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Protein Composition of TGFBI-R124C- and TGFBI-R555W- Associated Aggregates Suggests Multiple Mechanisms Leading to Lattice and Granular Corneal Dystrophy.

Courtney, David G, Toftgaard Poulsen, Ebbe, Kennedy, Susan, Moore, Johnny E, Atkinson, Sarah, Maurizi, Eleonora, Nesbit, M. Andrew, Moore, Tara and Enghild, Jan J (2015) Protein Composition of TGFBI-R124C- and TGFBI-R555W- Associated Aggregates Suggests Multiple Mechanisms Leading to Lattice and Granular Corneal Dystrophy. Investigative ophthalmology & visual science, 56 (8). pp. 4653-61. [Journal article]

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DOI: 10.1167/iovs.15-16922

Abstract

The study reveals previously unknown differences between the protein composition of GCD1 and LCD1 aggregates, and confirms the presence of the HtrA1 protease in LCD1-amyloid aggregates. In addition, we find mutation-specific differences in the processing of mutant TGFBIp species, which may contribute to the variable phenotypes noted in TGFBI-related dystrophies.

Item Type:Journal article
Keywords:Transforming growth factor beta-induced Granular Corneal Dystrophy Lattice Corneal Dystrophy
Faculties and Schools:Faculty of Life and Health Sciences > School of Biomedical Sciences
Faculty of Life and Health Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Genomic Medicine
Biomedical Sciences Research Institute > Stratified Medicine
ID Code:32235
Deposited By: Dr Andrew Nesbit
Deposited On:25 Aug 2015 15:50
Last Modified:23 May 2017 10:50

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