{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T19:46:31Z","timestamp":1792784791109,"version":"4.5.0"},"reference-count":45,"publisher":"American Chemical Society (ACS)","issue":"7","license":[{"start":{"date-parts":[[2016,5,6]],"date-time":"2016-05-06T00:00:00Z","timestamp":1462492800000},"content-version":"vor","delay-in-days":10,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/501100000781","name":"European Research Council","doi-asserted-by":"publisher","award":["ERC-2012-AdG-32294"],"award-info":[{"award-number":["ERC-2012-AdG-32294"]}],"id":[{"id":"10.13039\/501100000781","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000923","name":"Australian Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000923","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004352","name":"Suranaree University of Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004352","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004396","name":"Thailand Research Fund","doi-asserted-by":"publisher","award":["BRG5680012"],"award-info":[{"award-number":["BRG5680012"]}],"id":[{"id":"10.13039\/501100004396","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Office of the Higher Education Commission","id":[{"id":"https:\/\/ror.org\/05m5t2b63","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Institute for Protein Research, Osaka University","award":["ICR-14-03"],"award-info":[{"award-number":["ICR-14-03"]}],"id":[{"id":"https:\/\/ror.org\/035t8zc32","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2016,7,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Human glucosylcerebrosidase 2 (GBA2) of the CAZy family GH116 is responsible for the breakdown of glycosphingolipids on the cytoplasmic face of the endoplasmic reticulum and Golgi apparatus. Genetic defects in GBA2 result in spastic paraplegia and cerebellar ataxia, while cross-talk between GBA2 and GBA1 glucosylceramidases may affect Gaucher disease. Here, we report the first three-dimensional structure for any GH116 enzyme, Thermoanaerobacterium xylanolyticum TxGH116 \u03b2-glucosidase, alone and in complex with diverse ligands. These structures allow identification of the glucoside binding and active site residues, which are shown to be conserved with GBA2. Mutagenic analysis of TxGH116 and structural modeling of GBA2 provide a detailed structural and functional rationale for pathogenic missense mutations of GBA2.<\/jats:p>","DOI":"10.1021\/acschembio.6b00192","type":"journal-article","created":{"date-parts":[[2016,4,26]],"date-time":"2016-04-26T16:08:19Z","timestamp":1461686899000},"page":"1891-1900","source":"Crossref","is-referenced-by-count":49,"title":["Bacterial \u03b2-Glucosidase Reveals the Structural\nand Functional Basis of Genetic Defects in Human Glucocerebrosidase\n2 (GBA2)"],"prefix":"10.1021","volume":"11","author":[{"given":"Ratana","family":"Charoenwattanasatien","sequence":"first","affiliation":[{"name":"Osaka University , , 3-2 Yamadaoka, Suita , ,","place":["Osaka, Japan, 565-0871"]},{"name":"Suranaree Univerity of Technology , , ,","place":["Nakhon Ratchasima, Thailand, 30000"]},{"name":"Suranaree University of Technology , , ,","place":["Nakhon Ratchasima, Thailand, 30000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Salila","family":"Pengthaisong","sequence":"additional","affiliation":[{"name":"Suranaree Univerity of Technology , , ,","place":["Nakhon Ratchasima, Thailand, 30000"]},{"name":"Suranaree University of Technology , , ,","place":["Nakhon Ratchasima, Thailand, 30000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Imogen","family":"Breen","sequence":"additional","affiliation":[{"name":"The University of York , , ,","place":["York, United Kingdom, YO10 5DD"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Risa","family":"Mutoh","sequence":"additional","affiliation":[{"name":"Osaka University , , 3-2 Yamadaoka, Suita , ,","place":["Osaka, Japan, 565-0871"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sompong","family":"Sansenya","sequence":"additional","affiliation":[{"name":"Rajamangala University of Technology , , , ,","place":["Thanyaburi, Pathum Thani, Thailand, 12110"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yanling","family":"Hua","sequence":"additional","affiliation":[{"name":"Suranaree University of Technology , , ,","place":["Nakhon Ratchasima, Thailand, 30000"]},{"name":"Suranaree University of Technology , , ,","place":["Nakhon Ratchasima, Thailand, 30000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anupong","family":"Tankrathok","sequence":"additional","affiliation":[{"name":"Kalasin University , , ,","place":["Kalasin, Thailand, 46000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liang","family":"Wu","sequence":"additional","affiliation":[{"name":"The University of York , , ,","place":["York, United Kingdom, YO10 5DD"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chomphunuch","family":"Songsiriritthigul","sequence":"additional","affiliation":[{"name":"Suranaree University of Technology , , ,","place":["Nakhon Ratchasima, Thailand, 30000"]},{"name":"Synchrotron Light Research Institute , ,","place":["Nakhon Ratchasima, Thailand, 30000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hideaki","family":"Tanaka","sequence":"additional","affiliation":[{"name":"Osaka University , , 3-2 Yamadaoka, Suita , ,","place":["Osaka, Japan, 565-0871"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Spencer J.","family":"Williams","sequence":"additional","affiliation":[{"name":"University of Melbourne , , , ,","place":["Parkville, Victoria, Australia, 3010"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gideon J.","family":"Davies","sequence":"additional","affiliation":[{"name":"The University of York , , ,","place":["York, United Kingdom, YO10 5DD"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Genji","family":"Kurisu","sequence":"additional","affiliation":[{"name":"Osaka University , , 3-2 Yamadaoka, Suita , ,","place":["Osaka, Japan, 565-0871"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James R. Ketudat","family":"Cairns","sequence":"additional","affiliation":[{"name":"Suranaree Univerity of Technology , , ,","place":["Nakhon Ratchasima, Thailand, 30000"]},{"name":"Suranaree University of Technology , , ,","place":["Nakhon Ratchasima, Thailand, 30000"]},{"name":"Chulabhorn Research Institute , , ,","place":["Bangkok, Thailand, 10210"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2016,4,26]]},"reference":[{"key":"2026092909085535100_cit1","doi-asserted-by":"publisher","first-page":"D490","DOI":"10.1093\/nar\/gkt1178","article-title":"The carbohydrate-active\nenzymes database (CAZy) in 2013","volume":"42","author":"Lombard","year":"2014","journal-title":"Nucleic Acids\nRes."},{"key":"2026092909085535100_cit2","doi-asserted-by":"crossref","first-page":"37929","DOI":"10.1074\/jbc.M104290200","article-title":"Molecular cloning and\nexpression of human bile acid \u03b2-glucosidase","volume":"276","author":"Matern","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2026092909085535100_cit3","doi-asserted-by":"publisher","first-page":"20691","DOI":"10.1074\/jbc.M109.086470","article-title":"A new archaeal \u03b2-glycosidase\nfrom Sulfolobus solfataricus: seeding a novel retaining\n\u03b2-glycan-specific glycoside hydrolase family along with the\nhuman non-lysosomal glucosylceramidase GBA2","volume":"285","author":"Cobucci-Ponzano","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2026092909085535100_cit4","doi-asserted-by":"publisher","first-page":"11261","DOI":"10.1074\/jbc.272.17.11261","article-title":"Purification and characterization\nof a microsomal bile acid \u03b2-glucosidase from human liver","volume":"272","author":"Matern","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2026092909085535100_cit5","doi-asserted-by":"publisher","first-page":"2985","DOI":"10.1172\/JCI29224","article-title":"Mutation of \u03b2-glucosidase 2\ncauses glycolipid\nstorage disease and impaired male fertility","volume":"116","author":"Yildiz","year":"2006","journal-title":"J. Clin. Invest."},{"key":"2026092909085535100_cit6","doi-asserted-by":"publisher","first-page":"3381","DOI":"10.1074\/jbc.M112.414714","article-title":"The non-lysosomal \u03b2-glucosidase GBA2 is a non-integral\nmembrane-associated protein at the endoplasmic reticulum (ER) and\nGolgi","volume":"288","author":"Ko\u0308rschen","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2026092909085535100_cit7","doi-asserted-by":"publisher","first-page":"35351","DOI":"10.1074\/jbc.M114.593376","article-title":"A sensitive gel-based method combining distinct cyclophellitol-based\nprobes for the identification of acid\/base residues in human retaining\n\u03b2-glucosidases","volume":"289","author":"Kallemeijn","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2026092909085535100_cit8","doi-asserted-by":"publisher","first-page":"a004788","DOI":"10.1101\/cshperspect.a004788","article-title":"Glycosphingolipid\nfunctions","volume":"3","author":"Lingwood","year":"2011","journal-title":"Cold Spring Harbor Perspect. Biol."},{"key":"2026092909085535100_cit9","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1146\/annurev.immunol.25.022106.141711","article-title":"The biology\nof NKT cells","volume":"25","author":"Bendelac","year":"2007","journal-title":"Annu. Rev. 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Genet."},{"key":"2026092909085535100_cit13","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/j.ajhg.2012.12.012","article-title":"Mutations\nin GBA2 cause autosomal-recessive cerebellar ataxia with spasticity","volume":"92","author":"Hammer","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"2026092909085535100_cit14","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1111\/ahg.12045","article-title":"A novel GBA2 gene missense mutation\nin spastic ataxia","volume":"78","author":"Votsi","year":"2014","journal-title":"Ann. Hum. Genet."},{"key":"2026092909085535100_cit15","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1007\/s00415-013-7206-6","article-title":"Mutations\nin CYP2U1, DDHD2 and GBA2\ngenes are rare causes of complicated forms of hereditary spastic paraparesis","volume":"261","author":"Citterio","year":"2014","journal-title":"J. Neurol."},{"key":"2026092909085535100_cit16","doi-asserted-by":"publisher","first-page":"4934","DOI":"10.1073\/pnas.1400768111","article-title":"Glucocerebrosidase\n2 gene deletion\nrescues type 1 Gaucher disease","volume":"111","author":"Mistry","year":"2014","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"key":"2026092909085535100_cit17","doi-asserted-by":"publisher","first-page":"e0135889","DOI":"10.1371\/journal.pone.0135889","article-title":"Reducing GBA2 activity ameliorates\nneuropathology in Niemann-Pick Type C mice","volume":"10","author":"Marques","year":"2015","journal-title":"PLoS One"},{"key":"2026092909085535100_cit18","doi-asserted-by":"publisher","first-page":"489","DOI":"10.1096\/fj.12-215152","article-title":"The nonlysosomal\n\u03b2-glucosidase GBA2 promotes endoplasmic reticulum stress and\nimpairs tumorigenicity of human melanoma cells","volume":"27","author":"Sorli","year":"2013","journal-title":"FASEB J."},{"key":"2026092909085535100_cit19","doi-asserted-by":"publisher","first-page":"26522","DOI":"10.1074\/jbc.273.41.26522","article-title":"Generation of specific deoxynojirimycin-type inhibitors\nof the non-lysosomal glucosylceramidase","volume":"273","author":"Overkleeft","year":"1998","journal-title":"J.\nBiol. Chem."},{"key":"2026092909085535100_cit20","doi-asserted-by":"publisher","first-page":"26052","DOI":"10.1074\/jbc.M113.463562","article-title":"\u03b2-Glucosidase\n2 (GBA2) activity and imino sugar pharmacology","volume":"288","author":"Ridley","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2026092909085535100_cit21","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1016\/j.bbagen.2013.09.022","article-title":"The identification\nand molecular characterization of the first archaeal bifunctional\nexo-beta-glucosidase\/N-acetyl-beta-glucosaminidase demonstrate that\nfamily GH116 is made of three functionally distinct subfamilies","volume":"1840","author":"Ferrara","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"2026092909085535100_cit22","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1099\/00207713-43-1-41","article-title":"Taxonomic\ndistinction of saccharolytic thermophilic anaerobes: Description of Thermoanaerobacterium xylanolyticum gen. nov., sp. nov.,\nand Thermoanaerobacterium saccharolyticum gen. nov.,\nsp. nov.; Reclassification of Thermoanaerobium brockii, Clostridium thermosulfurogenes, and Clostridium thermohydrosulfiricum ElO0\u201369 as Thermoanaerobacter brockii comb. nov., Thermoanaerobacterium thermosulfurigenes comb. nov., and Thermoanaerobacter thermohydrosulfuricus comb. nov.,respectively; and transfer of Clostridium thermohydrosulfuricum 39E to Thermoanaerobacter ethanolicus","volume":"43","author":"Lee","year":"1993","journal-title":"Int. J. Syst. Bacteriol."},{"key":"2026092909085535100_cit23","doi-asserted-by":"publisher","first-page":"2256","DOI":"10.1107\/S0907444904026460","article-title":"Secondary-structure matching (SSM),\na new tool for\nfast protein structure alignment in three dimensions","volume":"60","author":"Krissinel","year":"2004","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"2026092909085535100_cit24","doi-asserted-by":"publisher","first-page":"1366","DOI":"10.1107\/S1399004714002788","article-title":"A novel beta-xylosidase\nstructure\nfrom Geobacillus thermoglucosidasius: the first crystal\nstructure of a glycoside hydrolase family GH52 enzyme reveals unpredicted\nsimilarity to other glycoside hydrolase folds","volume":"70","author":"Espina","year":"2014","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"2026092909085535100_cit25","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1016\/S0959-440X(97)80072-3","article-title":"Structural and sequence-based\nclassification of glycoside\nhydrolases","volume":"7","author":"Henrissat","year":"1997","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2026092909085535100_cit26","doi-asserted-by":"publisher","first-page":"951","DOI":"10.1016\/S0969-2126(01)00229-5","article-title":"The crystal\nstructure of a cyanogenic beta-glucosidase from white clover, a family\n1 glycosyl hydrolase","volume":"3","author":"Barrett","year":"1995","journal-title":"Structure"},{"key":"2026092909085535100_cit27","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/S0969-2126(99)80024-0","article-title":"Three-dimensional\nstructure of a\nbarley \u03b2-D-glucan exohydrolase, a family 3 glycosyl hydrolase","volume":"7","author":"Varghese","year":"1999","journal-title":"Structure"},{"key":"2026092909085535100_cit28","doi-asserted-by":"publisher","first-page":"1926","DOI":"10.1021\/bi972162m","article-title":"Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 \u00c5\nand its cellobiose complex\nat 2.0 \u00c5 resolution","volume":"37","author":"Davies","year":"1998","journal-title":"Biochemistry"},{"key":"2026092909085535100_cit29","doi-asserted-by":"publisher","first-page":"704","DOI":"10.1038\/sj.embor.embor873","article-title":"X-ray structure\nof human acid-\u03b2-glucosidase,\nthe defective enzyme in Gaucher disease","volume":"4","author":"Dvir","year":"2003","journal-title":"EMBO\nRep."},{"key":"2026092909085535100_cit30","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1146\/annurev.biochem.68.1.487","article-title":"Mutagenesis\nof glycosidases","volume":"68","author":"Ly","year":"1999","journal-title":"Annu. Rev. Biochem."},{"key":"2026092909085535100_cit31","doi-asserted-by":"publisher","first-page":"5887","DOI":"10.1021\/ja00171a043","article-title":"Unequivocal\ndemonstration of the involvement of a glutamate\nresidue as a nucleophile in the mechanism of a retaining glycosidase","volume":"112","author":"Withers","year":"1990","journal-title":"J. Am. Chem. Soc."},{"key":"2026092909085535100_cit32","doi-asserted-by":"publisher","first-page":"750","DOI":"10.1002\/(SICI)1521-3773(19990315)38:6&lt;750::AID-ANIE750&gt;3.0.CO;2-6","article-title":"Recent insights into inhibition, structure, and mechanism\nof configuration-retaining glycosidases","volume":"38","author":"Heightman","year":"1999","journal-title":"Angew.\nChem., Int. Ed."},{"key":"2026092909085535100_cit33","doi-asserted-by":"publisher","first-page":"979","DOI":"10.1002\/hlca.19970800329","article-title":"Structure-activity\nrelations for\nimidazo-pyridine-type inhibitors of \u03b2-D-glucosidases","volume":"80","author":"Granier","year":"1997","journal-title":"Helv. Chim. Acta"},{"key":"2026092909085535100_cit34","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1016\/j.bbrc.2015.07.112","article-title":"Lack of enzyme activity in GBA2 mutants\nassociated\nwith hereditary spastic paraplegia\/cerebellar ataxia (SPG46)","volume":"465","author":"Sultana","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2026092909085535100_cit35","doi-asserted-by":"publisher","first-page":"6371","DOI":"10.1021\/bi00186a042","article-title":"The acid\/base\ncatalyst in the exoglucanase\/xylanase from Cellulomonas fimi is glutamic acid 127: evidence from detailed kinetic studies of\nmutants","volume":"33","author":"MacLeod","year":"1994","journal-title":"Biochemistry"},{"key":"2026092909085535100_cit36","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1007\/s10545-010-9055-0","article-title":"The risk of Parkinson\u2019s\ndisease in type 1 Gaucher disease","volume":"33","author":"Bultron","year":"2010","journal-title":"J. Inherited\nMetab. Dis."},{"key":"2026092909085535100_cit37","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in\noscillation mode","volume-title":"Methods in Enzymology,\nMacromolecular Crystallography, part A","author":"Otwinowski","year":"1997"},{"key":"2026092909085535100_cit38","doi-asserted-by":"publisher","first-page":"582","DOI":"10.1107\/S0907444909012098","article-title":"Decision-making\nin structure solution using Bayesian estimates of map quality: the\nPHENIX AutoSol wizard","volume":"65","author":"Terwilliger","year":"2009","journal-title":"Acta Crystallogr., Sect.\nD: Biol. Crystallogr."},{"key":"2026092909085535100_cit39","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview\nof the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"2026092909085535100_cit40","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1107\/S0907444909042589","article-title":"Molecular\nreplacement with MOLREP","volume":"66","author":"Vagin","year":"2010","journal-title":"Acta Crystallogr.,\nSect. D: Biol. Crystallogr."},{"key":"2026092909085535100_cit41","doi-asserted-by":"publisher","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular\ngraphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr., Sect. D: Biol.\nCrystallogr."},{"key":"2026092909085535100_cit42","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5\nfor the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov","year":"2011","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"2026092909085535100_cit43","doi-asserted-by":"publisher","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: a program\nto check the stereochemical quality of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Crystallogr."},{"key":"2026092909085535100_cit44","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation\nfor macromolecular\ncrystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr., Sect. D:\nBiol. Crystallogr."},{"key":"2026092909085535100_cit45","doi-asserted-by":"publisher","first-page":"5.6.1","DOI":"10.1002\/0471250953.bi0506s15","article-title":"Comparative\nprotein structure modeling using Modeller","author":"Eswar","year":"2006","journal-title":"Current Protocols in Bioinformatics"}],"container-title":["ACS Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acschembio.6b00192","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/acbcct\/article-pdf\/11\/7\/1891\/67280203\/acschembio.6b00192.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/acbcct\/article-pdf\/11\/7\/1891\/67280203\/acschembio.6b00192.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T13:33:38Z","timestamp":1790688818000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/acbcct\/article\/11\/7\/1891\/843308\/Bacterial-Glucosidase-Reveals-the-Structural-and"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,4,26]]},"references-count":45,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2016,4,26]]},"published-print":{"date-parts":[[2016,7,15]]}},"URL":"https:\/\/doi.org\/10.1021\/acschembio.6b00192","relation":{},"ISSN":["1554-8929","1554-8937"],"issn-type":[{"value":"1554-8929","type":"print"},{"value":"1554-8937","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,4,26]]}}}