{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T04:33:13Z","timestamp":1783571593311,"version":"3.55.0"},"reference-count":53,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006492","name":"National Institute of Allergy and Infectious Diseases Division of Intramural Research","doi-asserted-by":"publisher","award":["U01 AI148114"],"award-info":[{"award-number":["U01 AI148114"]}],"id":[{"id":"10.13039\/100006492","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006492","name":"National Institute of Allergy and Infectious Diseases Division of Intramural Research","doi-asserted-by":"publisher","award":["P01AI162242"],"award-info":[{"award-number":["P01AI162242"]}],"id":[{"id":"10.13039\/100006492","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006492","name":"National Institute of Allergy and Infectious Diseases Division of Intramural Research","doi-asserted-by":"publisher","award":["R01 AI155975"],"award-info":[{"award-number":["R01 AI155975"]}],"id":[{"id":"10.13039\/100006492","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006492","name":"National Institute of Allergy and Infectious Diseases Division of Intramural Research","doi-asserted-by":"publisher","award":["R01 AI187028"],"award-info":[{"award-number":["R01 AI187028"]}],"id":[{"id":"10.13039\/100006492","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006492","name":"National Institute of Allergy and Infectious Diseases Division of Intramural Research","doi-asserted-by":"publisher","award":["AI174908"],"award-info":[{"award-number":["AI174908"]}],"id":[{"id":"10.13039\/100006492","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R24 GM136984"],"award-info":[{"award-number":["R24 GM136984"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["DMR-1933525"],"award-info":[{"award-number":["DMR-1933525"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Structure"],"published-print":{"date-parts":[[2026,3]]},"DOI":"10.1016\/j.str.2025.11.015","type":"journal-article","created":{"date-parts":[[2025,12,19]],"date-time":"2025-12-19T15:58:54Z","timestamp":1766159934000},"page":"454-462.e4","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["The impact of N-glycan conformational entropy on the binding affinity of Fc \u03b3 receptor IIIa\/CD16a"],"prefix":"10.1016","volume":"34","author":[{"given":"Paul G.","family":"Kremer","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William D.","family":"Tolbert","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eliza","family":"Gazaway","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Braulio G.","family":"Hernandez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marek K.","family":"Korzeniowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zofia A.","family":"Dyba","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tobias","family":"Grelsson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Oliver C.","family":"Grant","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William N.","family":"Lanzilotta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marzena","family":"Pazgier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert J.","family":"Woods","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3290-8649","authenticated-orcid":false,"given":"Adam W.","family":"Barb","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.str.2025.11.015_bib1","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1038\/s41586-023-06945-1","article-title":"Natural killer cell therapies","volume":"626","author":"Vivier","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.str.2025.11.015_bib2","doi-asserted-by":"crossref","DOI":"10.1016\/j.critrevonc.2021.103261","article-title":"Natural Killer cells and monoclonal antibodies: Two partners for successful antibody dependent cytotoxicity against tumor cells","volume":"160","author":"Gauthier","year":"2021","journal-title":"Crit. Rev. Oncol. Hematol."},{"key":"10.1016\/j.str.2025.11.015_bib3","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1016\/j.autrev.2016.02.006","article-title":"Targeting FcgammaRs to treat antibody-dependent autoimmunity","volume":"15","author":"Yu","year":"2016","journal-title":"Autoimmun. Rev."},{"key":"10.1016\/j.str.2025.11.015_bib4","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1186\/1471-2164-10-403","article-title":"Transcriptional profiling reveals developmental relationship and distinct biological functions of CD16+ and CD16- monocyte subsets","volume":"10","author":"Ancuta","year":"2009","journal-title":"BMC Genom."},{"key":"10.1016\/j.str.2025.11.015_bib5","doi-asserted-by":"crossref","first-page":"3716","DOI":"10.1182\/blood-2008-09-179754","article-title":"Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses","volume":"113","author":"Bruhns","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.str.2025.11.015_bib6","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102329","article-title":"The weaker-binding Fc \u03b3 receptor IIIa F158 allotype retains sensitivity to N-glycan composition and exhibits a destabilized antibody-binding interface","volume":"298","author":"Kremer","year":"2022","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2025.11.015_bib7","doi-asserted-by":"crossref","first-page":"4005","DOI":"10.1073\/pnas.0508123103","article-title":"Engineered antibody Fc variants with enhanced effector function","volume":"103","author":"Lazar","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.str.2025.11.015_bib8","doi-asserted-by":"crossref","first-page":"3477","DOI":"10.1074\/jbc.RA117.001207","article-title":"Restricted processing of CD16a\/Fc \u03b3 receptor IIIa","volume":"293","author":"Patel","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2025.11.015_bib9","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2022.960411","article-title":"Decoding human-macaque interspecies differences in Fc-effector functions: The structural basis for CD16-dependent effector function in Rhesus macaques","volume":"13","author":"Tolbert","year":"2022","journal-title":"Front. Immunol."},{"key":"10.1016\/j.str.2025.11.015_bib10","article-title":"Role of","volume":"13","author":"Van Coillie","year":"2022","journal-title":"Front. Immunol."},{"key":"10.1016\/j.str.2025.11.015_bib11","doi-asserted-by":"crossref","first-page":"16842","DOI":"10.1074\/jbc.RA118.004998","article-title":"CD16a with oligomannose-type","volume":"293","author":"Subedi","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2025.11.015_bib12","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.100083","article-title":"One N-glycan regulates natural killer cell antibody-dependent cell-mediated cytotoxicity and modulates Fc \u03b3 receptor IIIa\/CD16a structure","volume":"13","author":"Kremer","year":"2024","journal-title":"eLife"},{"key":"10.1016\/j.str.2025.11.015_bib13","doi-asserted-by":"crossref","first-page":"2178","DOI":"10.1074\/mcp.RA119.001607","article-title":"Primary Human Natural Killer Cells Retain Proinflammatory IgG1 at the Cell Surface and Express CD16a Glycoforms with Donor-dependent Variability","volume":"18","author":"Patel","year":"2019","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.str.2025.11.015_bib14","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1111\/imm.13662","article-title":"Inhibiting N-glycan processing increases the antibody binding affinity and effector function of human natural killer cells","volume":"170","author":"Rodriguez Benavente","year":"2023","journal-title":"Immunology"},{"key":"10.1016\/j.str.2025.11.015_bib15","doi-asserted-by":"crossref","first-page":"3849","DOI":"10.4049\/jimmunol.159.8.3849","article-title":"Cell type-specific glycoforms of Fc gamma RIIIa (CD16): differential ligand binding","volume":"159","author":"Edberg","year":"1997","journal-title":"J. Immunol."},{"key":"10.1016\/j.str.2025.11.015_bib16","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.RA120.015516","article-title":"Fc \u03b3 receptor IIIa\/CD16a processing correlates with the expression of glycan-related genes in human natural killer cells","volume":"296","author":"Patel","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2025.11.015_bib17","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1074\/mcp.RA119.001733","article-title":"Site-specific N-glycan Analysis of Antibody-binding Fc \u03b3 Receptors from Primary Human Monocytes","volume":"19","author":"Roberts","year":"2020","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.str.2025.11.015_bib18","doi-asserted-by":"crossref","first-page":"3275","DOI":"10.1073\/pnas.79.10.3275","article-title":"Human neutrophil Fc gamma receptor distribution and structure","volume":"79","author":"Fleit","year":"1982","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.str.2025.11.015_bib19","doi-asserted-by":"crossref","first-page":"1410","DOI":"10.4049\/jimmunol.132.3.1410","article-title":"Antibody 3G8, specific for the human neutrophil Fc receptor, reacts with natural killer cells","volume":"132","author":"Perussia","year":"1984","journal-title":"J. Immunol."},{"key":"10.1016\/j.str.2025.11.015_bib20","doi-asserted-by":"crossref","first-page":"7938","DOI":"10.1038\/s41598-024-58541-6","article-title":"Distinct CD16a features on human NK cells observed by flow cytometry correlate with increased ADCC","volume":"14","author":"Benavente","year":"2024","journal-title":"Sci. Rep."},{"key":"10.1016\/j.str.2025.11.015_bib21","doi-asserted-by":"crossref","first-page":"2404","DOI":"10.1182\/blood.V114.22.2404.2404","article-title":"3G8 and GMA161, Anti Fc\u03b3RIII Inhibitory Monoclonal Antibodies in the Treatment of Chronic Refractory ITP. (Summary of 2 Pilot Studies)","volume":"114","author":"Charles","year":"2009","journal-title":"Blood"},{"key":"10.1016\/j.str.2025.11.015_bib22","doi-asserted-by":"crossref","first-page":"1987","DOI":"10.1038\/s41591-025-03640-8","article-title":"Allogeneic NK cells with a bispecific innate cell engager in refractory relapsed lymphoma: a phase 1 trial","volume":"31","author":"Nieto","year":"2025","journal-title":"Nat. Med."},{"key":"10.1016\/j.str.2025.11.015_bib23","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1186\/s13045-020-01024-8","article-title":"Targeting B7-H3 via chimeric antigen receptor T cells and bispecific killer cell engagers augments antitumor response of cytotoxic lymphocytes","volume":"14","author":"Liu","year":"2021","journal-title":"J. Hematol. Oncol."},{"key":"10.1016\/j.str.2025.11.015_bib24","doi-asserted-by":"crossref","first-page":"1576","DOI":"10.4049\/jimmunol.157.4.1576","article-title":"The binding epitopes of human CD16 (Fc gamma RIII) monoclonal antibodies. Implications for ligand binding","volume":"157","author":"Tamm","year":"1996","journal-title":"J. Immunol."},{"key":"10.1016\/j.str.2025.11.015_bib25","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1107\/S0021889800018227","article-title":"Global indicators of X-ray data quality","volume":"34","author":"Weiss","year":"2001","journal-title":"J. Appl. Cryst."},{"key":"10.1016\/j.str.2025.11.015_bib26","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1126\/science.1218231","article-title":"Linking crystallographic model and data quality","volume":"336","author":"Karplus","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.str.2025.11.015_bib27","series-title":"Methods in Enzymology","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/S0076-6879(97)77021-6","article-title":"Free R value: Cross-validation in crystallography","author":"Brunger","year":"1997"},{"key":"10.1016\/j.str.2025.11.015_bib28","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1084\/jem.132.2.211","article-title":"An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity","volume":"132","author":"Wu","year":"1970","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.str.2025.11.015_bib29","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/0022-2836(73)90011-9","article-title":"Environment and exposure to solvent of protein atoms. Lysozyme and insulin","volume":"79","author":"Shrake","year":"1973","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.str.2025.11.015_bib30","doi-asserted-by":"crossref","first-page":"32848","DOI":"10.1074\/jbc.M806021200","article-title":"Crystal structures of the choline\/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states","volume":"283","author":"Oswald","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2025.11.015_bib31","doi-asserted-by":"crossref","first-page":"19899","DOI":"10.1074\/jbc.RA118.005273","article-title":"A single amino acid distorts the Fc \u03b3 receptor IIIb\/CD16b structure upon binding immunoglobulin G1 and reduces affinity relative to CD16a","volume":"293","author":"Roberts","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2025.11.015_bib32","doi-asserted-by":"crossref","DOI":"10.1016\/j.sbi.2025.103118","article-title":"Are N-linked glycans intrinsically disordered?","volume":"93","author":"Gazaway","year":"2025","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.str.2025.11.015_bib33","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.1039\/D1CP04809K","article-title":"Enhanced sampling without borders: on global biasing functions and how to reweight them","volume":"24","author":"Kamenik","year":"2022","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.str.2025.11.015_bib34","doi-asserted-by":"crossref","DOI":"10.1063\/1.2944250","article-title":"A statistical analysis of the precision of reweighting-based simulations","volume":"129","author":"Shen","year":"2008","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.str.2025.11.015_bib35","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.1007\/s12551-022-01030-9","article-title":"Use of multistate Bennett acceptance ratio method for free-energy calculations from enhanced sampling and free-energy perturbation","volume":"14","author":"Matsunaga","year":"2022","journal-title":"Biophys. Rev."},{"key":"10.1016\/j.str.2025.11.015_bib36","doi-asserted-by":"crossref","first-page":"3527","DOI":"10.1021\/acschembio.2c00714","article-title":"Glycan Conformation in the Heavily Glycosylated Protein, CEACAM1","volume":"17","author":"Rogals","year":"2022","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.str.2025.11.015_bib37","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1093\/glycob\/cww076","article-title":"3D implementation of the symbol nomenclature for graphical representation of glycans","volume":"26","author":"Thieker","year":"2016","journal-title":"Glycobiology"},{"key":"10.1016\/j.str.2025.11.015_bib38","doi-asserted-by":"crossref","first-page":"1478","DOI":"10.1016\/j.str.2014.08.002","article-title":"Restricted motion of the conserved immunoglobulin G1 N-glycan is essential for efficient Fc\u03b3RIIIa binding","volume":"22","author":"Subedi","year":"2014","journal-title":"Structure"},{"key":"10.1016\/j.str.2025.11.015_bib39","doi-asserted-by":"crossref","DOI":"10.3791\/53568","article-title":"High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension","author":"Subedi","year":"2015","journal-title":"J. Vis. Exp."},{"key":"10.1016\/j.str.2025.11.015_bib40","article-title":"Metabolic control of glycosylation forms for establishing glycan-dependent protein interaction networks","volume":"122","author":"Liu","year":"2025","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.str.2025.11.015_bib41","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1107\/S2059798323003595","article-title":"The CCP4 suite: integrative software for macromolecular crystallography","volume":"79","author":"Agirre","year":"2023","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.str.2025.11.015_bib42","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.str.2025.11.015_bib43","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.str.2025.11.015_bib44","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/S0076-6879(03)74014-2","article-title":"Macromolecular TLS refinement in REFMAC at moderate resolutions","volume":"374","author":"Winn","year":"2003","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.str.2025.11.015_bib45","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.str.2025.11.015_bib46","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","year":"1994","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.str.2025.11.015_bib47","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.str.2025.11.015_bib48","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"D66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.str.2025.11.015_bib49","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.str.2025.11.015_bib50","doi-asserted-by":"crossref","first-page":"2179","DOI":"10.1021\/acschembio.8b00342","article-title":"Antibody Fucosylation Lowers the FcgammaRIIIa\/CD16a Affinity by Limiting the Conformations Sampled by the N162-Glycan","volume":"13","author":"Falconer","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.str.2025.11.015_bib51","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1093\/glycob\/cwh008","article-title":"Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding","volume":"14","author":"Petrescu","year":"2004","journal-title":"Glycobiology"},{"key":"10.1016\/j.str.2025.11.015_bib52","doi-asserted-by":"crossref","first-page":"2247","DOI":"10.1002\/pro.5560041101","article-title":"Side-chain conformational entropy in protein folding","volume":"4","author":"Doig","year":"1995","journal-title":"Protein Sci."},{"key":"10.1016\/j.str.2025.11.015_bib53","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1002\/pro.3943","article-title":"UCSF ChimeraX: Structure visualization for researchers, educators, and developers","volume":"30","author":"Pettersen","year":"2021","journal-title":"Protein Sci."}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212625004757?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212625004757?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T20:55:01Z","timestamp":1778792101000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212625004757"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3]]},"references-count":53,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2026,3]]}},"alternative-id":["S0969212625004757"],"URL":"https:\/\/doi.org\/10.1016\/j.str.2025.11.015","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[2026,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The impact of N-glycan conformational entropy on the binding affinity of Fc \u03b3 receptor IIIa\/CD16a","name":"articletitle","label":"Article Title"},{"value":"Structure","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.str.2025.11.015","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}