A Glycine-to-Arginine Substitution in the Triple-Helical Domain of Type VII Collagen in a Family with Dominant Dystrophic Epidermolysis Bullosa Pruriginosa
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Dermatology,Molecular Biology,Biochemistry
Reference20 articles.
1. Cloning of human type VII collagen gene. Complete primary sequence of the α(VII) chain and identification of intragenic polymorphism;Christiano;J Biol Chem,1994
2. Structural organization of the human type VII collagen gene (COL7A1), comprised of more exons than any previously characterized gene;Christiano;Genomics,1994
3. Dominant dystrophic epidermolysis bullosa: identification of a glycine-to-serine substitution in the triple-helical domain of type VII collagen;Christiano;Proc Natl Acad Sci USA,1994
4. Pretibial epidermolysis bullosa: genetic linkage to COL7AI and identification of a glycine-to-cysteine substitution in the triple-helical domain of type VII collagen;Christiano;Hum Mol Genet,1995
5. A glycine-to-arginine substitution in the triple helical domain of type VII collagen;Christiano;J Invest Dermatol,1995
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