{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,27]],"date-time":"2026-06-27T06:26:16Z","timestamp":1782541576582,"version":"3.54.5"},"reference-count":183,"publisher":"Portland Press Ltd.","issue":"20","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2020,10,30]]},"abstract":"<jats:p>Sulfatases constitute a family of enzymes that specifically act in the hydrolytic degradation of sulfated metabolites by removing sulfate monoesters from various substrates, particularly glycolipids and glycosaminoglycans. A common essential feature of all known eukaryotic sulfatases is the posttranslational modification of a critical cysteine residue in their active site by oxidation to formylglycine (FGly), which is mediated by the FGly-generating enzyme in the endoplasmic reticulum and is indispensable for catalytic activity. The majority of the so far described sulfatases localize intracellularly to lysosomes, where they act in different catabolic pathways. Mutations in genes coding for lysosomal sulfatases lead to an accumulation of the sulfated substrates in lysosomes, resulting in impaired cellular function and multisystemic disorders presenting as lysosomal storage diseases, which also cover the mucopolysaccharidoses and metachromatic leukodystrophy. Bioinformatics analysis of the eukaryotic genomes revealed, besides the well described and long known disease-associated sulfatases, additional genes coding for putative enzymes with sulfatases activity, including arylsulfatase G as well as the arylsulfatases H, I, J and K, respectively. In this article, we review current knowledge about lysosomal sulfatases with a special focus on the just recently characterized family members arylsulfatase G and arylsulfatase K.<\/jats:p>","DOI":"10.1042\/bcj20200586","type":"journal-article","created":{"date-parts":[[2020,10,29]],"date-time":"2020-10-29T16:33:35Z","timestamp":1603989215000},"page":"3963-3983","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["Lysosomal sulfatases: a growing family"],"prefix":"10.1042","volume":"477","author":[{"given":"Torben","family":"L\u00fcbke","sequence":"first","affiliation":[{"name":"Department of Chemistry, Biochemistry I, Bielefeld University, 33615 Bielefeld, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9699-9351","authenticated-orcid":false,"given":"Markus","family":"Damme","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Biochemie, Christian-Albrechts-Universit\u00e4t zu Kiel, 24098 Kiel, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2020,10,29]]},"reference":[{"key":"2021112218152468900_BCJ-2020-0586C1","doi-asserted-by":"publisher","first-page":"3203","DOI":"10.1093\/hmg\/ddi351","article-title":"Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship","volume":"14","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C2","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1016\/S0969-2126(97)00185-8","article-title":"Structure of a human lysosomal sulfatase","volume":"5","year":"1997","journal-title":"Structure"},{"key":"2021112218152468900_BCJ-2020-0586C3","doi-asserted-by":"publisher","first-page":"736","DOI":"10.1016\/j.jmb.2012.08.020","article-title":"The structure of human GALNS reveals the molecular basis for mucopolysaccharidosis IV A","volume":"423","year":"2012","journal-title":"J. Mol. Biol."},{"key":"2021112218152468900_BCJ-2020-0586C4","doi-asserted-by":"publisher","first-page":"1321","DOI":"10.1107\/S1399004714002739","article-title":"Structure of sulfamidase provides insight into the molecular pathology of mucopolysaccharidosis IIIA","volume":"70","year":"2014","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2021112218152468900_BCJ-2020-0586C5","doi-asserted-by":"publisher","first-page":"3654","DOI":"10.1021\/bi9714924","article-title":"Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis","volume":"37","year":"1998","journal-title":"Biochemistry"},{"key":"2021112218152468900_BCJ-2020-0586C6","doi-asserted-by":"publisher","first-page":"15786","DOI":"10.1038\/ncomms15786","article-title":"Insights into Hunter syndrome from the structure of iduronate-2-sulfatase","volume":"8","year":"2017","journal-title":"Nat. Commun."},{"key":"2021112218152468900_BCJ-2020-0586C7","doi-asserted-by":"publisher","first-page":"562","DOI":"10.1086\/301746","article-title":"Biochemical characterization of arylsulfatase E and functional analysis of mutations found in patients with X-linked chondrodysplasia punctata","volume":"62","year":"1998","journal-title":"Am. J. Hum. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C8","doi-asserted-by":"publisher","first-page":"27724","DOI":"10.1074\/jbc.M802130200","article-title":"Sulf loss influences N-, 2-O-, and 6-O-sulfation of multiple heparan sulfate proteoglycans and modulates fibroblast growth factor signaling","volume":"283","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C9","doi-asserted-by":"publisher","first-page":"1195","DOI":"10.1210\/endo-122-4-1195","article-title":"Desulfation of 3,5,3'-triiodothyronine sulfate by microsomes from human and rat tissues","volume":"122","year":"1988","journal-title":"Endocrinology"},{"key":"2021112218152468900_BCJ-2020-0586C10","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1016\/0092-8674(95)90367-4","article-title":"A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy","volume":"81","year":"1995","journal-title":"Cell"},{"key":"2021112218152468900_BCJ-2020-0586C11","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1002\/path.4055","article-title":"Up-regulated expression of sulfatases (SULF1 and SULF2) as prognostic and metastasis predictive markers in human gastric cancer","volume":"228","year":"2012","journal-title":"J. Pathol."},{"key":"2021112218152468900_BCJ-2020-0586C12","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1186\/1479-5876-9-72","article-title":"SULFs in human neoplasia: implication as progression and prognosis factors","volume":"9","year":"2011","journal-title":"J. Transl. Med."},{"key":"2021112218152468900_BCJ-2020-0586C13","doi-asserted-by":"publisher","first-page":"3327","DOI":"10.1242\/dev.007674","article-title":"SULF1 and SULF2 regulate heparan sulfate-mediated GDNF signaling for esophageal innervation","volume":"134","year":"2007","journal-title":"Development"},{"key":"2021112218152468900_BCJ-2020-0586C14","doi-asserted-by":"publisher","first-page":"935","DOI":"10.1517\/14728222.2010.504718","article-title":"Sulf-2: an extracellular modulator of cell signaling and a cancer target candidate","volume":"14","year":"2010","journal-title":"Expert. Opin. Ther. Targets"},{"key":"2021112218152468900_BCJ-2020-0586C15","doi-asserted-by":"publisher","first-page":"787","DOI":"10.1161\/CIRCRESAHA.119.315023","article-title":"Heparan sulfate-editing extracellular sulfatases enhance VEGF bioavailability for ischemic heart repair","volume":"125","year":"2019","journal-title":"Circ. Res."},{"key":"2021112218152468900_BCJ-2020-0586C16","doi-asserted-by":"publisher","first-page":"473","DOI":"10.1126\/science.1174447","article-title":"A gene network regulating lysosomal biogenesis and function","volume":"325","year":"2009","journal-title":"Science"},{"key":"2021112218152468900_BCJ-2020-0586C17","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1111\/nyas.13131","article-title":"Transcription factor EB: from master coordinator of lysosomal pathways to candidate therapeutic target in degenerative storage diseases","volume":"1371","year":"2016","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"2021112218152468900_BCJ-2020-0586C18","doi-asserted-by":"publisher","first-page":"3852","DOI":"10.1093\/hmg\/ddr306","article-title":"Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways","volume":"20","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C19","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1016\/0092-8674(95)90314-3","article-title":"A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency","volume":"82","year":"1995","journal-title":"Cell"},{"key":"2021112218152468900_BCJ-2020-0586C20","doi-asserted-by":"publisher","first-page":"2561","DOI":"10.1073\/pnas.89.7.2561","article-title":"Multiple sulfatase deficiency: catalytically inactive sulfatases are expressed from retrovirally introduced sulfatase cDNAs","volume":"89","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C21","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1007\/BF00295367","article-title":"Genetic complementation of steroid sulphatase after somatic cell hybridization of X-linked ichthyosis and multiple sulphatase deficiency","volume":"70","year":"1985","journal-title":"Hum. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C22","doi-asserted-by":"publisher","first-page":"6496","DOI":"10.1073\/pnas.76.12.6496","article-title":"Genetic complementation studies of multiple sulfatase deficiency","volume":"76","year":"1979","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C23","doi-asserted-by":"publisher","first-page":"6166","DOI":"10.1073\/pnas.77.10.6166","article-title":"Complementation of arylsulfatase A in somatic hybrids of metachromatic leukodystrophy and multiple sulfatase deficiency disorder fibroblasts","volume":"77","year":"1980","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C24","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1006\/jmbi.2000.4297","article-title":"Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis","volume":"305","year":"2001","journal-title":"J. Mol. Biol."},{"key":"2021112218152468900_BCJ-2020-0586C25","doi-asserted-by":"publisher","first-page":"11963","DOI":"10.1073\/pnas.94.22.11963","article-title":"Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum","volume":"94","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C26","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1016\/S0092-8674(03)00347-7","article-title":"Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme","volume":"113","year":"2003","journal-title":"Cell"},{"key":"2021112218152468900_BCJ-2020-0586C27","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1016\/S0092-8674(03)00348-9","article-title":"The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases","volume":"113","year":"2003","journal-title":"Cell"},{"key":"2021112218152468900_BCJ-2020-0586C28","doi-asserted-by":"publisher","first-page":"541","DOI":"10.1016\/j.cell.2005.03.001","article-title":"Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme","volume":"121","year":"2005","journal-title":"Cell"},{"key":"2021112218152468900_BCJ-2020-0586C29","doi-asserted-by":"publisher","first-page":"2084","DOI":"10.1093\/emboj\/18.8.2084","article-title":"Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases","volume":"18","year":"1999","journal-title":"Embo J."},{"key":"2021112218152468900_BCJ-2020-0586C30","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1038\/nchembio878","article-title":"Introducing genetically encoded aldehydes into proteins","volume":"3","year":"2007","journal-title":"Nat. Chem. Biol."},{"key":"2021112218152468900_BCJ-2020-0586C31","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1073\/pnas.0507592102","article-title":"A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme","volume":"103","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C32","doi-asserted-by":"publisher","first-page":"3262","DOI":"10.1111\/febs.13347","article-title":"Eukaryotic formylglycine-generating enzyme catalyses a monooxygenase type of reaction","volume":"282","year":"2015","journal-title":"Febs J."},{"key":"2021112218152468900_BCJ-2020-0586C33","doi-asserted-by":"publisher","first-page":"7049","DOI":"10.1039\/C9SC01723B","article-title":"Structure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen","volume":"10","year":"2019","journal-title":"Chem. Sci."},{"key":"2021112218152468900_BCJ-2020-0586C34","doi-asserted-by":"publisher","first-page":"5370","DOI":"10.1073\/pnas.1818274116","article-title":"Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate O2 activation","volume":"116","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C35","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1111\/dmcn.13600","article-title":"Treatment strategies for lysosomal storage disorders","volume":"60","year":"2018","journal-title":"Dev. Med. Child Neurol."},{"issue":"Pt 3","key":"2021112218152468900_BCJ-2020-0586C36","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1042\/bj2940657","article-title":"Overexpression of N-acetylgalactosamine-4-sulphatase induces a multiple sulphatase deficiency in mucopolysaccharidosis-type-VI fibroblasts","volume":"294","year":"1993","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C37","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1146\/annurev-med-122313-085916","article-title":"Lysosomal storage diseases: from pathophysiology to therapy","volume":"66","year":"2015","journal-title":"Annu. Rev. Med."},{"key":"2021112218152468900_BCJ-2020-0586C38","doi-asserted-by":"publisher","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","year":"2016","journal-title":"Sci. Rep."},{"key":"2021112218152468900_BCJ-2020-0586C39","doi-asserted-by":"publisher","first-page":"655","DOI":"10.1002\/bab.1660","article-title":"Production and characterization of a human lysosomal recombinant iduronate-2-sulfatase produced in Pichia pastoris","volume":"65","year":"2018","journal-title":"Biotechnol. Appl. Biochem."},{"key":"2021112218152468900_BCJ-2020-0586C40","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1007\/s12275-013-2416-2","article-title":"Low-scale expression and purification of an active putative iduronate 2-sulfate sulfatase-Like enzyme from Escherichia coli K12","volume":"51","year":"2013","journal-title":"J. Microbiol."},{"key":"2021112218152468900_BCJ-2020-0586C41","doi-asserted-by":"publisher","first-page":"5844","DOI":"10.1038\/s41598-017-06367-w","article-title":"Improvement in the production of the human recombinant enzyme N-acetylgalactosamine-6-sulfatase (rhGALNS) in Escherichia coli using synthetic biology approaches","volume":"7","year":"2017","journal-title":"Sci. Rep."},{"key":"2021112218152468900_BCJ-2020-0586C42","doi-asserted-by":"publisher","first-page":"25560","DOI":"10.1074\/jbc.273.40.25560","article-title":"Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine","volume":"273","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C43","doi-asserted-by":"publisher","first-page":"2212","DOI":"10.1074\/jbc.M209435200","article-title":"Posttranslational modification of serine to formylglycine in bacterial sulfatases. Recognition of the modification motif by the iron-sulfur protein AtsB","volume":"278","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C44","doi-asserted-by":"publisher","first-page":"15375","DOI":"10.1074\/jbc.274.22.15375","article-title":"The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase","volume":"274","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C45","doi-asserted-by":"publisher","first-page":"5840","DOI":"10.1038\/ncomms6840","article-title":"A non-conserved miRNA regulates lysosomal function and impacts on a human lysosomal storage disorder","volume":"5","year":"2014","journal-title":"Nat. Commun."},{"key":"2021112218152468900_BCJ-2020-0586C46","doi-asserted-by":"publisher","DOI":"10.1002\/btpr.2974","article-title":"Inhibition of endogenous miR-23a\/miR-377 in CHO cells enhances difficult-to-express recombinant lysosomal sulfatase activity","volume":"36","year":"2020","journal-title":"Biotechnol. Prog."},{"key":"2021112218152468900_BCJ-2020-0586C47","doi-asserted-by":"publisher","first-page":"15173","DOI":"10.1074\/jbc.M413698200","article-title":"Expression, localization, structural, and functional characterization of pFGE, the paralog of the Calpha-formylglycine-generating enzyme","volume":"280","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C48","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1016\/S0076-6879(05)00016-9","article-title":"Three-dimensional structures of sulfatases","volume":"400","year":"2005","journal-title":"Methods Enzymol."},{"key":"2021112218152468900_BCJ-2020-0586C49","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1016\/S0969-2126(01)00609-8","article-title":"1.3 a structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family","volume":"9","year":"2001","journal-title":"Structure"},{"key":"2021112218152468900_BCJ-2020-0586C50","doi-asserted-by":"publisher","first-page":"22989","DOI":"10.1074\/jbc.M211497200","article-title":"Structure of human estrone sulfatase suggests functional roles of membrane association","volume":"278","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C51","doi-asserted-by":"publisher","first-page":"386","DOI":"10.1016\/S0162-0134(03)00176-4","article-title":"Crystal structure of a covalent intermediate of endogenous human arylsulfatase A","volume":"96","year":"2003","journal-title":"J. Inorg. Biochem."},{"key":"2021112218152468900_BCJ-2020-0586C52","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1016\/j.ejcb.2009.10.008","article-title":"Mannose phosphorylation in health and disease","volume":"89","year":"2010","journal-title":"Eur. J. Cell Biol."},{"key":"2021112218152468900_BCJ-2020-0586C53","doi-asserted-by":"crossref","first-page":"5015","DOI":"10.1016\/S0021-9258(18)83692-4","article-title":"Mannose processing is an important determinant in the assembly of phosphorylated high mannose-type oligosaccharides","volume":"264","year":"1989","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C54","doi-asserted-by":"publisher","first-page":"21067","DOI":"10.1074\/jbc.273.33.21067","article-title":"Lysine-based structure responsible for selective mannose phosphorylation of cathepsin D and cathepsin L defines a common structural motif for lysosomal enzyme targeting","volume":"273","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C55","doi-asserted-by":"crossref","first-page":"14490","DOI":"10.1016\/S0021-9258(17)36649-8","article-title":"Lysine is a common determinant for mannose phosphorylation of lysosomal proteins","volume":"269","year":"1994","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C56","doi-asserted-by":"publisher","first-page":"32653","DOI":"10.1074\/jbc.M304865200","article-title":"Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-phosphotransferase","volume":"278","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C57","doi-asserted-by":"publisher","first-page":"1623","DOI":"10.1091\/mbc.12.6.1623","article-title":"Lysosomal hydrolase mannose 6-phosphate uncovering enzyme resides in the trans-Golgi network","volume":"12","year":"2001","journal-title":"Mol. Biol. Cell"},{"key":"2021112218152468900_BCJ-2020-0586C58","doi-asserted-by":"crossref","first-page":"3374","DOI":"10.1016\/S0021-9258(19)39778-9","article-title":"Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B","volume":"265","year":"1990","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C59","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.1016\/S0021-9258(19)85079-2","article-title":"Cloning and expression of human arylsulfatase A","volume":"264","year":"1989","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C60","doi-asserted-by":"publisher","first-page":"30019","DOI":"10.1074\/jbc.M113.499541","article-title":"Arylsulfatase K, a novel lysosomal sulfatase","volume":"288","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C61","doi-asserted-by":"publisher","first-page":"11388","DOI":"10.1074\/jbc.M709917200","article-title":"Arylsulfatase G, a novel lysosomal sulfatase","volume":"283","year":"2008","journal-title":"J. Biol. Chem."},{"issue":"Pt 1","key":"2021112218152468900_BCJ-2020-0586C62","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1042\/bj3270089","article-title":"Expression, purification and characterization of recombinant caprine N-acetylglucosamine-6-sulphatase","volume":"327","year":"1997","journal-title":"Biochem. J."},{"issue":"Pt 1","key":"2021112218152468900_BCJ-2020-0586C63","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1042\/bj3240033","article-title":"alpha-Glucosidase and N-acetylglucosamine-6-sulphatase are the major mannose-6-phosphate glycoproteins in human urine","volume":"324","year":"1997","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C64","doi-asserted-by":"publisher","first-page":"368","DOI":"10.1016\/j.bbapap.2006.12.004","article-title":"The human urine mannose 6-phosphate glycoproteome","volume":"1774","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112218152468900_BCJ-2020-0586C65","doi-asserted-by":"publisher","first-page":"1942","DOI":"10.1074\/mcp.M600030-MCP200","article-title":"Identification and validation of mannose 6-phosphate glycoproteins in human plasma reveal a wide range of lysosomal and non-lysosomal proteins","volume":"5","year":"2006","journal-title":"Mol. Cell Proteom."},{"key":"2021112218152468900_BCJ-2020-0586C66","doi-asserted-by":"publisher","first-page":"58","DOI":"10.1074\/mcp.M700217-MCP200","article-title":"Proteomics analysis of serum from mutant mice reveals lysosomal proteins selectively transported by each of the two mannose 6-phosphate receptors","volume":"7","year":"2008","journal-title":"Mol. Cell Proteom."},{"key":"2021112218152468900_BCJ-2020-0586C67","doi-asserted-by":"publisher","first-page":"19191","DOI":"10.1074\/jbc.271.32.19191","article-title":"Rat brain contains high levels of mannose-6-phosphorylated glycoproteins including lysosomal enzymes and palmitoyl-protein thioesterase, an enzyme implicated in infantile neuronal lipofuscinosis","volume":"271","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C68","doi-asserted-by":"publisher","first-page":"1806","DOI":"10.1074\/mcp.M112.026179","article-title":"Extending the mannose 6-phosphate glycoproteome by high resolution\/accuracy mass spectrometry analysis of control and acid phosphatase 5-deficient mice","volume":"12","year":"2013","journal-title":"Mol. Cell Proteom."},{"key":"2021112218152468900_BCJ-2020-0586C69","doi-asserted-by":"publisher","first-page":"1520","DOI":"10.1002\/pmic.200401054","article-title":"The human brain mannose 6-phosphate glycoproteome: a complex mixture composed of multiple isoforms of many soluble lysosomal proteins","volume":"5","year":"2005","journal-title":"Proteomics"},{"key":"2021112218152468900_BCJ-2020-0586C70","doi-asserted-by":"publisher","first-page":"686","DOI":"10.1074\/mcp.M500343-MCP200","article-title":"Identification of sites of mannose 6-phosphorylation on lysosomal proteins","volume":"5","year":"2006","journal-title":"Mol. Cell Proteom."},{"key":"2021112218152468900_BCJ-2020-0586C71","doi-asserted-by":"publisher","first-page":"90","DOI":"10.1111\/j.1399-0004.1983.tb02218.x","article-title":"Mucolipidosis II. The clinical, radiological and biochemical features in three cases","volume":"24","year":"1983","journal-title":"Clin. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C72","doi-asserted-by":"publisher","first-page":"956","DOI":"10.1016\/0006-291X(75)90768-8","article-title":"Abnormal lysosomal hydrolases excreted by cultured fibroblasts in I-cell disease (mucolipidosis II)","volume":"67","year":"1975","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021112218152468900_BCJ-2020-0586C73","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1007\/BF01799072","article-title":"I-cell disease","volume":"2","year":"1980","journal-title":"J. Inherit. Metab. Dis."},{"key":"2021112218152468900_BCJ-2020-0586C74","first-page":"262","article-title":"Targeting of phosphomannosyl- deficient arylsulfatase A to lysosomes of I-cell fibroblasts","volume":"45","year":"1988","journal-title":"Eur. J. Cell Biol."},{"key":"2021112218152468900_BCJ-2020-0586C75","doi-asserted-by":"publisher","first-page":"27992","DOI":"10.1074\/jbc.M114.584144","article-title":"Molecular characterization of arylsulfatase G: expression, processing, glycosylation, transport, and activity","volume":"289","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C76","doi-asserted-by":"publisher","first-page":"438","DOI":"10.1074\/mcp.M116.063636","article-title":"Quantitative proteome analysis of mouse liver lysosomes provides evidence for mannose 6-phosphate-independent targeting mechanisms of acid hydrolases in mucolipidosis II","volume":"16","year":"2017","journal-title":"Mol. Cell Proteom."},{"key":"2021112218152468900_BCJ-2020-0586C77","first-page":"i","article-title":"Assay of arylsulphatase of rat tissues","volume":"51","year":"1952","journal-title":"Biochem. J."},{"issue":"Pt 2","key":"2021112218152468900_BCJ-2020-0586C78","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1042\/bj2880539","article-title":"A cDNA clone for human glucosamine-6-sulphatase reveals differences between arylsulphatases and non-arylsulphatases","volume":"288","year":"1992","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C79","doi-asserted-by":"publisher","first-page":"15C","DOI":"10.1042\/bj0930015C","article-title":"Abnormal sulphatase activities in two human diseases (metachromatic leucodystrophy and gargoylism)","volume":"93","year":"1964","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C80","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1007\/978-1-4684-7735-1_15","article-title":"P-Nitrocatechol sulfate for arylsulfatase assay: detection of metachromatic leukodystrophy variants","volume":"68","year":"1976","journal-title":"Adv. Exp. Med. Biol."},{"key":"2021112218152468900_BCJ-2020-0586C81","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1007\/978-1-4684-7735-1_16","article-title":"Arylsulfatases A and B in metachromatic leukodystrophy and Maroteaux-Lamy syndrome: studies with 4-methylumelliferyl sulfate","volume":"68","year":"1976","journal-title":"Adv. Exp. Med. Biol."},{"key":"2021112218152468900_BCJ-2020-0586C82","doi-asserted-by":"publisher","first-page":"675","DOI":"10.1023\/A:1012763026526","article-title":"A fluorimetric enzyme assay for the diagnosis of MPS II (Hunter disease)","volume":"24","year":"2001","journal-title":"J. Inherit. Metab. Dis."},{"key":"2021112218152468900_BCJ-2020-0586C83","doi-asserted-by":"publisher","first-page":"935","DOI":"10.1007\/BF00711508","article-title":"A fluorimetric enzyme assay for the diagnosis of Sanfilippo disease type D (MPS IIID)","volume":"16","year":"1993","journal-title":"J. Inherit. Metab. Dis."},{"key":"2021112218152468900_BCJ-2020-0586C84","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/0009-8981(90)90339-T","article-title":"A fluorimetric enzyme assay for the diagnosis of Morquio disease type A (MPS IV A)","volume":"187","year":"1990","journal-title":"Clin. Chim. Acta"},{"key":"2021112218152468900_BCJ-2020-0586C85","doi-asserted-by":"publisher","first-page":"150","DOI":"10.1016\/0076-6879(78)50013-X","article-title":"Radioactive substrates for iduronate sulfatase and alpha-L-iduronidase","volume":"50","year":"1978","journal-title":"Methods Enzymol."},{"key":"2021112218152468900_BCJ-2020-0586C86","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1016\/S0008-6215(00)85765-1","article-title":"alpha-L-iduronidase, beta-D-glucuronidase, and 2-sulfo-L-iduronate 2-sulfatase: preparation and characterization of radioactive substrates from heparin","volume":"69","year":"1979","journal-title":"Carbohydr. Res."},{"key":"2021112218152468900_BCJ-2020-0586C87","doi-asserted-by":"publisher","first-page":"1152","DOI":"10.1021\/ac102777s","article-title":"Tandem mass spectrometry for the direct assay of lysosomal enzymes in dried blood spots: application to screening newborns for mucopolysaccharidosis II (Hunter syndrome)","volume":"83","year":"2011","journal-title":"Anal. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C88","doi-asserted-by":"publisher","first-page":"128","DOI":"10.1373\/clinchem.2010.149880","article-title":"Tandem mass spectrometry for the direct assay of lysosomal enzymes in dried blood spots: application to screening newborns for mucopolysaccharidosis IVA","volume":"57","year":"2011","journal-title":"Clin. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C89","doi-asserted-by":"publisher","first-page":"9587","DOI":"10.1021\/ac102090v","article-title":"Tandem mass spectrometry for the direct assay of lysosomal enzymes in dried blood spots: application to screening newborns for mucopolysaccharidosis VI (Maroteaux-Lamy syndrome)","volume":"82","year":"2010","journal-title":"Anal. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C90","doi-asserted-by":"publisher","first-page":"557","DOI":"10.1021\/bc200609x","article-title":"New substrates and enzyme assays for the detection of mucopolysaccharidosis III (Sanfilippo syndrome) types A, B, C, and D by tandem mass spectrometry","volume":"23","year":"2012","journal-title":"Bioconjug. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C91","doi-asserted-by":"publisher","first-page":"1925","DOI":"10.1373\/clinchem.2008.108456","article-title":"Diagnosis of metachromatic leukodystrophy by immune quantification of arylsulphatase A protein and activity in dried blood spots","volume":"54","year":"2008","journal-title":"Clin. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C92","doi-asserted-by":"publisher","first-page":"10310","DOI":"10.1073\/pnas.1202071109","article-title":"Arylsulfatase G inactivation causes loss of heparan sulfate 3-O-sulfatase activity and mucopolysaccharidosis in mice","volume":"109","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C93","doi-asserted-by":"publisher","first-page":"473","DOI":"10.1021\/ac4023555","article-title":"A new analytical bench assay for the determination of arylsulfatase a activity toward galactosyl-3-sulfate ceramide: implication for metachromatic leukodystrophy diagnosis","volume":"86","year":"2014","journal-title":"Anal. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C94","doi-asserted-by":"publisher","first-page":"14821","DOI":"10.1073\/pnas.93.25.14821","article-title":"Phenotype of arylsulfatase A-deficient mice: relationship to human metachromatic leukodystrophy","volume":"93","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C95","doi-asserted-by":"publisher","first-page":"9482","DOI":"10.1523\/JNEUROSCI.2287-07.2007","article-title":"Increasing sulfatide synthesis in myelin-forming cells of arylsulfatase A-deficient mice causes demyelination and neurological symptoms reminiscent of human metachromatic leukodystrophy","volume":"27","year":"2007","journal-title":"J. Neurosci."},{"key":"2021112218152468900_BCJ-2020-0586C96","first-page":"657","article-title":"The pathology of the feline model of mucopolysaccharidosis VI","volume":"101","year":"1980","journal-title":"Am. J. Pathol."},{"key":"2021112218152468900_BCJ-2020-0586C97","doi-asserted-by":"publisher","first-page":"1099","DOI":"10.1172\/JCI116268","article-title":"Arylsulfatase B-deficient mucopolysaccharidosis in rats","volume":"91","year":"1993","journal-title":"J. Clin. Invest."},{"key":"2021112218152468900_BCJ-2020-0586C98","doi-asserted-by":"publisher","first-page":"8214","DOI":"10.1073\/pnas.93.16.8214","article-title":"Targeted disruption of the arylsulfatase B gene results in mice resembling the phenotype of mucopolysaccharidosis VI","volume":"93","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C99","doi-asserted-by":"publisher","first-page":"230","DOI":"10.1177\/030098589803500311","article-title":"Clinical and morphologic features of mucopolysaccharidosis type II in a dog: naturally occurring model of Hunter syndrome","volume":"35","year":"1998","journal-title":"Vet. Pathol."},{"key":"2021112218152468900_BCJ-2020-0586C100","doi-asserted-by":"publisher","first-page":"924","DOI":"10.1007\/s10545-007-0641-8","article-title":"The characterization of a murine model of mucopolysaccharidosis II (Hunter syndrome)","volume":"30","year":"2007","journal-title":"J. Inherit. Metab. Dis."},{"key":"2021112218152468900_BCJ-2020-0586C101","doi-asserted-by":"publisher","first-page":"3349","DOI":"10.1093\/hmg\/ddg366","article-title":"Mouse model of N-acetylgalactosamine-6-sulfate sulfatase deficiency (Galns-\/-) produced by targeted disruption of the gene defective in Morquio A disease","volume":"12","year":"2003","journal-title":"Hum. Mol. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C102","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1016\/j.ymgme.2007.02.009","article-title":"Murine model (Galns(tm(C76S)slu)) of MPS IVA with missense mutation at the active site cysteine conserved among sulfatase proteins","volume":"91","year":"2007","journal-title":"Mol. Genet. Metab."},{"key":"2021112218152468900_BCJ-2020-0586C103","doi-asserted-by":"publisher","first-page":"3321","DOI":"10.1093\/hmg\/ddi364","article-title":"Development of MPS IVA mouse (Galnstm(hC79S.mC76S)slu) tolerant to human N-acetylgalactosamine-6-sulfate sulfatase","volume":"14","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C104","doi-asserted-by":"publisher","first-page":"760","DOI":"10.1007\/BF01800018","article-title":"N-acetylglucosamine 6-sulphatase deficiency in a Nubian goat: a model of Sanfilippo syndrome type D (mucopolysaccharidosis IIID)","volume":"15","year":"1992","journal-title":"J. Inherit. Metab. Dis."},{"key":"2021112218152468900_BCJ-2020-0586C105","doi-asserted-by":"publisher","first-page":"1535","DOI":"10.1093\/hmg\/ddx058","article-title":"Disease correction by AAV-mediated gene therapy in a new mouse model of mucopolysaccharidosis type IIID","volume":"26","year":"2017","journal-title":"Hum. Mol. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C106","doi-asserted-by":"publisher","first-page":"74","DOI":"10.1203\/00006450-199807000-00012","article-title":"Sulfamidase deficiency in a family of Dachshunds: a canine model of mucopolysaccharidosis IIIA (Sanfilippo A)","volume":"44","year":"1998","journal-title":"Pediatr. Res."},{"key":"2021112218152468900_BCJ-2020-0586C107","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1093\/glycob\/11.1.99","article-title":"A novel missense mutation in lysosomal sulfamidase is the basis of MPS III A in a spontaneous mouse mutant","volume":"11","year":"2001","journal-title":"Glycobiology"},{"key":"2021112218152468900_BCJ-2020-0586C108","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1007\/s10545-017-0044-4","article-title":"A novel conditional Sgsh knockout mouse model recapitulates phenotypic and neuropathic deficits of Sanfilippo syndrome","volume":"40","year":"2017","journal-title":"J. Inherit. Metab. Dis."},{"key":"2021112218152468900_BCJ-2020-0586C109","doi-asserted-by":"publisher","first-page":"3433","DOI":"10.1042\/BCJ20200546","article-title":"Arylsulfatase K inactivation causes mucopolysaccharidosis due to deficient glucuronate desulfation of heparan and chondroitin sulfate","volume":"477","year":"2020","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C110","doi-asserted-by":"publisher","first-page":"14775","DOI":"10.1073\/pnas.0914206107","article-title":"A canine Arylsulfatase G (ARSG) mutation leading to a sulfatase deficiency is associated with neuronal ceroid lipofuscinosis","volume":"107","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"Suppl 1","key":"2021112218152468900_BCJ-2020-0586C111","first-page":"141","article-title":"Morquio A syndrome: diagnosis and current and future therapies","volume":"12","year":"2014","journal-title":"Pediatr. Endocrinol. Rev."},{"key":"2021112218152468900_BCJ-2020-0586C112","doi-asserted-by":"publisher","first-page":"861","DOI":"10.2174\/138920111795542714","article-title":"Mucopolysaccharidosis type II (Hunter syndrome): clinical picture and treatment","volume":"12","year":"2011","journal-title":"Curr. Pharm. Biotechnol."},{"key":"2021112218152468900_BCJ-2020-0586C113","doi-asserted-by":"publisher","first-page":"e1228","DOI":"10.1542\/peds.2008-0999","article-title":"Multidisciplinary management of Hunter syndrome","volume":"124","year":"2009","journal-title":"Pediatrics"},{"issue":"Suppl 2","key":"2021112218152468900_BCJ-2020-0586C114","doi-asserted-by":"publisher","first-page":"S2","DOI":"10.1038\/bmt.2008.275","article-title":"Metachromatic leukodystrophy: an overview of current and prospective treatments","volume":"42","year":"2008","journal-title":"Bone Marrow Transpl."},{"key":"2021112218152468900_BCJ-2020-0586C115","doi-asserted-by":"crossref","first-page":"20977","DOI":"10.1016\/S0021-9258(17)31917-8","article-title":"Glycosylation and phosphorylation of arylsulfatase A","volume":"269","year":"1994","journal-title":"J. Biol. Chem."},{"issue":"Pt 1","key":"2021112218152468900_BCJ-2020-0586C116","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1042\/bj2970123","article-title":"Four monoclonal antibodies inhibit the recognition of arylsulphatase A by the lysosomal enzyme phosphotransferase","volume":"297","year":"1994","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C117","doi-asserted-by":"publisher","first-page":"1810","DOI":"10.1093\/hmg\/ddz020","article-title":"Evolutionary redesign of the lysosomal enzyme arylsulfatase A increases efficacy of enzyme replacement therapy for metachromatic leukodystrophy","volume":"28","year":"2019","journal-title":"Hum. Mol. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C118","doi-asserted-by":"publisher","first-page":"619","DOI":"10.1016\/0005-2744(68)90008-9","article-title":"Cerebroside 3-sulfate as a physiological substrate of arylsulfatase A","volume":"151","year":"1968","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112218152468900_BCJ-2020-0586C119","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/S0163-7827(97)00011-8","article-title":"Chemistry and functional distribution of sulfoglycolipids","volume":"36","year":"1997","journal-title":"Prog. Lipid Res."},{"key":"2021112218152468900_BCJ-2020-0586C120","doi-asserted-by":"publisher","first-page":"593","DOI":"10.1001\/archneur.1965.00470060029003","article-title":"Metachromatic form of diffuse cerebral sclerosis. V. The nature and significance of low sulfatase activity: a controlled study of brain, liver and kidney in four patients with metachromatic leukodystrophy (MLD)","volume":"13","year":"1965","journal-title":"Arch. Neurol."},{"key":"2021112218152468900_BCJ-2020-0586C121","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1016\/0006-291X(65)90137-3","article-title":"Evidence for the genetic block in metachromatic leucodystrophy (Ml)","volume":"19","year":"1965","journal-title":"Biochem. Biophys. Res Commun."},{"key":"2021112218152468900_BCJ-2020-0586C122","doi-asserted-by":"publisher","first-page":"1700","DOI":"10.1016\/j.febslet.2009.10.021","article-title":"Lysosomal degradation of membrane lipids","volume":"584","year":"2010","journal-title":"FEBS Lett."},{"key":"2021112218152468900_BCJ-2020-0586C123","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1111\/j.1432-1033.1991.tb16222.x","article-title":"Glycosphingolipid specificity of the human sulfatide activator protein","volume":"200","year":"1991","journal-title":"Eur. J. Biochem."},{"key":"2021112218152468900_BCJ-2020-0586C124","doi-asserted-by":"publisher","first-page":"561","DOI":"10.1016\/0005-2744(77)90288-1","article-title":"The activator of cerebroside sulphatase. Binding studies with enzyme and substrate demonstrating the detergent function of the activator protein","volume":"481","year":"1977","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112218152468900_BCJ-2020-0586C125","doi-asserted-by":"publisher","first-page":"3074","DOI":"10.1073\/pnas.80.10.3074","article-title":"Immunological evidence for deficiency in an activator protein for sulfatide sulfatase in a variant form of metachromatic leukodystrophy","volume":"80","year":"1983","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C126","doi-asserted-by":"publisher","first-page":"2845","DOI":"10.1093\/brain\/awz205","article-title":"Arylsulfatase A, a genetic modifier of Parkinson's disease, is an alpha-synuclein chaperone","volume":"142","year":"2019","journal-title":"Brain"},{"key":"2021112218152468900_BCJ-2020-0586C127","doi-asserted-by":"publisher","first-page":"725","DOI":"10.1007\/s10067-013-2423-z","article-title":"Attenuated osteoarticular phenotype of type VI mucopolysaccharidosis: a report of four patients and a review of the literature","volume":"33","year":"2014","journal-title":"Clin. Rheumatol."},{"key":"2021112218152468900_BCJ-2020-0586C128","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1111\/j.1399-0004.1987.tb02779.x","article-title":"Mental retardation in a patient with Maroteaux-Lamy","volume":"31","year":"1987","journal-title":"Clin. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C129","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1002\/glia.22604","article-title":"Arylsulfatase B modulates neurite outgrowth via astrocyte chondroitin-4-sulfate: dysregulation by ethanol","volume":"62","year":"2014","journal-title":"Glia"},{"key":"2021112218152468900_BCJ-2020-0586C130","doi-asserted-by":"publisher","first-page":"e57415","DOI":"10.1371\/journal.pone.0057415","article-title":"Arylsulfatase B improves locomotor function after mouse spinal cord injury","volume":"8","year":"2013","journal-title":"PLoS One"},{"key":"2021112218152468900_BCJ-2020-0586C131","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1042\/bj2460347","article-title":"Human liver N-acetylglucosamine-6-sulphate sulphatase. Purification and characterization","volume":"246","year":"1987","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C132","doi-asserted-by":"publisher","first-page":"192","DOI":"10.1136\/jmg.40.3.192","article-title":"Sanfilippo syndrome type D: identification of the first mutation in the N-acetylglucosamine-6-sulphatase gene","volume":"40","year":"2003","journal-title":"J. Med. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C133","doi-asserted-by":"publisher","first-page":"6822","DOI":"10.1073\/pnas.77.11.6822","article-title":"Sanfilippo disease type D: deficiency of N-acetylglucosamine-6-sulfate sulfatase required for heparan sulfate degradation","volume":"77","year":"1980","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112218152468900_BCJ-2020-0586C134","doi-asserted-by":"publisher","first-page":"805","DOI":"10.1203\/00006450-197807000-00015","article-title":"N-acetylglucosamine-6-sulfate sulfatase in man: deficiency of the enzyme in a new mucopolysaccharidosis","volume":"12","year":"1978","journal-title":"Pediatr. Res."},{"key":"2021112218152468900_BCJ-2020-0586C135","first-page":"141","article-title":"N-acetylglucosamine 6-sulfate residues in keratan sulfate and heparan sulfate are desulfated by the same enzyme","volume":"6","year":"1983","journal-title":"Biochem. Int."},{"key":"2021112218152468900_BCJ-2020-0586C136","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1111\/j.1432-1033.1985.tb09138.x","article-title":"Intralysosomal formation and metabolic fate of N-acetylglucosamine 6-sulfate from keratan sulfate","volume":"151","year":"1985","journal-title":"Eur. J. Biochem."},{"key":"2021112218152468900_BCJ-2020-0586C137","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1007\/BF00280560","article-title":"Chromosomal localization of the gene for human glucosamine-6-sulphatase to 12q14","volume":"79","year":"1988","journal-title":"Hum. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C138","doi-asserted-by":"publisher","first-page":"841","DOI":"10.1042\/BJ20041811","article-title":"Purification of a 75\u2005kDa protein from the organelle matrix of human neutrophils and identification as N-acetylglucosamine-6-sulphatase","volume":"387","year":"2005","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C139","doi-asserted-by":"publisher","first-page":"54","DOI":"10.1016\/j.ymgme.2013.04.002","article-title":"Review of clinical presentation and diagnosis of mucopolysaccharidosis IVA","volume":"110","year":"2013","journal-title":"Mol Genet. Metab."},{"key":"2021112218152468900_BCJ-2020-0586C140","doi-asserted-by":"publisher","first-page":"965","DOI":"10.1093\/oxfordjournals.jbchem.a123697","article-title":"N-acetylgalactosamine-6-sulfate sulfatase in human placenta: purification and characteristics","volume":"110","year":"1991","journal-title":"J. Biochem."},{"issue":"Pt 1","key":"2021112218152468900_BCJ-2020-0586C141","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1042\/bj3290145","article-title":"Recombinant human sulphamidase: expression, amplification, purification and characterization","volume":"329","year":"1998","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C142","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1042\/bj2340083","article-title":"Human liver sulphamate sulphohydrolase. Determinations of native protein and subunit Mr values and influence of substrate agylcone structure on catalytic properties","volume":"234","year":"1986","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C143","doi-asserted-by":"publisher","first-page":"1251","DOI":"10.1006\/bbrc.2001.4265","article-title":"Heparan N-sulfatase: in vitro mutagenesis of potential N-glycosylation sites","volume":"280","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021112218152468900_BCJ-2020-0586C144","doi-asserted-by":"publisher","first-page":"465","DOI":"10.1038\/ng1295-465","article-title":"Cloning of the sulphamidase gene and identification of mutations in Sanfilippo A syndrome","volume":"11","year":"1995","journal-title":"Nat. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C145","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1007\/s10545-008-0838-5","article-title":"Sanfilippo syndrome: a mini-review","volume":"31","year":"2008","journal-title":"J. Inherit. Metab. Dis."},{"key":"2021112218152468900_BCJ-2020-0586C146","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1136\/adc.69.3.403","article-title":"Management of mucopolysaccharidosis type III","volume":"69","year":"1993","journal-title":"Arch. Dis. Child."},{"key":"2021112218152468900_BCJ-2020-0586C147","doi-asserted-by":"publisher","first-page":"462","DOI":"10.1111\/apa.12169","article-title":"Mucopolysaccharidosis type III (Sanfilippo syndrome) and misdiagnosis of idiopathic developmental delay, attention deficit\/hyperactivity disorder or autism spectrum disorder","volume":"102","year":"2013","journal-title":"Acta Paediatr."},{"key":"2021112218152468900_BCJ-2020-0586C148","doi-asserted-by":"publisher","first-page":"132","DOI":"10.3389\/fcell.2020.00132","article-title":"Retinal degeneration in MPS-IIIA mouse model","volume":"8","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"2021112218152468900_BCJ-2020-0586C149","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1001\/jama.281.3.249","article-title":"Prevalence of lysosomal storage disorders","volume":"281","year":"1999","journal-title":"JAMA"},{"key":"2021112218152468900_BCJ-2020-0586C150","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1186\/1750-1172-5-14","article-title":"Expression of the disease on female carriers of X-linked lysosomal disorders: a brief review","volume":"5","year":"2010","journal-title":"Orphanet. J. Rare Dis."},{"key":"2021112218152468900_BCJ-2020-0586C151","doi-asserted-by":"publisher","first-page":"270","DOI":"10.1016\/j.pediatrneurol.2004.10.009","article-title":"Mucopolysaccharidosis type II in females: case report and review of literature","volume":"32","year":"2005","journal-title":"Pediatr. Neurol."},{"key":"2021112218152468900_BCJ-2020-0586C152","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1007\/s00431-007-0635-4","article-title":"Mucopolysaccharidosis type II (Hunter syndrome): a clinical review and recommendations for treatment in the era of enzyme replacement therapy","volume":"167","year":"2008","journal-title":"Eur. J. Pediatr."},{"key":"2021112218152468900_BCJ-2020-0586C153","doi-asserted-by":"publisher","first-page":"987","DOI":"10.1126\/science.149.3687.987","article-title":"Hurler's syndrome: demonstration of an inherited disorder of connective tissue in cell culture","volume":"149","year":"1965","journal-title":"Science"},{"key":"2021112218152468900_BCJ-2020-0586C154","doi-asserted-by":"publisher","first-page":"106","DOI":"10.1016\/0005-2744(81)90088-7","article-title":"Identification and partial characterization of two enzyme forms of iduronate sulfatase from human placenta","volume":"661","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112218152468900_BCJ-2020-0586C155","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1042\/bj2710075","article-title":"Human liver iduronate-2-sulphatase. Purification, characterization and catalytic properties","volume":"271","year":"1990","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C156","doi-asserted-by":"publisher","first-page":"433","DOI":"10.1093\/oxfordjournals.jbchem.a133715","article-title":"Purification and some properties of human liver iduronate sulfatase","volume":"91","year":"1982","journal-title":"J. Biochem."},{"key":"2021112218152468900_BCJ-2020-0586C157","doi-asserted-by":"publisher","first-page":"813","DOI":"10.1038\/sj.ejhg.5200887","article-title":"Molecular and biochemical characterisation of a novel sulphatase gene: Arylsulfatase G (ARSG)","volume":"10","year":"2002","journal-title":"Eur. J. Hum. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C158","doi-asserted-by":"publisher","first-page":"1856","DOI":"10.1093\/hmg\/ddu603","article-title":"Ataxia is the major neuropathological finding in arylsulfatase G-deficient mice: similarities and dissimilarities to Sanfilippo disease (mucopolysaccharidosis type III)","volume":"24","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C159","doi-asserted-by":"publisher","first-page":"921","DOI":"10.1002\/mds.25791","article-title":"Genome-wide association study in musician's dystonia: a risk variant at the arylsulfatase G locus?","volume":"29","year":"2014","journal-title":"Mov. Disord."},{"key":"2021112218152468900_BCJ-2020-0586C160","doi-asserted-by":"publisher","first-page":"e85352","DOI":"10.1371\/journal.pone.0085352","article-title":"Expression and replication studies to identify new candidate genes involved in normal hearing function","volume":"9","year":"2014","journal-title":"PLoS One"},{"key":"2021112218152468900_BCJ-2020-0586C161","doi-asserted-by":"publisher","first-page":"1004","DOI":"10.1038\/gim.2017.227","article-title":"A homozygous founder missense variant in arylsulfatase G abolishes its enzymatic activity causing atypical Usher syndrome in humans","volume":"20","year":"2018","journal-title":"Genet. Med."},{"key":"2021112218152468900_BCJ-2020-0586C162","doi-asserted-by":"publisher","first-page":"100736","DOI":"10.1016\/j.ajoc.2020.100736","article-title":"Identification of a novel homozygous ARSG mutation as the second cause of Usher syndrome type 4","volume":"19","year":"2020","journal-title":"Am. J. Ophthalmol. Case Rep."},{"key":"2021112218152468900_BCJ-2020-0586C163","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1021\/acschembio.6b01033","article-title":"Arylsulfatase K is the lysosomal 2-sulfoglucuronate sulfatase","volume":"12","year":"2017","journal-title":"ACS Chem. Biol."},{"key":"2021112218152468900_BCJ-2020-0586C164","doi-asserted-by":"publisher","first-page":"3010","DOI":"10.1021\/pr800135v","article-title":"The mannose 6-phosphate glycoprotein proteome","volume":"7","year":"2008","journal-title":"J. Proteome Res."},{"key":"2021112218152468900_BCJ-2020-0586C165","doi-asserted-by":"publisher","first-page":"1274","DOI":"10.1093\/glycob\/cwq089","article-title":"Target selection of heparan sulfate hexuronic acid 2-O-sulfotransferase","volume":"20","year":"2010","journal-title":"Glycobiology"},{"key":"2021112218152468900_BCJ-2020-0586C166","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1007\/BF00711390","article-title":"Molecular defect of caprine N-acetylglucosamine-6-sulphatase deficiency. A single base substitution creates a stop codon in the 5\u2032-region of the coding sequence","volume":"18","year":"1995","journal-title":"J. Inherit. Metab. Dis."},{"key":"2021112218152468900_BCJ-2020-0586C167","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1007\/s004180100286","article-title":"Lysosomal sulfoglycolipid storage in the kidneys of mice deficient for arylsulfatase A (ASA) and of double-knockout mice deficient for ASA and galactosylceramide synthase","volume":"116","year":"2001","journal-title":"Histochem. Cell Biol."},{"key":"2021112218152468900_BCJ-2020-0586C168","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1186\/1476-511X-5-21","article-title":"Modest phenotypic improvements in ASA-deficient mice with only one UDP-galactose:ceramide-galactosyltransferase gene","volume":"5","year":"2006","journal-title":"Lipids Health Dis."},{"key":"2021112218152468900_BCJ-2020-0586C169","doi-asserted-by":"publisher","first-page":"1120","DOI":"10.1167\/iovs.15-17645","article-title":"Degeneration of photoreceptor cells in arylsulfatase G-deficient mice","volume":"57","year":"2016","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"2021112218152468900_BCJ-2020-0586C170","doi-asserted-by":"publisher","first-page":"982","DOI":"10.1093\/glycob\/cwi090","article-title":"Developmental and regional expression of heparan sulfate sulfotransferase genes in the mouse brain","volume":"15","year":"2005","journal-title":"Glycobiology"},{"key":"2021112218152468900_BCJ-2020-0586C171","doi-asserted-by":"publisher","first-page":"36283","DOI":"10.1074\/jbc.M112.403360","article-title":"A genetic model of substrate reduction therapy for mucopolysaccharidosis","volume":"287","year":"2012","journal-title":"J. Biol. Chem."},{"key":"2021112218152468900_BCJ-2020-0586C172","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1007\/s11011-016-9895-x","article-title":"Glycosaminoglycan levels and structure in a mucopolysaccharidosis IIIA mice and the effect of a highly secreted sulfamidase engineered to cross the blood-brain barrier","volume":"32","year":"2017","journal-title":"Metab. Brain Dis."},{"key":"2021112218152468900_BCJ-2020-0586C173","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1089\/hum.2015.170","article-title":"A preclinical study evaluating AAVrh10-based gene therapy for sanfilippo syndrome","volume":"27","year":"2016","journal-title":"Hum. Gene Ther."},{"key":"2021112218152468900_BCJ-2020-0586C174","doi-asserted-by":"publisher","first-page":"374","DOI":"10.1002\/jgm.2816","article-title":"Correction of murine mucopolysaccharidosis type IIIA central nervous system pathology by intracerebroventricular lentiviral-mediated gene delivery","volume":"16","year":"2014","journal-title":"J. Gene Med."},{"key":"2021112218152468900_BCJ-2020-0586C175","doi-asserted-by":"publisher","first-page":"1938","DOI":"10.1038\/mt.2013.141","article-title":"Myeloid\/Microglial driven autologous hematopoietic stem cell gene therapy corrects a neuronopathic lysosomal disease","volume":"21","year":"2013","journal-title":"Mol. Ther."},{"key":"2021112218152468900_BCJ-2020-0586C176","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1007\/8904_2012_169","article-title":"Neonatal bone marrow transplantation in MPS IIIA mice","volume":"8","year":"2013","journal-title":"JIMD Rep."},{"key":"2021112218152468900_BCJ-2020-0586C177","doi-asserted-by":"publisher","first-page":"675","DOI":"10.1002\/emmm.201202083","article-title":"A highly secreted sulphamidase engineered to cross the blood-brain barrier corrects brain lesions of mice with mucopolysaccharidoses type IIIA","volume":"5","year":"2013","journal-title":"EMBO Mol. Med."},{"key":"2021112218152468900_BCJ-2020-0586C178","doi-asserted-by":"publisher","first-page":"600","DOI":"10.1038\/mt.2008.305","article-title":"Enzyme replacement improves ataxic gait and central nervous system histopathology in a mouse model of metachromatic leukodystrophy","volume":"17","year":"2009","journal-title":"Mol. Ther."},{"key":"2021112218152468900_BCJ-2020-0586C179","doi-asserted-by":"publisher","first-page":"2760","DOI":"10.1093\/hmg\/ddr175","article-title":"Intracerebroventricular enzyme infusion corrects central nervous system pathology and dysfunction in a mouse model of metachromatic leukodystrophy","volume":"20","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C180","doi-asserted-by":"publisher","first-page":"2599","DOI":"10.1093\/hmg\/dds086","article-title":"Efficacy of enzyme replacement therapy in an aggravated mouse model of metachromatic leukodystrophy declines with age","volume":"21","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"2021112218152468900_BCJ-2020-0586C181","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1042\/bj2280443","article-title":"Absence of keratan sulphate from skeletal tissues of mouse and rat","volume":"228","year":"1985","journal-title":"Biochem. J."},{"key":"2021112218152468900_BCJ-2020-0586C182","doi-asserted-by":"publisher","first-page":"506","DOI":"10.1126\/science.1247363","article-title":"Exome sequencing links corticospinal motor neuron disease to common neurodegenerative disorders","volume":"343","year":"2014","journal-title":"Science"},{"key":"2021112218152468900_BCJ-2020-0586C183","doi-asserted-by":"publisher","first-page":"710","DOI":"10.1016\/j.bbamcr.2008.11.015","article-title":"Molecular basis of multiple sulfatase deficiency, mucolipidosis II\/III and niemann-Pick C1 disease - lysosomal storage disorders caused by defects of non-lysosomal proteins","volume":"1793","year":"2009","journal-title":"Biochim. Biophys. Acta"}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/477\/20\/3963\/896158\/bcj-2020-0586.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/477\/20\/3963\/896158\/bcj-2020-0586.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T02:32:55Z","timestamp":1637634775000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/477\/20\/3963\/226805\/Lysosomal-sulfatases-a-growing-family"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,10,29]]},"references-count":183,"journal-issue":{"issue":"20","published-print":{"date-parts":[[2020,10,30]]}},"URL":"https:\/\/doi.org\/10.1042\/bcj20200586","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,10,29]]}}}