{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,4]],"date-time":"2026-07-04T13:20:20Z","timestamp":1783171220414,"version":"3.54.6"},"reference-count":74,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,6,1]],"date-time":"2026-06-01T00:00:00Z","timestamp":1780272000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,6,1]],"date-time":"2026-06-01T00:00:00Z","timestamp":1780272000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,5,11]],"date-time":"2026-05-11T00:00:00Z","timestamp":1778457600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003407","name":"Ministero dell\u2019Istruzione, dell\u2019Universit\u00e0 e della Ricerca","doi-asserted-by":"publisher","award":["ECS00000041 - VITALITY \\u2013 CUP H33C22000430006"],"award-info":[{"award-number":["ECS00000041 - VITALITY \\u2013 CUP H33C22000430006"]}],"id":[{"id":"10.13039\/501100003407","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2026,6]]},"DOI":"10.1016\/j.ijbiomac.2026.152185","type":"journal-article","created":{"date-parts":[[2026,5,5]],"date-time":"2026-05-05T23:54:29Z","timestamp":1778025269000},"page":"152185","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Predicting the success of an antibody: Biochemical and biophysical characterization of the humanized monoclonal antibody Dia-T51"],"prefix":"10.1016","volume":"366","author":[{"given":"Tania","family":"Vanzolini","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valentina","family":"Fiori","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomas","family":"Di Mambro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mauro","family":"Magnani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2026.152185_bb0005","doi-asserted-by":"crossref","first-page":"9","DOI":"10.4161\/19420862.2015.989042","article-title":"The therapeutic monoclonal antibody market","volume":"7","author":"Ecker","year":"2015","journal-title":"mAbs"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0010","doi-asserted-by":"crossref","first-page":"84","DOI":"10.4161\/mabs.2.1.10677","article-title":"Antibodies to watch in 2010","volume":"2","author":"Reichert","year":"2010","journal-title":"mAbs"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0015","doi-asserted-by":"crossref","DOI":"10.1080\/19420862.2024.2443538","article-title":"Antibodies to watch in 2025","volume":"17","author":"Crescioli","year":"2025","journal-title":"mAbs"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0020","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1073\/pnas.1616408114","article-title":"Biophysical properties of the clinical-stage antibody landscape","volume":"114","author":"Jain","year":"2017","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0025","doi-asserted-by":"crossref","first-page":"1885","DOI":"10.1002\/jps.24430","article-title":"Developability assessment during the selection of novel therapeutic antibodies","volume":"104","author":"Jarasch","year":"2015","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0030","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/j.biochi.2020.08.019","article-title":"Antibody stability: a key to performance - analysis, influences and improvement","volume":"177","author":"Ma","year":"2020","journal-title":"Biochimie"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0035","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1002\/biot.200800091","article-title":"A rapid, sensitive and economical assessment of monoclonal antibody conformational stability by intrinsic tryptophan fluorescence spectroscopy","volume":"3","author":"Garidel","year":"2008","journal-title":"Biotechnol. J."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0040","series-title":"Biophys. Ther. Protein Dev.","first-page":"173","article-title":"Biophysical analysis in support of development of protein pharmaceuticals","author":"Alavattam","year":"2013"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0045","doi-asserted-by":"crossref","first-page":"e428","DOI":"10.1016\/S1473-3099(23)00692-8","article-title":"Global incidence and mortality of severe fungal disease","volume":"24","author":"Denning","year":"2024","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0050","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1038\/s41579-022-00720-1","article-title":"Tackling the emerging threat of antifungal resistance to human health","volume":"20","author":"Fisher","year":"2022","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0055","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1053\/j.semdp.2019.04.010","article-title":"Emerging and reemerging fungal infections","volume":"36","author":"Lockhart","year":"2019","journal-title":"Semin. Diagn. Pathol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0060","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1007\/s00253-023-12884-8","article-title":"Old and new strategies in therapy and diagnosis against fungal infections","volume":"108","author":"Vanzolini","year":"2024","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0065","doi-asserted-by":"crossref","first-page":"18026","DOI":"10.1038\/nrdp.2018.26","article-title":"Invasive candidiasis","volume":"4","author":"Pappas","year":"2018","journal-title":"Nat. Rev. Dis. Primer"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0070","doi-asserted-by":"crossref","DOI":"10.1128\/microbiolspec.FUNK-0035-2016","article-title":"The fungal Cell Wall: structure, biosynthesis, and function","volume":"5","author":"Gow","year":"2017","journal-title":"Microbiol. Spectr."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0075","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1111\/j.1600-0463.2008.01013.x","article-title":"A novel monoclonal antibody recognizing \u03b2(1\u20133) glucans in intact cells of Candida and Cryptococcus","volume":"116","author":"Kondori","year":"2008","journal-title":"APMIS"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0080","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0215535","article-title":"Novel mouse monoclonal antibodies specifically recognizing \u03b2-(1\u21923)-D-glucan antigen","volume":"14","author":"Matveev","year":"2019","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0085","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0005392","article-title":"Protection by anti-beta-glucan antibodies is associated with restricted beta-1,3 glucan binding specificity and inhibition of fungal growth and adherence","volume":"4","author":"Torosantucci","year":"2009","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0090","doi-asserted-by":"crossref","DOI":"10.3390\/antib9040053","article-title":"Structure, function, and therapeutic use of IgM antibodies","volume":"9","author":"Keyt","year":"2020","journal-title":"Antibodies"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0095","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1084\/jem.20050749","article-title":"A novel glyco-conjugate vaccine against fungal pathogens","volume":"202","author":"Torosantucci","year":"2005","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0100","doi-asserted-by":"crossref","first-page":"5085","DOI":"10.1128\/IAI.00278-07","article-title":"An anti-beta-glucan monoclonal antibody inhibits growth and capsule formation of Cryptococcus neoformans in vitro and exerts therapeutic, anticryptococcal activity in vivo","volume":"75","author":"Rachini","year":"2007","journal-title":"Infect. Immun."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0105","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.femsim.2004.12.012","article-title":"Role of anti-beta-glucan antibody in host defense against fungi","volume":"44","author":"Ishibashi","year":"2005","journal-title":"FEMS Immunol. Med. Microbiol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0110","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0276786","article-title":"Development and in vitro characterization of a humanized scFv against fungal infections","volume":"17","author":"Di Mambro","year":"2022","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0115","author":"Di Mambro"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0120","doi-asserted-by":"crossref","first-page":"19500","DOI":"10.1038\/s41598-021-98659-5","article-title":"A new humanized antibody is effective against pathogenic fungi in vitro","volume":"11","author":"Di Mambro","year":"2021","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0125","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1038\/s44259-026-00198-4","article-title":"Candidozyma auris-infected galleria mellonella larvae: the effect of the humanized monoclonal antibody Dia-T51 and its synergy with amphotericin B","volume":"4","author":"Vanzolini","year":"2026","journal-title":"Npj Antimicrob. Resist."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0130","first-page":"13","article-title":"Developability assessment at early-stage discovery to enable development of antibody-derived therapeutics","volume":"6","author":"Zhang","year":"2023","journal-title":"Antib. Ther."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0135","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1007\/978-1-0716-1450-1_4","article-title":"Assessment of therapeutic antibody Developability by combinations of in vitro and in silico methods","volume":"2313","author":"Wolf P\u00e9rez","year":"2022","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0140","doi-asserted-by":"crossref","first-page":"4025","DOI":"10.1073\/pnas.1810576116","article-title":"Five computational developability guidelines for therapeutic antibody profiling","volume":"116","author":"Raybould","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0145","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.xphs.2015.11.002","article-title":"Immunogenicity of therapeutic protein aggregates","volume":"105","author":"Moussa","year":"2016","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0150","doi-asserted-by":"crossref","first-page":"413","DOI":"10.2147\/BTT.S486345","article-title":"Biophysical analysis of therapeutic antibodies in the early development pipeline","volume":"18","author":"Willis","year":"2024","journal-title":"Biol. Targets Ther."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0155","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/j.ejpb.2017.06.029","article-title":"High-concentration protein formulations: how high is high?","volume":"119","author":"Garidel","year":"2017","journal-title":"Eur. J. Pharm. Biopharm. Off. J. Arbeitsgemeinschaft Pharm. Verfahrenstechnik EV"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0160","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.xphs.2019.08.009","article-title":"Physicochemical stability of monoclonal antibodies: a review","volume":"109","author":"Le Basle","year":"2020","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0165","doi-asserted-by":"crossref","first-page":"W315","DOI":"10.1093\/nar\/gky497","article-title":"BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra","volume":"46","author":"Micsonai","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0170","doi-asserted-by":"crossref","first-page":"E3095","DOI":"10.1073\/pnas.1500851112","article-title":"Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy","volume":"112","author":"Micsonai","year":"2015","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0175","first-page":"15151","article-title":"Analysis of the structure of 14 therapeutic antibodies using circular dichroism spectroscopy","volume":"96","author":"Bruque","year":"2024","journal-title":"Anal. Chem."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0180","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/0022-1759(89)90350-5","article-title":"Comparison of immunoglobulin binding capacities and ligand leakage using eight different protein a affinity chromatography matrices","volume":"124","author":"F\u00fcglistaller","year":"1989","journal-title":"J. Immunol. Methods"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0185","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/0161-5890(78)90070-6","article-title":"Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein a-sepharose","volume":"15","author":"Ey","year":"1978","journal-title":"Immunochemistry"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0190","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2020.106332","article-title":"Molecular characteristics and antioxidant activity of laminarin extracted from the seaweed species Laminaria hyperborea, using hydrothermal-assisted extraction and a multi-step purification procedure","volume":"112","author":"Rajauria","year":"2021","journal-title":"Food Hydrocoll."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0195","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1038\/s42003-023-04927-7","article-title":"ImmuneBuilder: deep-learning models for predicting the structures of immune proteins","volume":"6","author":"Abanades","year":"2023","journal-title":"Commun. Biol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0200","doi-asserted-by":"crossref","first-page":"D1140","DOI":"10.1093\/nar\/gkt1043","article-title":"SAbDab: the structural antibody database","volume":"42","author":"Dunbar","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0205","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/0022-2836(71)90324-X","article-title":"The interpretation of protein structures: estimation of static accessibility","volume":"55","author":"Lee","year":"1971","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0210","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0022-2836(76)90191-1","article-title":"The nature of the accessible and buried surfaces in proteins","volume":"105","author":"Chothia","year":"1976","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0215","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1006\/abio.1994.1499","article-title":"Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy","volume":"222","author":"Mach","year":"1994","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0220","doi-asserted-by":"crossref","DOI":"10.1016\/j.ab.2019.113450","article-title":"A method to probe protein structure from UV absorbance spectra","volume":"587","author":"Biter","year":"2019","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0225","doi-asserted-by":"crossref","first-page":"2703","DOI":"10.1002\/jps.20461","article-title":"Solution behavior of a novel type 1 interferon, interferon-tau","volume":"94","author":"Katayama","year":"2005","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0230","doi-asserted-by":"crossref","DOI":"10.1016\/j.heliyon.2023.e21712","article-title":"Determining suitable surfactant concentration ranges to avoid protein unfolding in pharmaceutical formulations using UV analysis","volume":"9","author":"Waters","year":"2023","journal-title":"Heliyon"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0235","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/0005-2795(77)90154-4","article-title":"Second derivative spectrophotometry as an effective tool for examining phenylalanine residues in proteins","volume":"494","author":"Ichikawa","year":"1977","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0240","doi-asserted-by":"crossref","first-page":"19819","DOI":"10.1073\/pnas.0709915104","article-title":"Localizing frustration in native proteins and protein assemblies","volume":"104","author":"Ferreiro","year":"2007","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0245","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/0003-9861(90)90587-O","article-title":"Determination of tryptophan, tyrosine, and phenylalanine by second derivative spectrophotometry","volume":"277","author":"Nozaki","year":"1990","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0250","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1111\/j.1432-1033.1978.tb12622.x","article-title":"Second-derivative spectroscopy of proteins. A method for the quantitative determination of aromatic amino acids in proteins","volume":"90","author":"Balestrieri","year":"1978","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0255","doi-asserted-by":"crossref","first-page":"1518","DOI":"10.1016\/j.jmb.2008.01.093","article-title":"The intrinsic contributions of tyrosine, serine, glycine and arginine to the affinity and specificity of antibodies","volume":"377","author":"Birtalan","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0260","doi-asserted-by":"crossref","first-page":"1871","DOI":"10.1021\/bi00303a044","article-title":"Determination of tyrosine exposure in proteins by second-derivative spectroscopy","volume":"23","author":"Ragone","year":"1984","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0265","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1126\/science.1546293","article-title":"Structural evidence for induced fit as a mechanism for antibody-antigen recognition","volume":"255","author":"Rini","year":"1992","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0270","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/S0968-0004(03)00135-X","article-title":"Conformational diversity and protein evolution \u2013 a 60-year-old hypothesis revisited","volume":"28","author":"James","year":"2003","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0275","doi-asserted-by":"crossref","first-page":"11606","DOI":"10.1021\/ac503140j","article-title":"Circular dichroism spectroscopy as a tool for monitoring aggregation in monoclonal antibody therapeutics","volume":"86","author":"Joshi","year":"2014","journal-title":"Anal. Chem."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0280","article-title":"Oxidation and deamidation of monoclonal antibody products: potential impact on stability, biological activity, and efficacy","volume":"111","author":"Gupta","year":"2021","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0285","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1080\/19420862.2018.1548233","article-title":"Deamidation and isomerization liability analysis of 131 clinical-stage antibodies","volume":"11","author":"Lu","year":"2018","journal-title":"mAbs"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0290","doi-asserted-by":"crossref","first-page":"2192","DOI":"10.1021\/acs.analchem.8b04768","article-title":"Selective tryptophan oxidation of monoclonal antibodies: oxidative stress and modeling prediction","volume":"91","author":"Pavon","year":"2019","journal-title":"Anal. Chem."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0295","doi-asserted-by":"crossref","first-page":"2192","DOI":"10.1021\/acs.analchem.8b04768","article-title":"Selective tryptophan oxidation of monoclonal antibodies: oxidative stress and modeling prediction","volume":"91","author":"Pavon","year":"2019","journal-title":"Anal. Chem."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0300","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1007\/s11095-018-2545-8","article-title":"Impact of tryptophan oxidation in complementarity-determining regions of two monoclonal antibodies on structure-function characterized by hydrogen-deuterium exchange mass spectrometry and surface Plasmon resonance","volume":"36","author":"Hageman","year":"2019","journal-title":"Pharm. Res."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0305","doi-asserted-by":"crossref","first-page":"1525","DOI":"10.1080\/19420862.2016.1231277","article-title":"Oxidation in the complementarity-determining regions differentially influences the properties of therapeutic antibodies","volume":"8","author":"Dashivets","year":"2016","journal-title":"mAbs"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0310","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0100736","article-title":"Structure-based prediction of asparagine and aspartate degradation sites in antibody variable regions","volume":"9","author":"Sydow","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0315","doi-asserted-by":"crossref","first-page":"4367","DOI":"10.1073\/pnas.071066498","article-title":"Prediction of protein deamidation rates from primary and three-dimensional structure","volume":"98","author":"Robinson","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0320","doi-asserted-by":"crossref","unstructured":"Y. Yan, S. Tang, S. Wang, N. Li, Assessing the impact of CDR Deamidation and isomerization on mAb target binding using affinity-resolved 2D-SEC-SCX-MS analysis, J. Am. Soc. Mass Spectrom. 36 (n.d.) 2682\u20132691. doi:https:\/\/doi.org\/10.1021\/jasms.5c00284.","DOI":"10.1021\/jasms.5c00284"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0325","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1011881","article-title":"LAP: liability antibody profiler by sequence & structural mapping of natural and therapeutic antibodies","volume":"20","author":"Sat\u0142awa","year":"2024","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0330","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/jmbi.1998.1843","article-title":"Anatomy of hot spots in protein interfaces","volume":"280","author":"Bogan","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0335","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2013.00302","article-title":"The structural basis of antibody-antigen recognition","volume":"4","author":"Sela-Culang","year":"2013","journal-title":"Front. Immunol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0340","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1080\/19420862.2018.1548233","article-title":"Deamidation and isomerization liability analysis of 131 clinical-stage antibodies","volume":"11","author":"Lu","year":"2019","journal-title":"mAbs"},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0345","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1007\/s11095-025-03825-3","article-title":"In vitro stability study of a panel of commercial antibodies at physiological pH and temperature as a guide to screen biologic candidate molecules for the potential risk of in vivo asparagine Deamidation and activity loss","volume":"42","author":"Garg","year":"2025","journal-title":"Pharm. Res."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0350","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1007\/s12551-016-0218-6","article-title":"Dynamic light scattering: a practical guide and applications in biomedical sciences","volume":"8","author":"Stetefeld","year":"2016","journal-title":"Biophys. Rev."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0355","doi-asserted-by":"crossref","first-page":"3952","DOI":"10.3390\/ijms22083952","article-title":"Monoclonal antibody aggregation associated with free radical induced oxidation","volume":"22","author":"Zheng","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0360","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.ijbiomac.2018.01.099","article-title":"Protein folding, misfolding and aggregation: a tale of constructive to destructive assembly","volume":"112","author":"Khan","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0365","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2025.143725","article-title":"Assessing amyloid fibrils and amorphous aggregates: a review","volume":"311","author":"Basha","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2026.152185_bb0370","doi-asserted-by":"crossref","DOI":"10.1042\/BSR20181415","article-title":"Congo red and amyloids: history and relationship","volume":"39","author":"Yakupova","year":"2019","journal-title":"Biosci. Rep."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813026021124?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813026021124?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,7,4]],"date-time":"2026-07-04T12:51:47Z","timestamp":1783169507000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813026021124"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6]]},"references-count":74,"alternative-id":["S0141813026021124"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2026.152185","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2026,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Predicting the success of an antibody: Biochemical and biophysical characterization of the humanized monoclonal antibody Dia-T51","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2026.152185","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"152185"}}