{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T18:01:06Z","timestamp":1791482466716,"version":"4.3.4"},"reference-count":49,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100011093","name":"University of Phayao","doi-asserted-by":"publisher","award":["PBTSC66023"],"award-info":[{"award-number":["PBTSC66023"]}],"id":[{"id":"10.13039\/501100011093","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011093","name":"University of Phayao","doi-asserted-by":"publisher","award":["PBTSC66002"],"award-info":[{"award-number":["PBTSC66002"]}],"id":[{"id":"10.13039\/501100011093","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011093","name":"University of Phayao","doi-asserted-by":"publisher","award":["FF66-UoE016"],"award-info":[{"award-number":["FF66-UoE016"]}],"id":[{"id":"10.13039\/501100011093","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","id":[{"id":"10.13039\/501100004396","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011752","name":"Synchrotron Light Research Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100011752","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100017170","name":"Thailand Science Research and Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100017170","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004192","name":"National Science and Technology Development Agency","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004192","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chemico-Biological Interactions"],"published-print":{"date-parts":[[2023,10]]},"DOI":"10.1016\/j.cbi.2023.110717","type":"journal-article","created":{"date-parts":[[2023,9,17]],"date-time":"2023-09-17T01:17:22Z","timestamp":1694913442000},"page":"110717","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":19,"special_numbering":"C","title":["Structural basis for inhibition of a GH116 \u03b2-glucosidase and its missense mutants by GBA2 inhibitors: Crystallographic and quantum chemical study"],"prefix":"10.1016","volume":"384","author":[{"given":"Wijitra","family":"Meelua","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9315-0395","authenticated-orcid":false,"given":"Natechanok","family":"Thinkumrob","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patchreenart","family":"Saparpakorn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9405-4293","authenticated-orcid":false,"given":"Salila","family":"Pengthaisong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Supa","family":"Hannongbua","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3042-1626","authenticated-orcid":false,"given":"James R.","family":"Ketudat Cairns","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5041-3343","authenticated-orcid":false,"given":"Jitrayut","family":"Jitonnom","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbi.2023.110717_bib1","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1073\/pnas.83.6.1660","article-title":"Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site","volume":"83","author":"Dinur","year":"1986","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.cbi.2023.110717_bib2","doi-asserted-by":"crossref","first-page":"37929","DOI":"10.1074\/jbc.M104290200","article-title":"Molecular cloning and expression of human bile acid \u03b2-glucosidase","volume":"276","author":"Matern","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2023.110717_bib3","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.ajhg.2012.12.012","article-title":"Mutations in GBA2 cause autosomal-recessive cerebellar ataxia with spasticity","volume":"92","author":"Hammer","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.cbi.2023.110717_bib4","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.ajhg.2012.11.021","article-title":"Loss of function of glucocerebrosidase GBA2 is responsible for motor neuron defects in hereditary spastic paraplegia","volume":"92","author":"Martin","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.cbi.2023.110717_bib5","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1007\/s00415-013-7206-6","article-title":"Mutations in CYP2U1, DDHD2 and GBA2 genes are rare causes of complicated forms of hereditary spastic paraparesis","volume":"261","author":"Citterio","year":"2014","journal-title":"J. Neurol."},{"key":"10.1016\/j.cbi.2023.110717_bib6","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1111\/ahg.12045","article-title":"A novel GBA2 gene missense mutation in spastic ataxia","volume":"78","author":"Votsi","year":"2014","journal-title":"Ann. Hum. Genet."},{"key":"10.1016\/j.cbi.2023.110717_bib7","doi-asserted-by":"crossref","first-page":"4934","DOI":"10.1073\/pnas.1400768111","article-title":"Glucocerebrosidase 2 gene deletion rescues type 1 Gaucher disease","volume":"111","author":"Mistry","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.cbi.2023.110717_bib8","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1111\/j.1365-2141.2004.05351.x","article-title":"Gaucher disease: pathological mechanisms and modern management","volume":"129","author":"Jmoudiak","year":"2005","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.cbi.2023.110717_bib9","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1016\/j.cbpa.2007.05.035","article-title":"Gaucher disease","volume":"11","author":"Butters","year":"2007","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.cbi.2023.110717_bib10","doi-asserted-by":"crossref","DOI":"10.3390\/ijms18020441","article-title":"A review of Gaucher disease pathophysiology, clinical presentation and treatments","volume":"18","author":"Stirnemann","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.cbi.2023.110717_bib11","doi-asserted-by":"crossref","first-page":"35351","DOI":"10.1074\/jbc.M114.593376","article-title":"A sensitive gel-based method combining distinct cyclophellitol-based probes for the identification of acid\/base residues in human retaining \u03b2-glucosidases","volume":"289","author":"Kallemeijn","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2023.110717_bib12","doi-asserted-by":"crossref","first-page":"1891","DOI":"10.1021\/acschembio.6b00192","article-title":"Bacterial \u03b2-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2)","volume":"11","author":"Charoenwattanasatien","year":"2016","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.cbi.2023.110717_bib13","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2020.00271","article-title":"Small molecule chaperones for the treatment of Gaucher disease and GBA1-associated Parkinson disease","volume":"8","author":"Han","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.cbi.2023.110717_bib14","doi-asserted-by":"crossref","first-page":"10647","DOI":"10.1021\/bi201619z","article-title":"Binding of 3,4,5,6-tetrahydroxyazepanes to the acid-\u03b2-glucosidase active site: implications for pharmacological chaperone design for Gaucher disease","volume":"50","author":"Orwig","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2023.110717_bib15","doi-asserted-by":"crossref","first-page":"26522","DOI":"10.1074\/jbc.273.41.26522","article-title":"Generation of specific deoxynojirimycin-type inhibitors of the non-lysosomal glucosylceramidase","volume":"273","author":"Overkleeft","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2023.110717_bib16","doi-asserted-by":"crossref","first-page":"26052","DOI":"10.1074\/jbc.M113.463562","article-title":"\u03b2-Glucosidase 2 (GBA2) activity and imino sugar pharmacology","volume":"288","author":"Ridley","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2023.110717_bib17","doi-asserted-by":"crossref","first-page":"D490","DOI":"10.1093\/nar\/gkt1178","article-title":"The carbohydrate-active enzymes database (CAZy) in 2013","volume":"42","author":"Lombard","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.cbi.2023.110717_bib18","doi-asserted-by":"crossref","first-page":"D233","DOI":"10.1093\/nar\/gkn663","article-title":"The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics","volume":"37","author":"Cantarel","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.cbi.2023.110717_bib19","doi-asserted-by":"crossref","first-page":"343","DOI":"10.3390\/catal12030343","article-title":"Systematic functional and computational analysis of glucose-binding residues in glycoside hydrolase family GH116","volume":"12","author":"Huang","year":"2022","journal-title":"Catalysts"},{"key":"10.1016\/j.cbi.2023.110717_bib20","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1021\/acscentsci.7b00214","article-title":"1,6-Cyclophellitol cyclosulfates: a new class of irreversible glycosidase inhibitor","volume":"3","author":"Artola","year":"2017","journal-title":"ACS Cent. Sci."},{"key":"10.1016\/j.cbi.2023.110717_bib21","doi-asserted-by":"crossref","first-page":"14192","DOI":"10.1021\/jacs.7b07352","article-title":"A fluorescence polarization activity-based protein profiling assay in the discovery of potent, selective inhibitors for human nonlysosomal glucosylceramidase","volume":"139","author":"Lahav","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2023.110717_bib22","doi-asserted-by":"crossref","first-page":"4214","DOI":"10.1021\/jacs.9b00056","article-title":"Functionalized cyclophellitols are selective glucocerebrosidase inhibitors and induce a bona fide neuropathic Gaucher model in zebrafish","volume":"141","author":"Artola","year":"2019","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2023.110717_bib23","doi-asserted-by":"crossref","first-page":"20691","DOI":"10.1074\/jbc.M109.086470","article-title":"A new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2","volume":"285","author":"Cobucci-Ponzano","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2023.110717_bib24","doi-asserted-by":"crossref","first-page":"5850","DOI":"10.1021\/acscatal.3c00620","article-title":"Reaction mechanism of glycoside hydrolase family 116 utilizes perpendicular protonation","volume":"13","author":"Pengthaisong","year":"2023","journal-title":"ACS Catal."},{"key":"10.1016\/j.cbi.2023.110717_bib25","doi-asserted-by":"crossref","first-page":"16965","DOI":"10.1021\/jacs.0c05592","article-title":"Glycoside hydrolases restrict the side chain conformation of their substrates to gain additional transition state stabilization","volume":"142","author":"Quirke","year":"2020","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2023.110717_bib26","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0233856","article-title":"Truncated mutants of beta-glucosidase 2 (GBA2) are localized in the mitochondrial matrix and cause mitochondrial fragmentation","volume":"15","author":"Sultana","year":"2020","journal-title":"PLoS One"},{"key":"10.1016\/j.cbi.2023.110717_bib27","doi-asserted-by":"crossref","first-page":"5678","DOI":"10.1021\/cr5004419","article-title":"The ONIOM method and its applications","volume":"115","author":"Chung","year":"2015","journal-title":"Chem. Rev."},{"key":"10.1016\/j.cbi.2023.110717_bib28","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 oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.cbi.2023.110717_bib29","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1107\/S0907444909042589","article-title":"Molecular replacement with MOLREP","volume":"66","author":"Vagin","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cbi.2023.110717_bib30","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cbi.2023.110717_bib31","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cbi.2023.110717_bib32","doi-asserted-by":"crossref","first-page":"1354","DOI":"10.1021\/ja00839a011","article-title":"General definition of ring puckering coordinates","volume":"97","author":"Cremer","year":"1975","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2023.110717_bib33","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.cbi.2023.110717_bib34","series-title":"Gaussian 09","author":"Frisch","year":"2009"},{"key":"10.1016\/j.cbi.2023.110717_bib35","series-title":"Gaussian 16 Revision C.02","author":"Frisch","year":"2019"},{"key":"10.1016\/j.cbi.2023.110717_bib36","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1002\/prot.20660","article-title":"Very fast empirical prediction and rationalization of protein pKa values","volume":"61","author":"Li","year":"2005","journal-title":"Proteins"},{"key":"10.1016\/j.cbi.2023.110717_bib37","doi-asserted-by":"crossref","first-page":"2090","DOI":"10.1016\/j.procbio.2012.07.026","article-title":"New biocatalytic route for the production of enantioenriched \u03b2-alanine derivatives starting from 5- and 6-monosubstituted dihydrouracils","volume":"47","author":"Mart\u00ednez-G\u00f3mez","year":"2012","journal-title":"Process Biochem."},{"key":"10.1016\/j.cbi.2023.110717_bib38","doi-asserted-by":"crossref","DOI":"10.1016\/j.cbi.2022.110227","article-title":"Roles of hybrid donepezil scaffolds as potent human acetylcholinesterase inhibitors using in silico interaction analysis, drug-likeness, and pharmacokinetics prediction","volume":"368","author":"Honorio","year":"2022","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2023.110717_bib39","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1002\/prot.20690","article-title":"Binding energy analysis for wild-type and Y181C mutant HIV-1 RT\/8-Cl TIBO complex structures: quantum chemical calculations based on the ONIOM method","volume":"61","author":"Saen-oon","year":"2005","journal-title":"Proteins"},{"key":"10.1016\/j.cbi.2023.110717_bib40","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1039\/c1md00162k","article-title":"Key interactions of the mutant HIV-1 reverse transcriptase\/efavirenz: an evidence obtained from ONIOM method","volume":"2","author":"Boonsri","year":"2011","journal-title":"Med. Chem. Commun."},{"key":"10.1016\/j.cbi.2023.110717_bib41","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1080\/00268977000101561","article-title":"The calculation of small molecular interactions by the differences of separate total energies. Some procedures with reduced errors","volume":"19","author":"Boys","year":"1970","journal-title":"Mol. Phys."},{"key":"10.1016\/j.cbi.2023.110717_bib42","doi-asserted-by":"crossref","first-page":"1793","DOI":"10.3390\/molecules27061793","article-title":"Computational screening of phenylamino-phenoxy-quinoline derivatives against the main protease of SARS-CoV-2 using molecular docking and the ONIOM method","volume":"27","author":"Patnin","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.cbi.2023.110717_bib43","article-title":"Inhibition of a putative dihydropyrimidinase from Pseudomonas aeruginosa PAO1 by flavonoids and substrates of cyclic amidohydrolases","volume":"10","author":"Huang","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.cbi.2023.110717_bib44","series-title":"Discovery Studio Modeling Environment","year":"2016"},{"key":"10.1016\/j.cbi.2023.110717_bib45","doi-asserted-by":"crossref","first-page":"6041","DOI":"10.1021\/acscatal.5b01547","article-title":"A single glycosidase harnesses different pyranoside ring transition state conformations for hydrolysis of mannosides and glucosides","volume":"5","author":"Tankrathok","year":"2015","journal-title":"ACS Catal."},{"key":"10.1016\/j.cbi.2023.110717_bib46","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.carres.2010.11.014","article-title":"Synthesis of polyhydroxy 7- and N-alkyl-azepanes as potent glycosidase inhibitors","volume":"346","author":"Shih","year":"2011","journal-title":"Carbohydr. Res."},{"key":"10.1016\/j.cbi.2023.110717_bib47","doi-asserted-by":"crossref","first-page":"8977","DOI":"10.1039\/C4OB00325J","article-title":"N- and C-alkylation of seven-membered iminosugars generates potent glucocerebrosidase inhibitors and F508del-CFTR correctors","volume":"12","author":"D\u00e9sir\u00e9","year":"2014","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.cbi.2023.110717_bib48","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.bioorg.2014.11.003","article-title":"Synthesis of 2-carboxymethyl polyhydroxyazepanes and their evaluation as glycosidase inhibitors","volume":"58","author":"Taghzouti","year":"2015","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.cbi.2023.110717_bib49","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1038\/s41586-021-03828-1","article-title":"Highly accurate protein structure prediction for the human proteome","volume":"596","author":"Tunyasuvunakool","year":"2021","journal-title":"Nature"}],"container-title":["Chemico-Biological Interactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279723003848?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279723003848?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T18:43:32Z","timestamp":1777401812000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0009279723003848"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,10]]},"references-count":49,"alternative-id":["S0009279723003848"],"URL":"https:\/\/doi.org\/10.1016\/j.cbi.2023.110717","relation":{},"ISSN":["0009-2797"],"issn-type":[{"value":"0009-2797","type":"print"}],"subject":[],"published":{"date-parts":[[2023,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural basis for inhibition of a GH116 \u03b2-glucosidase and its missense mutants by GBA2 inhibitors: Crystallographic and quantum chemical study","name":"articletitle","label":"Article Title"},{"value":"Chemico-Biological Interactions","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbi.2023.110717","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"110717"}}