Collagens, modifying enzymes and their mutations in humans, flies and worms.

By J. Myllyharju, K. Kivirikko. Trends in Genetics, 2004

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View Paper: https://www.semanticscholar.org/paper/e4b0dabb6b9752b51412882823666b603b004e3f

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Citations in the corpus

Collagens at a glance (2007, background): “These include several hydroxylases, two collagen glycosyltransferases and peptidyl cis-trans isomerase, in addition to protein disulphide isomerase (PDI) (for a review, see Myllyharju and Kivirikko, 2004).”
Interstitial fluid and lymph formation and transport: physiological regulation and roles in inflammation and cancer. (2012, background): “There are 28 types of collagen reported to date in vertebrates, that based on supramolecular assemblies and other features can be grouped into nine distinct families (227, 309).”
Dynamic interplay between the collagen scaffold and tumor evolution (2010, background): “Such collagen-derived proteolytic fragments include endostatin (from type XVIII collagen), restin (from type XV collagen) and tumstatin (from type IV collagen) that have anti-angiogenic and tumor growth inhibitory functions [4,105].”
Ascorbic acid: Chemistry, biology and the treatment of cancer (2012, background): “There are at least three isozymes of collagen prolyl hydroxylase in humans each with distinct α subunits; but they all have protein disulfide isomerases (PDIs) to serve as β subunits, which catalyze the formation of intra- and interchain disulfide bonds during collagen synthesis [67].”
Mammalian collagen IV (2008, background): “Biosynthesis and Modifications Similar to other collagens, the biosynthesis of collagen IV is a complex process involving many co- and posttranslational modifications catalyzed by several specific and nonspecific enzymes (Myllyharju and Kivirikko, 2004).”
The extracellular matrix at a glance (2010, background): “Myofibroblasts, which have a high capacity to synthesize ECM components and are highly contractile, can promote the formation of large, rigid collagen bundles that, if crosslinked by LOX enzymes, mechanically strengthen and stiffen the tissue (Szauter et al., 2005).”
New Perspectives on Osteogenesis Imperfecta (2011, neutral): “Procollagen is extensively hydroxylated and glycosylated post-translationally ( Box 1 )”