Analysis of Mutations in the Copper B Binding Region Associated With Type I (Tyrosinase-Related) Oculocutaneous Albinism
Author:
Publisher
Wiley
Subject
Cell Biology,Clinical Biochemistry,Developmental Biology,Plant Science,Agronomy and Crop Science
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1600-0749.1992.tb00549.x/fullpdf
Reference29 articles.
1. The reaction of CN− with the binuclear copper site of Neurospora tyrosinase: its relevance for a comparison between tyrosinase and hemocyanin active sites
2. A single base insertion in the putative transmembrane domain of the tyrosinase gene as a cause for tyrosinase-negative oculocutaneous albinism.
3. Complete Amino-Acid Sequence of a Functional Unit from a Molluscan Hemocyanin(Helix pomatia)
4. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
5. 3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin
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2. Functional validation of the albinism-associated tyrosinase T373K SNP by CRISPR/Cas9-mediated homology-directed repair (HDR) in rabbits;EBioMedicine;2018-10
3. Oculocutaneous albinism type 1: link between mutations, tyrosinase conformational stability, and enzymatic activity;Pigment Cell & Melanoma Research;2017-01
4. Tyrosinase and ocular diseases: Some novel thoughts on the molecular basis of oculocutaneous albinism type 1;Progress in Retinal and Eye Research;2007-07
5. Polymorphisms in the genes for oculocutaneous albinism type 1 and type 4 in the German population;Pigment Cell Research;2007-06
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