{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T11:29:50Z","timestamp":1792668590379,"version":"4.5.0"},"reference-count":390,"publisher":"The Endocrine Society","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2002,10,1]]},"DOI":"10.1210\/er.2001-0040","type":"journal-article","created":{"date-parts":[[2002,10,8]],"date-time":"2002-10-08T18:39:46Z","timestamp":1034102386000},"page":"703-732","source":"Crossref","is-referenced-by-count":436,"title":["Sulfonation and Molecular Action"],"prefix":"10.1210","volume":"23","author":[{"given":"Charles A.","family":"Strott","sequence":"first","affiliation":[{"name":"Section on Steroid Regulation, Endocrinology and Reproduction Research Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-4510"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"80","published-online":{"date-parts":[[2016,11,7]]},"reference":[{"key":"2019041121493060600_R1","author":"Huxtable","year":"1986"},{"key":"2019041121493060600_R2","author":"Mitchell","year":"1996"},{"key":"2019041121493060600_R3","first-page":"239","article-title":"Heparan sulphates as membrane receptors for the fibroblast growth factors.","volume":"32","author":"Gallagher","year":"1994","journal-title":"Eur J Clin Chem Clin Biochem"},{"key":"2019041121493060600_R4","doi-asserted-by":"crossref","first-page":"1270","DOI":"10.1096\/fasebj.10.11.8836040","article-title":"Heparan sulfate: a piece of information.","volume":"10","author":"Salmivirta","year":"1996","journal-title":"FASEB J"},{"key":"2019041121493060600_R5","doi-asserted-by":"crossref","first-page":"R9","DOI":"10.1016\/S1074-5521(99)80014-3","article-title":"Carbohydrate sulfotransferases: mediators of extracellular communication","volume":"6","author":"Bowman","year":"1999","journal-title":"Chem Biol"},{"key":"2019041121493060600_R6","doi-asserted-by":"crossref","first-page":"S91","DOI":"10.1096\/fasebj.13.9001.s91","article-title":"The syndecans, tuners of transmembrane signaling","volume":"13","author":"Zimmermann","year":"1999","journal-title":"FASEB J"},{"key":"2019041121493060600_R7","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1146\/annurev.ph.50.030188.002051","article-title":"Tyrosine sulfation and the secretory. pathway.","volume":"50","author":"Huttner","year":"1988","journal-title":"Annu Rev Physiol"},{"key":"2019041121493060600_R8","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0009-2797(94)90068-X","article-title":"Protein tyrosine sulfation, 1993\u2014an update.","volume":"92","author":"Niehrs","year":"1994","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R9","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1096\/fasebj.10.10.8751716","article-title":"From legumes to leukocytes: biological roles for sulfated carbohydrates.","volume":"10","author":"Hooper","year":"1996","journal-title":"FASEB J"},{"key":"2019041121493060600_R10","doi-asserted-by":"crossref","first-page":"1520","DOI":"10.1210\/endo.137.5.8612480","article-title":"Glycosylation: to what end for the glycoprotein hormones?","volume":"137","author":"Baenziger","year":"1996","journal-title":"Endocrinology"},{"key":"2019041121493060600_R11","first-page":"1","author":"Makita","year":"1985"},{"key":"2019041121493060600_R12","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/0005-2760(94)90262-3","article-title":"Metabolic and functional aspects of sulfogalactolipids.","volume":"1211","author":"Vos","year":"1994","journal-title":"Biochim Biophys Acta"},{"key":"2019041121493060600_R13","author":"Kuchel","year":"1982"},{"key":"2019041121493060600_R14","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/0009-2797(94)90071-X","article-title":"Role of sulfation in thyroid hormone metabolism.","volume":"92","author":"Visser","year":"1994","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R15","first-page":"121","article-title":"Metabolism and function of ascorbic acid and its metabolites.","volume":"27","author":"Tolbert","year":"1985","journal-title":"Int J Vitam Nutr Res Suppl"},{"key":"2019041121493060600_R16","first-page":"219","author":"Roberts","year":"1970"},{"key":"2019041121493060600_R17","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1016\/S0022-2275(20)39454-2","article-title":"Synthesis of lithocholic acid sulfates and their identification in human bile.","volume":"12","author":"Palmer","year":"1971","journal-title":"J Lipid Res"},{"key":"2019041121493060600_R18","doi-asserted-by":"crossref","first-page":"5536","DOI":"10.1016\/S0021-9258(19)69234-3","article-title":"Synthesis and biological activity of vitramin D3 3\u03b2-sulfate.","volume":"256","author":"Nagubandi","year":"1981","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R19","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/0014-5793(85)80002-8","article-title":"25-hydroxyvitamin D3 3-sulfate is a major circulating form of vitamin D in man.","volume":"191","author":"Axelson","year":"1985","journal-title":"FEBS Lett"},{"key":"2019041121493060600_R20","first-page":"74","author":"Roy","year":"1970"},{"key":"2019041121493060600_R21","author":"Mathews","year":"1990"},{"key":"2019041121493060600_R22","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1126\/science.128.3324.575","article-title":"Biological sulfate activation and transfer.","volume":"128","author":"Lipmann","year":"1958","journal-title":"Science"},{"key":"2019041121493060600_R23","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1146\/annurev.bi.29.070160.002023","article-title":"Metabolism of sulfur compounds (sulfate metabolism).","volume":"29","author":"Gregory","year":"1960","journal-title":"Annu Rev Biochem"},{"key":"2019041121493060600_R24","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/0020-711X(80)90003-8","article-title":"3\u2032-Phosphoadenosine 5\u2032-phosphosulfate: metabolism in mammalian tissues.","volume":"12","author":"Farooqui","year":"1980","journal-title":"Int J Biochem"},{"key":"2019041121493060600_R25","first-page":"107","author":"Mulder","year":"1990"},{"key":"2019041121493060600_R26","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1002\/humu.1","article-title":"Mutations in the diastrophic dysplasia sulfate transporter (DTDST) gene (SLC26A2): 22 novel mutations, mutation review, associated skeletal phenotypes, and diagnostic relevance.","volume":"17","author":"Rossi","year":"2001","journal-title":"Hum Mutat"},{"key":"2019041121493060600_R27","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1038\/ng0196-100","article-title":"Achondrogenesis type IB is caused by mutations in the diastrophic dysplasia sulphate transporter gene.","volume":"12","author":"Superti-Furga","year":"1996","journal-title":"Nat Genet"},{"key":"2019041121493060600_R28","first-page":"255","article-title":"Atelosteogenesis type II is caused by mutations in the diastrophic dysplasia sulfate-transporter gene (DTDST): evidence for a phenotypic series involving three chrondrodysplasias.","volume":"58","author":"Hastbacka","year":"1996","journal-title":"Am J Hum Genet"},{"key":"2019041121493060600_R29","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1002\/(SICI)1096-8628(19960503)63:1<144::AID-AJMG25>3.0.CO;2-N","article-title":"A chondrodysplasia family produced by mutations in the diastrophic dysplasia sulfate transporter gene: genotype\/phenotype correlations.","volume":"63","author":"Superti-Furga","year":"1996","journal-title":"Am J Hum Genet"},{"key":"2019041121493060600_R30","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1530\/eje.0.1380623","article-title":"Surprising news: a putative sulfate transporter is defective in Pendred\u2019s syndrome.","volume":"138","author":"Rutishauser","year":"1998","journal-title":"Eur J Endocrinol"},{"key":"2019041121493060600_R31","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1093\/hmg\/10.2.153","article-title":"Targeted disruption of mouse Pds provides insight about the inner-ear defects encountered in Pendred syndrome.","volume":"10","author":"Everett","year":"2001","journal-title":"Hum Mol Genet"},{"key":"2019041121493060600_R32","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1038\/ng1297-411","article-title":"Pendred syndrome is caused by mutations in a putative sulphate transporter gene (PDS).","volume":"17","author":"Everett","year":"1997","journal-title":"Nat Genet"},{"key":"2019041121493060600_R33","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1038\/7783","article-title":"The Pendred syndrome gene encodes a chloride-iodide transport protein.","volume":"21","author":"Scott","year":"1999","journal-title":"Nat Genet"},{"key":"2019041121493060600_R34","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1210\/endo.141.2.7303","article-title":"Pendrin, the protein encoded by the Pendred syndrome gene (PDS), is an apical porter of iodide in the thyroid and is regulated by thyroglobulin in FRTL-5 cells.","volume":"141","author":"Royaux","year":"2000","journal-title":"Endocrinology"},{"key":"2019041121493060600_R35","doi-asserted-by":"crossref","first-page":"6408","DOI":"10.1021\/ja01605a028","article-title":"The mechanism of \u201cactive sulfate\u201d formation.","volume":"78","author":"Bandurski","year":"1956","journal-title":"J Am Chem Soc"},{"key":"2019041121493060600_R36","doi-asserted-by":"crossref","first-page":"6409","DOI":"10.1021\/ja01605a029","article-title":"The enzymatic sequence in the biosynthesis of active sulfate.","volume":"78","author":"Robbins","year":"1956","journal-title":"J Am Chem Soc"},{"key":"2019041121493060600_R37","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1016\/S0021-9258(18)64727-1","article-title":"Separation of the two enzymatic phases in active sulfate synthesis.","volume":"233","author":"Robbins","year":"1958","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R38","doi-asserted-by":"crossref","first-page":"5920","DOI":"10.1021\/bi00185a032","article-title":"Rat chondrosarcoma ATP-sulfurylase and adenosine 5\u2032-phosphosulfate kinase reside on a single bifunctional protein.","volume":"33","author":"Lyle","year":"1994","journal-title":"Biochemistry (Mosc)"},{"key":"2019041121493060600_R39","doi-asserted-by":"crossref","first-page":"515","DOI":"10.3109\/10409239309085137","article-title":"The physical biochemistry and molecular genetics of sulfate activation.","volume":"28","author":"Leyh","year":"1993","journal-title":"Crit Rev Biochem Mol Biol"},{"key":"2019041121493060600_R40","doi-asserted-by":"crossref","first-page":"4163","DOI":"10.1002\/j.1460-2075.1988.tb03312.x","article-title":"Phosphorylation of an 85-kd membrane protein by a novel mechanism.","volume":"7","author":"Seydel","year":"1988","journal-title":"EMBO J"},{"key":"2019041121493060600_R41","doi-asserted-by":"crossref","first-page":"6822","DOI":"10.1021\/bi00188a010","article-title":"Intermediate channeling between ATP sulfurylase and adenosine 5\u2032-phosphosulfate kinase from rat chondrosarcoma.","volume":"33","author":"Lyle","year":"1994","journal-title":"Biochemistry (Mosc)"},{"key":"2019041121493060600_R42","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0009-2797(97)00129-4","article-title":"Sulfate activation and transport in mammals: system components and mechanisms.","volume":"109","author":"Schwartz","year":"1998","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R43","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/0378-1119(95)00450-K","article-title":"A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities.","volume":"165","author":"Rosenthal","year":"1995","journal-title":"Gene"},{"key":"2019041121493060600_R44","doi-asserted-by":"crossref","first-page":"29453","DOI":"10.1074\/jbc.270.49.29453","article-title":"The isolation and characterization of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5\u2032-phosphosulfate kinase.","volume":"270","author":"Li","year":"1995","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R45","doi-asserted-by":"crossref","first-page":"19311","DOI":"10.1074\/jbc.273.30.19311","article-title":"Molecular cloning, expression and characterization of human bifunctional 3\u2032-phosphoadenosine 5\u2032-phosphosulfate synthase and its functional domains.","volume":"273","author":"Venkatachalam","year":"1998","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R46","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1271\/bbb.62.1037","article-title":"cDNA cloning, expression and characterization of the human bifunctional ATP sulfurylase\/adenosine 5\u2032-phosphosulfate kinase enzyme.","volume":"62","author":"Yanagisawa","year":"1998","journal-title":"Biosci Biotechnol Biochem"},{"key":"2019041121493060600_R47","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1096\/fasebj.12.7.603","article-title":"Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase.","volume":"12","author":"Girard","year":"1998","journal-title":"FASEB J"},{"key":"2019041121493060600_R48","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S0925-4773(97)00136-6","article-title":"cDNA sequence and expression pattern of the Drosophila melanogaster PAPS synthetase gene: a new salivary gland marker.","volume":"68","author":"Jullien","year":"1997","journal-title":"Mech Dev"},{"key":"2019041121493060600_R49","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1042\/bj20020044","article-title":"Characterization and expression of human bifunctional 3\u2032-phosphoadenosine 5\u2032-phosphosulfate synthase isoforms.","volume":"364","author":"Fuda","year":"2002","journal-title":"Biochem J"},{"key":"2019041121493060600_R50","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1006\/bbrc.2000.2123","article-title":"Human 3\u2032-phosphoadenosine 5\u2032-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization.","volume":"268","author":"Xu","year":"2000","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R51","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1002\/j.1460-2075.1982.tb01276.x","article-title":"Distantly related sequences in the \u03b1- and \u03b2-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.","volume":"1","author":"Walker","year":"1982","journal-title":"EMBO J"},{"key":"2019041121493060600_R52","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1016\/0968-0004(90)90281-F","article-title":"The P-loop\u2014a common motif in ATP- and GTP-binding proteins.","volume":"15","author":"Saraste","year":"1990","journal-title":"Trends Biochem Sci"},{"key":"2019041121493060600_R53","doi-asserted-by":"crossref","first-page":"9450","DOI":"10.1074\/jbc.273.16.9450","article-title":"Deletion and site-directed mutagenesis of the ATP-binding motif (P-loop) in the bifunctional murine ATP-sulfurylase\/adenosine 5\u2032-phosphosulfate kinase enzyme.","volume":"273","author":"Deyrup","year":"1998","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R54","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1002\/prot.340220306","article-title":"The cytidylyltransferase superfamily: identification of the nucleotide-binding site and fold prediction.","volume":"22","author":"Bork","year":"1995","journal-title":"Proteins"},{"key":"2019041121493060600_R55","doi-asserted-by":"crossref","first-page":"2601","DOI":"10.1074\/jbc.274.5.2601","article-title":"Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3\u2032-phosphoadenosine 5\u2032-phosphosulfate synthase.","volume":"274","author":"Venkatachalam","year":"1999","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R56","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1038\/2458","article-title":"Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse.","volume":"20","author":"ul Haque","year":"1998","journal-title":"Nat Genet"},{"key":"2019041121493060600_R57","doi-asserted-by":"crossref","first-page":"8681","DOI":"10.1073\/pnas.95.15.8681","article-title":"A member of a family of sulfate-activating enzymes causes murine brachymorphism.","volume":"95","author":"Kurima","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R58","doi-asserted-by":"crossref","first-page":"33306","DOI":"10.1074\/jbc.274.47.33306","article-title":"Genomic organization of the mouse and human genes encoding the ATP sulfurylase\/adenosine 5\u2032-phosphosulfate kinase isoform SK2.","volume":"274","author":"Kurima","year":"1999","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R59","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1096\/fasebj.14.2.345","article-title":"Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells.","volume":"14","author":"Besset","year":"2000","journal-title":"FASEB J"},{"key":"2019041121493060600_R60","doi-asserted-by":"crossref","first-page":"2284","DOI":"10.1210\/endo.133.5.8404682","article-title":"Estrogen and hydroxysteroid sulfotransferases in guinea pig adrenal cortex: cellular and subcellular distributions.","volume":"133","author":"Whitnall","year":"1993","journal-title":"Endocrinology"},{"key":"2019041121493060600_R61","doi-asserted-by":"crossref","first-page":"1541","DOI":"10.1210\/endo.131.3.1380444","article-title":"Spatio-temporal expression of estrogen sulfotransferase within the hepatic lobule of male rats: implication of in situ estrogen inactivation in androgen action.","volume":"131","author":"Mancini","year":"1992","journal-title":"Endocrinology"},{"key":"2019041121493060600_R62","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1006\/bbrc.2001.5032","article-title":"Transcriptional regulation of human 3\u2032-phosphoadenosine 5\u2032-phosphosulfate sulfate synthase 1.","volume":"284","author":"Shimizu","year":"2001","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R63","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1042\/bj3630263","article-title":"Transcriptional regulation of human 3\u2032-phosphoadenosine 5\u2032-phosphosulfate sulfate synthase 2.","volume":"363","author":"Shimizu","year":"2002","journal-title":"Biochem J"},{"key":"2019041121493060600_R64","first-page":"70","author":"Mulder","year":"1981"},{"key":"2019041121493060600_R65","author":"Roy","year":"1970"},{"key":"2019041121493060600_R66","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/0005-2744(70)90032-X","article-title":"Enzymatic dephosphorylation of 3\u2032-phosphoadenosine 5\u2032-phosphosulfate to adenosine 5\u2032-phosphosulfate in sheep brain.","volume":"198","author":"Farooqui","year":"1970","journal-title":"Biochim Biophys Acta"},{"key":"2019041121493060600_R67","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/0005-2744(73)90269-6","article-title":"Separation and properties of the soluble 3\u2032-phosphoadenosine 5\u2032-phosphosulfate degrading enzymes of bovine liver.","volume":"315","author":"Denner","year":"1973","journal-title":"Biochim Biophys Acta"},{"key":"2019041121493060600_R68","first-page":"18","article-title":"The enzymatic degradation nucleotide sulphatophosphate anhydrides.","volume":"85","author":"Lewis","year":"1962","journal-title":"Biochem J"},{"key":"2019041121493060600_R69","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/0304-4165(69)90006-3","article-title":"Subcellular distribution of two enzyme systems which degrade 3\u2032-phosphoadenosine 5\u2032-phosphosulfate (\u201cactive sulfate\u201d).","volume":"192","author":"Austin","year":"1969","journal-title":"Biochim Biophys Acta"},{"key":"2019041121493060600_R70","doi-asserted-by":"crossref","first-page":"1275","DOI":"10.3181\/00379727-140-36657","article-title":"The intracellular localization in the rat adrenal of enzymes which degrade 3\u2032-phosphoadenosine 5\u2032-phosphosulfate.","volume":"140","author":"Fry","year":"1972","journal-title":"Proc Soc Exp Biol"},{"key":"2019041121493060600_R71","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/0005-2744(70)90013-6","article-title":"Purification and properties of two adenosine 5\u2032-phosphosulfate sulphohydrolases from rat liver and their possible role in the degradation of 3\u2032-phosphoadenosine 5\u2032-phosphosulfate","volume":"220","author":"Bailey-Wood","year":"1970","journal-title":"Biochim Biophys Acta"},{"key":"2019041121493060600_R72","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/0005-2744(70)90130-0","article-title":"Properties and subcellular distribution of two sulfatases which degrade adenosine 5\u2032-phosphosulfate.","volume":"198","author":"Armstrong","year":"1970","journal-title":"Biochim Biophys Acta"},{"key":"2019041121493060600_R73","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/0005-2744(73)90008-9","article-title":"Purification of a soluble adenosine 5\u2032-phosphosulfate sulphohydrolase from bovine liver.","volume":"302","author":"Stokes","year":"1973","journal-title":"Biochim Biophys Acta"},{"key":"2019041121493060600_R74","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1126\/science.7809627","article-title":"A salt-sensitive 3\u2032(2\u2032),5\u2032-bisphosphate nucleotidase involved in sulfate activation.","volume":"267","author":"Murguia","year":"1995","journal-title":"Science"},{"key":"2019041121493060600_R75","doi-asserted-by":"crossref","first-page":"3157","DOI":"10.1002\/j.1460-2075.1992.tb05392.x","article-title":"A novel conserved salt-induced protein is an important determinant of salt tolerance.","volume":"11","author":"Gaxiola","year":"1992","journal-title":"EMBO J"},{"key":"2019041121493060600_R76","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1096\/fasebj.11.6.9194521","article-title":"The importance of 3\u2032-phosphoadenosine 5\u2032-phosphosulfate (PAPS) in the regulation of sulfation.","volume":"11","author":"Klaassen","year":"1997","journal-title":"FASEB J"},{"key":"2019041121493060600_R77","doi-asserted-by":"crossref","first-page":"2113","DOI":"10.1016\/S0021-9258(17)43324-2","article-title":"Adenosine 5\u2032-phosposulfate kinase from Penicillium chrysogenum. Purification and kinetic characterization.","volume":"259","author":"Renosto","year":"1984","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R78","doi-asserted-by":"crossref","first-page":"9433","DOI":"10.1016\/S0021-9258(18)60550-2","article-title":"Sulfate-activating enzymes of Penicillium chrysogenum.","volume":"264","author":"Renosto","year":"1989","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R79","first-page":"190","article-title":"The effect of inhibitors of mitochondrial energy production on hepatic glutathione, UDP-glucuronic acid, and adenosine 3\u2032-phosphate-5\u2032-phosphosulfate concentrations.","volume":"14","author":"Dills","year":"1986","journal-title":"Drug Metab Dispos"},{"key":"2019041121493060600_R80","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/0041-008X(90)90025-P","article-title":"Effect of sulfhydryl-deficient diets on hepatic metallothionein, glutathione, and adenosine 3\u2032-phosphate 5\u2032-phosphosulfate (PAPS) levels in rats.","volume":"102","author":"Sendelbach","year":"1990","journal-title":"Toxicol Appl Pharamcol"},{"key":"2019041121493060600_R81","first-page":"1015","article-title":"Homeostasis of sulfate and 3\u2032-phosphoadenosine 5\u2032-phosphosulfate in rats after acetaminophen administration.","volume":"261","author":"Hyo","year":"1992","journal-title":"J Pharmacol Exp Ther"},{"key":"2019041121493060600_R82","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/0009-2797(94)90059-0","article-title":"Major hydroxysteroid sulfotransferase STa in rat liver cytosol may consist of two microheterogeneous subunits","volume":"92","author":"Ogura","year":"1994","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R83","first-page":"725","article-title":"Sulfation of acetaminophen and acetaminophen-induced alterations in sulfate and 3\u2032-phosphopadenosine 5\u2032-phosphosulfate homeostasis in rats with deficient dietary intake of sulfur.","volume":"22","author":"Gregus","year":"1994","journal-title":"Drug Metab Dispos"},{"key":"2019041121493060600_R84","first-page":"133","article-title":"Comparison of adenosine 3\u2032-phosphate 5\u2032-phosphosulfate concentrations in tissues from different laboratory animals.","volume":"15","author":"Brzeznicka","year":"1987","journal-title":"Drug Metab Dispos"},{"key":"2019041121493060600_R85","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1007\/BF00679793","article-title":"Distribution of 2-naphthol sulphotransferase and its endogenous substrate adenosine 3\u2032-phosphate 5\u2032-phosphosulfate in human tissues.","volume":"37","author":"Cappiello","year":"1989","journal-title":"J Clin Pharmacol"},{"key":"2019041121493060600_R86","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1159\/000480940","article-title":"Sulphotransferase and its substrate; adenosine-3\u2032-phosphate-5\u2032-phosphosulfate in human fetal liver and placenta.","volume":"14","author":"Cappiello","year":"1990","journal-title":"Dev Pharmacol"},{"key":"2019041121493060600_R87","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/S0304-4165(00)00016-7","article-title":"Diversity and functions of glycoaminoglycan sulfotransferases.","volume":"1474","author":"Habuchi","year":"2000","journal-title":"Biochim Biophys Acta"},{"key":"2019041121493060600_R88","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/S0014-5793(00)01111-X","article-title":"Targeted disruption of NDST-1 gene leads to pulminary hypoplasia and neonatal respiratory distress in mice.","volume":"467","author":"Fan","year":"2000","journal-title":"FEBS Lett"},{"key":"2019041121493060600_R89","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1093\/oxfordjournals.jbchem.a021961","article-title":"Molecular cloning and expression of an amine sulfotransferase cDNA: a new family of cytosolic sulfotransferases in mammals.","volume":"123","author":"Yoshinari","year":"1998","journal-title":"J Biochem"},{"key":"2019041121493060600_R90","first-page":"33","article-title":"International sulfation workshop.","volume":"16","author":"Falany","year":"1996","journal-title":"ISSX Newsletter"},{"key":"2019041121493060600_R91","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1146\/annurev.pharmtox.40.1.159","article-title":"Pharmacogenetics of sulfotransferase.","volume":"40","author":"Nagata","year":"2000","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"2019041121493060600_R92","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1042\/bj3460857","article-title":"Molecular cloning and expression of novel sulfotransferase-like cDNAs from human and rat brain.","volume":"346","author":"Falany","year":"2000","journal-title":"Biochem J"},{"key":"2019041121493060600_R93","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/S0378-1119(02)00431-6","article-title":"Highly conserved mouse and human brain sulfotransferases: molecular cloning, expression, and functional characterization.","volume":"285","author":"Sakakibara","year":"2002","journal-title":"Gene"},{"key":"2019041121493060600_R94","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/bbrc.2002.6658","article-title":"Catecholestrogen sulfation: possible role in carcinogenesis.","volume":"292","author":"Adjei","year":"2002","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R95","doi-asserted-by":"crossref","first-page":"2311","DOI":"10.1096\/fasebj.6.6.1347506","article-title":"Neuroactive steroids.","volume":"6","author":"Paul","year":"1992","journal-title":"FASEB J"},{"key":"2019041121493060600_R96","first-page":"553","article-title":"Minoxidil sulfate is the active metabolite that stimulates hair follicles.","volume":"95","author":"Buhl","year":"1990","journal-title":"AACN Clin Issues"},{"key":"2019041121493060600_R97","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/0022-4731(73)90076-9","article-title":"The specificity of the estrogen receptor of human uterus.","volume":"4","author":"Hahnel","year":"1973","journal-title":"J Steroid Biochem"},{"key":"2019041121493060600_R98","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/0009-2797(94)90074-4","article-title":"Sulfonation in chemical carcinogenesis\u2014history and present status.","volume":"92","author":"Miller","year":"1994","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R99","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1096\/fasebj.11.5.9141497","article-title":"Bioactivation of mutagens via sulfation.","volume":"11","author":"Glatt","year":"1997","journal-title":"FASEB J"},{"key":"2019041121493060600_R100","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/S0009-2797(97)00134-8","article-title":"Bioactivation of benzylic and allylic alcohols via sulfo-conjugation.","volume":"109","author":"Surh","year":"1998","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R101","doi-asserted-by":"crossref","first-page":"1709","DOI":"10.1093\/carcin\/19.10.1709","article-title":"Rat, but not human, sulfotransferase activates a tamoxifen metabolite to produce DNA adducts and gene mutations in bacteria and mammalian cells in culture.","volume":"19","author":"Glatt","year":"1998","journal-title":"Carcinogenesis"},{"key":"2019041121493060600_R102","doi-asserted-by":"crossref","first-page":"1851","DOI":"10.1093\/carcin\/21.10.1851","article-title":"Major inter-species differences in the rates of O-sulphonation and O-glucuronylation of \u03b1-hydroxytamoxifen in vitro: a metabolic disparity protecting human liver from the formation of tamoxifen-DNA adducts.","volume":"21","author":"Boocock","year":"2000","journal-title":"Carcinogenesis"},{"key":"2019041121493060600_R103","doi-asserted-by":"crossref","first-page":"47747","DOI":"10.1074\/jbc.R100049200","article-title":"Carbohydrate-modifying sulfotransferases: structure, function, and pathophysiology.","volume":"276","author":"Fukuda","year":"2001","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R104","doi-asserted-by":"crossref","first-page":"13825","DOI":"10.1021\/bi0011072","article-title":"Role of tyrosine sulfation and serine phosphorylation in the processing of procholecystokinin and its secretion in transfected atT-20 cells.","volume":"39","author":"Vishnuvardhan","year":"2000","journal-title":"Biochemistry (Mosc)"},{"key":"2019041121493060600_R105","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1021\/jm00208a006","article-title":"Cholecystokinin (pancreozymin). 4. Synthesis and properties of a biologically active analogue of the C-terminal heptapeptide with \u03b5-hydroxynorleucine sulfate replacing tyrosine sulfate.","volume":"21","author":"Bodanszky","year":"1978","journal-title":"J Med Chem"},{"key":"2019041121493060600_R106","doi-asserted-by":"crossref","first-page":"2896","DOI":"10.1073\/pnas.95.6.2896","article-title":"Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins.","volume":"95","author":"Ouyang","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R107","doi-asserted-by":"crossref","first-page":"11134","DOI":"10.1073\/pnas.95.19.11134","article-title":"Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2.","volume":"95","author":"Beisswanger","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R108","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/S0959-437X(97)80153-0","article-title":"The sulfatase gene family.","volume":"7","author":"Parenti","year":"1997","journal-title":"Curr Opin Genet Dev"},{"key":"2019041121493060600_R109","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1038\/nsb1197-904","article-title":"Crystal structure of estrogen sulphotransferase.","volume":"4","author":"Kakuta","year":"1997","journal-title":"Nature Struct Biol"},{"key":"2019041121493060600_R110","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1006\/jmbi.1999.3153","article-title":"Crystal structure of human catecholamine sulfotransferase.","volume":"293","author":"Bidwell","year":"1999","journal-title":"J Mol Biol"},{"key":"2019041121493060600_R111","doi-asserted-by":"crossref","first-page":"37862","DOI":"10.1074\/jbc.274.53.37862","article-title":"X-ray crystal structure of human dopamine sulfotransferase, SULT1A3.","volume":"274","author":"Dajani","year":"1999","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R112","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0014-5793(00)01479-4","article-title":"Crystal structure of SULT2A3, human hydroxysteroid sullfotransferase.","volume":"475","author":"Pedersen","year":"2000","journal-title":"FEBS Lett"},{"key":"2019041121493060600_R113","doi-asserted-by":"crossref","first-page":"17928","DOI":"10.1074\/jbc.M111651200","article-title":"Crystal structure of the human estrogen sulfotransferase-PAPS complex.","volume":"277","author":"Pedersen","year":"2002","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R114","doi-asserted-by":"crossref","first-page":"10673","DOI":"10.1074\/jbc.274.16.10673","article-title":"Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase\/N-sulfotransferase 1.","volume":"274","author":"Kakuta","year":"1999","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R115","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1002\/jbt.1","article-title":"Crystal structure-based studies of cytosolic sulfotransferase.","volume":"15","author":"Yoshinari","year":"2001","journal-title":"J Biochem Mol Toxicol"},{"key":"2019041121493060600_R116","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1210\/edrv-17-6-670","article-title":"Steroid sulfotransferases.","volume":"17","author":"Strott","year":"1996","journal-title":"Endocr Rev"},{"key":"2019041121493060600_R117","first-page":"S87","article-title":"Steroid sulfotransferases","volume":"150","author":"Luu-The","year":"1996","journal-title":"J Endocrinol"},{"key":"2019041121493060600_R118","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1006\/geno.1998.5518","article-title":"Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene.","volume":"53","author":"Her","year":"1998","journal-title":"Genomics"},{"key":"2019041121493060600_R119","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1006\/bbrc.1998.8872","article-title":"Molecular cloning, expression, and functional characterization of novel mouse sulfotransferases.","volume":"247","author":"Sakakibara","year":"1998","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R120","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1016\/S0006-291X(05)81514-1","article-title":"Molecular cloning of the alcohol\/hydroxysteroid form (hSTa) of sulfotransferase from human liver","volume":"187","author":"Kong","year":"1992","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R121","first-page":"865","article-title":"Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of cDNA.","volume":"41","author":"Otterness","year":"1992","journal-title":"Mol Pharmacol"},{"key":"2019041121493060600_R122","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1042\/bj2720597","article-title":"Human liver steroid sulphotransferase sulphates bile acids.","volume":"272","author":"Radominska","year":"1990","journal-title":"Biochem J"},{"key":"2019041121493060600_R123","first-page":"268","article-title":"Cholesterol sulfation in human liver.","volume":"21","author":"Aksoy","year":"1993","journal-title":"Drug Metab Dispos"},{"key":"2019041121493060600_R124","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/S1054-3589(08)61037-6","article-title":"Biochemistry of cytosolic sulfotransferases involved in bioactivation.","volume":"27","author":"Falany","year":"1994","journal-title":"Adv Pharmacol"},{"key":"2019041121493060600_R125","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/0960-0760(94)90077-9","article-title":"Steroid sulfation by expressed human cytosolic sulfotransferases.","volume":"48","author":"Falany","year":"1994","journal-title":"J Steroid Biochem Mol Biol"},{"key":"2019041121493060600_R126","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1096\/fasebj.11.4.9068609","article-title":"Enzymology of human cytosolic sulfotransferases.","volume":"11","author":"Falany","year":"1997","journal-title":"FASEB J"},{"key":"2019041121493060600_R127","doi-asserted-by":"crossref","first-page":"2978","DOI":"10.1210\/endo.142.7.8244","article-title":"Cholesterol and hydroxycholesterol sulfotransferases: identification, distinction from dehydroepiandrosterone sulfotransferase, and differential tissue expression.","volume":"142","author":"Javitt","year":"2001","journal-title":"Endocrinology"},{"key":"2019041121493060600_R128","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/S0960-0760(01)00064-4","article-title":"Expression and characterization of the human 3\u03b2-hydroxysteroid sulfotransferases (SULT2B1a and SULT2B1b).","volume":"77","author":"Meloche","year":"2001","journal-title":"J Steroid Biochem Mol Biol"},{"key":"2019041121493060600_R129","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1006\/bbrc.2001.5746","article-title":"Biochemical characterization and tissue distribution of human SULT2B1.","volume":"288","author":"Geese","year":"2001","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R130","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/0167-4781(96)00065-6","article-title":"Structural relationships among members of the mammalian sulfotransferase gene family.","volume":"1307","author":"Rikke","year":"1996","journal-title":"Biochim Biophys Acta"},{"key":"2019041121493060600_R131","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1096\/fasebj.11.1.9034160","article-title":"Sulfotransferase molecular biology: cDNAs and genes.","volume":"11","author":"Weinshilboum","year":"1997","journal-title":"FASEB J"},{"key":"2019041121493060600_R131A","doi-asserted-by":"crossref","first-page":"36161","DOI":"10.1074\/jbc.M207165200","article-title":"Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase.","volume":"277","author":"Fuda","year":"2002","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R132","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1006\/bbrc.2000.3643","article-title":"Expression profiling of human sulfotransferase and sulfatase gene superfamilies in epithelial tissues and cultured cells.","volume":"277","author":"Dooley","year":"2000","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R133","first-page":"1619","article-title":"Cholesterol sulfate activates multiple protein kinase C isozymes and induces granular cell differentiation in cultured murine keratinocytes.","volume":"6","author":"Denning","year":"1995","journal-title":"Cell Growth Differ"},{"key":"2019041121493060600_R134","doi-asserted-by":"crossref","first-page":"1098","DOI":"10.1046\/j.1523-1747.1998.00441.x","article-title":"Cholesterol sulfate activates transcription of transglutaminase 1 gene in normal human keratinocytes.","volume":"111","author":"Kawabe","year":"1998","journal-title":"J Invest Dermatol"},{"key":"2019041121493060600_R135","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1016\/S0022-2275(20)31663-1","article-title":"Cholesterol sulfate stimulates involucrin transcription in keratinocytes by increasing Fra-1, Fra-2, and Jun D.","volume":"42","author":"Hanley","year":"2001","journal-title":"J Lipid Res"},{"key":"2019041121493060600_R136","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1111\/1523-1747.ep12276731","article-title":"Increased cholesterolsulfate and cholesterol sulfotransferase activity in relation to the multi-step process of differentiation in human epidermal keratinocytes.","volume":"92","author":"Jetten","year":"1989","journal-title":"J Invest Dermatol"},{"key":"2019041121493060600_R137","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1139\/o01-132","article-title":"Purification and characterization of cholesterol sulfotransferase from rat skin.","volume":"79","author":"Rearick","year":"2001","journal-title":"Biochem Cell Biol"},{"key":"2019041121493060600_R138","doi-asserted-by":"crossref","first-page":"21856","DOI":"10.1074\/jbc.273.34.21856","article-title":"Tissue-specific and androgen-repressible regulation of the rat dehydroepiandrosterone sulfotransferase gene promoter.","volume":"273","author":"Song","year":"1998","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R139","doi-asserted-by":"crossref","first-page":"42549","DOI":"10.1074\/jbc.M107557200","article-title":"Dehydroepiandrosterone sulfotransferase gene induction by bile acid activated farnesoid X receptor.","volume":"276","author":"Song","year":"2001","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R140","first-page":"589","article-title":"Estrogen sulfotransferase of the rat liver: complementary DNA cloning and age- and sex-specific regulation of messenger RNA","volume":"6","author":"Demyan","year":"1992","journal-title":"Mol Endocrinol"},{"key":"2019041121493060600_R141","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1210\/endo.135.3.8070389","article-title":"Characterization of guinea pig estrogen sulfotransferase expressed by Chinese Hamster Ovary cell-K1 stable transfectants.","volume":"135","author":"Tomizuka","year":"1994","journal-title":"Endocrinology"},{"key":"2019041121493060600_R142","doi-asserted-by":"crossref","first-page":"30019","DOI":"10.1074\/jbc.274.42.30019","article-title":"Substrate gating confers steroid specificity to estrogen sulfotransferase.","volume":"274","author":"Petrotchenko","year":"1999","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R143","doi-asserted-by":"crossref","first-page":"23496","DOI":"10.1016\/S0021-9258(19)49490-8","article-title":"Isolation of two distinct 3-hydroxysteroid sulfotransferases from the guinea pig adrenal.","volume":"268","author":"Driscoll","year":"1993","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R144","doi-asserted-by":"crossref","first-page":"21562","DOI":"10.1074\/jbc.274.31.21562","article-title":"Identifcation by chimera formation and site-selected mutagenesis of a key amino acid residue involved in determining stereospecificity of guinea pig 3-hydroxysteroid sulfotransferase isoforms.","volume":"274","author":"Park","year":"1999","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R145","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/S0014-5793(01)02129-9","article-title":"The dimerization motif of cytosolic sulfotransferases.","volume":"490","author":"Petrotchenko","year":"2001","journal-title":"FEBS Lett"},{"key":"2019041121493060600_R146","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1016\/S0306-4530(98)00071-7","article-title":"Neurosteroids: a novel function of the brain.","volume":"23","author":"Baulieu","year":"1998","journal-title":"Psychoneuroendocrinology"},{"key":"2019041121493060600_R147","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/S0165-6147(00)01706-5","article-title":"Neurosteroids on our minds.","volume":"22","author":"Puia","year":"2001","journal-title":"Trends Pharmacol Sci"},{"key":"2019041121493060600_R148","doi-asserted-by":"crossref","first-page":"4089","DOI":"10.1073\/pnas.95.8.4089","article-title":"Dehydroepiandrosterone (DHEA) and Dehydroepiandrosterone sulfate (DHEAS) as neuroactive steroids.","volume":"95","author":"Baulieu","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R149","doi-asserted-by":"crossref","first-page":"4678","DOI":"10.1073\/pnas.95.8.4678","article-title":"Dehydroepiandrosterone: a potential signalling molecule for neocortical organization during development.","volume":"95","author":"Compagnone","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R150","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0031-9384(98)00256-X","article-title":"The neurosteroids DHEA and DHEAS may influence cognitive performance by altering affective state.","volume":"66","author":"Frye","year":"1999","journal-title":"Physiol Behav"},{"key":"2019041121493060600_R151","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/S0031-9384(00)00446-7","article-title":"Memory-enhancing effects of DHEAS in aged mice on a win-shift water escape task.","volume":"72","author":"Markowski","year":"2001","journal-title":"Physiol Behav"},{"key":"2019041121493060600_R152","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0006-8993(98)00640-4","article-title":"Pregnenolone sulfate exacerbates NMDA-induced death of hippocampal neurons.","volume":"803","author":"Weaver","year":"1998","journal-title":"Brain Res"},{"key":"2019041121493060600_R153","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1080\/00016489850183692","article-title":"The neurosteroid pregnenolone sulfate excites medial vestibular nucleus neurons.","volume":"533","author":"Yamamoto","year":"1998","journal-title":"Acta Otolaryngol Suppl (Stockh)"},{"key":"2019041121493060600_R154","doi-asserted-by":"crossref","first-page":"3757","DOI":"10.1046\/j.1460-9568.1999.00816.x","article-title":"The neurosteroid pregnenolone sulphate increases dopamine release and the dopaminergic resonse to morphine in the rat nucleus accumbens.","volume":"11","author":"Barrot","year":"1999","journal-title":"Eur J Neurosci"},{"key":"2019041121493060600_R155","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0006-8993(99)01964-2","article-title":"Pregnenolone sulfate increases hippocampal acetylcholine release and spatial recognition.","volume":"852","author":"Darnaudery","year":"2000","journal-title":"Brain Res"},{"key":"2019041121493060600_R156","doi-asserted-by":"crossref","first-page":"62","DOI":"10.3109\/09513599809024971","article-title":"Nongenomic effects of neurosteroids.","volume":"12","author":"Revelli","year":"1998","journal-title":"Gynecol Endocrinol"},{"key":"2019041121493060600_R157","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/S0039-128X(97)00013-5","article-title":"Hydroxysteroid sulfotransferase activity in the rat brain and liver as a function of aging.","volume":"62","author":"Rajkowski","year":"1997","journal-title":"Steroids"},{"key":"2019041121493060600_R158","doi-asserted-by":"crossref","first-page":"848","DOI":"10.1046\/j.1471-4159.1999.720848.x","article-title":"Immunocytochemical localization and biological activity of hydroxysteroid sulfotransferase in the frog brain.","volume":"72","author":"Beaujean","year":"1999","journal-title":"J Neurochem"},{"key":"2019041121493060600_R159","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0305-0491(00)00199-1","article-title":"In vivo evidence for the production of sulfated steroids in the frog brain.","volume":"126","author":"Menash-Nyagan","year":"2000","journal-title":"Comp Biochem Physiol B Biochem Mol Biol"},{"key":"2019041121493060600_R160","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1159\/000054541","article-title":"Ovine fetal estrogen sulfotyransferase in brain regions important for hypothalamus-pituitary-adrenal axis control.","volume":"71","author":"Purinton","year":"2000","journal-title":"Neuroendocrinology"},{"key":"2019041121493060600_R161","first-page":"3558","article-title":"The zona reticularis is the site of biosynthesis of dehydroepiandrosterone and dehydroepiandrosterone sulfate in the adult adrenal cortex resulting from its low expression of 3\u03b2-hydroxysteroid dehydrogenase.","volume":"81","author":"Endoh","year":"1996","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R162","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1210\/jcem-59-3-551","article-title":"Age changes and sex differences in serum dehydroepiandrosterone sulfate concentrations throughout adulthood.","volume":"59","author":"Orentreich","year":"1984","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R163","first-page":"1086","article-title":"Changes in serum concentrations of conjugated and unconjugated steroids in 40- to 80-year-old men.","volume":"79","author":"Belanger","year":"1994","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R164","first-page":"3561","article-title":"Sexual dimorphism in the influence of advanced aging on adrenal hormone levels: The Rancho Bernardo Study.","volume":"85","author":"Laughlin","year":"2000","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R165","doi-asserted-by":"crossref","first-page":"8167","DOI":"10.1073\/pnas.161278698","article-title":"Dehydroepiandrosterone sulfate and longevity: new clues for an old friend.","volume":"98","author":"Yen","year":"2001","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R166","doi-asserted-by":"crossref","first-page":"3147","DOI":"10.1210\/jcem.81.9.8784058","article-title":"Dehydroepiandrosterone (DHEA): a fountain of youth?","volume":"81","author":"Baulieu","year":"1996","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R167","first-page":"589","article-title":"Regulation of estrogen activity by sulfation in human MCF-7 breast cancer cells.","volume":"9","author":"Falany","year":"1997","journal-title":"Oncol Res"},{"key":"2019041121493060600_R168","first-page":"555","article-title":"Expression of estrogen sulfotransferase in MCF-7 cells by cDNA transfection suppresses the estrogen response: potential role of the enzyme in regulating estrogen-dependent growth of breast epithelial cells.","volume":"286","author":"Qian","year":"1998","journal-title":"J Pharmacol Exp Ther"},{"key":"2019041121493060600_R169","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1042\/bst0270323","article-title":"Regulation of steroid sulphatase and oestradiol 17\u03b2-hydroxysteroid dehydrogenase in breast cancer.","volume":"27","author":"Purohit","year":"1999","journal-title":"Biochem Soc Trans"},{"key":"2019041121493060600_R170","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0960-0760(99)00023-0","article-title":"The regulation of oestrone sulphate formation in breast cancer cells.","volume":"68","author":"Purohit","year":"1999","journal-title":"J Steroid Biochem Mol Biol"},{"key":"2019041121493060600_R171","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/S0960-0760(00)00077-7","article-title":"Stimulation of MCF-7 breast cancer cell proliferation by estrone sulfate and dehydroepiandrosterone sulfate: inhibition by novel non-steroidal steroid sulfatase inhibitors.","volume":"73","author":"Billich","year":"2000","journal-title":"J Steroid Biochem Mol Biol"},{"key":"2019041121493060600_R172","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/S0009-2797(97)00138-5","article-title":"Inhibition of androgen action by dehydroepiandrosterone sulfotransferase transfected in PC-3 prostate cancer cells.","volume":"109","author":"Chan","year":"1998","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R173","doi-asserted-by":"crossref","first-page":"1897","DOI":"10.1210\/endo.141.5.7530","article-title":"Potent inhibition of estrogen sulfotransferase by hydroxylated PCB metabolites: a novel pathway explaining the estrogenic activity of PCBs.","volume":"141","author":"Kester","year":"2000","journal-title":"Endocrinology"},{"key":"2019041121493060600_R174","doi-asserted-by":"crossref","first-page":"1142","DOI":"10.1210\/jcem.87.3.8311","article-title":"Potent inhibition of estrogen sulfotransferase by hydroxylated metabolites of polyhalogenated aromatic hydrocarbons reveals alternative mechanism for estrogenic activity of endocrine disrupters.","volume":"87","author":"Kester","year":"2002","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R175","author":"Qian"},{"key":"2019041121493060600_R176","doi-asserted-by":"crossref","first-page":"5342","DOI":"10.1210\/endo.142.12.8540","article-title":"Targeted disruption of the mouse estrogen sulfotransferase gene reveals a role of estrogen metabolism in intracrine and paracrine estrogen regulation.","volume":"142","author":"Qian","year":"2001","journal-title":"Endocrinology"},{"key":"2019041121493060600_R177","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1089\/105072501300176363","article-title":"Update on intrathyroidal iodine metabolism.","volume":"11","author":"Dunn","year":"2001","journal-title":"Thyroid"},{"key":"2019041121493060600_R178","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1006\/bbrc.1999.1173","article-title":"Sulfated tyrosines of thyroglobulin are involved in thyroid hormone synthesis.","volume":"262","author":"Nlend","year":"1999","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R179","first-page":"10","article-title":"Pathways of thyroid hormone metabolism.","volume":"23","author":"Visser","year":"1996","journal-title":"Acta Med Austriaca"},{"key":"2019041121493060600_R180","doi-asserted-by":"crossref","first-page":"7089","DOI":"10.1073\/pnas.77.12.7089","article-title":"Oligosaccharide moieties of glycoprotein hormones: bovine lutropin resists enzymatic deglycosylation because of terminal O-sulfated N-acetylhexosamines.","volume":"77","author":"Parsons","year":"1980","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R181","doi-asserted-by":"crossref","first-page":"15631","DOI":"10.1016\/S0021-9258(17)36305-6","article-title":"Cell-free sulfation of human and bovine pituitary hormones.","volume":"260","author":"Green","year":"1985","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R182","first-page":"1","author":"Dunn","year":"1985"},{"key":"2019041121493060600_R183","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.1210\/endo-97-6-1432","article-title":"Site of iodination in the rat thyroid gland deduced from electron microscopic autoradiograph.","volume":"97","author":"Ekholm","year":"1975","journal-title":"Endocrinology"},{"key":"2019041121493060600_R184","doi-asserted-by":"crossref","first-page":"1271","DOI":"10.1016\/S0021-9258(18)96770-0","article-title":"Glycoprotein biosynthesis. Studies on thyroglobulin.","volume":"241","author":"Spiro","year":"1966","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R185","doi-asserted-by":"crossref","first-page":"10304","DOI":"10.1016\/S0021-9258(18)61113-5","article-title":"Characterization or phosphate residues on thyroglobulin.","volume":"262","author":"Consiglio","year":"1987","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R186","first-page":"399","article-title":"Secretion of sulfated thyroglobulin.","volume":"39","author":"Herzog","year":"1986","journal-title":"Eur J Cell Biol"},{"key":"2019041121493060600_R187","doi-asserted-by":"crossref","first-page":"14351","DOI":"10.1016\/S0021-9258(18)68227-4","article-title":"Occurrence of sulfate in the asparagine-linked complex carbohydrate units of thyroglobulin. Identification and localization of galactose 3-sulfate and N-acetylglucosamine 6-sulfate residues in the human and calf proteins.","volume":"263","author":"Spiro","year":"1988","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R188","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1007\/BF00214377","article-title":"Sulfation of thyroglobulin: a ubiquitous modification in vertebrates.","volume":"252","author":"Baumeister","year":"1988","journal-title":"Cell Tissue Res"},{"key":"2019041121493060600_R189","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1530\/eje.0.1410061","article-title":"Thyrotropin regulates tyrosine sulfation of thyroglobulin.","volume":"141","author":"Nlend","year":"1999","journal-title":"Eur J Endocrinol"},{"key":"2019041121493060600_R190","doi-asserted-by":"crossref","first-page":"13541","DOI":"10.1016\/S0021-9258(18)80031-X","article-title":"Consensus sequences for early iodination and hormonogenesis in human thyroglobulin.","volume":"264","author":"Lamas","year":"1989","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R191","doi-asserted-by":"crossref","first-page":"21700","DOI":"10.1074\/jbc.272.35.21700","article-title":"New consensus features for tyrosine 0-sulfation determined by mutational analysis.","volume":"272","author":"Bundgaard","year":"1997","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R192","first-page":"126","author":"Chopra","year":"1991"},{"key":"2019041121493060600_R193","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1530\/eje.0.1340012","article-title":"Role of sulfate in thyroid hormone sulfation.","volume":"134","author":"Visser","year":"1996","journal-title":"Eur J Endocrinol"},{"key":"2019041121493060600_R194","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1210\/endo-108-2-454","article-title":"Sulfate transfer to thyroid hormones and their analogs by hepatic aryl sulfotransferases.","volume":"108","author":"Sekura","year":"1981","journal-title":"Endocrinology"},{"key":"2019041121493060600_R195","first-page":"189","article-title":"A radioimmunoassay for measurement of 3,5,3\u2032-triiodothyronine sulfate: studies in thyroidal and nonthyroidal diseases, pregnancy, and neonatal life.","volume":"75","author":"Chopra","year":"1992","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R196","first-page":"145","article-title":"A radioimmunoassay for measurement of thyroxine sulfate.","volume":"76","author":"Chopra","year":"1993","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R197","first-page":"1583","article-title":"A study of the serum 3,5,3\u2032-triiodothyronine sulfate concentration in normal and hypothyroid fetuses at various gestational stages.","volume":"76","author":"Santini","year":"1993","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R198","first-page":"1062","article-title":"Studies on the biological activity of triiodothyronine sulfate.","volume":"74","author":"Spauding","year":"1992","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R199","first-page":"688","article-title":"3,5,3\u2032-Triiodothyronine (T3) sulfate: a major metabolite in T3 metabolism in man.","volume":"78","author":"LoPresti","year":"1994","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R200","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1126\/science.6857270","article-title":"Sulfation preceding deiodination of iodothyronines in rat hepatocytes","volume":"221","author":"Otten","year":"1983","journal-title":"Science"},{"key":"2019041121493060600_R201","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/0304-4165(93)90086-N","article-title":"Reduced T3 deiodination by the human hepatoblastoma cell line HepG2 caused by deficient T3 sulfation.","volume":"1157","author":"van Stralen","year":"1993","journal-title":"Biochim Biophys Acta"},{"key":"2019041121493060600_R202","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/1043-2760(90)90055-8","article-title":"The role of sulfation in thyroid hormone metabolism.","volume":"1","author":"Visser","year":"1990","journal-title":"Trends Endocrinol Metab"},{"key":"2019041121493060600_R203","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1210\/endo-129-3-1375","article-title":"Deiodination of iodothyronine sulfamates by type I iodothyronine deiodinase of rat liver.","volume":"129","author":"Rutgers","year":"1991","journal-title":"Endocrinology"},{"key":"2019041121493060600_R204","doi-asserted-by":"crossref","first-page":"3364","DOI":"10.1016\/S0021-9258(18)94075-5","article-title":"Characterization of a thyroid sulfotransferase responsible for the 3-O-sulfation of terminal \u03b2-d-galactosyl residues in N-linked carbohydrate units.","volume":"264","author":"Kato","year":"1989","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R205","doi-asserted-by":"crossref","first-page":"25697","DOI":"10.1074\/jbc.M101558200","article-title":"Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal\u03b21\u00c63 galNac residue in O-glycans.","volume":"276","author":"Seko","year":"2001","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R206","doi-asserted-by":"crossref","first-page":"24388","DOI":"10.1074\/jbc.M103135200","article-title":"Molecular cloning and expression of a novel human \u03b2-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans.","volume":"276","author":"Suzuki","year":"2001","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R207","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1002\/j.1460-2075.1990.tb08077.x","article-title":"Purification and characterization of tyrosylprotein sulfotransferase.","volume":"9","author":"Niehrs","year":"1990","journal-title":"EMBO J"},{"key":"2019041121493060600_R208","doi-asserted-by":"crossref","first-page":"24770","DOI":"10.1074\/jbc.273.38.24770","article-title":"Molecular cloning and expression of human and mouse tryosylprotein sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in Caenorhabditis elegans.","volume":"273","author":"Ouyang","year":"1998","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R209","doi-asserted-by":"crossref","first-page":"1816","DOI":"10.1210\/endo-122-5-1816","article-title":"Triiodothyronine: a substrate for the thermostable and thermolabile forms of human phenol sulfotransferase.","volume":"122","author":"Young","year":"1988","journal-title":"Endocrinology"},{"key":"2019041121493060600_R210","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1089\/thy.1995.5.61","article-title":"Human liver triiodothyronine sulfotransferase: copurification with phenol sulfotransferases.","volume":"5","author":"Anderson","year":"1995","journal-title":"Thyroid"},{"key":"2019041121493060600_R211","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/S0009-2797(97)00139-7","article-title":"Characterization of thyroid hormone sulfotransferases.","volume":"109","author":"Visser","year":"1998","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R212","first-page":"1357","article-title":"Characterization of human iodothyronine sulfotransferases.","volume":"84","author":"Kester","year":"1999","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R213","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1677\/joe.0.1710525","article-title":"Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3\u2032,5-triiodothyronine as the substrate.","volume":"171","author":"Li","year":"2001","journal-title":"J Endocrinol"},{"key":"2019041121493060600_R214","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1093\/oxfordjournals.jbchem.a021846","article-title":"Molecular cloning and characterization of rat ST1B1 and human ST1B2 cDNAs, encoding thyroid hormone sulfoteransferases.","volume":"122","author":"Fujita","year":"1997","journal-title":"J Biochem (Tokyo)"},{"key":"2019041121493060600_R215","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1124\/mol.53.2.274","article-title":"Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver.","volume":"53","author":"Wang","year":"1998","journal-title":"Mol Pharmacol"},{"key":"2019041121493060600_R216","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1006\/bbrc.1999.1419","article-title":"Sulfation of iodothyronines by recombinant human liver steroid sulfotransferases.","volume":"263","author":"Li","year":"1999","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R217","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1210\/jcem.84.7.5975","article-title":"Sulfation of thyroid hormone by estrogen sulfotransferase.","volume":"84","author":"Kester","year":"1999","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R218","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1016\/S0006-2952(00)00475-5","article-title":"Sulfation of iodothyronines by human sulfotransferase 1C1 (SULT1C1).","volume":"60","author":"Li","year":"2000","journal-title":"Biochem Pharmacol"},{"key":"2019041121493060600_R219","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1248\/bpb.22.446","article-title":"Enzymatic characterization of human cytosolic sulfotransferases; identification of ST1B2 as a thyroid hormone sulfotransferase.","volume":"22","author":"Fujita","year":"1999","journal-title":"Biol Pharm Bull"},{"key":"2019041121493060600_R220","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1006\/geno.1997.4683","article-title":"Human sulfotransferase SULT1C1:cDNA cloning, tissue-specific expression and chromosomal localization.","volume":"41","author":"Her","year":"1997","journal-title":"Genomics"},{"key":"2019041121493060600_R221","first-page":"2734","article-title":"Sulfation of thyroid hormone and dopamine during human development: ontogeny of phenol sulfotransferases and arysulfatases in liver, lung, and brain.","volume":"86","author":"Richard","year":"2001","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R222","first-page":"680","article-title":"A new method for the hydrolysis of conjugated catecholamines.","volume":"90","author":"Buu","year":"1977","journal-title":"J Lab Clin Med"},{"key":"2019041121493060600_R223","first-page":"141","article-title":"Conjugation patterns of endogenous plasma catecholamines in human and rat.","volume":"101","author":"Wang","year":"1983","journal-title":"J Lab Clin Med"},{"key":"2019041121493060600_R224","first-page":"2254","article-title":"Role of sulfate conjugation in catecholamines in blood pressure regulation.","volume":"45","author":"Kuchel","year":"1986","journal-title":"Fed Proc"},{"key":"2019041121493060600_R225","doi-asserted-by":"crossref","first-page":"2029","DOI":"10.1016\/0006-2952(84)90569-0","article-title":"Conjugated normetanephrine in human and rat plasma and erythrocytes.","volume":"33","author":"Yoneda","year":"1984","journal-title":"Biochem Pharmacol"},{"key":"2019041121493060600_R226","first-page":"E537","article-title":"Plasma and platelet catecholamine and catecholamine sulfate response to various exercise tests","volume":"267","author":"Strobel","year":"1994","journal-title":"Am. Physiol. Soc."},{"key":"2019041121493060600_R227","doi-asserted-by":"crossref","first-page":"17","DOI":"10.3109\/07435808509035421","article-title":"Circadian variations of free and sulfoconjugated catecholamines in normal subjects.","volume":"11","author":"Kuchel","year":"1985","journal-title":"Endocr Res"},{"key":"2019041121493060600_R228","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1139\/y81-047","article-title":"Platelet phenolsulfotransferase and catecholamines: physiological and pathological variations in humans.","volume":"59","author":"Abenhaim","year":"1981","journal-title":"Can J Physiol Pharmacol"},{"key":"2019041121493060600_R229","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/S0378-4347(00)84516-8","article-title":"Determination of dopamine-3- and 4-O-sulfate in human plasma and urine by anion-exchange high performance liquid chromatography with fluorimetric detection.","volume":"342","author":"Yamamoto","year":"1985","journal-title":"J Chromatog"},{"key":"2019041121493060600_R230","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1016\/0024-3205(94)00333-5","article-title":"The potential of intact human platelets for sulfoconjugation of norepinephrine in vitro.","volume":"55","author":"Mielke","year":"1994","journal-title":"Life Sci"},{"key":"2019041121493060600_R231","first-page":"288","article-title":"Catecholamine sulfates and platlet phenol sulfotransferase activity in essential hypertension.","volume":"104","author":"Kuchel","year":"1984","journal-title":"J Lab Clin Med"},{"key":"2019041121493060600_R232","first-page":"532","article-title":"Human liver and conjugation of catecholamines.","volume":"109","author":"Tyce","year":"1987","journal-title":"J Lab Clin Med"},{"key":"2019041121493060600_R233","first-page":"354","article-title":"Clinical implications of genetic and acquired defects in catecholamine synthesis and metabolism.","volume":"17","author":"Kuchel","year":"1994","journal-title":"Clin Invest Med"},{"key":"2019041121493060600_R234","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1002\/chir.530050807","article-title":"Stereoselective sulfate conjugation of isoproterenol in humans: comparison of hepatic, intestinal, and platelet activity.","volume":"5","author":"Pesola","year":"1993","journal-title":"Chirality"},{"key":"2019041121493060600_R235","first-page":"681","article-title":"Conjugated catechoamines in human plasma: where are they coming from?","volume":"116","author":"Cuche","year":"1990","journal-title":"J Lab Clin Med"},{"key":"2019041121493060600_R236","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1161\/01.HYP.2.2.177","article-title":"Free and conjugated plasma catecholamines in hypertensive patients with and without pheochromocytoma.","volume":"2","author":"Kuchel","year":"1980","journal-title":"Hypertension"},{"key":"2019041121493060600_R237","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1080\/07435808509032980","article-title":"The platelet phenolsulfotransferase is not indispensable for the sulfoconjugation of plasma catecholamines.","volume":"11","author":"Kuchel","year":"1985","journal-title":"Endocr Res"},{"key":"2019041121493060600_R238","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1016\/S0022-2143(96)90045-1","article-title":"Plasma sulfoconjugated dopamine levels are normal in patients with autonomic failure.","volume":"128","author":"Yamamoto","year":"1996","journal-title":"J Lab Clin Med"},{"key":"2019041121493060600_R239","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.3109\/00498259609050256","article-title":"Design, production and characterization of antibodies discriminating between phenol- and monoamine-sulphating forms of human phenol sulphotransferase.","volume":"26","author":"Rubin","year":"1996","journal-title":"Xenobiotica"},{"key":"2019041121493060600_R240","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0009-2797(97)00117-8","article-title":"Biology and function of the reversible sulfation pathway catalyzed by human sulfotransferases and sulfatases.","volume":"109","author":"Coughtrie","year":"1998","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R241","doi-asserted-by":"crossref","first-page":"2523","DOI":"10.1210\/jcem.84.7.5864","article-title":"Sources and physiological significance of plasma dopamine sulfate.","volume":"84","author":"Goldstein","year":"1999","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R242","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1042\/bj3020497","article-title":"Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor- sensitivity studies.","volume":"302","author":"Veronese","year":"1994","journal-title":"Biochem J"},{"key":"2019041121493060600_R243","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1007\/BF00497020","article-title":"Thermolabile and thermostable human platelet phenol sulfotransferase. Substrate specificity and physical separation.","volume":"324","author":"Reiter","year":"1983","journal-title":"Naunyn Schmiedebergs Arch Pharmacol"},{"key":"2019041121493060600_R244","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1016\/0006-2952(87)90108-0","article-title":"Human liver phenol sulfotransferase: assay conditions, biochemical properties and partial purification of isozymes of the thermostable form.","volume":"36","author":"Campbell","year":"1987","journal-title":"Biochem Pharmacol"},{"key":"2019041121493060600_R245","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/1357-2725(95)00164-6","article-title":"cDNA cloning and expression of a new form of human aryl sulfotransferase.","volume":"28","author":"Zhu","year":"1996","journal-title":"Int J Biochem Cell Biol"},{"key":"2019041121493060600_R246","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/S0006-2952(99)00145-8","article-title":"Human phenol sulfotransferases SULT1A2 and SULT1A1: genetic polymorphisms, allozyme properties, and human liver genotype-phenotype correlations.","volume":"58","author":"Raftogianis","year":"1999","journal-title":"Biochem Pharmacol"},{"key":"2019041121493060600_R247","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1006\/geno.1993.1494","article-title":"Mapping of the phenolsulfotransferase gene (STP) to human chromosome 16p12.1\u2013p11.2 and to mouse chromosome 7.","volume":"18","author":"Dooley","year":"1993","journal-title":"Genomics"},{"key":"2019041121493060600_R248","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1006\/geno.1994.1494","article-title":"Thermolabile phenol sulfotranssferase (STM): localization to human chromosome 16p11.2.","volume":"23","author":"Aksoy","year":"1994","journal-title":"Genomics"},{"key":"2019041121493060600_R249","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1006\/bbrc.1994.2810","article-title":"Genetic organization and DNA sequence of the human catecholamine-sulfating phenol sulfotransferase gene (STM).","volume":"205","author":"Dooley","year":"1994","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R250","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1006\/geno.1996.4575","article-title":"Cloning, structural organization, and chromosomal mapping of the human phenol sulfotransferase STP2 gene.","volume":"40","author":"Gaedigk","year":"1997","journal-title":"Genomics"},{"key":"2019041121493060600_R251","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1006\/bbrc.1993.2018","article-title":"Identification of two human brain aryl sulfotransferase cDNAs.","volume":"195","author":"Zhu","year":"1993","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R252","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1006\/bbrc.1994.1159","article-title":"Human liver thermolabile phenol sulfotransferase cDNA cloning, expression and characterization.","volume":"198","author":"Wood","year":"1994","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R253","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1006\/bbrc.1995.1414","article-title":"Human platelet phenol sulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form.","volume":"208","author":"Jones","year":"1995","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R254","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/S0009-2797(97)00144-0","article-title":"Localization of aryl sulfotransferase expression in human tissues using hybridization histochemistry and immunohistochemistry.","volume":"109","author":"Windmill","year":"1998","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R255","first-page":"755","article-title":"Effect of intravenous dopamine infusion on plasma concentrations of dopamine and dopamine sulfate in men, during and up to 18 h after infusion.","volume":"55","author":"Onasch","year":"2000","journal-title":"Eur J Pharmacol"},{"key":"2019041121493060600_R256","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1097\/00005344-198511000-00030","article-title":"Adrenergic and dopaminergic properties of dopamine sulfoconjugates.","volume":"7","author":"Kyncl","year":"1985","journal-title":"J Cardiovasc Pharmacol"},{"key":"2019041121493060600_R257","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/0014-2999(87)90531-0","article-title":"Sulfoconjugatd catecholamines: lack of \u03b2-adrenoceptor binding and adenylate cyclase stimulation in human mononuclear leukocytes.","volume":"143","author":"Michel","year":"1987","journal-title":"Eur J Pharmacol"},{"key":"2019041121493060600_R258","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1007\/BF00168808","article-title":"3- and 4-O-Sulfoconjugated and methylated dopamine: highly reduced binding affinity to dopamine D2 receptors in rat striated membranes.","volume":"338","author":"Werle","year":"1988","journal-title":"Naunyn Schmiedeberg\u2019s Arch Pharmacol"},{"key":"2019041121493060600_R259","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1139\/y91-141","article-title":"O-Methylated and sulfoconjugated catecholamines: differential activities at human platelet \u03b12-adrenoceptors.","volume":"69","author":"Lenz","year":"1991","journal-title":"Can J Physiol Pharmacol"},{"key":"2019041121493060600_R260","first-page":"E431","article-title":"Dopamine-3-sulfate inhibits aldosterone secretion in cultured bovine adrenal cells","volume":"247","author":"Racz","year":"1982","journal-title":"Am J Physiol"},{"key":"2019041121493060600_R261","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/0024-3205(96)00301-3","article-title":"Physiological significance of plasma sulfoconjugated dopamine in patients with hypertension-clinical and experimental studies.","volume":"59","author":"Yoshizumi","year":"1996","journal-title":"Life Sci"},{"key":"2019041121493060600_R262","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1248\/bpb.22.657","article-title":"Plasma levels of free and sulfoconjugated catecholamines in patients with ahterosclerosis.","volume":"22","author":"Ozawa","year":"1999","journal-title":"Biol Pharm Bull"},{"key":"2019041121493060600_R263","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1093\/genetics\/122.4.905","article-title":"Genetic polymorphism for human platelet themostable phenol sulfotransferase (TS PST) activity.","volume":"122","author":"Price","year":"1989","journal-title":"Genetics"},{"key":"2019041121493060600_R264","doi-asserted-by":"crossref","first-page":"S135","DOI":"10.1097\/00008571-199512001-00015","article-title":"Primary structures and properties of two related forms of aryl sulfotransferases in human liver","volume":"5","author":"Ozawa","year":"1995","journal-title":"Pharmacogenetics"},{"key":"2019041121493060600_R265","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1006\/bbrc.1997.7466","article-title":"Phenol sulfotransferase pharmacogenetics in humans: association of common SULT1A1 alleles with TS PST phenotype.","volume":"239","author":"Raftogianis","year":"1997","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R266","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/S0009-2797(97)00135-X","article-title":"Genetic polymorphisms in human liver phenol sulfotransferases involved in the bioactivation of N-hydroxy derivatives of carcinogenic arylamines and herterocyclic amines.","volume":"109","author":"Ozawa","year":"1998","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R267","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1042\/bj3370045","article-title":"Phenol sulphotransferase SULT1A1 polymorphism: molecular diagnosis and allele frequencies in Caucasian and African populations.","volume":"337","author":"Coughtrie","year":"1999","journal-title":"Biochem J"},{"key":"2019041121493060600_R268","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1097\/00008571-200102000-00007","article-title":"Sulfation pharamacogenetics: SULT1A1 and SULT1A2 allele frequencies in Caucasian, Chinese and African-American subjects.","volume":"11","author":"Carlini","year":"2001","journal-title":"Pharmacogenetics"},{"key":"2019041121493060600_R269","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1007\/s100380170093","article-title":"Catalog of 320 single nucleotide polymorphisms (SNPs) in 20 quinone oxidoreductase and sulfotransferase genes.","volume":"46","author":"Iida","year":"2001","journal-title":"J Hum Genet"},{"key":"2019041121493060600_R270","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0009-2797(97)00118-X","article-title":"Cloning of the human phenol sulfotransferase gene family: three genes implicated in the metabolism of catecholamines, thyroid hormones and drugs.","volume":"109","author":"Dooley","year":"1998","journal-title":"Chem Biol Interact"},{"key":"2019041121493060600_R271","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1016\/S0021-9258(17)35234-1","article-title":"Sulfationof Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor.","volume":"266","author":"Leyte","year":"1991","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R272","doi-asserted-by":"crossref","first-page":"3315","DOI":"10.1021\/bi00128a003","article-title":"identification and functional importance of tyrosine sulfate residues within recombinant factor VIII.","volume":"31","author":"Pittman","year":"1992","journal-title":"Biochemistry (Mosc)"},{"key":"2019041121493060600_R273","doi-asserted-by":"crossref","first-page":"22677","DOI":"10.1074\/jbc.270.39.22677","article-title":"Tyrosine sulfation of P-selectin gycoprotein ligand-1 is required for high affinity binding to P-selectin.","volume":"270","author":"Wilkins","year":"1995","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R274","doi-asserted-by":"crossref","first-page":"13946","DOI":"10.1021\/bi00250a050","article-title":"Tyrosine sulfation of the glycoprotein Ib-IX complex: identification of the sulfated residues and effect on ligand binding.","volume":"33","author":"Dong","year":"1994","journal-title":"Biochemistry (Mosc)"},{"key":"2019041121493060600_R275","doi-asserted-by":"crossref","first-page":"4929","DOI":"10.1021\/bi952456c","article-title":"Mocarhagin, a novel cobra venom mettaloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ib\u03b1. Identification of the sulfated tyrosine\/anionic sequence Tyr-276-Glu-282 of the glycoprotein Ib\u03b1 as a binding site for von Willebrand factor and \u03b1-thrombin.","volume":"35","author":"Ward","year":"1996","journal-title":"Biochemistry (Mosc)"},{"key":"2019041121493060600_R276","doi-asserted-by":"crossref","first-page":"16690","DOI":"10.1074\/jbc.M101035200","article-title":"Tyrosine sulfation of glycoprotein Ib\u03b1.","volume":"276","author":"Dong","year":"2001","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R277","doi-asserted-by":"crossref","first-page":"1786","DOI":"10.1016\/S0021-9258(17)36009-X","article-title":"Identification of the site of sulfation of the fourth component of human complement.","volume":"261","author":"Hortin","year":"1986","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R278","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.1073\/pnas.86.4.1338","article-title":"Sulfation of tyrosine residues increases activity of the fourth component of complement.","volume":"86","author":"Hortin","year":"1989","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R279","doi-asserted-by":"crossref","first-page":"20095","DOI":"10.1016\/S0021-9258(17)32132-4","article-title":"Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage.","volume":"269","author":"Michnick","year":"1994","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R280","doi-asserted-by":"crossref","first-page":"1446","DOI":"10.1016\/S0006-291X(87)80294-2","article-title":"Sulfation of the choriogonadotropin \u03b1-subunit in human placental extracts.","volume":"148","author":"Bielinska","year":"1987","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R281","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1021\/jm00218a011","article-title":"Cholecystokinin (pancreozymin). 3. Synthesis and properties of an analogue of the C-terminal heptapeptide with serine sulfate replacing tyrosine sulfate.","volume":"20","author":"Bodanszky","year":"1977","journal-title":"J Med Chem"},{"key":"2019041121493060600_R282","doi-asserted-by":"crossref","first-page":"565","DOI":"10.3109\/00365528309181639","article-title":"Variations in the sulfation of circulating gastrins in gastrointestinal diseases.","volume":"18","author":"Andersen","year":"1983","journal-title":"Scand J Gastroenterol"},{"key":"2019041121493060600_R283","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/S0021-9258(19)57352-5","article-title":"Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin. II. Distribution of sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones.","volume":"263","author":"Green","year":"1988","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R284","author":"Baenziger","year":"1988"},{"key":"2019041121493060600_R285","doi-asserted-by":"crossref","first-page":"21665","DOI":"10.1074\/jbc.270.37.21665","article-title":"Evolutionary conservation of the sulfated oligosaccharides on vertebrate glycoprotein hormones that control circulatory half-life.","volume":"270","author":"Manzella","year":"1995","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R286","doi-asserted-by":"crossref","first-page":"12998","DOI":"10.1016\/S0021-9258(18)42373-3","article-title":"Pro-opiomelanocortin synthesized by corticotrophs bears asparagine-linked oligosaccharides terminating with SO4-4GalNAc\u03b21, 4GlcNAc\u03b21,2Man\u03b1.","volume":"267","author":"Skelton","year":"1992","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R287","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/S0065-230X(08)60403-0","article-title":"The tumor biology of gastrin and cholecystokinin.","volume":"63","author":"Rehfeld","year":"1994","journal-title":"Adv Cancer Res"},{"key":"2019041121493060600_R288","first-page":"251","article-title":"The predominant cholecystokinin in human plasma and intestine is cholecystokinin-33.","volume":"86","author":"Rehfeld","year":"2001","journal-title":"J Clin Endocrinol Metab"},{"key":"2019041121493060600_R289","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1471-4159.1985.tb07105.x","article-title":"Neuronal cholecystokinin: one or multiple transmitters?","volume":"44","author":"Rehfeld","year":"1985","journal-title":"J Neurochem"},{"key":"2019041121493060600_R290","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1111\/j.1432-1033.1968.tb00433.x","article-title":"Structure of porcine cholecystokinin- pancreozymin. Cleavage with thrombin and with trypsin.","volume":"6","author":"Mutt","year":"1968","journal-title":"Eur J Biochem"},{"key":"2019041121493060600_R291","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1146\/annurev.physiol.59.1.221","article-title":"Cholecystokinin cells","volume":"59","author":"Liddle","year":"1997","journal-title":"Annu Rev Physiol"},{"key":"2019041121493060600_R292","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1006\/frne.1997.0163","article-title":"Phylogeny of the cholecystokinin\/gastrin family.","volume":"19","author":"Johnsen","year":"1998","journal-title":"Front Neuroendocrinol"},{"key":"2019041121493060600_R293","doi-asserted-by":"crossref","first-page":"1931","DOI":"10.1073\/pnas.82.7.1931","article-title":"Molecular cloning of the human cholecystokinin gene by use of a synthetic probe containing deoxyinosine.","volume":"82","author":"Takahashi","year":"1985","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R294","first-page":"353","article-title":"Structure of human cholecystokinin gene and its chromosomal location.","volume":"1986","author":"Takahashi","year":"1986","journal-title":"Gene"},{"key":"2019041121493060600_R295","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1007\/978-3-540-49421-8_13","article-title":"The cholecystokinin-gastrin family of peptides and their receptors.","volume":"26","author":"Rehfeld","year":"1999","journal-title":"Results Probl Cell Differ"},{"key":"2019041121493060600_R296","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.ph.50.030188.002001","article-title":"Peptide \u03b1-amidation.","volume":"50","author":"Eipper","year":"1988","journal-title":"Annu Rev Physiol"},{"key":"2019041121493060600_R297","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/S0303-7207(96)03903-2","article-title":"Where does amidation take place?","volume":"123","author":"Martinez","year":"1996","journal-title":"Mol Cell Endocrinol"},{"key":"2019041121493060600_R298","doi-asserted-by":"crossref","first-page":"107","DOI":"10.2220\/biomedres.3.107","article-title":"Cholecystokinin: a hormone and neurotransmitter.","volume":"3","author":"Williams","year":"1982","journal-title":"Biomed Res"},{"key":"2019041121493060600_R299","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1111\/j.1432-1033.1993.tb18061.x","article-title":"The peripheral cholecystokinin receptors.","volume":"215","author":"Silvente-Poirot","year":"1993","journal-title":"Eur J Biochem"},{"key":"2019041121493060600_R300","first-page":"G628","article-title":"Cholecystokinin receptors","volume":"269","author":"Wank","year":"1995","journal-title":"Am J Physiol"},{"key":"2019041121493060600_R301","doi-asserted-by":"crossref","first-page":"5554","DOI":"10.1016\/S0021-9258(19)83812-7","article-title":"Interactions of COOH-terminal fragments of cholecystokinin with receptors on dispersed acini from guinea pig pancreas.","volume":"257","author":"Jensen","year":"1982","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R302","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1006\/bbrc.1993.1610","article-title":"Molecular cloning and functional expression of the human gallbladder cholecystokinin A receptor","volume":"193","author":"Ulrich","year":"1993","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R303","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1006\/bbrc.1993.1894","article-title":"Molecular cloning, functional expression and chromosomal localization of the human cholecystokinin type A receptor.","volume":"194","author":"de Weerth","year":"1993","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R304","doi-asserted-by":"crossref","first-page":"3125","DOI":"10.1073\/pnas.89.7.3125","article-title":"Purification, molecular cloning, and functional expression of the cholecystokinin receptor from rat pancreas.","volume":"89","author":"Wank","year":"1992","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R305","doi-asserted-by":"crossref","first-page":"14380","DOI":"10.1074\/jbc.273.23.14380","article-title":"Met-95 of the cholecystokinin-A receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state.","volume":"273","author":"Gigoux","year":"1998","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R306","doi-asserted-by":"crossref","first-page":"2347","DOI":"10.1110\/ps.8.11.2347","article-title":"Arginine 197 of the cholecystokinin-A receptor binding site interacts with the sulfate of the peptide agonist cholecystokinin.","volume":"8","author":"Gigoux","year":"1999","journal-title":"Protein Sci"},{"key":"2019041121493060600_R307","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1016\/0165-6147(89)90192-2","article-title":"Interaction of CCK with pancreatic acinar cells.","volume":"10","author":"Jensen","year":"1989","journal-title":"Trends Pharmacol Sci"},{"issue":"Suppl 1","key":"2019041121493060600_R308","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1159\/000200509","article-title":"Role of gastrin as a trophic hormone","volume":"47","author":"Walsh","year":"1990","journal-title":"Digestion"},{"key":"2019041121493060600_R309","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1136\/gut.5.2.103","article-title":"The consitution and properties of two gastrins extracted from hog antral mucosa. Part I. The isolation of two gastrins from hog antral mucosa.","volume":"5","author":"Gregory","year":"1964","journal-title":"Gut"},{"key":"2019041121493060600_R310","first-page":"931","article-title":"The antral hormone gastrin","volume":"204","author":"Gregory","year":"1964","journal-title":"Structure of gastrin. Nature"},{"key":"2019041121493060600_R311","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/S0016-5085(19)34287-8","article-title":"Memorial lecture: the isolation and chemistry of gastrin.","volume":"51","author":"Gregory","year":"1966","journal-title":"Gastroenterology"},{"key":"2019041121493060600_R312","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1002\/j.1460-2075.1995.tb07013.x","article-title":"Post-poly(Glu) cleavage and degradation modified by O-sulfated tyrosine: a novel post-translational processing mechanism.","volume":"14","author":"Rehfeld","year":"1995","journal-title":"EMBO J"},{"key":"2019041121493060600_R313","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/978-1-4684-7248-6_9","article-title":"The gastrins: structure and heterogeneity.","volume":"106","author":"Gregory","year":"1978","journal-title":"Adv Exp Med Biol"},{"key":"2019041121493060600_R314","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/0016-6480(85)90134-0","article-title":"Species variation in the tyrosine sulfation of mammalian gastrins.","volume":"58","author":"Andersen","year":"1985","journal-title":"Gen Comp Endocrinol"},{"key":"2019041121493060600_R315","doi-asserted-by":"crossref","first-page":"2866","DOI":"10.1073\/pnas.80.10.2866","article-title":"Molecular cloning of human gastrin cDNA: evidence for evoution of gastrin by gene duplication.","volume":"80","author":"Boel","year":"1983","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R316","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/0378-1119(83)90035-5","article-title":"Molecular cloning of human gastrin precursor cDNA.","volume":"26","author":"Kato","year":"1983","journal-title":"Gene"},{"key":"2019041121493060600_R317","doi-asserted-by":"crossref","first-page":"8197","DOI":"10.1093\/nar\/11.23.8197","article-title":"Molecular cloning of the human gastrin gene.","volume":"11","author":"Kato","year":"1983","journal-title":"Nucleic Acids Res"},{"key":"2019041121493060600_R318","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1073\/pnas.81.4.1067","article-title":"Structure of a human gastrin gene.","volume":"81","author":"Wiborg","year":"1984","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R319","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/0006-291X(92)91557-7","article-title":"Molecular cloning of the human brain and gastric cholecystokinin receptor: structure, functional expression and chromosomal localization.","volume":"189","author":"Pisegna","year":"1992","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R320","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1126\/science.6246582","article-title":"Cholecystokinin receptors in the brain: characterization and distribution.","volume":"208","author":"Saito","year":"1980","journal-title":"Science"},{"key":"2019041121493060600_R321","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1007\/BF01927609","article-title":"Effect of sulfated anda non-sulfated gastrin and octapeptide-cholecystokinin on cat gall bladder in vitro.","volume":"32","author":"Chowdhury","year":"1976","journal-title":"Experientia"},{"key":"2019041121493060600_R322","first-page":"E186","article-title":"Secretory effects of gastrins on isolated perfused procine pancreas","volume":"238","author":"Jensen","year":"1980","journal-title":"Am J Physiol"},{"key":"2019041121493060600_R323","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/0196-9781(89)90114-9","article-title":"Importance of sulfation of gastrin or cholecystokinin (CCK) on affinity for gastrin and CCK recptors.","volume":"10","author":"Huang","year":"1989","journal-title":"Peptides"},{"key":"2019041121493060600_R324","doi-asserted-by":"crossref","first-page":"739","DOI":"10.3109\/00365529008997601","article-title":"Does sulfation of gastrin influence gastric acid secretion in man?","volume":"25","author":"Cantor","year":"1990","journal-title":"Scand J Gastroenterol"},{"key":"2019041121493060600_R325","doi-asserted-by":"crossref","first-page":"1220","DOI":"10.1016\/S0016-5085(87)91081-X","article-title":"Comparison of the metabolism of sulfated and unsulfated heptadecapeptide gastrin in humans.","volume":"92","author":"Pauwels","year":"1987","journal-title":"Gastroenterology"},{"key":"2019041121493060600_R326","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1038\/295519a0","article-title":"O-Sulphated leu-enkephalin in brain.","volume":"295","author":"Unsworth","year":"1982","journal-title":"Nature"},{"key":"2019041121493060600_R327","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1254\/jjp.52.493","article-title":"Pharmacological activity of angiotensin-II modified by tyrosine sulfation.","volume":"52","author":"Hagiwara","year":"1990","journal-title":"Jpn J Pharmacol"},{"key":"2019041121493060600_R328","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0303-7207(97)00211-6","article-title":"Intracellular transport, sorting, and proteolytic processing of regulated secretory proteins does not require protein sulfation.","volume":"136","author":"van Kuppeveld","year":"1997","journal-title":"Mol Cell Endocrinol"},{"key":"2019041121493060600_R329","doi-asserted-by":"crossref","first-page":"7468","DOI":"10.1073\/pnas.78.12.7468","article-title":"Metabolic labeling of lutropin with [35S]sulfate.","volume":"78","author":"Hortin","year":"1981","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R330","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/0303-7207(86)90104-8","article-title":"Sulfated LH subunits and a tyrosine-sulfated secretory protein (secretogranin II) in female rat adenohypophyses: changes with age and stimulation of release by LHRH.","volume":"44","author":"Cozzi","year":"1986","journal-title":"Mol Cell Endocrinol"},{"key":"2019041121493060600_R331","doi-asserted-by":"crossref","first-page":"15623","DOI":"10.1016\/S0021-9258(17)36304-4","article-title":"Structural elucidation of the disulfated oligosaccharide from bovine lutropin.","volume":"260","author":"Green","year":"1985","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R332","doi-asserted-by":"crossref","first-page":"16309","DOI":"10.1016\/S0021-9258(18)66567-6","article-title":"Biosynthesis of sulfated asparagine-linked oligosaccharides on bovine lutropin.","volume":"261","author":"Green","year":"1986","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R333","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/S0021-9258(19)57351-3","article-title":"Asparagine-linked oligosaccharides on lutropin, follitropin, and thyrotropin. I. Structural elucidation of the sulfated and sialylated oligosaccharides on bovine, ovine, and human pituitary glycoprotein hormones.","volume":"263","author":"Green","year":"1988","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R334","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1007\/BF00230637","article-title":"Differential processing of Asn-linked oligosaccharides on pituitary glycoprotein hormones: implication fo biologic function.","volume":"72","author":"Green","year":"1986","journal-title":"Mol Cell Biochem"},{"key":"2019041121493060600_R335","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1073\/pnas.89.1.334","article-title":"Circulatory half-life but not interaction with the lutropin\/chorionic gonadotropin receptor is modulated by sulfation of bovine lutropin oligosaccharies.","volume":"89","author":"Baenziger","year":"1992","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R336","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1016\/0092-8674(91)90287-9","article-title":"A hepatic reticuloendothelial cell receptor specifric for SO4-4GalNAc\u03b21, 4GlcNAc\u03b21,2Man\u03b1that mediates rapid clearance of lutropin.","volume":"67","author":"Fiete","year":"1991","journal-title":"Cell"},{"key":"2019041121493060600_R337","doi-asserted-by":"crossref","first-page":"1490","DOI":"10.1210\/endo.133.4.8404588","article-title":"Purification and characterization of recombinant human thryrotropin (TSH) isoforms produced by Chinese hamster ovary cells: the role of sialylation and sulfation in TSH bioactivity.","volume":"133","author":"Szkudlinski","year":"1993","journal-title":"Endocrinology"},{"key":"2019041121493060600_R338","doi-asserted-by":"crossref","first-page":"3325","DOI":"10.1210\/endo.136.8.7628367","article-title":"Asparagine-linked oligosaccharide structures determine clearance and oragan distribution of pituitary and recombinant thyrotropin.","volume":"136","author":"Szkudlinski","year":"1995","journal-title":"Endocrinology"},{"key":"2019041121493060600_R339","doi-asserted-by":"crossref","first-page":"29378","DOI":"10.1074\/jbc.270.49.29378","article-title":"Expression of human thyrotropin in cell lines with different glycosylation patterns combined with mutagenesis of specific glycosylation sites. Characterization of a novel role for the oligosaccharides in the in vitro and in vivo bioactivity.","volume":"270","author":"Grossmann","year":"1995","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R340","doi-asserted-by":"crossref","first-page":"9062","DOI":"10.1073\/pnas.92.20.9062","article-title":"Subunit-specific functions of N-linked oligosaccharides in human thyrotropin: role of terminal residues of \u03b1- and \u03b2-subunit oligosaccharides in metabolic clearance and bioactivity.","volume":"92","author":"Szkudlinski","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R341","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1055\/s-2007-979933","article-title":"Effects of continuous, pulsatile and bolus administration of pitutitary rat thyrotropin and recombinant human thyrotropin in a chronically cannulated rat.","volume":"27","author":"Leitolf","year":"1995","journal-title":"Horm Metab Res"},{"key":"2019041121493060600_R342","doi-asserted-by":"crossref","first-page":"3014","DOI":"10.1073\/pnas.74.7.3014","article-title":"Common precursor to corticotropins and endorphins.","volume":"74","author":"Mains","year":"1977","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R343","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1139\/o86-166","article-title":"Posttranslational modifications of proopiomelanocortin in rat intermediate lobe cells.","volume":"64","author":"Bourbonnais","year":"1986","journal-title":"Biochem Cell Biol"},{"key":"2019041121493060600_R344","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1093\/glycob\/3.3.225","article-title":"The Lewis \u00d7 epitope is a major non-reducing structure in the sulphated N-glycans attached to Asn-65 of bovine pro-opiomelanocortin.","volume":"3","author":"Siciliano","year":"1993","journal-title":"Glycobiology"},{"key":"2019041121493060600_R345","doi-asserted-by":"crossref","first-page":"14629","DOI":"10.1074\/jbc.272.23.14629","article-title":"Isolation of the SO4-4-GalNAc\u03b21, 4GlcNAc\u03b21,2Man\u03b1-specific receptor from rat liver.","volume":"272","author":"Fiete","year":"1997","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R346","doi-asserted-by":"crossref","first-page":"17052","DOI":"10.1074\/jbc.M101027200","article-title":"The manose\/N-acetylgalactosamine-4-SO4 receptor displays greater specificity for multivalent than monovalent ligands.","volume":"276","author":"Roseman","year":"2001","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R347","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1146\/annurev.bi.50.070181.002341","article-title":"Glycoprotein hormones: structure and function.","volume":"50","author":"Pierce","year":"1981","journal-title":"Annu Rev Biochem"},{"key":"2019041121493060600_R348","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1146\/annurev.bi.54.070185.003215","article-title":"Assembly of asparagine-linked oligosaccharides.","volume":"54","author":"Kornfeld","year":"1985","journal-title":"Annu Rev Biochem"},{"key":"2019041121493060600_R349","doi-asserted-by":"crossref","first-page":"17142","DOI":"10.1016\/S0021-9258(19)47351-1","article-title":"Characteriztion of a sulfotransferase responsible for the 4-O-sulfation of terminal \u03b2-N-acetyl-d-galactosamine of asparagine-linked oligosaccharides of glycoprotein hormones.","volume":"266","author":"Skelton","year":"1991","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R350","doi-asserted-by":"crossref","first-page":"11127","DOI":"10.1073\/pnas.90.23.11127","article-title":"Estrogen modulates expresion of the gycosyltransferases that synthsize sulfated oligosaccharides on lutropin.","volume":"90","author":"Dharmesh","year":"1993","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R351","doi-asserted-by":"crossref","first-page":"38402","DOI":"10.1074\/jbc.M007821200","article-title":"Molecular cloning and expression of the pituitary glycoprotein hormone N-acetylgalactosamine-4-O-sulfotransferase.","volume":"275","author":"Xia","year":"2000","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R352","doi-asserted-by":"crossref","first-page":"40605","DOI":"10.1074\/jbc.M007983200","article-title":"Molecular cloning and characterization of GalNAc 4-sulfotransferase expressed in human pitutitary gland.","volume":"275","author":"Okuda","year":"2000","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R353","doi-asserted-by":"crossref","first-page":"10861","DOI":"10.1074\/jbc.M011560200","article-title":"Molecular cloning and expression of an N-acetylgalactosamine-4-O-sulfotransferase that transfers sulfate to terminal and non- terminal \u03b21,4-linked N-acetylgalactosamine.","volume":"276","author":"Kang","year":"2001","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R354","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1093\/oxfordjournals.jbchem.a022590","article-title":"Essential roles of carbohydrate signals in development, immune response and tissue functions, as revealed by gene targeting.","volume":"127","author":"Muramatsu","year":"2000","journal-title":"J Biochem"},{"key":"2019041121493060600_R355","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1007\/s000180050031","article-title":"Cell surface heparan sulfate proteoglycans and lipoprotein metabolism","volume":"56","author":"Kolset","year":"1999","journal-title":"Cell Mol Life Sci"},{"key":"2019041121493060600_R356","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1089\/thy.2000.10.551","article-title":"Binding of rat thyroglobulin to heparan sulfate proteoglycans.","volume":"10","author":"Marino","year":"2000","journal-title":"Thyroid"},{"key":"2019041121493060600_R357","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1007\/BF00437470","article-title":"Involvement of heparan sulfate and related molecules in sequestration and growth promoting activity of fibroblast growth factor.","volume":"15","author":"Vlodavsky","year":"1996","journal-title":"Cancer Metastasis Rev"},{"key":"2019041121493060600_R358","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/S0092-8674(00)80051-3","article-title":"Structural basis for FGF receptor dimerization and activation.","volume":"98","author":"Plotnikov","year":"1999","journal-title":"Cell"},{"key":"2019041121493060600_R359","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1006\/excr.2000.5126","article-title":"Testosterone-induced growth of S115 mouse mammary tumor cells is dependent on heparan sulfate.","volume":"264","author":"Borgenstrom","year":"2001","journal-title":"Exp Cell Res"},{"key":"2019041121493060600_R360","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/0092-8674(90)90801-K","article-title":"Signal transduction by receptors with tyrosine kinase activity.","volume":"61","author":"Ullrich","year":"1990","journal-title":"Cell"},{"key":"2019041121493060600_R361","doi-asserted-by":"crossref","first-page":"16868","DOI":"10.1074\/jbc.M011226200","article-title":"Binding of heparin\/heparan sulfate to fibroblast growth factor receptor 4.","volume":"276","author":"Loo","year":"2001","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R362","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1146\/annurev.bi.58.070189.003043","article-title":"The heparin-binding (fibroblast) growth factor family of proteins.","volume":"58","author":"Burgess","year":"1989","journal-title":"Annu Rev Biochem"},{"key":"2019041121493060600_R363","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/S0065-230X(08)60305-X","article-title":"The FGF family of growth factors and oncogenes.","volume":"59","author":"Basillico","year":"1992","journal-title":"Adv Cancer Res"},{"key":"2019041121493060600_R364","first-page":"1","article-title":"Structural and functional diversity in the FGF receptor multigene family.","volume":"60","author":"Johnson","year":"1993","journal-title":"Adv Cancer Res"},{"key":"2019041121493060600_R365","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj3270001","article-title":"Syndecans: multifunctional cell-surface co-receptors.","volume":"327","author":"Carey","year":"1997","journal-title":"Biochem J"},{"key":"2019041121493060600_R366","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/1074-5521(95)90025-X","article-title":"In the clutches of proteoglycans: how does heparan sulfate regulate FGF binding?","volume":"2","author":"Rapraeger","year":"1995","journal-title":"Chem Biol"},{"key":"2019041121493060600_R367","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1146\/annurev.cb.08.110192.002053","article-title":"Biology of the syndecans: a family of transmembrane heparan sulfate proteoglycans.","volume":"8","author":"Bernfield","year":"1992","journal-title":"Annu Rev Cell Biol"},{"key":"2019041121493060600_R368","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1146\/annurev.bi.60.070191.002303","article-title":"Proteoglycans: structures and interactions.","volume":"60","author":"Kjellen","year":"1991","journal-title":"Annu Rev Biochem"},{"key":"2019041121493060600_R369","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1093\/embo-reports\/kvd045","article-title":"The EXT1\/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis.","volume":"1","author":"Senay","year":"2000","journal-title":"EMBO Rep"},{"key":"2019041121493060600_R370","doi-asserted-by":"crossref","first-page":"3885","DOI":"10.1073\/pnas.90.9.3885","article-title":"A single protein catalyzes both N-deacetylation and N-sulfation during the biosynthesis of heparan sulfate.","volume":"90","author":"Wei","year":"1993","journal-title":"Proc Natl Acad Sci USA"},{"key":"2019041121493060600_R371","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/0888-7543(95)80206-2","article-title":"Cloning of the human heparan sulfate-N-deacetylase\/N-sulfotransferase gene from the Treacher Collins syndrome candidate region at 5q32\u2013q33.1.","volume":"26","author":"Dixon","year":"1995","journal-title":"Genomics"},{"key":"2019041121493060600_R372","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1042\/bj3320303","article-title":"cDNA cloning, genomic organization and chromosomal localization of human heparan glucosaminyl N-deacetylase\/N-sulphotransferase-2.","volume":"332","author":"Humphries","year":"1998","journal-title":"Biochem J"},{"key":"2019041121493060600_R373","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.1074\/jbc.274.5.2690","article-title":"Molecular cloning and expression of a third member of the heparan sulfate\/heparin GlcNAc N-deacetylase\/N-sulfotransferase family.","volume":"274","author":"Aikawa","year":"1999","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R374","doi-asserted-by":"crossref","first-page":"5876","DOI":"10.1074\/jbc.M009606200","article-title":"Multiple isozymes of heparan sulfate\/heparin GlcNAc N-deacetylase\/N-sulfotransferase.","volume":"276","author":"Aikawa","year":"2001","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R375","doi-asserted-by":"crossref","first-page":"25926","DOI":"10.1074\/jbc.C000359200","article-title":"Defective heparan sulfate biosynthesis and neonatal lethality in mice lacking N-deacetylase\/N-sulfotransferase-1.","volume":"275","author":"Ringvall","year":"2000","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R376","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1038\/23481","article-title":"Heparin is essential for the storage of specific granule protease in mast cells.","volume":"400","author":"Humphries","year":"1999","journal-title":"Nature"},{"key":"2019041121493060600_R377","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1038\/23488","article-title":"Abnormal mast cells in mice deficient in a heparin-synthesizing enzyme.","volume":"400","author":"Forsberg","year":"1999","journal-title":"Nature"},{"key":"2019041121493060600_R378","doi-asserted-by":"crossref","first-page":"5548","DOI":"10.1021\/bi002926p","article-title":"Substrate specificity of the heparan sulfate hexuroinc acid 2-O-sulfotransferase.","volume":"40","author":"Rong","year":"2001","journal-title":"Biochemistry (Mosc)"},{"key":"2019041121493060600_R379","doi-asserted-by":"crossref","first-page":"1894","DOI":"10.1101\/gad.12.12.1894","article-title":"Renal agenesis in mice homogygous for a gene trap mutation in the gene encoding heparan sulfate 2-sulfotransferase.","volume":"12","author":"Bullock","year":"1998","journal-title":"Genes Dev"},{"key":"2019041121493060600_R380","doi-asserted-by":"crossref","first-page":"28008","DOI":"10.1074\/jbc.272.44.28008","article-title":"Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase.","volume":"272","author":"Shworak","year":"1997","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R381","doi-asserted-by":"crossref","first-page":"5170","DOI":"10.1074\/jbc.274.8.5170","article-title":"Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase.","volume":"274","author":"Shworak","year":"1999","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R382","doi-asserted-by":"crossref","first-page":"5185","DOI":"10.1074\/jbc.274.8.5185","article-title":"Expression of heparan sulsfate D-glucosaminyl 3-O-sulfotransferase isoforms refeals novel substrate specificities.","volume":"274","author":"Liu","year":"1999","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R383","doi-asserted-by":"crossref","first-page":"27998","DOI":"10.1074\/jbc.273.43.27998","article-title":"The retinoic acid and cAMP-dependent up-regulation of 3-O-sulfotransferase-1 leads to a dramatic augmentation of anticoagulantly active heparan sulfate biosynthesis in F9 embryonal carcinoma cells.","volume":"273","author":"Zhang","year":"1998","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R384","doi-asserted-by":"crossref","first-page":"9208","DOI":"10.1074\/jbc.273.15.9208","article-title":"Molecular characterization and expression of heparan-sulfate 6-sulfotransferase.","volume":"273","author":"Habuchi","year":"1998","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R385","doi-asserted-by":"crossref","first-page":"2859","DOI":"10.1074\/jbc.275.4.2859","article-title":"The occurrence of three isoforms of heparan sulfate 6-O-sulfotransferase having different specificities for hexuronic acid adjacent to the targeted N-sulfoglucosamine.","volume":"275","author":"Habuchi","year":"2000","journal-title":"J Biol Chem"},{"key":"2019041121493060600_R386","doi-asserted-by":"crossref","first-page":"928","DOI":"10.1006\/bbrc.2001.4668","article-title":"Sulfation of endothelial mucin by corneal karatan N-acetylglucosamine 6-O-suflotransferase (GST-4\u03b2).","volume":"282","author":"Bartes","year":"2001","journal-title":"Biochem Biophys Res Commun"},{"key":"2019041121493060600_R387","first-page":"261","article-title":"Mutations in corneal carbohydrate sulfotransferase 6 gene (CHST6) cause macular dystrophy in Iceland.","volume":"13","author":"Liu","year":"2000","journal-title":"Mol Vis"},{"key":"2019041121493060600_R388","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1097\/00008571-200112000-00002","article-title":"Human sulfotransferase SULT1C1 pharmacogenetics: gene resequencing and functional genomic studies.","volume":"11","author":"Freimuth","year":"2001","journal-title":"Pharmacogenetics"},{"key":"2019041121493060600_R389","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1038\/sj.tpj.6500089","article-title":"Human sulfotransferase SULT2A1 pharmacogenetics: genotype-to-phenotype.","volume":"2","author":"Thomae","year":"2002","journal-title":"Pharmacogenetics J"}],"container-title":["Endocrine Reviews"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/edrv\/article-pdf\/23\/5\/703\/8861190\/edrv0703.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,1,7]],"date-time":"2024-01-07T02:43:55Z","timestamp":1704595435000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/edrv\/article\/23\/5\/703\/2424369"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,10,1]]},"references-count":390,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2016,11,7]]},"published-print":{"date-parts":[[2002,10,1]]}},"URL":"https:\/\/doi.org\/10.1210\/er.2001-0040","relation":{},"ISSN":["0163-769X","1945-7189"],"issn-type":[{"value":"0163-769X","type":"print"},{"value":"1945-7189","type":"electronic"}],"subject":[],"published":{"date-parts":[[2002,10,1]]}}}