ADAMTS5 expression and function in myoblast fusion and muscle regeneration Kintakas, Christopher 2016, ADAMTS5 expression and function in myoblast fusion and muscle regeneration, PhD thesis, School of Medicine, Deakin Univeristy. Attached Files Name Description MIMEType Size Downloads Title ADAMTS5 expression and function in myoblast fusion and muscle regeneration Author Kintakas, Christopher Institution Deakin Univeristy School School of Medicine Faculty Faculty of Health Degree type Research doctorate Degree name PhD Date submitted 2016-12 Keyword(s) extracellular matrix (ECM) skeletal muscle homeostasis Duchenne muscular dystrophy (DMD), dystrophin mutation ADAMTS5 Summary This research investigated the role of an enzyme called ADAMTS5 in models of skeletal muscle regeneration and muscular dystrophy. This work has led to further investigations to better understand how ADAMTS5 and related proteins may be targeted as a potential treatment for muscular dystrophy. Language eng Field of Research 060106 Cellular Interactions (incl Adhesion, Matrix, Cell Wall) 060103 Cell Development, Proliferation and Death 111601 Cell Physiology Socio Economic Objective 920116 Skeletal System and Disorders (incl. Arthritis) Description of original 152 pages : colour illustrations, tables, graphs Dewey Decimal Classification 616.748 Restricted until 2019-05-25 Copyright notice ©The author Persistent URL http://hdl.handle.net/10536/DRO/DU:30097732 Document type: Thesis Collection: Higher degree theses (citation only)   Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved. Versions Version Filter Type Tue, 11 Jul 2017, 14:04:20 EST Wed, 12 Jul 2017, 08:42:55 EST Wed, 12 Jul 2017, 08:44:08 EST Wed, 12 Jul 2017, 09:55:50 EST Wed, 12 Jul 2017, 10:02:35 EST Filtered Full Citation counts:   Cited 0 times in TR Web of Science Cited 0 times in Scopus Search Google Scholar Access Statistics: 25 Abstract Views, 5 File Downloads  -  Detailed Statistics Created: Tue, 11 Jul 2017, 14:04:05 EST by Kate Percival

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