ReviewProceedings of the Japan Academy. Series B, Physical and biological sciences2012
Synthesis of neoproteoglycans using the transglycosylation reaction as a reverse reaction of endo-glycosidases.
Review in Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 13 citations in OpenAlex.
- Effect of a chondroitin sulfate chain linked to the bikunin core peptide on gene expression in lipopolysaccharide-treated uterine cervical fibroblasts.Biochemistry and biophysics reports · 2025Article
- Endoglycosidases for the Synthesis of Polysaccharides and Glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2016Review
- Chemoenzymatic synthesis of glycosaminoglycans: re-creating, re-modeling and re-designing nature's longest or most complex carbohydrate chains.Glycobiology · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A method for the synthesis of carbohydrate chains (glycosaminoglycans) and their coupling to peptides was investigated using proteoglycans. Glycosidases generally catalyze a hydrolytic reaction, but can also mediate the reverse reaction, which in this case is a transglycosylation. In the transglycosylation reaction of bovine testicular hyaluronidase, which is an endoglycosidase, glycosaminoglycans (hyaluronan and chondroitin sulfates) release disaccharide (uronic acid-N-acetylhexosamine) moieties from non-reducing terminal sites, and then the liberated disaccharides are transferred immediately to the non-reducing termini of other glycosaminoglycan chains. Using such continuous reactions, it is possible to synthesize glycosaminoglycan chains according to a specific design. It then becomes possible to transfer glycosaminoglycan chains synthesized on a peptide to other peptides using the transglycosylation reaction of endo-β-xylosidase acting on the linkage region between a peptide and glycosaminoglycan chains of proteoglycans. We believe this approach will open a new field for the synthesis of homogeneous proteoglycans or their corresponding analogues.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.