{"entity": "researcher", "timestamp": "2026-08-22T08:32:20.482Z", "family": "Li", "given": "Honglian", "initials": "H", "orcid": "0000-0002-5820-3121", "affiliations": ["Department of Medical Biochemistry and Microbiology, University of Uppsala, Husargatan 3, 75123, Uppsala, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/7a3ac57ba039433b8eacad4504af66fd.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/7a3ac57ba039433b8eacad4504af66fd"}}, "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": "562b856a3ed24a748a9c2d4443482280", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/562b856a3ed24a748a9c2d4443482280.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/562b856a3ed24a748a9c2d4443482280"}}, "title": "Heparanase Modulates Chromatin Accessibility.", "authors": [{"family": "Li", "given": "Honglian", "initials": "H", "orcid": "0000-0002-5820-3121", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/7a3ac57ba039433b8eacad4504af66fd.json"}}, {"family": "Zhang", "given": "Hua", "initials": "H"}, {"family": "Wenz", "given": "Amelie", "initials": "A", "orcid": "0000-0003-1929-382X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/262d770d769340bc8cf743701280a879.json"}}, {"family": "Kang", "given": "Ziqi", "initials": "Z"}, {"family": "Wang", "given": "Helen", "initials": "H"}, {"family": "Vlodavsky", "given": "Israel", "initials": "I"}, {"family": "Chen", "given": "Xingqi", "initials": "X", "orcid": "0000-0002-5657-2839", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5ffb9d3c94e54fac97be6c78586940eb.json"}}, {"family": "Li", "given": "Jinping", "initials": "J"}], "type": "journal article", "published": "2023-03-14", "journal": {"title": "Cells", "issn": "2073-4409", "volume": "12", "issue": "6", "issn-l": "2073-4409"}, "abstract": "Heparanase is the sole endoglucuronidase that degrades heparan sulfate in the cell surface and extracellular matrix (ECM). Several studies have reported the localization of heparanase in the cell nucleus, but the functional role of the nuclear enzyme is still obscure. Subjecting mouse embryonic fibroblasts (MEFs) derived from heparanase knockout (Hpse-KO) mice and applying transposase-accessible chromatin with sequencing (ATAC-seq), we revealed that heparanase is involved in the regulation of chromatin accessibility. Integrating with genome-wide analysis of chromatin states revealed an overall low activity in the enhancer and promoter regions of Hpse-KO MEFs compared with wild-type (WT) MEFs. Western blot analysis of MEFs and tissues derived from Hpse-KO vs. WT mice confirmed reduced expression of H3K27ac (acetylated lysine at N-terminal position 27 of the histone H3 protein). Our results offer a mechanistic explanation for the well-documented attenuation of inflammatory responses and tumor growth in Hpse-KO mice.", "doi": "10.3390/cells12060891", "pmid": "36980232", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC10047235"}, {"db": "pii", "key": "cells12060891"}], "notes": [], "created": "2026-08-21T13:02:12.488Z", "modified": "2026-08-21T13:02:12.581Z"}]}