ArticleJournal of analytical & pharmaceutical research2018
Dynamic analysis of human tyrosinase intra-melanosomal domain and mutant variants to further understand oculocutaneous albinism type 1.
Article in Journal of analytical & pharmaceutical research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Human recombinant tyrosinase destabilization caused by the double mutation R217Q/R402Q.Protein science : a publication of the Protein Society · 2025Article
- Mutational spectrum associated with oculocutaneous albinism and Hermansky-Pudlak syndrome in nine Pakistani families.BMC ophthalmology · 2024Article
- Trajectory maps: molecular dynamics visualization and analysis.NAR genomics and bioinformatics · 2024Article
- Biophysical Compatibility of a Heterotrimeric Tyrosinase-TYRP1-TYRP2 Metalloenzyme Complex.Frontiers in pharmacology · 2021Article
- FunctionalJournal of analytical & pharmaceutical research · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Human tyrosinase (Tyr) is a Type I membrane glycoprotein that is the rate-limiting enzyme for controlling the production of melanin pigment in melanosomes. Currently, ~300 Tyr mutations are known to be involved in the genetic disease oculocutaneous albinism type 1 (OCA1), which exists in two forms, OCA1A and OCA1B. OCA1A is caused by a full loss of Tyr enzymatic activity, resulting in the absence of pigment in the skin, hair, and eyes, while OCA1B has reduced Tyr activity and pigment. Here, we used molecular modeling to try to understand the role of genetic changes at the protein level in inherited disease. The significant part of Tyr intra-melanosomal domain and five OCA1 mutant variants were built by homology modeling, glycosylated
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Registered trials
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