Human keratin 8 mutations that disturb filament assembly observed in inflammatory bowel disease patients

• Main Authors: Owens, D.W, Wilson, N.J, Hill, A.J.M, Rugg, E.L, Porter, R.M, Hutcheson, A.M, Quinlan, R.A, van Heel, D, Parkes, M, Jewell, D.P, Campbell, S.S, Ghosh, S, Satsangi, J, Lane, E.B
• Other Authors: PATHOLOGY
• Format: Article
• Published: 2020
• Subjects: asparagine; cysteine; dimer; glycine; isoleucine; keratin; keratin 8; unclassified drug; valine; article; cell assay; cell differentiation; cell division; controlled study; Crohn disease; cytoskeleton; disease association; disease course; disease severity; enteritis; epidermis; epithelium cell; genetic risk; human; human cell; human cell culture; in vitro study; in vivo study; intermediate filament; intestine epithelium; intestine epithelium cell; missense mutation; oxidative stress; prediction; priority journal; protein polymerization; ulcerative colitis; Animals; Antibodies, Monoclonal; Base Sequence; Cell Differentiation; Chromosomes, Human, Pair 12; Colitis, Ulcerative; Crohn Disease; Dimerization; Electrophoresis, Polyacrylamide Gel; Humans; Inflammation; Inflammatory Bowel Diseases; Keratin-8; Keratins; Mice; Microfilaments; Models, Genetic; Molecular Sequence Data; Mutation; Oxidative Stress; Polymers; Protein Binding; Protein Conformation; Sequence Analysis, DNA; Time Factors; Transfection; Xenopus
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/181109
• Institution: National University of Singapore

10.1242/jcs.01043