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He began his research on glycoconjugates in 1971, and he has been active in the field ever since. He did some of the very earliest studies on cell surface heparan sulfate proteoglycans (eg. Developmental Biol. (1975) 44, 253). He characterized the roles of sulfated glycosaminoglycans and hyaluronic acids in the development of corneal transparency, and he performed early studies on the importance of proteoglycan sulfotransferases (eg. J. Biol. Chem. (1976) 251, 6513; J. Biol. Chem. (1978) 253, 347). He showed that keratan sulfate I proteoglycan is synthesized by the N-linked biosynthetic pathway, and he established that the sequon, Asn-X-Ser(Thr) is the minimal structural requirement for recognition by the N-glycan oligosaccharyltransferase. Hart’s laboratory performed some of the earliest studies mapping N-glycan attachment sites and they were among the first to show that N-linked protein glycosylation heterogeneity is site specific and highly regulated by cellular physiology (eg. J. Biol. Chem. (1985) 260, 4046). His group further showed that site-specific N-linked glycosylation is tightly controlled also by protein structure at all levels, even up to the level quaternary structure (eg. J. Biol. Chem. (1986) 261:13186-13196).
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