | Primary biochemical, electron-microscopy, ensemble-motility, and single-molecule study | Holló et al., October 2023, JBC 299:105243, DOI |
| Inner-ear stereocilia | MYO7A localizes at the upper tip-link density, where it associates with harmonin/USH1C, SANS/USH1G and CDH23 and mechanically couples the tip link to stereociliary F-actin. Through the PCDH15–TMC1/TMC2 complex on the adjacent shorter stereocilium, it supports tip-link tension, mechanotransduction-current amplitude, stereocilia organization, hearing and balance. (miyoshi2024pathophysiologyofhuman pages 11-12, hollo2024molecularregulatorymechanism pages 8-9) | Dimerized human MYO7A has been reported to move at 11.0 ± 0.6 nm/s; MYO7A disruption reduces mechanotransduction currents and produces tip-link abnormalities. | Authoritative 2024 review synthesizing biochemical, localization, genetic and conditional-deletion experiments | Miyoshi et al., March 2024, DOI |
| Retinal pigment epithelium | MYO7A couples RPE cargo to cortical actin. The RAB27A–MyRIP–MYO7A machinery captures or positions melanosomes in the actin-rich apical domain; MYO7A also contributes to photoreceptor-outer-segment phagosome internalization/clearance and lysosomal transport. Loss causes abnormal melanosome localization, delayed phagosome processing and retinal transport defects. (radhakrishnan2022theroleof pages 19-21, radhakrishnan2022theroleof pages 9-11) | No definitive human kinetic rate reported; Myo7a-null experimental models show melanosome and phagosome trafficking defects. | Cell-biological and animal-model evidence synthesized in a retinal motor-protein review | Radhakrishnan et al., April 2022, DOI |
| MYO7A retinal natural history | A multicenter prospective study followed people with biallelic MYO7A-associated Usher syndrome at baseline and two annual visits. Retinal progression was generally slow; significant decline was detected in better-eye visual acuity, while fundus-autofluorescence patterns stratified structural and functional severity and were proposed as trial-selection biomarkers. (testa2024multicentriclongitudinalprospective pages 1-2) | 53 patients, mean age 33.6 ± 16.7 years; 50 included longitudinally. Baseline better-eye BCVA 66.4 ± 17.9 ETDRS letters, macular sensitivity 9.7 ± 9.9 dB, ellipsoid-zone width 2,807.5 ± 2,374.6 μm. Foveal patch in 31.4%, central hypoautofluorescence in 17.6%, ring pattern in 43.1% of assessed eyes. | Prospective multicenter human natural-history study | Testa et al., June 2024, IOVS 65:25, DOI |
| Dual-AAV8 clinical translation | AAVB-081 uses two AAV8 vectors to deliver/reconstitute MYO7A beyond the capacity of a single AAV. The multicenter, open-label, sequential dose-escalation study administers one subretinal dose to adults with molecularly confirmed MYO7A-related USH1B retinitis pigmentosa. Its principal objective is long-term safety; perimetry provides exploratory efficacy outcomes. (NCT06591793 chunk 1) | Phase 1/2; planned 15 adults, ages 18–50; three dose levels; adverse events, microperimetry and static perimetry followed for 61 months; study start July 2, 2024; estimated completion July 2029. | Recruiting interventional human trial; no efficacy result yet | AAVantgarde Bio, 2024, ClinicalTrials.gov NCT06591793 |
Table: Compact evidence matrix linking MYO7A architecture and molecular mechanisms to its auditory and retinal functions, human natural history, and dual-AAV clinical translation. Quantitative findings are separated by evidence type to distinguish established biology from ongoing clinical testing.
MYO7A catalyzes the standard myosin reaction:
ATP + H₂O → ADP + inorganic phosphate, coupled to conformational changes that generate force and plus-end-directed movement on filamentous actin.
Its relevant substrates are therefore ATP and F-actin—not a transported small molecule. Cargo specificity resides largely in the tail and adaptor proteins rather than in the ATPase active site. MYO7A is characterized as a slow, high-duty-ratio motor, a design suited to long actin attachment, tension maintenance, organelle capture and slow cargo movement rather than rapid bulk transport. (coluccio2020myosinsanddisease. pages 280-282, radhakrishnan2022theroleof pages 9-11)
Holló and colleagues’ primary biochemical analysis, published October 2023 in Journal of Biological Chemistry, found that the long N-terminal isoform had an actin-activated ATPase Vmax of 0.83 ± 0.14 s⁻¹ and apparent actin Km of 27 ± 5 μM. The short isoform was markedly less active—0.13 ± 0.06 s⁻¹ and 8 ± 1.1 μM, respectively. Actin-gliding velocities were 5.4 ± 0.9 nm/s for the long and 3.0 ± 0.9 nm/s for the short construct. These unusually low speeds reinforce the interpretation that MYO7A is optimized for sustained mechanical work. N-terminal GFP tagging reduced activity, an important experimental caveat because a tag can make the long isoform behave more like the short one. Holló et al., 2023, DOI. (hollo2024molecularregulatorymechanism pages 5-6, hollo2024molecularregulatorymechanism pages 8-9)
Purified full-length MYO7A is predominantly monomeric and folded. Tail interaction with the head–neck region suppresses ATPase activity, preventing wasteful motor activity in the absence of cargo. Cargo/adaptor engagement can open the molecule and promote dimerization or clustering, yielding a processive two-headed motor. (coluccio2020myosinsanddisease. pages 280-282, miyoshi2024pathophysiologyofhuman pages 17-18, hollo2024molecularregulatorymechanism pages 6-8)
Artificial zipper-dimerized MYO7A moved at 4.3 ± 1.5 nm/s, with a characteristic run length of 378 nm and run duration of 137 s. Full-length MYO7A complexed with the melanosome adaptor MyRIP moved at 7.8 ± 4.2 nm/s, with a 552-nm run length and 113-s attachment. Thus, MyRIP is not merely a passive cargo hook: it can assemble a motile motor–adaptor complex. Elevated Ca²⁺ inhibits motility and promotes calmodulin dissociation, whereas Ca²⁺-insensitive CALML4 may help preserve lever-arm integrity. (hollo2024molecularregulatorymechanism pages 6-8, hollo2024molecularregulatorymechanism pages 5-6)
MYO7A is enriched in the actin-rich stereocilia of cochlear and vestibular hair cells and localizes particularly to the upper tip-link density. There it interacts with harmonin/USH1C, SANS/USH1G and CDH23. The tip link spans adjacent stereocilia; PCDH15 at its lower end couples to the TMC1/TMC2 mechanotransduction-channel complex. MYO7A and associated Usher proteins connect the upper complex to stereociliary F-actin, maintain tension and support appropriate mechanotransduction-channel gating. (hollo2024molecularregulatorymechanism pages 12-12, miyoshi2024pathophysiologyofhuman pages 11-12)
This is broader than vesicle transport: MYO7A functions as a force-generating anchor and tension regulator. Its slow, persistent actin interaction is well matched to this role. Loss or disruption produces malformed stereocilia, tip-link abnormalities and reduced mechanotransduction currents. Conditional postnatal deletion can diminish currents even when some tip links remain, indicating a continuing physiological role beyond initial bundle construction. The 2023 biochemical study further proposed that splice-isoform differences could tune tip-link tension along the cochlear tonotopic axis, although this remains a mechanistic model rather than established human physiology. (miyoshi2024pathophysiologyofhuman pages 11-12, hollo2024molecularregulatorymechanism pages 8-9)
The strongest retinal cell-biological evidence places MYO7A in the RPE, especially its actin-rich apical domain. RAB27A on melanosomes recruits MyRIP, which links the organelle to MYO7A. This machinery transfers, captures or retains melanosomes on cortical actin after microtubule-dependent delivery. Correct apical melanosome positioning contributes to light absorption and retinal protection. (radhakrishnan2022theroleof pages 19-21, radhakrishnan2022theroleof pages 9-11)
MYO7A therefore operates within a coordinated transport pathway rather than acting alone: microtubule motors deliver melanosomes toward the apical region, and MYO7A supports their actin-dependent terminal movement and localization. The MyRIP-induced processivity measured in vitro supplies a molecular explanation for this RPE pathway. (hollo2024molecularregulatorymechanism pages 6-8)
RPE cells ingest shed photoreceptor outer-segment material each day. MYO7A participates in phagosome internalization, movement and lysosomal processing. MYO7A-deficient models show abnormal RPE cytoskeletal organization and delayed phagosome handling, providing a plausible route from motor dysfunction to chronic photoreceptor stress. (radhakrishnan2022theroleof pages 9-11)
Lower MYO7A levels have been reported at the photoreceptor connecting cilium. Myo7a-null mice expressing tagged rhodopsin showed rhodopsin accumulation in inner segments by two months, leading to the proposal that MYO7A cooperates with kinesin-2 in opsin passage toward the outer segment. MYO7A has also been linked to normal RPE65 localization and retinoid-cycle organization. These findings support a ciliary/photoreceptor role, but current evidence is more indirect and model-dependent than the RPE melanosome phenotype; it should not be represented as a fully resolved direct cargo pathway in human photoreceptors. (radhakrishnan2022theroleof pages 19-21, radhakrishnan2022theroleof pages 11-12)
Biallelic pathogenic variants generally reduce motor activity, destabilize the protein, impair cargo/partner binding or disrupt stereociliary and RPE localization. The resulting phenotype is USH1B: congenital severe-to-profound sensorineural hearing loss, vestibular areflexia or hypofunction and progressive retinal degeneration. MYO7A defects can also cause DFNB2 recessive deafness, DFNA11 dominant hearing loss or isolated retinitis pigmentosa, demonstrating that molecular consequence and residual function matter more than gene name alone. (miyoshi2024pathophysiologyofhuman pages 17-18, miyoshi2024pathophysiologyofhuman pages 11-12)
A 2021 computational analysis evaluated 706 disease-associated missense variants and estimated that 43.26% of HGMD and 41.9% of ClinVar variants had high predicted destabilizing effects. Motor and MyTH4 regions appeared particularly vulnerable. These are structural predictions—not direct functional assays—and should be used for hypothesis generation or variant prioritization rather than stand-alone pathogenicity classification. Sergeev & Kuppa, March 2021, DOI. (sergeev2021homologymodelingand pages 8-9)
The major 2023 advance was direct reconstitution of human MYO7A regulation and processivity. Holló et al. connected N-terminal splicing, light-chain composition, folded autoinhibition and cargo-adaptor-induced dimerization to measurable ATPase and single-molecule behavior. In expert interpretation, this supports a unified model in which MYO7A is kept inactive in transit or without cargo, then activated locally to transport organelles or maintain mechanical tension. (hollo2024molecularregulatorymechanism pages 6-8, hollo2024molecularregulatorymechanism pages 5-6, hollo2024molecularregulatorymechanism pages 8-9)
A June 2024 European multicenter prospective study followed 53 individuals with biallelic, mostly pathogenic MYO7A variants; mean age was 33.6 ± 16.7 years, and 50 contributed longitudinal data across baseline and two annual visits. Baseline better-eye visual acuity averaged 66.4 ± 17.9 ETDRS letters, macular sensitivity 9.7 ± 9.9 dB, and ellipsoid-zone width 2,807.5 ± 2,374.6 μm. Over follow-up, only better-eye visual acuity declined significantly; worse-eye parameters did not change significantly, confirming that short-interval progression is slow and trial endpoints must be highly sensitive. Testa et al., June 2024, DOI. (testa2024multicentriclongitudinalprospective pages 1-2)
Fundus-autofluorescence patterns stratified severity: a foveal patch occurred in 31.4%, central hypoautofluorescence in 17.6%, and a hyperautofluorescent ring in 43.1% of assessed eyes. Patch and central hypoautofluorescence patterns were associated with worse structural and functional measurements. The investigators recommend autofluorescence pattern as an objective staging and patient-selection biomarker for interventional trials. (testa2024multicentriclongitudinalprospective pages 1-2)
A 2024 zebrafish knockout study associated myo7aa deficiency with downregulation of Rho-GTPase-pathway genes and partial rescue by ATP/GTP supplementation. This is exploratory nonhuman evidence: it may identify secondary cytoskeletal responses but does not yet establish a direct human MYO7A signaling pathway or justify nucleotide supplementation clinically.
MYO7A is included in hereditary hearing-loss and inherited-retinal-disease sequencing panels. Molecular confirmation distinguishes USH1B from nonsyndromic deafness before retinal symptoms become obvious, supports recessive-risk counseling and identifies candidates for genotype-specific trials. Current hearing management includes hearing aids where useful and, frequently, cochlear implantation; no approved therapy presently corrects the MYO7A retinal defect. Genetic testing is particularly important because different MYO7A alleles can produce syndromic, hearing-only or retinal-only phenotypes. (miyoshi2024pathophysiologyofhuman pages 17-18, miyoshi2024pathophysiologyofhuman pages 11-12)
Usher syndrome prevalence estimates vary by ascertainment. A recent natural-history report cites 3–6 per 100,000 and approximately half of hereditary combined deaf-blindness, while a 2024 cochlear-implant review cites 4–17 per 100,000. These ranges should not be interpreted as MYO7A-specific prevalence. (testa2024multicentriclongitudinalprospective pages 1-2)
The principal current implementation is NCT06591793, “Study of Subretinally Injected AAVB-081 in Patients With Usher Syndrome Type IB Retinitis Pigmentosa.” It is a recruiting, multicenter, open-label, nonrandomized Phase 1/2 dose-escalation trial of AAVB-081, a dual-AAV8 MYO7A gene-replacement product. A single subretinal administration is planned across three dose cohorts in 15 adults aged 18–50 years with molecularly confirmed MYO7A-related USH1B. The study started July 2, 2024; completion is estimated for July 2029. The primary outcome is treatment-related adverse-event number and severity over 61 months; microperimetry and static perimetry are secondary efficacy measures. Sponsor: AAVantgarde Bio Srl. ClinicalTrials.gov, NCT06591793. (NCT06591793 chunk 1)
This trial overcomes MYO7A’s incompatibility with the approximately 4.7-kb payload of one AAV by splitting its expression cassette between two AAV8 vectors for intracellular reconstitution. Importantly, it is an ongoing safety/early-efficacy study; there are not yet published efficacy results in the retrieved record. (bhat2024keychallengesin pages 6-8, NCT06591793 chunk 1)
Dual-AAV systems have reconstituted full-length MYO7A in mouse, pig and nonhuman-primate retinal models. Lentiviral vectors, which accommodate roughly 9 kb, have corrected selected melanosome, phagosome and opsin-localization phenotypes in MYO7A-deficient mice. An earlier subretinal EIAV-lentiviral program expressing MYO7A isoform 2 entered human development but was abandoned before efficacy could be adequately assessed; it should not be cited as evidence of clinical benefit. (bhat2024keychallengesin pages 6-8, gilmore2023advancingtoolsfor pages 53-57)
Authoritative assessments converge on several barriers:
A further biological uncertainty is whether MYO7A’s major retinal-disease driver is primarily RPE melanosome/phagosome dysfunction, a direct photoreceptor-ciliary defect, or a combination. Human cell and organoid models may help separate these compartments, but animal phenotypes and localization observations should not automatically be equated with direct human cargo transport.
MYO7A is best functionally annotated as a regulated, slow actin motor and tension-bearing cargo adaptor. Its motor head hydrolyzes ATP; its IQ/light-chain neck transduces force; and its MyTH4–FERM/SH3 tail targets the motor to membrane cargo and Usher-protein assemblies. In hair cells it anchors and tensions the upper tip-link mechanotransduction complex. In RPE it couples melanosomes and phagosomes to apical actin and supports organelle positioning and degradation. These precise functions explain why pathogenic variants jointly disrupt hearing, balance and retinal survival.
The most important recent advances are the 2023 quantitative description of cargo-activated human MYO7A processivity, the 2024 prospective definition of slowly progressive retinal outcomes and staging biomarkers, and initiation of the first current dual-AAV8 MYO7A Phase 1/2 program. Clinical efficacy remains unproven, so present real-world use is molecular diagnosis, counseling, retinal monitoring and auditory rehabilitation, with gene replacement still investigational.
References
(coluccio2020myosinsanddisease. pages 280-282): L. M. Coluccio. Myosins and disease. Advances in experimental medicine and biology, 1239:245-316, 2020. URL: https://doi.org/10.1007/978-3-030-38062-5_12, doi:10.1007/978-3-030-38062-5_12. This article has 33 citations and is from a peer-reviewed journal.
(radhakrishnan2022theroleof pages 19-21): Rakesh Radhakrishnan, Venkateshwara R. Dronamraju, Matthias Leung, Andrew Gruesen, Ashish K. Solanki, Stephen Walterhouse, Heidi Roehrich, Grace Song, Rafael da Costa Monsanto, Sebahattin Cureoglu, René Martin, Altaf A. Kondkar, Frederik J. van Kuijk, Sandra R. Montezuma, Hans-Joachim Knöelker, Robert B. Hufnagel, and Glenn P. Lobo. The role of motor proteins in photoreceptor protein transport and visual function. Ophthalmic Genetics, 43:285-300, Apr 2022. URL: https://doi.org/10.1080/13816810.2022.2062391, doi:10.1080/13816810.2022.2062391. This article has 13 citations and is from a peer-reviewed journal.
(radhakrishnan2022theroleof pages 9-11): Rakesh Radhakrishnan, Venkateshwara R. Dronamraju, Matthias Leung, Andrew Gruesen, Ashish K. Solanki, Stephen Walterhouse, Heidi Roehrich, Grace Song, Rafael da Costa Monsanto, Sebahattin Cureoglu, René Martin, Altaf A. Kondkar, Frederik J. van Kuijk, Sandra R. Montezuma, Hans-Joachim Knöelker, Robert B. Hufnagel, and Glenn P. Lobo. The role of motor proteins in photoreceptor protein transport and visual function. Ophthalmic Genetics, 43:285-300, Apr 2022. URL: https://doi.org/10.1080/13816810.2022.2062391, doi:10.1080/13816810.2022.2062391. This article has 13 citations and is from a peer-reviewed journal.
(miyoshi2024pathophysiologyofhuman pages 11-12): Takushi Miyoshi, Inna A. Belyantseva, Mrudhula Sajeevadathan, and Thomas B. Friedman. Pathophysiology of human hearing loss associated with variants in myosins. Frontiers in Physiology, Mar 2024. URL: https://doi.org/10.3389/fphys.2024.1374901, doi:10.3389/fphys.2024.1374901. This article has 21 citations.
(miyoshi2024pathophysiologyofhuman pages 17-18): Takushi Miyoshi, Inna A. Belyantseva, Mrudhula Sajeevadathan, and Thomas B. Friedman. Pathophysiology of human hearing loss associated with variants in myosins. Frontiers in Physiology, Mar 2024. URL: https://doi.org/10.3389/fphys.2024.1374901, doi:10.3389/fphys.2024.1374901. This article has 21 citations.
(hollo2024molecularregulatorymechanism pages 5-6): Alexandra Holló, Neil Billington, Yasuharu Takagi, András Kengyel, James R. Sellers, and Rong Liu. Molecular regulatory mechanism of human myosin-7a. Journal of Biological Chemistry, 299:105243, Oct 2023. URL: https://doi.org/10.1016/j.jbc.2023.105243, doi:10.1016/j.jbc.2023.105243. This article has 11 citations and is from a domain leading peer-reviewed journal.
(hollo2024molecularregulatorymechanism pages 6-8): Alexandra Holló, Neil Billington, Yasuharu Takagi, András Kengyel, James R. Sellers, and Rong Liu. Molecular regulatory mechanism of human myosin-7a. Journal of Biological Chemistry, 299:105243, Oct 2023. URL: https://doi.org/10.1016/j.jbc.2023.105243, doi:10.1016/j.jbc.2023.105243. This article has 11 citations and is from a domain leading peer-reviewed journal.
(hollo2024molecularregulatorymechanism pages 8-9): Alexandra Holló, Neil Billington, Yasuharu Takagi, András Kengyel, James R. Sellers, and Rong Liu. Molecular regulatory mechanism of human myosin-7a. Journal of Biological Chemistry, 299:105243, Oct 2023. URL: https://doi.org/10.1016/j.jbc.2023.105243, doi:10.1016/j.jbc.2023.105243. This article has 11 citations and is from a domain leading peer-reviewed journal.
(testa2024multicentriclongitudinalprospective pages 1-2): Francesco Testa, Ester Carreño, L. Ingeborgh van den Born, Paolo Melillo, Irene Perea-Romero, Valentina Di Iorio, Giulia Risca, Clemente Maria Iodice, Ronald J. E. Pennings, Marianthi Karali, Sandro Banfi, Alberto Auricchio, Stefania Galimberti, Carmen Ayuso, and Francesca Simonelli. Multicentric longitudinal prospective study in a european cohort of myo7a patients: disease course and implications for gene therapy. Jun 2024. URL: https://doi.org/10.1167/iovs.65.6.25, doi:10.1167/iovs.65.6.25. This article has 8 citations and is from a domain leading peer-reviewed journal.
(NCT06591793 chunk 1): Study of Subretinally Injected AAVB-081 in Patients With Usher Syndrome Type IB (USH1B) Retinitis Pigmentosa. AAVantgarde Bio Srl. 2024. ClinicalTrials.gov Identifier: NCT06591793
(hollo2024molecularregulatorymechanism pages 12-12): Alexandra Holló, Neil Billington, Yasuharu Takagi, András Kengyel, James R. Sellers, and Rong Liu. Molecular regulatory mechanism of human myosin-7a. Journal of Biological Chemistry, 299:105243, Oct 2023. URL: https://doi.org/10.1016/j.jbc.2023.105243, doi:10.1016/j.jbc.2023.105243. This article has 11 citations and is from a domain leading peer-reviewed journal.
(radhakrishnan2022theroleof pages 11-12): Rakesh Radhakrishnan, Venkateshwara R. Dronamraju, Matthias Leung, Andrew Gruesen, Ashish K. Solanki, Stephen Walterhouse, Heidi Roehrich, Grace Song, Rafael da Costa Monsanto, Sebahattin Cureoglu, René Martin, Altaf A. Kondkar, Frederik J. van Kuijk, Sandra R. Montezuma, Hans-Joachim Knöelker, Robert B. Hufnagel, and Glenn P. Lobo. The role of motor proteins in photoreceptor protein transport and visual function. Ophthalmic Genetics, 43:285-300, Apr 2022. URL: https://doi.org/10.1080/13816810.2022.2062391, doi:10.1080/13816810.2022.2062391. This article has 13 citations and is from a peer-reviewed journal.
(sergeev2021homologymodelingand pages 8-9): Yuri V Sergeev and Annapurna Kuppa. Homology modeling and global computational mutagenesis of human myosin viia. Journal of analytical & pharmaceutical research, 10:41-48, Mar 2021. URL: https://doi.org/10.15406/japlr.2021.10.00364, doi:10.15406/japlr.2021.10.00364. This article has 3 citations.
(bhat2024keychallengesin pages 6-8): Rajeshwari Bhat, Bhargavi Nallamothu, Foram Shethia, Vatsal Chhaya, and Kapil Khambholja. Key challenges in developing a gene therapy for usher syndrome: machine-assisted scoping review. Journal of community genetics, 15:735-747, Nov 2024. URL: https://doi.org/10.1007/s12687-024-00749-0, doi:10.1007/s12687-024-00749-0. This article has 2 citations and is from a peer-reviewed journal.
(gilmore2023advancingtoolsfor pages 53-57): WB Gilmore. Advancing tools for treating usher syndrome 1b and elucidating the role of myosin viia in the retinal pigment epithelium. Unknown journal, 2023.
(bhat2024keychallengesin pages 9-10): Rajeshwari Bhat, Bhargavi Nallamothu, Foram Shethia, Vatsal Chhaya, and Kapil Khambholja. Key challenges in developing a gene therapy for usher syndrome: machine-assisted scoping review. Journal of community genetics, 15:735-747, Nov 2024. URL: https://doi.org/10.1007/s12687-024-00749-0, doi:10.1007/s12687-024-00749-0. This article has 2 citations and is from a peer-reviewed journal.