{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T17:49:24Z","timestamp":1790272164386,"version":"4.1.0"},"reference-count":56,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2026,2,16]],"date-time":"2026-02-16T00:00:00Z","timestamp":1771200000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Institute for the Study of Inborn Errors of Metabolism at Pontificia Universidad Javeriana","award":["120289301011ZZ"],"award-info":[{"award-number":["120289301011ZZ"]}]},{"name":"Pontificia Universidad Javeria"},{"DOI":"10.13039\/100013918","name":"Sanfilippo Children\u2019s Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100013918","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Fundacja Sanfilippo"},{"name":"Sanfilippo Initiative","award":["2022I_Bleriot-IIIB-PCT"],"award-info":[{"award-number":["2022I_Bleriot-IIIB-PCT"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>The interaction of a set of four N-acetyl-glucosamine (GlcNAc) glycomimetics with human N-acetyl-glucosaminidase (NAGLU), the genetically defective enzyme in patients suffering from mucopolysaccharidosis (MPS) IIIB, also known as Sanfilippo B syndrome, was investigated to identify potential pharmacological chaperones. Glycomimetic\u2013NAGLU binding was initially studied by molecular docking simulations and a thermal shift assay. The effects of the glycomimetics on NAGLU activity enhancement were studied in fibroblast cells from seven MPS IIIB patients. A significant increase in NAGLU activity in four cell lines in the presence of glycomimetic MK 8719, a molecule tested in a Phase 1 study in healthy volunteers to treat Alzheimer\u2019s disease, was demonstrated. Furthermore, MK 8719 prevented the increase in glycosaminoglycan (GAG) levels in four MPS IIIB fibroblast cells, suggesting that this molecule may be worth investigating further as a pharmacological chaperone for MPS IIIB. These results represent an important contribution towards the development of a specific therapy for MPS IIIB.<\/jats:p>","DOI":"10.3390\/biom16020313","type":"journal-article","created":{"date-parts":[[2026,2,16]],"date-time":"2026-02-16T14:55:47Z","timestamp":1771253747000},"page":"313","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Evaluation of GlcNAc-Configured Glycomimetics as Pharmacological Chaperones of NAGLU for the Treatment of Mucopolysaccharidosis IIIB"],"prefix":"10.3390","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8301-3170","authenticated-orcid":false,"given":"Nissrine","family":"Ballout","sequence":"first","affiliation":[{"name":"Toulouse Institute for Infectious and Inflammatory Diseases (Infinity), University of Toulouse, Inserm U1291, CNRS U5051, 31024 Toulouse, France"},{"name":"Biochemistry Laboratory, Federative Institute of Biology, CHU Toulouse, 31024 Toulouse, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1076-3610","authenticated-orcid":false,"given":"J\u00e9r\u00f4me","family":"D\u00e9sir\u00e9","sequence":"additional","affiliation":[{"name":"Organic Synthesis Team, Glycochemistry Group, IC2MP UMR CNRS 7285, Universit\u00e9 of Poitiers, 86073 Poitiers Cedex 9, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9670-6435","authenticated-orcid":false,"given":"Angela Johana","family":"Espejo-Mojica","sequence":"additional","affiliation":[{"name":"Institute for the Study of Inborn Errors of Metabolism, Faculty of Science Pontificia Universidad Javeriana Cra. 7 No. 43-82 Building 54, Lab 305A, Bogot\u00e1 110231, Colombia"},{"name":"Dogma Biotech, Bogot\u00e1 110231, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katherin","family":"Ni\u00f1o-Traslavi\u00f1a","sequence":"additional","affiliation":[{"name":"Institute for the Study of Inborn Errors of Metabolism, Faculty of Science Pontificia Universidad Javeriana Cra. 7 No. 43-82 Building 54, Lab 305A, Bogot\u00e1 110231, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0008-3503-1145","authenticated-orcid":false,"given":"Daniel","family":"Sandoval","sequence":"additional","affiliation":[{"name":"Dogma Biotech, Bogot\u00e1 110231, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6484-1173","authenticated-orcid":false,"given":"Carlos Javier","family":"Alm\u00e9ciga-D\u00edaz","sequence":"additional","affiliation":[{"name":"Institute for the Study of Inborn Errors of Metabolism, Faculty of Science Pontificia Universidad Javeriana Cra. 7 No. 43-82 Building 54, Lab 305A, Bogot\u00e1 110231, Colombia"},{"name":"Dogma Biotech, Bogot\u00e1 110231, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3209-9282","authenticated-orcid":false,"given":"Yves","family":"Bl\u00e9riot","sequence":"additional","affiliation":[{"name":"Organic Synthesis Team, Glycochemistry Group, IC2MP UMR CNRS 7285, Universit\u00e9 of Poitiers, 86073 Poitiers Cedex 9, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3059-9777","authenticated-orcid":false,"given":"J\u00e9r\u00f4me","family":"Ausseil","sequence":"additional","affiliation":[{"name":"Toulouse Institute for Infectious and Inflammatory Diseases (Infinity), University of Toulouse, Inserm U1291, CNRS U5051, 31024 Toulouse, France"},{"name":"Biochemistry Laboratory, Federative Institute of Biology, CHU Toulouse, 31024 Toulouse, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,2,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/nrd.2017.214","article-title":"Emptying the Stores: Lysosomal Diseases and Therapeutic Strategies","volume":"17","author":"Platt","year":"2018","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1146\/annurev-med-122313-085916","article-title":"Lysosomal Storage Diseases: From Pathophysiology to Therapy","volume":"66","author":"Parenti","year":"2015","journal-title":"Annu. Rev. Med."},{"key":"ref_3","unstructured":"Valle, D.L., Antonarakis, S., Ballabio, A., Beaudet, A.L., and Mitchell, G.A. (2019). The Mucopolysaccharidoses. The Online Metabolic and Molecular Bases of Inherited Disease, McGraw-Hill Education."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Hayes, A.J., and Melrose, J. (2023). HS, an Ancient Molecular Recognition and Information Storage Glycosaminoglycan, Equips HS-Proteoglycans with Diverse Matrix and Cell-Interactive Properties Operative in Tissue Development and Tissue Function in Health and Disease. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24021148"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Costi, S., Caporali, R.F., and Marino, A. (2023). Mucopolysaccharidosis: What Pediatric Rheumatologists and Orthopedics Need to Know. Diagnostics, 13.","DOI":"10.3390\/diagnostics13010075"},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Kaczor-Kami\u0144ska, M., Kami\u0144ski, K., and Wr\u00f3bel, M. (2022). Heparan Sulfate, Mucopolysaccharidosis IIIB and Sulfur Metabolism Disorders. Antioxidants, 11.","DOI":"10.3390\/antiox11040678"},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Benet\u00f3, N., Vilageliu, L., Grinberg, D., and Canals, I. (2020). Sanfilippo Syndrome: Molecular Basis, Disease Models and Therapeutic Approaches. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21217819"},{"key":"ref_8","unstructured":"National Organization for Rare Disorders (2024). Mucopolysaccharidosis Type III, National Organization for Rare Disorders. Available online: https:\/\/rarediseases.org\/rare-diseases\/mucopolysaccharidosis-type-iii\/."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.4103\/ijo.IJO_425_22","article-title":"Mucopolysaccharidosis: A Broad Review","volume":"70","author":"Nagpal","year":"2022","journal-title":"Indian J. Ophthalmol."},{"key":"ref_10","first-page":"133","article-title":"Mucopolysaccharidosis III (Sanfilippo Syndrome)\u2014Disease Presentation and Experimental Therapies","volume":"12","author":"Gilkes","year":"2014","journal-title":"Pediatr. Endocrinol. Rev."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"173562","DOI":"10.1016\/j.ejphar.2020.173562","article-title":"Update of Treatment for Mucopolysaccharidosis Type III (Sanfilippo Syndrome)","volume":"888","author":"Kong","year":"2020","journal-title":"Eur. J. Pharmacol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.ymgme.2017.10.007","article-title":"Treatment of Brain Disease in the Mucopolysaccharidoses","volume":"122","author":"Scarpa","year":"2017","journal-title":"Mol. Genet. Metab."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1002\/jimd.12316","article-title":"Novel Therapies for Mucopolysaccharidosis Type III","volume":"44","author":"Yilmaz","year":"2021","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"e226","DOI":"10.1016\/j.bbmt.2019.02.012","article-title":"Hematopoietic Stem Cell Transplantation for Mucopolysaccharidoses: Past, Present, and Future","volume":"25","author":"Taylor","year":"2019","journal-title":"Biol. Blood Marrow Transplant."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1016\/j.omtm.2022.10.013","article-title":"Brain Transplantation of Genetically Corrected Sanfilippo Type B Neural Stem Cells Induces Partial Cross-Correction of the Disease","volume":"27","author":"Pearse","year":"2022","journal-title":"Mol. Ther. Methods Clin. Dev."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.ymgme.2018.12.003","article-title":"Final Results of the Phase 1\/2, Open-Label Clinical Study of Intravenous Recombinant Human N-Acetyl-\u03b1-d-Glucosaminidase (SBC-103) in Children with Mucopolysaccharidosis IIIB","volume":"126","author":"Whitley","year":"2019","journal-title":"Mol. Genet. Metab."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.omtm.2017.05.009","article-title":"Clearance of Heparan Sulfate and Attenuation of CNS Pathology by Intracerebroventricular BMN 250 in Sanfilippo Type B Mice","volume":"6","author":"Lawrence","year":"2017","journal-title":"Mol. Ther. Methods Clin. Dev."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1007\/s10545-011-9342-4","article-title":"Genistein Supplementation in Patients Affected by Sanfilippo Disease","volume":"34","author":"Delgadillo","year":"2011","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1016\/S1474-4422(17)30169-2","article-title":"Intracerebral Gene Therapy in Children with Mucopolysaccharidosis Type IIIB Syndrome: An Uncontrolled Phase 1\/2 Clinical Trial","volume":"16","author":"Tardieu","year":"2017","journal-title":"Lancet Neurol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"355","DOI":"10.4103\/1673-5374.377606","article-title":"Mucopolysaccharidosis Type IIIB: A Current Review and Exploration of the AAV Therapy Landscape","volume":"19","author":"Rouse","year":"2024","journal-title":"Neural Regen. Res."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Losada D\u00edaz, J.C., Cepeda del Castillo, J., Rodriguez-L\u00f3pez, E.A., and Alm\u00e9ciga-D\u00edaz, C.J. (2020). Advances in the Development of Pharmacological Chaperones for the Mucopolysaccharidoses. Int. J. Mol. Sci., 21.","DOI":"10.20944\/preprints201910.0365.v1"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Keyzor, I., Shohet, S., Castelli, J., Sitaraman, S., Veleva-Rotse, B., Weimer, J.M., Fox, B., Willer, T., Tuske, S., and Crathorne, L. (2023). Therapeutic Role of Pharmacological Chaperones in Lysosomal Storage Disorders: A Review of the Evidence and Informed Approach to Reclassification. Biomolecules, 13.","DOI":"10.3390\/biom13081227"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1740","DOI":"10.1039\/C7SC04712F","article-title":"Tuning Protein Folding in Lysosomal Storage Diseases: The Chemistry behind Pharmacological Chaperones","volume":"9","author":"Pereira","year":"2018","journal-title":"Chem. Sci."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1023\/B:BOLI.0000042959.44318.7c","article-title":"Correlation between Enzyme Activity and Substrate Storage in a Cell Culture Model System for Gaucher Disease","volume":"27","author":"Schueler","year":"2004","journal-title":"J. Inherit. Metab. Dis."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1186\/s13023-014-0180-y","article-title":"Therapeutic Strategies Based on Modified U1 snRNAs and Chaperones for Sanfilippo C Splicing Mutations","volume":"9","author":"Matos","year":"2014","journal-title":"Orphanet J. Rare Dis."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2705","DOI":"10.1021\/jm301557k","article-title":"Pharmacological Chaperones as Therapeutics for Lysosomal Storage Diseases","volume":"56","author":"Boyd","year":"2013","journal-title":"J. Med. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2004","DOI":"10.1038\/mt.2014.138","article-title":"A Chaperone Enhances Blood \u03b1-Glucosidase Activity in Pompe Disease Patients Treated with Enzyme Replacement Therapy","volume":"22","author":"Parenti","year":"2014","journal-title":"Mol. Ther."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1002\/acn3.292","article-title":"Ambroxol Chaperone Therapy for Neuronopathic Gaucher Disease: A Pilot Study","volume":"3","author":"Narita","year":"2016","journal-title":"Ann. Clin. Transl. Neurol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1056\/NEJMoa1510198","article-title":"Treatment of Fabry\u2019s Disease with the Pharmacologic Chaperone Migalastat","volume":"375","author":"Germain","year":"2016","journal-title":"N. Engl. J. Med."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1007\/s40265-019-01090-4","article-title":"Migalastat: A Review in Fabry Disease","volume":"79","author":"McCafferty","year":"2019","journal-title":"Drugs"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1662","DOI":"10.1038\/s41431-020-0677-x","article-title":"Switch from Enzyme Replacement Therapy to Oral Chaperone Migalastat for Treating Fabry Disease: Real-Life Data","volume":"28","author":"Riccio","year":"2020","journal-title":"Eur. J. Hum. Genet."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Weidemann, F., Jovanovic, A., Herrmann, K., and Vardarli, I. (2022). Chaperone Therapy in Fabry Disease. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23031887"},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Morava, E., Baumgartner, M., Patterson, M., Rahman, S., Zschocke, J., and Peters, V. (2018). High-Throughput Screen Fails to Identify Compounds that Enhance Residual Enzyme Activity of Mutant N-Acetyl-\u03b1-Glucosaminidase in Mucopolysaccharidosis Type IIIB. JIMD Reports, Volume 39, Springer.","DOI":"10.1007\/978-3-662-57577-2"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"6560","DOI":"10.1073\/pnas.0711491105","article-title":"Structural and Mechanistic Insight into the Basis of Mucopolysaccharidosis IIIB","volume":"105","author":"Stubbs","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"17400","DOI":"10.1073\/pnas.1203924109","article-title":"Pharmacological Chaperones for Human \u03b1-N-Acetylgalactosaminidase","volume":"109","author":"Clark","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1790","DOI":"10.1021\/acs.jmedchem.2c01617","article-title":"N-Substituted l-Iminosugars for the Treatment of Sanfilippo Type B Syndrome","volume":"66","author":"Esposito","year":"2023","journal-title":"J. Med. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1618","DOI":"10.1111\/j.1742-4658.2010.07588.x","article-title":"The Pharmacological Chaperone Isofagomine Increases the Activity of the Gaucher Disease L444P Mutant Form of Beta-Glucosidase","volume":"277","author":"Khanna","year":"2010","journal-title":"FEBS J."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"4816","DOI":"10.1021\/bi9002265","article-title":"Effects of pH and Iminosugar Pharmacological Chaperones on Lysosomal Glycosidase Structure and Stability","volume":"48","author":"Lieberman","year":"2009","journal-title":"Biochemistry"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Weber, P., Thonhofer, M., Averill, S., Davies, G.J., Santana, A.G., M\u00fcller, P., Nasseri, S.A., Offen, W.A., Pabst, B.M., and Paschke, E. (2020). Mechanistic Insights into the Chaperoning of Human Lysosomal-Galactosidase Activity: Highly Functionalized Aminocyclopentanes and C-5a-Substituted Derivatives of 4-Epi-Isofagomine. Molecules, 25.","DOI":"10.3390\/molecules25174025"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2980","DOI":"10.1002\/tcr.202100269","article-title":"Pharmacological Chaperones for \u03b2-Galactosidase Related to GM1-Gangliosidosis and Morquio B: Recent Advances","volume":"21","author":"Thonhofer","year":"2021","journal-title":"Chem. Rec."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"11291","DOI":"10.1002\/chem.202101408","article-title":"Iminosugar C-Glycosides Work as Pharmacological Chaperones of NAGLU, a Glycosidase Involved in MPS IIIB Rare Disease","volume":"27","author":"Zhu","year":"2021","journal-title":"Chem. Eur. J."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"5598","DOI":"10.1016\/j.bmc.2009.06.022","article-title":"Design and Synthesis of Acetamido Tri- and Tetra-Hydroxyazepanes: Potent and Selective \u03b2-N-Acetylhexosaminidase Inhibitors","volume":"17","author":"Li","year":"2009","journal-title":"Bioorganic Med. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"9341","DOI":"10.1002\/chem.201200110","article-title":"Scalable Syntheses of Both Enantiomers of DNJNAc and DGJNAc from Glucuronolactone: The Effect of N-Alkylation on Hexosaminidase Inhibition","volume":"18","author":"Glawar","year":"2012","journal-title":"Chemistry"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1038\/nchembio.96","article-title":"A Potent Mechanism-Inspired O-GlcNAcase Inhibitor that Blocks Phosphorylation of Tau in Vivo","volume":"4","author":"Yuzwa","year":"2008","journal-title":"Nat. Chem. Biol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"10062","DOI":"10.1021\/acs.jmedchem.9b01090","article-title":"Discovery of MK-8719, a Potent O-GlcNAcase Inhibitor as a Potential Treatment for Tauopathies","volume":"62","author":"Selnick","year":"2019","journal-title":"J. Med. Chem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"9022","DOI":"10.1002\/chem.201701756","article-title":"Multivalency to Inhibit and Discriminate Hexosaminidases","volume":"23","author":"King","year":"2017","journal-title":"Chem. Eur. J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1124\/jpet.120.266122","article-title":"MK-8719, a Novel and Selective O-GlcNAcase Inhibitor That Reduces the Formation of Pathological Tau and Ameliorates Neurodegeneration in a Mouse Model of Tauopathy","volume":"374","author":"Wang","year":"2020","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"6886","DOI":"10.1039\/c3ob41334a","article-title":"An Approach to 8 Stereoisomers of Homonojirimycin from D-Glucose via Kinetic & Thermodynamic Azido-\u03b3-Lactones","volume":"11","author":"Glawar","year":"2013","journal-title":"Org. Biomol. Chem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"6175","DOI":"10.1021\/acs.jmedchem.9b00428","article-title":"Identification of Ezetimibe and Pranlukast as Pharmacological Chaperones for the Treatment of the Rare Disease Mucopolysaccharidosis Type IVA","volume":"62","author":"Hidalgo","year":"2019","journal-title":"J. Med. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.1021\/acsmedchemlett.0c00042","article-title":"Bromocriptine as a Novel Pharmacological Chaperone for Mucopolysaccharidosis IV A","volume":"11","author":"Pulido","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"e202400081","DOI":"10.1002\/cbic.202400081","article-title":"Identification of Orthosteric and Allosteric Pharmacological Chaperones for Mucopolysaccharidosis Type IIIB","volume":"25","author":"Losada","year":"2024","journal-title":"ChemBioChem"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.jsb.2019.02.005","article-title":"Structural Characterization of the \u03b1-N-Acetylglucosaminidase, a Key Enzyme in the Pathogenesis of Sanfilippo Syndrome B","volume":"205","author":"Birrane","year":"2019","journal-title":"J. Struct. Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock Vina: Improving the Speed and Accuracy of Docking with a New Scoring Function, Efficient Optimization, and Multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"29329","DOI":"10.1038\/srep29329","article-title":"Recombinant Human N-Acetylgalactosamine-6-Sulfate Sulfatase (GALNS) Produced in the Methylotrophic Yeast Pichia Pastoris","volume":"6","author":"Moreno","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"S106","DOI":"10.1016\/j.ymgme.2020.12.261","article-title":"Production and Characterization of a Recombinant Alpha-N-Acetyl Glucosaminidase Enzyme in the Pichia Pastoris Yeast","volume":"132","author":"Triana","year":"2021","journal-title":"Mol. Genet. Metab."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1038\/mt.2011.271","article-title":"Co-Administration with the Pharmacological Chaperone AT1001 Increases Recombinant Human \u03b1-Galactosidase A Tissue Uptake and Improves Substrate Reduction in Fabry Mice","volume":"20","author":"Benjamin","year":"2012","journal-title":"Mol. 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