T
Timothy E. Hardingham
Researcher at Wellcome Trust Centre for Cell-Matrix Research
Publications - Â 196
Citations - Â 12997
Timothy E. Hardingham is an academic researcher from Wellcome Trust Centre for Cell-Matrix Research. The author has contributed to research in topics: Cartilage & Proteoglycan. The author has an hindex of 65, co-authored 196 publications receiving 12490 citations. Previous affiliations of Timothy E. Hardingham include Royal Melbourne Hospital & University of Patras.
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Journal ArticleDOI
Proteoglycans: many forms and many functions.
TL;DR: The control of glycosaminoglycan structure is not well understood, but it does appear to be used to change the properties of proteoglycans to suit different biological needs.
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The specific interaction of hyaluronic acid with cartilage proteoglycans
Timothy E. Hardingham,Helen Muir +1 more
TL;DR: The addition of small amounts of hyaluronic acid to disaggregated cartilage proteoglyans produced a large increase in hydrodynamic size on gel chromatography and there was no such interaction when proteoglycans were mixed with other polyanions in comparable proportions.
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The role of link-protein in the structure of cartilage proteoglycan aggregates
TL;DR: The results showed that link-protein greatly strengthened the binding of proteoglycans to hyaluronate and suggest that under physiological conditions it 'locks' proteoglyCans on to the hyAluronate chain.
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Hyaluronic acid in cartilage and proteoglycan aggregation
Timothy E. Hardingham,Helen Muir +1 more
TL;DR: Dissociation of purified proteoglycan aggregates was shown to release an interacting component of buoyant density higher than that of the glycoprotein-link fraction of Hascall & Sajdera (1969), which suggested that each type of proteoglycans contained different protein cores.
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The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B.
TL;DR: Investigation on aggrecan the major proteoglycan of cartilage shows that in spite of a high keratan sulfate content the interglobular domain provides important sites for cleavage by different proteinases, including several members of the matrix metalloproteinase family.