ArticlePigment cell & melanoma research2017
Oculocutaneous albinism type 1: link between mutations, tyrosinase conformational stability, and enzymatic activity.
Article in Pigment cell & melanoma research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 60 citations in OpenAlex.
- Ampyrone is a direct agonist of human tyrosinase and a potential therapeutic for hypopigmentation disorders.JCI insight · 2026Article
- Mild Oculocutaneous Albinism Type 1B With Subtle Cutaneous Findings: A Dermatology-Oriented Case Report.Cureus · 2026Article
- Population- and haplotype-dependent variation aroundJID innovations : skin science from molecules to population health · 2026Article
- Insights from Computational Dynamic Active Site Mapping into Substrate Recognition and Mutation-Induced Dysfunction in Human Tyrosinase.International journal of molecular sciences · 2026Article
- A rescue assay for genetic diagnosis of oculocutaneous albinism using melanocytic MNT1 knock-out cells.Frontiers in genetics · 2026Article
- Genetic mutations disrupt the coordinated mode of tyrosinase's intra-melanosomal domain.Protein science : a publication of the Protein Society · 2025Article
- Human recombinant tyrosinase destabilization caused by the double mutation R217Q/R402Q.Protein science : a publication of the Protein Society · 2025Article
- The co-occurrence of genetic variants in the TYR and OCA2 genes confers susceptibility to albinism.Nature communications · 2024Article
- Genetic Linkage betweenInternational journal of molecular sciences · 2024Article
- Molecular Modeling of the Multiple-Substrate Activity of the Human Recombinant Intra-Melanosomal Domain of Tyrosinase and Its OCA1B-Related Mutant Variant P406L.International journal of molecular sciences · 2024Article
- Chromosome-level reference genome for North American bison (Bison bison) and variant database aids in identifying albino mutation.G3 (Bethesda, Md.) · 2023Article
- Evaluating the Cysteine-Rich and Catalytic Subdomains of Human Tyrosinase and OCA1-Related Mutants Using 1 μs Molecular Dynamics Simulation.International journal of molecular sciences · 2023Article
- In Vitro Reconstitution of the Melanin Pathway's Catalytic Activities Using Tyrosinase Nanoparticles.International journal of molecular sciences · 2022Article
- The contribution of common regulatory and protein-coding TYR variants to the genetic architecture of albinism.Nature communications · 2022Article
- Identification and characterization of two novel noncoding tyrosinase (TYR) gene variants leading to oculocutaneous albinism type 1.The Journal of biological chemistry · 2022Article
- Protein Biochemistry and Molecular Modeling of the Intra-Melanosomal Domain of Human Recombinant Tyrp2 Protein and OCA8-Related Mutant Variants.International journal of molecular sciences · 2022Article
- Evidence that the Ser192Tyr/Arg402Gln in cis Tyrosinase gene haplotype is a disease-causing allele in oculocutaneous albinism type 1B (OCA1B).NPJ genomic medicine · 2022Article
- Oculocutaneous albinism and bleeding diathesis due to a novel deletion in theFrontiers in genetics · 2022Article
- Assessing Foveal Structure in Individuals withOphthalmology science · 2021Article
- Tyrp1 Mutant Variants Associated with OCA3: Computational Characterization of Protein Stability and Ligand Binding.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Oculocutaneous albinism type 1 (OCA1) is an autosomal recessive disorder caused by mutations in the tyrosinase gene. Two subtypes of OCA1 have been described: severe OCA1A with complete absence of tyrosinase activity and less severe OCA1B with residual tyrosinase activity. Here, we characterize the recombinant human tyrosinase intramelanosomal domain and mutant variants, which mimic genetic changes in both subtypes of OCA1 patients. Proteins were prepared using site-directed mutagenesis, expressed in insect larvae, purified by chromatography, and characterized by enzymatic activities, tryptophan fluorescence, and Gibbs free energy changes. The OCA1A mutants showed very low protein expression and protein yield and are enzymatically inactive. Mutants mimicking OCA1B were biochemically similar to the wild type, but exhibited lower specific activities and protein stabilities. The results are consistent with clinical data, which indicates that OCA1A mutations inactivate tyrosinase and result in severe phenotype, while OCA1B mutations partially inactivate tyrosinase and result in OCA1B albinism.
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