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John A. McGrath

Researcher at King's College London

Publications -  674
Citations -  26684

John A. McGrath is an academic researcher from King's College London. The author has contributed to research in topics: Epidermolysis bullosa & Mutation. The author has an hindex of 75, co-authored 631 publications receiving 24078 citations. Previous affiliations of John A. McGrath include Ninewells Hospital & Southampton General Hospital.

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Three-dimensional imaging reveals major changes in skin microvasculature in lipoid proteinosis and lichen sclerosus

TL;DR: It is demonstrated that skin microvasculature is grossly altered when ECM1 is targeted by inherited mutations or acquired autoantibodies (lichen sclerosus) and that this glycoprotein appears to have an important role in regulating blood vessel physiology and anatomy in the skin.
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Molecular basis of EEC (ectrodactyly, ectodermal dysplasia, clefting) syndrome: five new mutations in the DNA-binding domain of the TP63 gene and genotype-phenotype correlation.

TL;DR: The role of TP63 in embryonic development and skin homeostasis, the significant intra‐ and interfamilial phenotypic variability in affected individuals and the emerging paradigm for genotype–phenotype correlation in this inherited ectodermal dysplasia syndrome are discussed.
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Five new homozygous mutations in the KIND1 gene in Kindler syndrome.

TL;DR: Five new homozygous mutations in individuals with KS are described and these and the previously published KIND1 mutations are assessed to explore further the clinical implications of determining Kind1 mutations in this unusual genodermatosis.
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Reduced expression of insulin-like growth factor-binding protein-3 (IGFBP-3) in Squamous cell carcinoma complicating recessive dystrophic epidermolysis bullosa.

TL;DR: Reduced expression of IGFBP-3 in RDEB SCC may provide a partial explanation for the aggressive behavior and poor prognosis of these tumors in this genodermatosis.

Psoriasis bullosa acquisita.

TL;DR: Preliminary evidence is provided that, for this patient at least, the autoantibody may be targeted against a skin component closely associated with type VII collagen (the epidermolysis bullosa acquisita antigen).