{"entity": "researcher", "timestamp": "2026-08-22T07:48:23.007Z", "family": "Li", "given": "Jin-Ping", "initials": "JP", "orcid": "0000-0002-4255-3581", "affiliations": ["Department of Medical Biochemistry and Microbiology, University of Uppsala, Husargatan 3, 75123, Uppsala, Sweden.", "SciLifeLab, Uppsala University, Husargatan 3, 75123, Uppsala, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/2ab4d6e3d5eb4551a1cc622b5917dc3b.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/2ab4d6e3d5eb4551a1cc622b5917dc3b"}}, "publications": [{"entity": "publication", "iuid": "c91ecd53381846a3aa62a6b266b7b410", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/c91ecd53381846a3aa62a6b266b7b410.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/c91ecd53381846a3aa62a6b266b7b410"}}, "title": "Inhibitors of dermatan sulfate epimerase 1 decreased accumulation of glycosaminoglycans in mucopolysaccharidosis type I fibroblasts.", "authors": [{"family": "Maccarana", "given": "Marco", "initials": "M", "orcid": "0000-0003-3549-8921", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ca8e408602c742478ab42e041504eb38.json"}}, {"family": "Li", "given": "Binjie", "initials": "B", "orcid": "0000-0003-4058-180X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b9474621a26f49558f430c91d61fce07.json"}}, {"family": "Li", "given": "Honglian", "initials": "H", "orcid": "0000-0002-5820-3121", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/7a3ac57ba039433b8eacad4504af66fd.json"}}, {"family": "Fang", "given": "Jianping", "initials": "J", "orcid": "0000-0002-1695-2693", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/19a0d0b14f1f4fd7afbc007555207b5c.json"}}, {"family": "Yu", "given": "Mingjia", "initials": "M", "orcid": "0000-0002-8906-7476", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/8e7da2d9779f41e68ad8e99ab4874812.json"}}, {"family": "Li", "given": "Jin-Ping", "initials": "JP", "orcid": "0000-0002-4255-3581", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2ab4d6e3d5eb4551a1cc622b5917dc3b.json"}}], "type": "journal article", "published": "2024-04-24", "journal": {"title": "Glycobiology", "issn": "1460-2423", "volume": "34", "issue": "6", "issn-l": "0959-6658"}, "abstract": "Genetic deficiency of alpha-L-iduronidase causes mucopolysaccharidosis type I (MPS-I) disease, due to accumulation of glycosaminoglycans (GAGs) including chondroitin/dermatan sulfate (CS/DS) and heparan sulfate (HS) in cells. Currently, patients are treated by infusion of recombinant iduronidase or by hematopoietic stem cell transplantation. An alternative approach is to reduce the L-iduronidase substrate, through limiting the biosynthesis of iduronic acid. Our earlier study demonstrated that ebselen attenuated GAGs accumulation in MPS-I cells, through inhibiting iduronic acid producing enzymes. However, ebselen has multiple pharmacological effects, which prevents its application for MPS-I. Thus, we continued the study by looking for novel inhibitors of dermatan sulfate epimerase 1 (DS-epi1), the main responsible enzyme for production of iduronic acid in CS/DS chains. Based on virtual screening of chemicals towards chondroitinase AC, we constructed a library with 1,064 compounds that were tested for DS-epi1 inhibition. Seventeen compounds were identified to be able to inhibit 27%-86% of DS-epi1 activity at 10 \u03bcM. Two compounds were selected for further investigation based on the structure properties. The results show that both inhibitors had a comparable level in inhibition of DS-epi1while they had negligible effect on HS epimerase. The two inhibitors were able to reduce iduronic acid biosynthesis in CS/DS and GAG accumulation in WT and MPS-I fibroblasts. Docking of the inhibitors into DS-epi1 structure shows high affinity binding of both compounds to the active site. The collected data indicate that these hit compounds may be further elaborated to a potential lead drug used for attenuation of GAGs accumulation in MPS-I patients.", "doi": "10.1093/glycob/cwae025", "pmid": "38760939", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11101759"}, {"db": "pii", "key": "7676076"}], "notes": [], "created": "2026-08-21T12:08:53.529Z", "modified": "2026-08-21T12:08:53.804Z"}, {"entity": "publication", "iuid": "a2a84f83b77f40269b83f336a515b525", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/a2a84f83b77f40269b83f336a515b525.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/a2a84f83b77f40269b83f336a515b525"}}, "title": "Heparan sulfate proteoglycan in Alzheimer's disease: aberrant expression and functions in molecular pathways related to amyloid-\u03b2 metabolism.", "authors": [{"family": "Ozsan McMillan", "given": "Ilayda", "initials": "I", "orcid": "0000-0003-2265-5852", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9ec112240d6845168f9cb25702a20ebf.json"}}, {"family": "Li", "given": "Jin-Ping", "initials": "JP", "orcid": "0000-0002-4255-3581", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2ab4d6e3d5eb4551a1cc622b5917dc3b.json"}}, {"family": "Wang", "given": "Lianchun", "initials": "L", "orcid": "0000-0003-1454-2719", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/85315d991d1e46b3a9ebe4c75e98b0ae.json"}}], "type": "journal article", "published": "2023-04-01", "journal": {"title": "Am. J. Physiol., Cell Physiol.", "issn": "1522-1563", "volume": "324", "issue": "4", "pages": "C893-C909", "issn-l": "0363-6143"}, "abstract": "Alzheimer's disease (AD) is the most common form of dementia. Currently, there is no effective treatment for AD, as its etiology remains poorly understood. Mounting evidence suggests that the accumulation and aggregation of amyloid-\u03b2 peptides (A\u03b2), which constitute amyloid plaques in the brain, is critical for initiating and accelerating AD pathogenesis. Considerable efforts have been dedicated to shedding light on the molecular basis and fundamental origins of the impaired A\u03b2 metabolism in AD. Heparan sulfate (HS), a linear polysaccharide of the glycosaminoglycan family, co-deposits with A\u03b2 in plaques in the AD brain, directly binds and accelerates A\u03b2 aggregation, and mediates A\u03b2 internalization and cytotoxicity. Mouse model studies demonstrate that HS regulates A\u03b2 clearance and neuroinflammation in vivo. Previous reviews have extensively explored these discoveries. Here, this review focuses on the recent advancements in understanding abnormal HS expression in the AD brain, the structural aspects of HS-A\u03b2 interaction, and the molecules involved in modulating A\u03b2 metabolism through HS interaction. Furthermore, this review presents a perspective on the potential effects of abnormal HS expression on A\u03b2 metabolism and AD pathogenesis. In addition, the review highlights the importance of conducting further research to differentiate the spatiotemporal components of HS structure and function in the brain and AD pathogenesis.", "doi": "10.1152/ajpcell.00247.2022", "pmid": "36878848", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC10069967"}], "notes": [], "created": "2026-08-21T12:27:53.614Z", "modified": "2026-08-21T12:27:53.755Z"}]}