{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T03:06:22Z","timestamp":1792033582523,"version":"4.4.0"},"reference-count":64,"publisher":"Elsevier BV","issue":"22","license":[{"start":{"date-parts":[[2024,11,1]],"date-time":"2024-11-01T00:00:00Z","timestamp":1730419200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,11,1]],"date-time":"2024-11-01T00:00:00Z","timestamp":1730419200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,9,20]],"date-time":"2024-09-20T00:00:00Z","timestamp":1726790400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100021824","name":"Government of Saskatchewan","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100021824","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["PJT-173264"],"award-info":[{"award-number":["PJT-173264"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008920","name":"University of Saskatchewan","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008920","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000196","name":"Canada Foundation for Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000196","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100013101","name":"National Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100013101","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2024,11]]},"DOI":"10.1016\/j.jmb.2024.168801","type":"journal-article","created":{"date-parts":[[2024,9,24]],"date-time":"2024-09-24T01:48:48Z","timestamp":1727142528000},"page":"168801","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"title":["Structural Analysis of Mammalian Sialic Acid Esterase"],"prefix":"10.1016","volume":"436","author":[{"given":"Danilo","family":"Ide","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexei","family":"Gorelik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katalin","family":"Illes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bhushan","family":"Nagar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2024.168801_b0005","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/bs.accb.2018.09.001","article-title":"Exploration of the sialic acid world","volume":"75","author":"Schauer","year":"2018","journal-title":"Adv. Carbohydr. Chem. Biochem."},{"key":"10.1016\/j.jmb.2024.168801_b0010","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/j.molmed.2008.06.002","article-title":"Sialic acids in human health and disease","volume":"14","author":"Varki","year":"2008","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.jmb.2024.168801_b0015","doi-asserted-by":"crossref","first-page":"15866","DOI":"10.1074\/jbc.273.25.15866","article-title":"The molecular basis for the absence of N-glycolylneuraminic acid in humans","volume":"273","author":"Irie","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2024.168801_b0020","doi-asserted-by":"crossref","first-page":"11751","DOI":"10.1073\/pnas.95.20.11751","article-title":"A mutation in human CMP-sialic acid hydroxylase occurred after the Homo-Pan divergence","volume":"95","author":"Chou","year":"1998","journal-title":"PNAS"},{"key":"10.1016\/j.jmb.2024.168801_b0025","first-page":"1","article-title":"Functions and biosynthesis of O-acetylated sialic acids","volume":"366","author":"Mandal","year":"2015","journal-title":"Top. Curr. Chem."},{"key":"10.1016\/j.jmb.2024.168801_b0030","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1007\/978-1-4419-7877-6_28","article-title":"O-Acetylated sialic acids and their role in immune defense","volume":"705","author":"Schauer","year":"2011","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.jmb.2024.168801_b0035","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100906","article-title":"Sialic acid O-acetylation: From biosynthesis to roles in health and disease","volume":"297","author":"Visser","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2024.168801_b0040","doi-asserted-by":"crossref","DOI":"10.1128\/mSphere.00379-16","article-title":"Distribution of O-acetylated sialic acids among target host tissues for influenza virus","volume":"2","author":"Wasik","year":"2017","journal-title":"mSphere"},{"key":"10.1016\/j.jmb.2024.168801_b0045","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.jaut.2013.05.003","article-title":"Rethinking mechanisms of autoimmune pathogenesis","volume":"45","author":"Pillai","year":"2013","journal-title":"J. Autoimmun."},{"key":"10.1016\/j.jmb.2024.168801_b0050","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1016\/j.it.2009.07.006","article-title":"Esterases and autoimmunity: the sialic acid acetylesterase pathway and the regulation of peripheral B cell tolerance","volume":"30","author":"Pillai","year":"2009","journal-title":"Trends Immunol."},{"key":"10.1016\/j.jmb.2024.168801_b0055","doi-asserted-by":"crossref","first-page":"7019","DOI":"10.1016\/S0021-9258(18)53140-9","article-title":"Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked oligosaccharides with alpha-2,6-linked sialic acids that are required for recognition","volume":"268","author":"Powell","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2024.168801_b0060","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1083\/jcb.126.2.549","article-title":"Natural ligands of the B cell adhesion molecule CD22 beta can be masked by 9-O-acetylation of sialic acids","volume":"126","author":"Sjoberg","year":"1994","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jmb.2024.168801_b0065","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1084\/jem.20081399","article-title":"B cell antigen receptor signal strength and peripheral B cell development are regulated by a 9-O-acetyl sialic acid esterase","volume":"206","author":"Cariappa","year":"2009","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.jmb.2024.168801_b0070","doi-asserted-by":"crossref","first-page":"e53453","DOI":"10.1371\/journal.pone.0053453","article-title":"M89V Sialic acid Acetyl Esterase (SIAE) and all other non-synonymous common variants of this gene are catalytically normal","volume":"8","author":"Chellappa","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2024.168801_b0075","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1038\/nature09115","article-title":"Functionally defective germline variants of sialic acid acetylesterase in autoimmunity","volume":"466","author":"Surolia","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2024.168801_b0080","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1038\/nrrheum.2013.78","article-title":"Gene-function studies in systemic lupus erythematosus","volume":"9","author":"Crispin","year":"2013","journal-title":"Nature Rev. Rheumatol."},{"key":"10.1016\/j.jmb.2024.168801_b0085","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1038\/gene.2011.89","article-title":"Association of primary biliary cirrhosis with variants in the CLEC16A, SOCS1, SPIB and SIAE immunomodulatory genes","volume":"13","author":"Hirschfield","year":"2012","journal-title":"Genes Immun."},{"key":"10.1016\/j.jmb.2024.168801_b0090","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1038\/ng.1037","article-title":"Rare and functional SIAE variants are not associated with autoimmune disease risk in up to 66,924 individuals of European ancestry","volume":"44","author":"Hunt","year":"2011","journal-title":"Nature Genet."},{"key":"10.1016\/j.jmb.2024.168801_b0095","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1111\/j.1399-0039.2011.01703.x","article-title":"Functionally defective germline variant of sialic acid acetylesterase (Met89Val) is not associated with type 1 diabetes mellitus and Graves' disease in a Polish population","volume":"78","author":"Szymanski","year":"2011","journal-title":"Tissue Antigens"},{"key":"10.1016\/j.jmb.2024.168801_b0100","doi-asserted-by":"crossref","first-page":"14162","DOI":"10.4238\/2015.October.29.38","article-title":"Lack of association between rare mutations of the SIAE gene and rheumatoid arthritis in a Han Chinese population","volume":"14","author":"Zhang","year":"2015","journal-title":"Genet. Mol. Res."},{"key":"10.1016\/j.jmb.2024.168801_b0105","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1530\/EJE-12-0579","article-title":"The role of functionally defective rare germline variants of sialic acid acetylesterase in autoimmune Addison's disease","volume":"167","author":"Gan","year":"2012","journal-title":"Eur. J. Endocrinol."},{"key":"10.1016\/j.jmb.2024.168801_b0110","doi-asserted-by":"crossref","first-page":"1514294","DOI":"10.1155\/2017\/1514294","article-title":"SIAE rare variants in juvenile idiopathic arthritis and primary antibody deficiencies","volume":"2017","author":"Sevdali","year":"2017","journal-title":"J. Immunol. Res."},{"key":"10.1016\/j.jmb.2024.168801_b0115","doi-asserted-by":"crossref","first-page":"22581","DOI":"10.1074\/jbc.274.32.22581","article-title":"Commitment to apoptosis by GD3 ganglioside depends on opening of the mitochondrial permeability transition pore","volume":"274","author":"Scorrano","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2024.168801_b0120","doi-asserted-by":"crossref","first-page":"1535","DOI":"10.1084\/jem.20020960","article-title":"Acetylation suppresses the proapoptotic activity of GD3 ganglioside","volume":"196","author":"Malisan","year":"2002","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.jmb.2024.168801_b0125","doi-asserted-by":"crossref","first-page":"950","DOI":"10.1093\/neuonc\/nor108","article-title":"Targeting the GD3 acetylation pathway selectively induces apoptosis in glioblastoma","volume":"13","author":"Birks","year":"2011","journal-title":"Neuro Oncol."},{"key":"10.1016\/j.jmb.2024.168801_b0130","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1002\/ijc.21788","article-title":"9-O-acetyl GD3 protects tumor cells from apoptosis","volume":"119","author":"Kniep","year":"2006","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.jmb.2024.168801_b0135","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1002\/jcb.21867","article-title":"O-acetylation of GD3 prevents its apoptotic effect and promotes survival of lymphoblasts in childhood acute lymphoblastic leukaemia","volume":"105","author":"Mukherjee","year":"2008","journal-title":"J. Cell. Biochem."},{"key":"10.1016\/j.jmb.2024.168801_b0140","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1084\/jem.20121482","article-title":"O-acetylated N-acetylneuraminic acid as a novel target for therapy in human pre-B acute lymphoblastic leukemia","volume":"210","author":"Parameswaran","year":"2013","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.jmb.2024.168801_b0145","doi-asserted-by":"crossref","first-page":"8609","DOI":"10.1038\/s41598-019-44950-5","article-title":"Human Sialic acid O-acetyl esterase (SIAE) \u2013 mediated changes in sensitivity to etoposide in a medulloblastoma cell line","volume":"9","author":"Mather","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jmb.2024.168801_b0150","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1038\/nchembio.1388","article-title":"Glycocalyx engineering reveals a Siglec-based mechanism for NK cell immunoevasion","volume":"10","author":"Hudak","year":"2014","journal-title":"Nature Chem. Biol."},{"key":"10.1016\/j.jmb.2024.168801_b0155","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1038\/s41591-019-0374-x","article-title":"Siglec-15 as an immune suppressor and potential target for normalization cancer immunotherapy","volume":"25","author":"Wang","year":"2019","journal-title":"Nature Med."},{"key":"10.1016\/j.jmb.2024.168801_b0160","doi-asserted-by":"crossref","first-page":"992","DOI":"10.1093\/glycob\/cwv034","article-title":"Human sialic acid acetyl esterase: Towards a better understanding of a puzzling enzyme","volume":"25","author":"Orizio","year":"2015","journal-title":"Glycobiology"},{"key":"10.1016\/j.jmb.2024.168801_b0165","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1093\/glycob\/cwx068","article-title":"Genomic and biochemical characterization of sialic acid acetylesterase (siae) in zebrafish","volume":"27","author":"Ravasio","year":"2017","journal-title":"Glycobiology"},{"key":"10.1016\/j.jmb.2024.168801_b0170","doi-asserted-by":"crossref","first-page":"25623","DOI":"10.1074\/jbc.274.36.25623","article-title":"Lysosomal and cytosolic sialic acid 9-O-acetylesterase activities can Be encoded by one gene via differential usage of a signal peptide-encoding exon at the N terminus","volume":"274","author":"Takematsu","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2024.168801_b0175","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1093\/oxfordjournals.jbchem.a122804","article-title":"Partial purification and characterization of sialate O-acetylesterase from bovine brain","volume":"106","author":"Schauer","year":"1989","journal-title":"J. Biochem."},{"key":"10.1016\/j.jmb.2024.168801_b0180","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1007\/s10719-008-9109-9","article-title":"Isolation and properties of two sialate-O-acetylesterases from horse liver with 4- and 9-O-acetyl specificities","volume":"25","author":"Schauer","year":"2008","journal-title":"Glycoconj. J."},{"key":"10.1016\/j.jmb.2024.168801_b0185","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2024.168801_b0190","doi-asserted-by":"crossref","first-page":"4049","DOI":"10.1038\/s41467-021-24277-4","article-title":"Xyloglucan processing machinery in Xanthomonas pathogens and its role in the transcriptional activation of virulence factors","volume":"12","author":"Vieira","year":"2021","journal-title":"Nature Commun."},{"key":"10.1016\/j.jmb.2024.168801_b0195","doi-asserted-by":"crossref","first-page":"1928","DOI":"10.1021\/acschembio.6b01140","article-title":"Catalytic Dyad in the SGNH hydrolase superfamily: In-depth insight into structural parameters tuning the catalytic process of extracellular lipase from Streptomyces rimosus","volume":"12","author":"Lescic Asler","year":"2017","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.jmb.2024.168801_b0200","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.jsb.2013.02.003","article-title":"Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297","volume":"182","author":"Murayama","year":"2013","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jmb.2024.168801_b0205","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1038\/nsb0395-218","article-title":"A novel variant of the catalytic triad in the Streptomyces scabies esterase","volume":"2","author":"Wei","year":"1995","journal-title":"Nature Struct. Biol."},{"key":"10.1016\/j.jmb.2024.168801_b0210","unstructured":"Woods, R.J. (2005\u20132024). GLYCAM Web. http:\/\/glycam.org."},{"key":"10.1016\/j.jmb.2024.168801_b0215","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2024.168801_b0220","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1093\/bioinformatics\/btt055","article-title":"GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit","volume":"29","author":"Pronk","year":"2013","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jmb.2024.168801_b0225","doi-asserted-by":"crossref","first-page":"6153","DOI":"10.1021\/acscatal.5b01539","article-title":"How the same core catalytic machinery catalyzes 17 different reactions: The serine-histidine-aspartate catalytic triad of alpha\/beta-hydrolase fold enzymes","volume":"5","author":"Rauwerdink","year":"2015","journal-title":"ACS Catal."},{"key":"10.1016\/j.jmb.2024.168801_b0230","doi-asserted-by":"crossref","first-page":"W210","DOI":"10.1093\/nar\/gkac387","article-title":"Dali server: structural unification of protein families","volume":"50","author":"Holm","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2024.168801_b0235","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1016\/j.jmb.2003.10.078","article-title":"Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain","volume":"335","author":"Abe","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2024.168801_b0240","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1042\/BJ20040892","article-title":"Carbohydrate-binding modules: fine-tuning polysaccharide recognition","volume":"382","author":"Boraston","year":"2004","journal-title":"Biochem. J"},{"key":"10.1016\/j.jmb.2024.168801_b0245","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2020.140437","article-title":"High-resolution structure of a modular hyperthermostable endo-beta-1,4-mannanase from Thermotoga petrophila: The ancillary immunoglobulin-like module is a thermostabilizing domain","volume":"1868","author":"da Silva","year":"2020","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"key":"10.1016\/j.jmb.2024.168801_b0250","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1016\/j.jbiotec.2011.07.016","article-title":"The cellulose-binding domain of cellobiohydrolase Cel7A from Trichoderma reesei is also a thermostabilizing domain","volume":"155","author":"Hall","year":"2011","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.jmb.2024.168801_b0255","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/j.jmb.2008.10.075","article-title":"Crystal structure and biochemical properties of a novel thermostable esterase containing an immunoglobulin-like domain","volume":"385","author":"Levisson","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2024.168801_b0260","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1016\/S0008-6215(03)00002-8","article-title":"Carbohydrate esterase family 4 enzymes: substrate specificity","volume":"338","author":"Caufrier","year":"2003","journal-title":"Carbohydr. Res."},{"issue":"Pt 7","key":"10.1016\/j.jmb.2024.168801_b0265","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1099\/00221287-146-7-1585","article-title":"The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity","volume":"146","author":"Degrassi","year":"2000","journal-title":"Microbiology (Reading)"},{"key":"10.1016\/j.jmb.2024.168801_b0270","doi-asserted-by":"crossref","first-page":"2158","DOI":"10.1002\/cbic.201000398","article-title":"Probing enzyme promiscuity of SGNH hydrolases","volume":"11","author":"Lescic Asler","year":"2010","journal-title":"Chembiochem"},{"key":"10.1016\/j.jmb.2024.168801_b0275","doi-asserted-by":"crossref","first-page":"19435","DOI":"10.1016\/S0021-9258(19)47319-5","article-title":"O-acetylation and de-O-acetylation of sialic acids. Purification, characterization, and properties of a glycosylated rat liver esterase specific for 9-O-acetylated sialic acids","volume":"264","author":"Higa","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2024.168801_b0280","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.jmb.2024.168801_b0285","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J. Appl. Cryst."},{"key":"10.1016\/j.jmb.2024.168801_b0290","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1107\/S2059798319011471","article-title":"Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix","volume":"75","author":"Liebschner","year":"2019","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.jmb.2024.168801_b0295","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1107\/S0907444912001308","article-title":"Towards automated crystallographic structure refinement with phenix.refine","volume":"68","author":"Afonine","year":"2012","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2024.168801_b0300","doi-asserted-by":"crossref","first-page":"3613","DOI":"10.1093\/bioinformatics\/btaa190","article-title":"GlycoGlyph: a glycan visualizing, drawing and naming application","volume":"36","author":"Mehta","year":"2020","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jmb.2024.168801_b0305","doi-asserted-by":"crossref","first-page":"W299","DOI":"10.1093\/nar\/gki370","article-title":"ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures","volume":"33","author":"Landau","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2024.168801_b0310","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1002\/jcc.21287","article-title":"CHARMM: the biomolecular simulation program","volume":"30","author":"Brooks","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jmb.2024.168801_b0315","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1002\/jcc.21367","article-title":"CHARMM general force field: A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields","volume":"31","author":"Vanommeslaeghe","year":"2010","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jmb.2024.168801_b0320","doi-asserted-by":"crossref","DOI":"10.1063\/1.3446812","article-title":"Optimizing working parameters of the smooth particle mesh Ewald algorithm in terms of accuracy and efficiency","volume":"133","author":"Wang","year":"2010","journal-title":"J. Chem. Phys."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283624004236?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283624004236?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,11,13]],"date-time":"2024-11-13T04:34:58Z","timestamp":1731472498000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283624004236"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,11]]},"references-count":64,"journal-issue":{"issue":"22","published-print":{"date-parts":[[2024,11]]}},"alternative-id":["S0022283624004236"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2024.168801","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2024,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural Analysis of Mammalian Sialic Acid Esterase","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2024.168801","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Author(s). Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"168801"}}