{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,7]],"date-time":"2026-09-07T20:28:28Z","timestamp":1788812908456,"version":"build-2803163510"},"reference-count":293,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["jpharmsci.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Pharmaceutical Sciences"],"published-print":{"date-parts":[[2025,6]]},"DOI":"10.1016\/j.xphs.2025.103771","type":"journal-article","created":{"date-parts":[[2025,3,25]],"date-time":"2025-03-25T18:34:59Z","timestamp":1742927699000},"page":"103771","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":8,"title":["Highly variable aggregation and glycosylation profiles and their roles in immunogenicity to protein-based therapeutics"],"prefix":"10.1016","volume":"114","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4611-7071","authenticated-orcid":false,"given":"Sina","family":"Sarsarshahi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9404-8176","authenticated-orcid":false,"given":"Sanghati","family":"Bhattacharya","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9157-3469","authenticated-orcid":false,"given":"Zeb R.","family":"Zacharias","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8776-4465","authenticated-orcid":false,"given":"Eman S.","family":"Kamel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5307-9854","authenticated-orcid":false,"given":"Jon C.D.","family":"Houtman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3370-6491","authenticated-orcid":false,"given":"Reza","family":"Nejadnik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0001","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.tibtech.2018.05.014","article-title":"The increasingly Human and profitable monoclonal antibody market","volume":"37","author":"Grilo","year":"2019","journal-title":"Trends Biotechnol"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0002","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1038\/s41587-022-01630-6","article-title":"Fresh from the biotech pipeline: fewer approvals, but biologics gain share","volume":"41","author":"Senior","year":"2023","journal-title":"Nat Biotechnol"},{"key":"10.1016\/j.xphs.2025.103771_bib0003","doi-asserted-by":"crossref","first-page":"113","DOI":"10.12688\/f1000research.9970.1","article-title":"Recent advances in (therapeutic protein) drug development","volume":"6","author":"Lagasse","year":"2017","journal-title":"F1000Res"},{"key":"10.1016\/j.xphs.2025.103771_bib0004","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/bs.mie.2021.04.021","article-title":"Transient expression of recombinant proteins in plants","volume":"660","author":"Nosaki","year":"2021","journal-title":"Methods Enzymol"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0005","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.3899\/jrheum.140538","article-title":"Incidence and management of infusion reactions to Infliximab in a prospective real-world community registry","volume":"42","author":"Choquette","year":"2015","journal-title":"J Rheumatol"},{"key":"10.1016\/j.xphs.2025.103771_bib0006","doi-asserted-by":"crossref","unstructured":"Eastwood D, Findlay L, Poole S, et al. Monoclonal antibody TGN1412 trial failure explained by species differences in CD28 expression on CD4 effector memory T-cells. Br J Pharmacol 2010; 161(3): 512-26.","DOI":"10.1111\/j.1476-5381.2010.00922.x"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0007","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1111\/j.1398-9995.2009.02280.x","article-title":"Anti-infliximab IgE and non-IgE antibodies and induction of infusion-related severe anaphylactic reactions","volume":"65","author":"Vultaggio","year":"2010","journal-title":"Allergy"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0008","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1159\/000336839","article-title":"Drug-specific Th2 cells and IgE antibodies in a patient with anaphylaxis to Rituximab","volume":"159","author":"Vultaggio","year":"2012","journal-title":"Int Arch Allergy Imm"},{"key":"10.1016\/j.xphs.2025.103771_bib0009","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.3389\/fimmu.2020.01301","article-title":"T-cell dependent immunogenicity of protein therapeutics pre-clinical assessment and mitigation-updated consensus and review 2020","volume":"11","author":"Jawa","year":"2020","journal-title":"Front Immunol"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0010","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1111\/j.1365-2222.1979.tb01527.x","article-title":"Anaphylactoid reactions to infusions of plasma-protein and Human-serum albumin - role of aggregated proteins and of stabilizers added during production","volume":"9","author":"Ring","year":"1979","journal-title":"Clin Allergy"},{"key":"10.1016\/j.xphs.2025.103771_bib0011","doi-asserted-by":"crossref","unstructured":"Ghaderi D, Taylor RE, Padler-Karavani V, Diaz S, Varki A. Implications of the presence of-glycolylneuraminic acid in recombinant therapeutic glycoproteins. Nat Biotechnol 2010; 28(8): 863-U145.","DOI":"10.1038\/nbt.1651"},{"issue":"12","key":"10.1016\/j.xphs.2025.103771_bib0012","doi-asserted-by":"crossref","first-page":"1263","DOI":"10.1080\/1744666X.2020.1684264","article-title":"Hypersensitivity reactions to biologics used in rheumatology","volume":"15","author":"Matucci","year":"2019","journal-title":"Expert Rev Clin Immu"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0013","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1007\/s00005-012-0189-7","article-title":"Immunogenicity to biologics: mechanisms, prediction and reduction","volume":"60","author":"Sethu","year":"2012","journal-title":"Arch Immunol Ther Exp"},{"issue":"10","key":"10.1016\/j.xphs.2025.103771_bib0014","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1016\/j.tibtech.2018.05.008","article-title":"Evaluating and mitigating the immunogenicity of therapeutic proteins","volume":"36","author":"Sauna","year":"2018","journal-title":"Trends Biotechnol"},{"issue":"8","key":"10.1016\/j.xphs.2025.103771_bib0015","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1080\/1744666X.2019.1630273","article-title":"Therapeutic drug monitoring with biologic agents in immune mediated inflammatory diseases","volume":"15","author":"Papamichael","year":"2019","journal-title":"Expert Rev Clin Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0016","doi-asserted-by":"crossref","first-page":"601","DOI":"10.3389\/fimmu.2019.00601","article-title":"Evaluation of in vitro assays to assess the modulation of dendritic cells functions by therapeutic antibodies and aggregates","volume":"10","author":"Morgan","year":"2019","journal-title":"Front Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0017","doi-asserted-by":"crossref","first-page":"1951","DOI":"10.3389\/fimmu.2020.01951","article-title":"The molecular mechanisms that underlie the immune biology of anti-drug antibody formation following treatment with monoclonal antibodies","volume":"11","author":"Vaisman-Mentesh","year":"2020","journal-title":"Front Immunol"},{"issue":"8","key":"10.1016\/j.xphs.2025.103771_bib0018","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1038\/ni.1900","article-title":"Control systems and decision making for antibody production","volume":"11","author":"Goodnow","year":"2010","journal-title":"Nat Immunol"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0019","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1007\/s281-001-8167-7","article-title":"Naive and memory B cells in T-cell-dependent and T-independent responses","volume":"23","author":"Zubler","year":"2001","journal-title":"Springer Semin Immunopathol"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0020","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1007\/s11095-011-0414-9","article-title":"Coupling of aggregation and immunogenicity in biotherapeutics: T- and B-cell immune epitopes may contain aggregation-prone regions","volume":"28","author":"Kumar","year":"2011","journal-title":"Pharm Res"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0021","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1038\/ni.2194","article-title":"B cell-helper neutrophils stimulate the diversification and production of immunoglobulin in the marginal zone of the spleen","volume":"13","author":"Puga","year":"2011","journal-title":"Nat Immunol"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0022","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1007\/s40259-023-00641-2","article-title":"Reducing immunogenicity by design: approaches to minimize immunogenicity of monoclonal antibodies","volume":"38","author":"Harris","year":"2024","journal-title":"BioDrugs"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0023","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1016\/j.coi.2011.03.004","article-title":"T cell-independent B cell memory","volume":"23","author":"Defrance","year":"2011","journal-title":"Curr Opin Immunol"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0024","doi-asserted-by":"crossref","first-page":"131","DOI":"10.2174\/138945009787354511","article-title":"Reducing the immunogenicity of protein therapeutics","volume":"10","author":"Onda","year":"2009","journal-title":"Curr Drug Targets"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0025","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1039\/D1CB00067E","article-title":"Aggregation of protein therapeutics enhances their immunogenicity: causes and mitigation strategies","volume":"2","author":"Lundahl","year":"2021","journal-title":"RSC Chem Biol"},{"issue":"10","key":"10.1016\/j.xphs.2025.103771_bib0026","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1111\/apt.12507","article-title":"Review article: immunogenicity of anti-TNF biologics in IBD - the role of patient, product and prescriber factors","volume":"38","author":"Moss","year":"2013","journal-title":"Aliment Pharmacol Ther"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0027","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1038\/nrrheum.2013.4","article-title":"Immunogenicity of anti-TNF biologic therapies for rheumatoid arthritis","volume":"9","author":"Van Schouwenburg","year":"2013","journal-title":"Nat Rev Rheumatol"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0028","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1002\/jps.22276","article-title":"Impact of product-related factors on immunogenicity of biotherapeutics","volume":"100","author":"Singh","year":"2011","journal-title":"J Pharm Sci"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0029","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1182\/blood-2008-02-124941","article-title":"Dynamics of factor VIII interactions determine its immunologic fate in hemophilia A","volume":"112","author":"Lacroix-Desmazes","year":"2008","journal-title":"Blood"},{"issue":"28","key":"10.1016\/j.xphs.2025.103771_bib0030","doi-asserted-by":"crossref","first-page":"25118","DOI":"10.1074\/jbc.M110.160457","article-title":"Classification and characterization of therapeutic antibody aggregates","volume":"286","author":"Joubert","year":"2011","journal-title":"J Biol Chem"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0031","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0086322","article-title":"Aggregation of human recombinant monoclonal antibodies influences the capacity of dendritic cells to stimulate adaptive T-cell responses in vitro","volume":"9","author":"Rombach-Riegraf","year":"2014","journal-title":"PLoS One"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0032","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.cellimm.2015.03.002","article-title":"Therapeutic outcomes, assessments, risk factors and mitigation efforts of immunogenicity of therapeutic protein products","volume":"295","author":"Yin","year":"2015","journal-title":"Cell Immunol"},{"issue":"10","key":"10.1016\/j.xphs.2025.103771_bib0033","doi-asserted-by":"crossref","first-page":"1394","DOI":"10.1023\/A:1012168621337","article-title":"Development and use of enzyme-linked immunosorbent assays (ELISA) for the detection of protein aggregates in interferon-alpha (IFN-alpha) formulations","volume":"14","author":"Braun","year":"1997","journal-title":"Pharm Res"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0034","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1016\/j.xphs.2019.10.064","article-title":"Shocking data on parcel shipments of protein solutions","volume":"109","author":"Siska","year":"2020","journal-title":"J Pharm Sci"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0035","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1016\/j.xphs.2019.10.050","article-title":"Mechanical shock during shipping of medications: the roles of packaging and transportation vendors","volume":"109","author":"Dill","year":"2020","journal-title":"J Pharm Sci"},{"issue":"8","key":"10.1016\/j.xphs.2025.103771_bib0036","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.1016\/j.xphs.2018.04.005","article-title":"Postproduction handling and administration of protein pharmaceuticals and potential instability issues","volume":"107","author":"Nejadnik","year":"2018","journal-title":"J Pharm Sci"},{"issue":"12","key":"10.1016\/j.xphs.2025.103771_bib0037","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1007\/s11095-005-8177-9","article-title":"Structural characterization and immunogenicity in wild-type and immune tolerant mice of degraded recombinant human interferon alpha2b","volume":"22","author":"Hermeling","year":"2005","journal-title":"Pharm Res"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0038","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1002\/jps.24292","article-title":"Assessment of the immunogenicity of mechanically induced interferon aggregates in a transgenic mouse model","volume":"104","author":"Human","year":"2015","journal-title":"J Pharm Sci"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0039","doi-asserted-by":"crossref","first-page":"740","DOI":"10.4161\/mabs.22066","article-title":"Immunogenicity of different stressed IgG monoclonal antibody formulations in immune tolerant transgenic mice","volume":"4","author":"Filipe","year":"2012","journal-title":"MAbs"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0040","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1007\/s11095-014-1472-6","article-title":"Investigation of the immunogenicity of different types of aggregates of a murine monoclonal antibody in mice","volume":"32","author":"Freitag","year":"2015","journal-title":"Pharm Res"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0041","doi-asserted-by":"crossref","first-page":"1454","DOI":"10.1007\/s11095-011-0621-4","article-title":"Tungsten-induced denaturation and aggregation of epoetin alfa during primary packaging as a cause of immunogenicity","volume":"29","author":"Seidl","year":"2012","journal-title":"Pharm Res"},{"issue":"11","key":"10.1016\/j.xphs.2025.103771_bib0042","doi-asserted-by":"crossref","first-page":"4953","DOI":"10.1002\/jps.22683","article-title":"Glass particles as an adjuvant: A model for adverse immunogenicity of therapeutic proteins","volume":"100","author":"Fradkin","year":"2011","journal-title":"J Pharm Sci"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0043","doi-asserted-by":"crossref","first-page":"1812","DOI":"10.1007\/s11095-010-0172-0","article-title":"Aggregated recombinant human interferon beta induces antibodies but no memory in immune-tolerant transgenic mice","volume":"27","author":"van Beers","year":"2010","journal-title":"Pharm Res"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0044","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1002\/jps.20529","article-title":"Influence of aggregation on immunogenicity of recombinant human factor VIII in hemophilia A mice","volume":"95","author":"Purohit","year":"2006","journal-title":"J Pharm Sci"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0045","doi-asserted-by":"crossref","first-page":"2055","DOI":"10.1002\/jps.23091","article-title":"Native-like aggregates of factor VIII are immunogenic in von Willebrand factor deficient and hemophilia a mice","volume":"101","author":"Pisal","year":"2012","journal-title":"J Pharm Sci"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0046","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1210\/jcem-51-4-691","article-title":"Role of aggregated Human growth-hormone (Hgh) in development of antibodies to hgh","volume":"51","author":"Moore","year":"1980","journal-title":"J Clin Endocr Metab"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0047","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"},{"issue":"30","key":"10.1016\/j.xphs.2025.103771_bib0048","doi-asserted-by":"crossref","first-page":"25266","DOI":"10.1074\/jbc.M111.330902","article-title":"Highly aggregated antibody therapeutics can enhance the in vitro innate and late-stage T-cell immune responses","volume":"287","author":"Joubert","year":"2012","journal-title":"J Biol Chem"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0049","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1007\/s11095-014-1541-x","article-title":"Small amounts of sub-visible aggregates enhance the immunogenic potential of monoclonal antibody therapeutics","volume":"32","author":"Ahmadi","year":"2015","journal-title":"Pharm Res"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0050","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1080\/19420862.2018.1551044","article-title":"Influence of N-glycosylation on effector functions and thermal stability of glycoengineered IgG1 monoclonal antibody with homogeneous glycoforms","volume":"11","author":"Wada","year":"2019","journal-title":"MAbs"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0051","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1002\/jps.2600840108","article-title":"Physical stabilization of insulin by glycosylation","volume":"84","author":"Baudys","year":"1995","journal-title":"J Pharm Sci"},{"key":"10.1016\/j.xphs.2025.103771_bib0052","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.jpba.2017.12.061","article-title":"Influence of glycan modification on IgG1 biochemical and biophysical properties","volume":"151","author":"Pawlowski","year":"2018","journal-title":"J Pharm Biomed Anal"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0053","doi-asserted-by":"crossref","first-page":"568","DOI":"10.4161\/mabs.3.6.17922","article-title":"The impact of glycosylation on monoclonal antibody conformation and stability","volume":"3","author":"Zheng","year":"2011","journal-title":"MAbs"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0054","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1111\/imm.13481","article-title":"Therapeutic antibody glycosylation impacts antigen recognition and immunogenicity","volume":"166","author":"Wolf","year":"2022","journal-title":"Immunology"},{"key":"10.1016\/j.xphs.2025.103771_bib0055","doi-asserted-by":"crossref","first-page":"725","DOI":"10.3389\/fimmu.2020.00725","article-title":"Immunogenicity of bioproducts: cellular models to evaluate the impact of therapeutic antibody aggregates","volume":"11","author":"Nabhan","year":"2020","journal-title":"Front Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0056","article-title":"Clear and present danger? Engineered nanoparticles and the immune system","volume":"142","author":"Fadeel","year":"2012","journal-title":"Swiss Med Wkly"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0057","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1038\/s41392-021-00687-0","article-title":"Pattern recognition receptors in health and diseases","volume":"6","author":"Li","year":"2021","journal-title":"Signal Transduct Target Ther"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0058","doi-asserted-by":"crossref","DOI":"10.3390\/cancers11030418","article-title":"Use of dendritic cell receptors as targets for enhancing anti-cancer immune responses","volume":"11","author":"Hossain","year":"2019","journal-title":"Cancers"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0059","doi-asserted-by":"crossref","first-page":"1866","DOI":"10.1002\/jps.24444","article-title":"Antibody glycosylation and its impact on the pharmacokinetics and pharmacodynamics of monoclonal antibodies and Fc-fusion proteins","volume":"104","author":"Liu","year":"2015","journal-title":"J Pharm Sci"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0060","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1038\/nri.2017.142","article-title":"NF-kappaB, inflammation, immunity and cancer: coming of age","volume":"18","author":"Taniguchi","year":"2018","journal-title":"Nat Rev Immunol"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0061","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-018-29850-4","article-title":"Aggregates of IVIG or Avastin, but not HSA, modify the response to model innate immune response modulating impurities","volume":"8","author":"Polumuri","year":"2018","journal-title":"Sci Rep"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0062","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/j.xphs.2019.09.007","article-title":"Growth hormone aggregates activation of human dendritic cells is controlled by Rac1 and PI3 kinase signaling pathways","volume":"109","author":"Nabhan","year":"2020","journal-title":"J Pharm Sci"},{"key":"10.1016\/j.xphs.2025.103771_bib0063","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2024.1360369","article-title":"An updated management approach of Pompe disease patients with high-sustained anti-rhGAA IgG antibody titers: experience with bortezomib-based immunomodulation","volume":"15","author":"Desai","year":"2024","journal-title":"Front Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0064","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2020.614856","article-title":"Editorial: immunogenicity of proteins used as therapeutics","volume":"11","author":"Sauna","year":"2020","journal-title":"Front Immunol"},{"issue":"10","key":"10.1016\/j.xphs.2025.103771_bib0065","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1007\/s00066-019-01497-8","article-title":"An evaluation of the effect of bortezomib on radiation-induced urinary bladder dysfunction","volume":"195","author":"Sarsarshahi","year":"2019","journal-title":"Strahlenther Onkol"},{"issue":"8","key":"10.1016\/j.xphs.2025.103771_bib0066","doi-asserted-by":"crossref","first-page":"2894","DOI":"10.1016\/j.xphs.2021.04.005","article-title":"Subvisible particles in solutions of remicade in intravenous saline activate immune system pathways in in vitro human cell systems","volume":"110","author":"Pardeshi","year":"2021","journal-title":"J Pharm Sci"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0067","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1038\/icb.2016.100","article-title":"Effect of growth hormone and IgG aggregates on dendritic cells activation and T-cells polarization","volume":"95","author":"Gallais","year":"2017","journal-title":"Immunol Cell Biol"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0068","doi-asserted-by":"crossref","first-page":"1736","DOI":"10.1007\/s11095-016-1914-4","article-title":"Physical characterization and innate immunogenicity of aggregated intravenous immunoglobulin (IGIV) in an in vitro cell-based model","volume":"33","author":"Moussa","year":"2016","journal-title":"Pharm Res"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0069","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1016\/j.xphs.2019.10.046","article-title":"Fcgamma receptor activation by human monoclonal antibody aggregates","volume":"109","author":"Tada","year":"2020","journal-title":"J Pharm Sci"},{"key":"10.1016\/j.xphs.2025.103771_bib0070","doi-asserted-by":"crossref","DOI":"10.1016\/j.jim.2021.113147","article-title":"Comparability study of monocyte derived dendritic cells, primary monocytes, and THP1 cells for innate immune responses","volume":"498","author":"Wen","year":"2021","journal-title":"J Immunol Methods"},{"issue":"14","key":"10.1016\/j.xphs.2025.103771_bib0071","doi-asserted-by":"crossref","first-page":"1656","DOI":"10.1016\/j.molimm.2011.04.024","article-title":"Complement activation by (auto-) antibodies","volume":"48","author":"Daha","year":"2011","journal-title":"Mol Immunol"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0072","doi-asserted-by":"crossref","first-page":"4287","DOI":"10.1073\/pnas.0910609107","article-title":"Mature dendritic cells use endocytic receptors to capture and present antigens","volume":"107","author":"Platt","year":"2010","journal-title":"Proc Natl Acad Sci USA"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0073","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1016\/j.clim.2013.09.006","article-title":"T-cell dependent immunogenicity of protein therapeutics: preclinical assessment and mitigation","volume":"149","author":"Jawa","year":"2013","journal-title":"Clin Immunol"},{"issue":"8","key":"10.1016\/j.xphs.2025.103771_bib0074","doi-asserted-by":"crossref","first-page":"3303","DOI":"10.1182\/blood-2008-02-138073","article-title":"Activation of natural regulatory T cells by IgG Fc-derived peptide \"tregitopes\"","volume":"112","author":"De Groot","year":"2008","journal-title":"Blood"},{"key":"10.1016\/j.xphs.2025.103771_bib0075","doi-asserted-by":"crossref","first-page":"2469","DOI":"10.3389\/fimmu.2018.02469","article-title":"Regulation of the germinal center response","volume":"9","author":"Stebegg","year":"2018","journal-title":"Front Immunol"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0076","doi-asserted-by":"crossref","DOI":"10.1080\/19420862.2019.1707418","article-title":"T cell epitope mapping of secukinumab and ixekizumab in healthy donors","volume":"12","author":"Spindeldreher","year":"2020","journal-title":"MAbs"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0077","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1038\/s41423-019-0304-3","article-title":"Impact of human sequences in variable domains of therapeutic antibodies on the location of CD4 T-cell epitopes","volume":"17","author":"Meunier","year":"2020","journal-title":"Cell Mol Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0078","doi-asserted-by":"crossref","first-page":"500","DOI":"10.3389\/fimmu.2017.00500","article-title":"Characterization of CD4 T cell epitopes of infliximab and rituximab identified from healthy donors","volume":"8","author":"Hamze","year":"2017","journal-title":"Front Immunol"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0079","doi-asserted-by":"crossref","first-page":"254","DOI":"10.4161\/mabs.1.3.8035","article-title":"Potential aggregation prone regions in biotherapeutics: a survey of commercial monoclonal antibodies","volume":"1","author":"Wang","year":"2009","journal-title":"MAbs"},{"issue":"8","key":"10.1016\/j.xphs.2025.103771_bib0080","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0159328","article-title":"Use of in vitro assays to assess immunogenicity risk of antibody-based biotherapeutics","volume":"11","author":"Joubert","year":"2016","journal-title":"PLoS One"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0081","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0178544","article-title":"Quantitative analysis of the CD4+ T cell response to therapeutic antibodies in healthy donors using a novel T cell:PBMC assay","volume":"12","author":"Schultz","year":"2017","journal-title":"PLoS One"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0082","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/j.cell.2019.03.016","article-title":"B cell responses: cell interaction dynamics and decisions","volume":"177","author":"Cyster","year":"2019","journal-title":"Cell"},{"key":"10.1016\/j.xphs.2025.103771_bib0083","doi-asserted-by":"crossref","first-page":"775","DOI":"10.3389\/fimmu.2017.00775","article-title":"TLR7\/TLR9- and B cell receptor-signaling crosstalk: promotion of potentially dangerous B cells","volume":"8","author":"Suthers","year":"2017","journal-title":"Front Immunol"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0084","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.immuni.2012.08.002","article-title":"Regulation of humoral immunity by complement","volume":"37","author":"Carroll","year":"2012","journal-title":"Immunity"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0085","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1038\/nri3383","article-title":"Marginal zone B cells: virtues of innate-like antibody-producing lymphocytes","volume":"13","author":"Cerutti","year":"2013","journal-title":"Nat Rev Immunol"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0086","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1007\/s11095-019-2586-7","article-title":"Impact of a heat shock protein impurity on the immunogenicity of biotherapeutic monoclonal antibodies","volume":"36","author":"Rane","year":"2019","journal-title":"Pharm Res"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0087","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1093\/toxsci\/kfw121","article-title":"Editor's highlight: subvisible aggregates of immunogenic proteins promote a Th1-type response","volume":"153","author":"Ratanji","year":"2016","journal-title":"Toxicol Sci"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0088","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1002\/jps.22790","article-title":"Classification of protein aggregates","volume":"101","author":"Narhi","year":"2012","journal-title":"J Pharm Sci"},{"issue":"31","key":"10.1016\/j.xphs.2025.103771_bib0089","doi-asserted-by":"crossref","first-page":"7133","DOI":"10.1021\/bi00483a001","article-title":"Dominant forces in protein folding","volume":"29","author":"Dill","year":"1990","journal-title":"Biochemistry"},{"issue":"24","key":"10.1016\/j.xphs.2025.103771_bib0090","doi-asserted-by":"crossref","first-page":"14142","DOI":"10.1073\/pnas.95.24.14142","article-title":"A transient expansion of the native state precedes aggregation of recombinant human interferon-gamma","volume":"95","author":"Kendrick","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0091","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.ijbiomac.2006.06.018","article-title":"Control of aggregation in protein refolding: cooperative effects of artificial chaperone and cold temperature","volume":"40","author":"Yazdanparast","year":"2007","journal-title":"Int J Biol Macromol"},{"key":"10.1016\/j.xphs.2025.103771_bib0092","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijpharm.2020.119523","article-title":"Protein aggregation and immunogenicity of biotherapeutics","volume":"585","author":"Pham","year":"2020","journal-title":"Int J Pharm"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0093","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1016\/j.tibtech.2014.05.005","article-title":"Therapeutic protein aggregation: mechanisms, design, and control","volume":"32","author":"Roberts","year":"2014","journal-title":"Trends Biotechnol"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0094","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/j.xphs.2019.10.048","article-title":"Accelerated aggregation studies of monoclonal antibodies: considerations for storage stability","volume":"109","author":"Walchli","year":"2020","journal-title":"J Pharm Sci"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0095","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.ejps.2009.06.001","article-title":"Structural properties of monoclonal antibody aggregates induced by freeze-thawing and thermal stress","volume":"38","author":"Hawe","year":"2009","journal-title":"Eur J Pharmaceut Sci"},{"issue":"30","key":"10.1016\/j.xphs.2025.103771_bib0096","doi-asserted-by":"crossref","first-page":"8939","DOI":"10.1021\/jp4035369","article-title":"Measuring and modeling hemoglobin aggregation below the freezing temperature","volume":"117","author":"Rosa","year":"2013","journal-title":"J Phys Chem B"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0097","doi-asserted-by":"crossref","first-page":"1292","DOI":"10.1021\/acs.molpharmaceut.6b00816","article-title":"Extensive chemical modifications in the primary protein structure of IgG1 subvisible particles are necessary for breaking immune tolerance","volume":"14","author":"Boll","year":"2017","journal-title":"Mol Pharm"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0098","doi-asserted-by":"crossref","first-page":"2344","DOI":"10.1007\/s11095-015-1627-0","article-title":"The immunogenicity of antibody aggregates in a novel transgenic mouse model","volume":"32","author":"Bessa","year":"2015","journal-title":"Pharm Res"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0099","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/j.xphs.2022.09.022","article-title":"Relationship between aggregation of therapeutic proteins and agitation parameters: acceleration and frequency","volume":"112","author":"Kizuki","year":"2023","journal-title":"J Pharm Sci"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0100","doi-asserted-by":"crossref","first-page":"2743","DOI":"10.1016\/j.xphs.2021.02.029","article-title":"Machine learning and accelerated stress approaches to differentiate potential causes of aggregation in polyclonal antibody formulations during shipping","volume":"110","author":"Witeof","year":"2021","journal-title":"J Pharm Sci"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0101","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1016\/j.xphs.2021.09.027","article-title":"Miniaturized forced degradation of therapeutic proteins and ADCs by agitation-induced aggregation using orbital shaking of microplates","volume":"111","author":"Johann","year":"2022","journal-title":"J Pharm Sci"},{"key":"10.1016\/j.xphs.2025.103771_bib0102","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1016\/j.ejpb.2017.07.006","article-title":"The film tells the story: physical-chemical characteristics of IgG at the liquid-air interface","volume":"119","author":"Koepf","year":"2017","journal-title":"Eur J Pharm Biopharm"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0103","doi-asserted-by":"crossref","first-page":"1601","DOI":"10.1002\/jps.23973","article-title":"Protein aggregation and particle formation in prefilled glass syringes","volume":"103","author":"Gerhardt","year":"2014","journal-title":"J Pharm Sci"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0104","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1002\/jps.24184","article-title":"Effects of syringe material and silicone oil lubrication on the stability of pharmaceutical proteins","volume":"104","author":"Krayukhina","year":"2015","journal-title":"J Pharm Sci"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0105","doi-asserted-by":"crossref","first-page":"3167","DOI":"10.1002\/jps.21719","article-title":"Silicone oil- and agitation-induced aggregation of a monoclonal antibody in aqueous solution","volume":"98","author":"Thirumangalathu","year":"2009","journal-title":"J Pharm Sci"},{"key":"10.1016\/j.xphs.2025.103771_bib0106","doi-asserted-by":"crossref","first-page":"109","DOI":"10.3389\/fimmu.2015.00109","article-title":"Immunogenicity of anti-TNF-alpha biotherapies: II. Clinical relevance of methods used for anti-drug antibody detection","volume":"6","author":"Bendtzen","year":"2015","journal-title":"Front Immunol"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0107","doi-asserted-by":"crossref","first-page":"256","DOI":"10.4161\/mabs.2.3.11641","article-title":"The immunogenicity of humanized and fully human antibodies residual immunogenicity resides in the CDR regions","volume":"2","author":"Harding","year":"2010","journal-title":"MAbs"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0108","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1002\/j.1460-2075.1985.tb03709.x","article-title":"The generative grammar of the immune system","volume":"4","author":"Jerne","year":"1985","journal-title":"EMBO J"},{"key":"10.1016\/j.xphs.2025.103771_bib0109","doi-asserted-by":"crossref","DOI":"10.1016\/j.cellimm.2020.104235","article-title":"Immunogenic properties of immunoglobulin superfamily members within complex biological networks","volume":"358","author":"Odales","year":"2020","journal-title":"Cell Immunol"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0110","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.xphs.2019.05.031","article-title":"Considerations for the design of antibody-based therapeutics","volume":"109","author":"Goulet","year":"2020","journal-title":"J Pharm Sci"},{"key":"10.1016\/j.xphs.2025.103771_bib0111","doi-asserted-by":"crossref","DOI":"10.1155\/2016\/3072586","article-title":"Understanding the supersensitive anti-drug antibody assay: unexpected high anti-drug antibody incidence and its clinical relevance","volume":"2016","author":"Song","year":"2016","journal-title":"J Immunol Res"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0112","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1208\/s12248-014-9599-2","article-title":"Assessment and reporting of the clinical immunogenicity of therapeutic proteins and peptides-harmonized terminology and tactical recommendations","volume":"16","author":"Shankar","year":"2014","journal-title":"AAPS J"},{"issue":"10","key":"10.1016\/j.xphs.2025.103771_bib0113","doi-asserted-by":"crossref","first-page":"1633","DOI":"10.1093\/ibd\/izac200","article-title":"Systematic review and meta-analysis: loss of response and need for dose escalation of Infliximab and Adalimumab in ulcerative colitis","volume":"29","author":"Savelkoul","year":"2023","journal-title":"Inflamm Bowel Dis"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0114","doi-asserted-by":"crossref","first-page":"2637","DOI":"10.1002\/prot.23085","article-title":"Mutational analysis of domain antibodies reveals aggregation hotspots within and near the complementarity determining regions","volume":"79","author":"Perchiacca","year":"2011","journal-title":"Proteins"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0115","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.ijpharm.2010.02.025","article-title":"Protein aggregation\u2013pathways and influencing factors","volume":"390","author":"Wang","year":"2010","journal-title":"Int J Pharm"},{"issue":"1-2","key":"10.1016\/j.xphs.2025.103771_bib0116","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.ijpharm.2018.08.043","article-title":"Protein aggregation - mechanisms, detection, and control","volume":"550","author":"Wang","year":"2018","journal-title":"Int J Pharm"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0117","doi-asserted-by":"crossref","first-page":"874","DOI":"10.1080\/19420862.2017.1320463","article-title":"Infliximab crystal structures reveal insights into self-association","volume":"9","author":"Lerch","year":"2017","journal-title":"MAbs"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0118","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1038\/s41584-020-00540-8","article-title":"Immunogenicity of biologic agents in rheumatology","volume":"17","author":"Strand","year":"2021","journal-title":"Nat Rev Rheumatol"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0119","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1093\/jb\/mvaa116","article-title":"Glycosylation decreases aggregation and immunogenicity of adalimumab Fab secreted from Pichia pastoris","volume":"169","author":"Nakamura","year":"2021","journal-title":"J Biochem"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0120","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1007\/s40259-017-0231-8","article-title":"Immunogenicity of biologics in chronic inflammatory diseases: a systematic review","volume":"31","author":"Strand","year":"2017","journal-title":"BioDrugs"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0121","doi-asserted-by":"crossref","first-page":"428","DOI":"10.4161\/mabs.12304","article-title":"Characterization of golimumab, a human monoclonal antibody specific for human tumor necrosis factor alpha","volume":"2","author":"Shealy","year":"2010","journal-title":"MAbs"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0122","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1373\/clinchem.2015.242875","article-title":"Immunogenicity assessment of tumor necrosis factor antagonists in the clinical laboratory","volume":"62","author":"Lazar-Molnar","year":"2016","journal-title":"Clin Chem"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0123","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1007\/s40744-019-0157-3","article-title":"Immunogenicity of Sarilumab monotherapy in patients with rheumatoid arthritis who were inadequate responders or intolerant to disease-modifying antirheumatic drugs","volume":"6","author":"Wells","year":"2019","journal-title":"Rheumatol Ther"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0124","doi-asserted-by":"crossref","DOI":"10.3390\/antib5030019","article-title":"Antibody aggregation: insights from sequence and structure","volume":"5","author":"Li","year":"2016","journal-title":"Antibodies"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0125","doi-asserted-by":"crossref","DOI":"10.1080\/19420862.2020.1791399","article-title":"A general evidence-based sequence variant control limit for recombinant therapeutic protein development","volume":"12","author":"Zhang","year":"2020","journal-title":"MAbs"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0126","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0128940","article-title":"Amino acid substitutions improve the immunogenicity of H7N7HA protein and protect mice against lethal H7N7 viral challenge","volume":"10","author":"Kumar","year":"2015","journal-title":"PLoS One"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0127","doi-asserted-by":"crossref","first-page":"2909","DOI":"10.1002\/jps.21566","article-title":"Protein aggregation: pathways, induction factors and analysis","volume":"98","author":"Mahler","year":"2009","journal-title":"J Pharm Sci"},{"key":"10.1016\/j.xphs.2025.103771_bib0128","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.molimm.2018.11.020","article-title":"Identification of B cell epitopes enhanced by protein unfolding and aggregation","volume":"105","author":"Eyes","year":"2019","journal-title":"Mol Immunol"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0129","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1089\/jir.2015.0108","article-title":"Immunogenicity of recombinant human interferon beta-1b in immune-tolerant transgenic mice corresponds with the biophysical characteristics of aggregates","volume":"36","author":"Abdolvahab","year":"2016","journal-title":"J Interferon Cytokine Res"},{"issue":"11","key":"10.1016\/j.xphs.2025.103771_bib0130","doi-asserted-by":"crossref","first-page":"3691","DOI":"10.1002\/jps.24592","article-title":"The effect of small oligomeric protein aggregates on the immunogenicity of intravenous and subcutaneous administered antibodies","volume":"104","author":"Fathallah","year":"2015","journal-title":"J Pharm Sci"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0131","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1007\/s11095-018-2368-7","article-title":"Formulation stabilization and disaggregation of bevacizumab, ranibizumab and aflibercept in dilute solutions","volume":"35","author":"Giannos","year":"2018","journal-title":"Pharm Res"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0132","doi-asserted-by":"crossref","first-page":"1521","DOI":"10.1016\/j.xphs.2018.01.021","article-title":"Sweeping of adsorbed therapeutic protein on prefillable syringes promotes micron aggregate generation","volume":"107","author":"Maruno","year":"2018","journal-title":"J Pharm Sci"},{"issue":"8","key":"10.1016\/j.xphs.2025.103771_bib0133","doi-asserted-by":"crossref","first-page":"3302","DOI":"10.1002\/jps.22097","article-title":"An industry perspective on the monitoring of subvisible particles as a quality attribute for protein therapeutics","volume":"99","author":"Singh","year":"2010","journal-title":"J Pharm Sci"},{"issue":"11","key":"10.1016\/j.xphs.2025.103771_bib0134","doi-asserted-by":"crossref","first-page":"2847","DOI":"10.1016\/j.xphs.2018.06.029","article-title":"Submicron size particles of a murine monoclonal antibody are more immunogenic than soluble oligomers or micron size particles upon subcutaneous administration in mice","volume":"107","author":"Kijanka","year":"2018","journal-title":"J Pharm Sci"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0135","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1007\/s11095-013-1154-9","article-title":"In vivo fluorescence imaging of IgG1 aggregates after subcutaneous and intravenous injection in mice","volume":"31","author":"Filipe","year":"2014","journal-title":"Pharm Res"},{"issue":"10","key":"10.1016\/j.xphs.2025.103771_bib0136","doi-asserted-by":"crossref","first-page":"5278","DOI":"10.4049\/jimmunol.1203131","article-title":"Differential uptake of nanoparticles and microparticles by pulmonary APC subsets induces discrete immunological imprints","volume":"191","author":"Hardy","year":"2013","journal-title":"J Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0137","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.jconrel.2014.06.038","article-title":"Insight into nanoparticle cellular uptake and intracellular targeting","volume":"190","author":"Yameen","year":"2014","journal-title":"J Control Release"},{"key":"10.1016\/j.xphs.2025.103771_bib0138","article-title":"Modulation of immune responses by particle size and shape","volume":"11","author":"Baranov","year":"2020","journal-title":"Front Immunol"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0139","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1038\/s41565-021-00858-8","article-title":"Key principles and methods for studying the endocytosis of biological and nanoparticle therapeutics","volume":"16","author":"Rennick","year":"2021","journal-title":"Nat Nanotechnol"},{"key":"10.1016\/j.xphs.2025.103771_bib0140","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2022.915412","article-title":"Immunogenicity risk assessment of spontaneously occurring therapeutic monoclonal antibody aggregates","volume":"13","author":"Swanson","year":"2022","journal-title":"Front Immunol"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0141","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/0142-9612(88)90033-6","article-title":"Effect of the size and surface charge of polymer microspheres on their phagocytosis by macrophage","volume":"9","author":"Tabata","year":"1988","journal-title":"Biomaterials"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0142","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1002\/eji.200737984","article-title":"Nanoparticles target distinct dendritic cell populations according to their size","volume":"38","author":"Manolova","year":"2008","journal-title":"Eur J Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0143","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijpharm.2022.122490","article-title":"In vitro and in vivo immunogenicity assessment of protein aggregate characteristics","volume":"631","author":"Thorlaksen","year":"2023","journal-title":"Int J Pharm"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0144","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1016\/j.xphs.2019.04.021","article-title":"Monoclonal antibody dimers induced by low pH, heat, or light exposure are not immunogenic upon subcutaneous administration in a mouse model","volume":"109","author":"Kijanka","year":"2020","journal-title":"J Pharm Sci"},{"issue":"25","key":"10.1016\/j.xphs.2025.103771_bib0145","doi-asserted-by":"crossref","first-page":"5128","DOI":"10.1039\/C9SM00751B","article-title":"Entry modes of ellipsoidal nanoparticles on a membrane during clathrin-mediated endocytosis","volume":"15","author":"Deng","year":"2019","journal-title":"Soft Matter"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0146","doi-asserted-by":"crossref","first-page":"2632","DOI":"10.1039\/C5SM01869B","article-title":"Shape-dependent internalization kinetics of nanoparticles by membranes","volume":"12","author":"Chen","year":"2016","journal-title":"Soft Matter"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0147","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1021\/acsnano.8b05340","article-title":"Membrane wrapping efficiency of elastic nanoparticles during endocytosis: size and shape matter","volume":"13","author":"Shen","year":"2019","journal-title":"ACS Nano"},{"issue":"22","key":"10.1016\/j.xphs.2025.103771_bib0148","doi-asserted-by":"crossref","first-page":"6113","DOI":"10.1073\/pnas.1521974113","article-title":"Target shape dependence in a simple model of receptor-mediated endocytosis and phagocytosis","volume":"113","author":"Richards","year":"2016","journal-title":"Proc Natl Acad Sci USA"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0149","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1039\/C9SM02367D","article-title":"Particle engulfment by strongly asymmetric membranes with area reservoirs","volume":"17","author":"Agudo-Canalejo","year":"2021","journal-title":"Soft Matter"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0150","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1007\/s00204-015-1458-0","article-title":"Towards understanding of nanoparticle-protein corona","volume":"89","author":"Ge","year":"2015","journal-title":"Arch Toxicol"},{"issue":"23","key":"10.1016\/j.xphs.2025.103771_bib0151","doi-asserted-by":"crossref","first-page":"11227","DOI":"10.1039\/C9NR02710F","article-title":"Stochastic modeling of nanoparticle internalization and expulsion through receptor-mediated transcytosis","volume":"11","author":"Deng","year":"2019","journal-title":"Nanoscale"},{"key":"10.1016\/j.xphs.2025.103771_bib0152","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.cis.2014.02.012","article-title":"Wrapping of nanoparticles by membranes","volume":"208","author":"Bahrami","year":"2014","journal-title":"Adv Colloid Interface Sci"},{"issue":"41","key":"10.1016\/j.xphs.2025.103771_bib0153","doi-asserted-by":"crossref","first-page":"14684","DOI":"10.1021\/jacs.7b07768","article-title":"Sweet\" architecture-dependent uptake of glycocalyx-mimicking nanoparticles based on biodegradable aliphatic polyesters by macrophages","volume":"139","author":"Wu","year":"2017","journal-title":"J Am Chem Soc"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0154","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1038\/s41567-018-0186-9","article-title":"Physical biology of the cancer cell glycocalyx","volume":"14","author":"Chin-Hun","year":"2018","journal-title":"Nat Phys"},{"issue":"37","key":"10.1016\/j.xphs.2025.103771_bib0155","doi-asserted-by":"crossref","first-page":"7490","DOI":"10.1039\/C9SM00618D","article-title":"Wrapping of a nanowire by a supported lipid membrane","volume":"15","author":"Khosravanizadeh","year":"2019","journal-title":"Soft Matter"},{"issue":"100","key":"10.1016\/j.xphs.2025.103771_bib0156","doi-asserted-by":"crossref","DOI":"10.1098\/rsif.2014.0769","article-title":"Regulation of the membrane wrapping transition of a cylindrical target by cytoskeleton adhesion","volume":"11","author":"Hashemi","year":"2014","journal-title":"J R Soc Interface"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0157","doi-asserted-by":"crossref","first-page":"5350","DOI":"10.1021\/acs.nanolett.8b00786","article-title":"Controlling cargo trafficking in multicomponent membranes","volume":"18","author":"Curk","year":"2018","journal-title":"Nano Lett"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0158","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1007\/s11095-024-03678-2","article-title":"A high threshold of biotherapeutic aggregate numbers is needed to induce an immunogenic response in vitro, in vivo, and in the clinic","volume":"41","author":"Cohen","year":"2024","journal-title":"Pharm Res"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0159","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1016\/j.xphs.2022.02.001","article-title":"Use of In vitro Human skin models to assess potential immune activation In response to biotherapeutic attributes and process-related impurities","volume":"111","author":"Tokuda","year":"2022","journal-title":"J Pharm Sci"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0160","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1016\/j.xphs.2019.09.026","article-title":"Silicone oil particles in prefilled syringes with human monoclonal antibody, representative of real-world drug products, did not increase immunogenicity in in vivo and in vitro model systems","volume":"109","author":"Joh","year":"2020","journal-title":"J Pharm Sci"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0161","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1016\/j.xphs.2019.10.066","article-title":"Characterization of subvisible particles in biotherapeutic prefilled syringes: the role of polysorbate and protein on the formation of silicone oil and protein subvisible particles after drop shock","volume":"109","author":"Jiao","year":"2020","journal-title":"J Pharm Sci"},{"issue":"10","key":"10.1016\/j.xphs.2025.103771_bib0162","doi-asserted-by":"crossref","first-page":"3555","DOI":"10.1002\/jps.23243","article-title":"Workshop on predictive science of the immunogenicity aspects of particles in biopharmaceutical products","volume":"101","author":"Marszal","year":"2012","journal-title":"J Pharm Sci"},{"issue":"12","key":"10.1016\/j.xphs.2025.103771_bib0163","doi-asserted-by":"crossref","first-page":"2817","DOI":"10.1007\/s11095-017-2262-8","article-title":"Chemical and biophysical characteristics of monoclonal antibody solutions containing aggregates formed during metal catalyzed oxidation","volume":"34","author":"Narhi","year":"2017","journal-title":"Pharm Res"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0164","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1002\/jps.24379","article-title":"Physical characterization and in vitro biological impact of highly aggregated antibodies separated into size-enriched populations by fluorescence-activated cell sorting","volume":"104","author":"Telikepalli","year":"2015","journal-title":"J Pharm Sci"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0165","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1042\/BST20170483","article-title":"O-linked mucin-type glycosylation in breast cancer","volume":"46","author":"Burchell","year":"2018","journal-title":"Biochem Soc Trans"},{"key":"10.1016\/j.xphs.2025.103771_bib0166","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2022.1006866","article-title":"Advanced assessment through intact glycopeptide analysis of Infliximab's biologics and biosimilar","volume":"9","author":"Kim","year":"2022","journal-title":"Front Mol Biosci"},{"key":"10.1016\/j.xphs.2025.103771_bib0167","doi-asserted-by":"crossref","DOI":"10.1016\/j.jchromb.2022.123186","article-title":"Correlative N-glycan and charge variant analysis of cetuximab expressed in murine, Chinese hamster and human expression systems","volume":"1194","author":"Trappe","year":"2022","journal-title":"J Chromatogr B Analyt Technol Biomed Life Sci"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0168","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1080\/07388551.2020.1869684","article-title":"Characterization of glycosylation in monoclonal antibodies and its importance in therapeutic antibody development","volume":"41","author":"Kaur","year":"2021","journal-title":"Crit Rev Biotechnol"},{"key":"10.1016\/j.xphs.2025.103771_bib0169","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1007\/978-94-007-1257-7_12","article-title":"The role of glycosylation in therapeutic antibodies","volume":"7","author":"Spearman","year":"2011","journal-title":"Antibody Express Prod"},{"key":"10.1016\/j.xphs.2025.103771_bib0170","doi-asserted-by":"crossref","first-page":"520","DOI":"10.3389\/fimmu.2014.00520","article-title":"IgG subclasses and allotypes: from structure to effector functions","volume":"5","author":"Vidarsson","year":"2014","journal-title":"Front Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0171","doi-asserted-by":"crossref","first-page":"1554","DOI":"10.3389\/fimmu.2017.01554","article-title":"Crystallizable fragment glycoengineering for therapeutic antibodies development","volume":"8","author":"Li","year":"2017","journal-title":"Front Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0172","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2023.114757","article-title":"Enhancing pharmacokinetic and pharmacodynamic properties of recombinant therapeutic proteins by manipulation of sialic acid content","volume":"163","author":"Chia","year":"2023","journal-title":"Biomed Pharmacother"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0173","doi-asserted-by":"crossref","DOI":"10.3390\/antib11010005","article-title":"New opportunities in glycan engineering for therapeutic proteins","volume":"11","author":"Zhong","year":"2022","journal-title":"Antibodies"},{"issue":"14","key":"10.1016\/j.xphs.2025.103771_bib0174","doi-asserted-by":"crossref","first-page":"4251","DOI":"10.1111\/febs.15909","article-title":"Recent advances on smart glycoconjugate vaccines in infections and cancer","volume":"289","author":"Anderluh","year":"2022","journal-title":"FEBS J"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0175","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1038\/s41541-021-00409-1","article-title":"Combined effects of glycan chain length and linkage type on the immunogenicity of glycoconjugate vaccines","volume":"6","author":"Anish","year":"2021","journal-title":"NPJ Vaccines"},{"key":"10.1016\/j.xphs.2025.103771_bib0176","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-1-0716-1241-5_1","article-title":"Glycosylation of therapeutic proteins: a critical quality attribute","volume":"2271","author":"Delobel","year":"2021","journal-title":"Methods Mol Biol"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0177","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1038\/s41573-021-00160-1","article-title":"Author correction: the clinical impact of glycobiology: targeting selectins, siglecs and mammalian glycans","volume":"20","author":"Smith","year":"2021","journal-title":"Nat Rev Drug Discov"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0178","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1006\/abio.1997.2036","article-title":"Characterization of monoclonal antibody glycosylation: comparison of expression systems and identification of terminal alpha-linked galactose","volume":"247","author":"Sheeley","year":"1997","journal-title":"Anal Biochem"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0179","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1093\/glycob\/cwm137","article-title":"A plant-derived human monoclonal antibody induces an anti-carbohydrate immune response in rabbits","volume":"18","author":"Jin","year":"2008","journal-title":"Glycobiology"},{"key":"10.1016\/j.xphs.2025.103771_bib0180","doi-asserted-by":"crossref","first-page":"21","DOI":"10.3389\/fimmu.2020.00021","article-title":"Glycosylated biotherapeutics: immunological effects of N-glycolylneuraminic acid","volume":"11","author":"Yehuda","year":"2020","journal-title":"Front Immunol"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0181","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1208\/s12248-016-9878-1","article-title":"Pre-existing antibody: biotherapeutic modality-based review","volume":"18","author":"Gorovits","year":"2016","journal-title":"Aaps j"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0182","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1016\/j.xphs.2020.12.003","article-title":"The impact of product and process related critical quality attributes on immunogenicity and adverse immunological effects of biotherapeutics","volume":"110","author":"Wen","year":"2021","journal-title":"J Pharm Sci"},{"key":"10.1016\/j.xphs.2025.103771_bib0183","doi-asserted-by":"crossref","DOI":"10.1155\/2016\/6262383","article-title":"Emerging technologies and generic assays for the detection of anti-drug antibodies","volume":"2016","author":"Partridge","year":"2016","journal-title":"J Immunol Res"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0184","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.bbagen.2007.11.003","article-title":"The Galalpha1,3Galbeta1,4GlcNAc-R (alpha-Gal) epitope: a carbohydrate of unique evolution and clinical relevance","volume":"1780","author":"Macher","year":"2008","journal-title":"Biochim Biophys Acta"},{"issue":"15","key":"10.1016\/j.xphs.2025.103771_bib0185","doi-asserted-by":"crossref","first-page":"11451","DOI":"10.1074\/jbc.275.15.11451","article-title":"Beta(1,2)-xylose and alpha(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens","volume":"275","author":"van Ree","year":"2000","journal-title":"J Biol Chem"},{"issue":"3-4","key":"10.1016\/j.xphs.2025.103771_bib0186","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1007\/s10719-015-9590-x","article-title":"Glycan structure and serum half-life of recombinant CTLA4Ig, an immunosuppressive agent, expressed in suspension-cultured rice cells with coexpression of human beta1,4-galactosyltransferase and human CTLA4Ig","volume":"32","author":"Kang","year":"2015","journal-title":"Glycoconj J"},{"issue":"21","key":"10.1016\/j.xphs.2025.103771_bib0187","doi-asserted-by":"crossref","first-page":"8227","DOI":"10.1073\/pnas.86.21.8227","article-title":"Isolation of a cDNA encoding a murine UDPgalactose:beta-D-galactosyl- 1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase: expression cloning by gene transfer","volume":"86","author":"Larsen","year":"1989","journal-title":"Proc Natl Acad Sci USA"},{"issue":"11","key":"10.1016\/j.xphs.2025.103771_bib0188","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1056\/NEJMoa074943","article-title":"Cetuximab-induced anaphylaxis and IgE specific for galactose-\u03b1-1,3-galactose","volume":"358","author":"Chung","year":"2008","journal-title":"N Engl J Med"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0189","first-page":"159","article-title":"Immunomodulation by LFA3TIP, an LFA-3\/IgG1 fusion protein: cell line dependent glycosylation effects on pharmacokinetics and pharmacodynamic markers","volume":"2","author":"Meier","year":"1995","journal-title":"Ther Immunol"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0190","doi-asserted-by":"crossref","first-page":"1366","DOI":"10.1016\/j.xphs.2018.11.029","article-title":"The mechanistic impact of N-glycosylation on stability, pharmacokinetics, and immunogenicity of therapeutic proteins","volume":"108","author":"Zhou","year":"2019","journal-title":"J Pharm Sci"},{"issue":"11","key":"10.1016\/j.xphs.2025.103771_bib0191","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1038\/nbt1110-1153","article-title":"Chinese hamster ovary cells can produce galactose-alpha-1,3-galactose antigens on proteins","volume":"28","author":"Bosques","year":"2010","journal-title":"Nat Biotechnol"},{"issue":"21","key":"10.1016\/j.xphs.2025.103771_bib0192","doi-asserted-by":"crossref","first-page":"8965","DOI":"10.1073\/pnas.0702120104","article-title":"A role for exposed mannosylations in presentation of human therapeutic self-proteins to CD4+ T lymphocytes","volume":"104","author":"Dasgupta","year":"2007","journal-title":"Proc Natl Acad Sci"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0193","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1093\/glycob\/cwn061","article-title":"Strategies for carbohydrate recognition by the mannose 6-phosphate receptors","volume":"18","author":"Dahms","year":"2008","journal-title":"Glycobiology"},{"key":"10.1016\/j.xphs.2025.103771_bib0194","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.128362","article-title":"Unveiling the multifaceted landscape of N-glycosylation in antibody variable domains: insights and implications","volume":"257","author":"Melo-Braga","year":"2024","journal-title":"Int J Biol Macromol"},{"issue":"16","key":"10.1016\/j.xphs.2025.103771_bib0195","doi-asserted-by":"crossref","first-page":"5128","DOI":"10.1039\/C6CS00897F","article-title":"The ENGases: versatile biocatalysts for the production of homogeneous N-linked glycopeptides and glycoproteins","volume":"46","author":"Fairbanks","year":"2017","journal-title":"Chem Soc Rev"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0196","doi-asserted-by":"crossref","DOI":"10.3390\/cancers14040911","article-title":"Glycans as targets for drug delivery in cancer","volume":"14","author":"Diniz","year":"2022","journal-title":"Cancers"},{"issue":"20","key":"10.1016\/j.xphs.2025.103771_bib0197","doi-asserted-by":"crossref","first-page":"15672","DOI":"10.1021\/acs.chemrev.2c00021","article-title":"Synthetic glycans to improve current glycoconjugate vaccines and fight antimicrobial resistance","volume":"122","author":"Del Bino","year":"2022","journal-title":"Chem Rev"},{"issue":"23","key":"10.1016\/j.xphs.2025.103771_bib0198","doi-asserted-by":"crossref","DOI":"10.3390\/cancers14235840","article-title":"Insights into the role of sialylation in cancer metastasis, immunity, and therapeutic opportunity","volume":"14","author":"Huang","year":"2022","journal-title":"Cancers"},{"key":"10.1016\/j.xphs.2025.103771_bib0199","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2022.106267","article-title":"A toolbox of diverse arginine N-glycosylated peptides and specific antibodies","volume":"130","author":"Jiang","year":"2023","journal-title":"Bioorg Chem"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0200","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.1016\/S0021-9258(19)76994-4","article-title":"The role of sialic acid in determining the survival of glycoproteins in the circulation","volume":"246","author":"Morell","year":"1971","journal-title":"J Biol Chem"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0201","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/0020-711X(88)90359-X","article-title":"Clearance of certain modified haptoglobins from the rabbit circulation","volume":"20","author":"Dobryszycka","year":"1988","journal-title":"Int J Biochem"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0202","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.ymgme.2020.02.009","article-title":"Vestronidase alfa: recombinant human beta-glucuronidase as an enzyme replacement therapy for MPS VII","volume":"130","author":"Cadaoas","year":"2020","journal-title":"Mol Genet Metab"},{"issue":"13","key":"10.1016\/j.xphs.2025.103771_bib0203","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/0024-3205(90)90094-8","article-title":"Pharmacokinetic analysis of the plasma disappearance of ovine follitropin and analogues in the male rat","volume":"46","author":"Sebok","year":"1990","journal-title":"Life Sci"},{"key":"10.1016\/j.xphs.2025.103771_bib0204","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.jbiotec.2020.12.016","article-title":"Bifunctional GM-CSF-derived peptides as tools for O-glycoengineering and protein tagging","volume":"327","author":"Sales","year":"2021","journal-title":"J Biotechnol"},{"key":"10.1016\/j.xphs.2025.103771_bib0205","doi-asserted-by":"crossref","DOI":"10.1093\/protein\/gzac010","article-title":"Engineering the enzyme toolbox to tailor glycosylation in small molecule natural products and protein biologics","volume":"36","author":"Ouadhi","year":"2023","journal-title":"Protein Eng Des Sel"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0206","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/s41581-019-0129-4","article-title":"Glycosylation in health and disease","volume":"15","author":"Reily","year":"2019","journal-title":"Nat Rev Nephrol"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0207","doi-asserted-by":"crossref","DOI":"10.3390\/ijms18020131","article-title":"N-glycoprofiling analysis for carbohydrate composition and site-occupancy determination in a poly-glycosylated protein: Human thyrotropin of different origins","volume":"18","author":"Ribela","year":"2017","journal-title":"Int J Mol Sci"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0208","doi-asserted-by":"crossref","first-page":"2557","DOI":"10.1002\/jps.22054","article-title":"Delivery of therapeutic proteins","volume":"99","author":"Pisal","year":"2010","journal-title":"J Pharm Sci"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0209","doi-asserted-by":"crossref","first-page":"212","DOI":"10.2174\/1872211312666180717164758","article-title":"Clinical application of polysialylated deoxyribonuclease and erythropoietin","volume":"12","author":"Meng","year":"2018","journal-title":"Recent Pat Drug Deliv Formul"},{"key":"10.1016\/j.xphs.2025.103771_bib0210","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.addr.2021.01.021","article-title":"Chemical (neo)glycosylation of biological drugs","volume":"171","author":"Walther","year":"2021","journal-title":"Adv Drug Deliv Rev"},{"key":"10.1016\/j.xphs.2025.103771_bib0211","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.ejpb.2019.03.018","article-title":"N-glycans of complex glycosylated biopharmaceuticals and their impact on protein clearance","volume":"139","author":"Higel","year":"2019","journal-title":"Eur J Pharm Biopharm"},{"issue":"14","key":"10.1016\/j.xphs.2025.103771_bib0212","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1182\/blood-2018-09-874636","article-title":"Increased galactose expression and enhanced clearance in patients with low von Willebrand factor","volume":"133","author":"Aguila","year":"2019","journal-title":"Blood"},{"key":"10.1016\/j.xphs.2025.103771_bib0213","article-title":"Glycoengineering of pertuzumab and its impact on the pharmacokinetic\/pharmacodynamic properties","volume":"7","author":"Luo","year":"2017","journal-title":"Sci Rep"},{"key":"10.1016\/j.xphs.2025.103771_bib0214","doi-asserted-by":"crossref","first-page":"S68","DOI":"10.1016\/S0049-3848(16)30370-X","article-title":"Platelet clearance by the hepatic Ashwell-Morrell receptor: mechanisms and biological significance","volume":"141","author":"Hoffmeister","year":"2016","journal-title":"Thromb Res"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0215","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1080\/19420862.2015.1102812","article-title":"A comparison of anti-HER2 IgA and IgG1 in vivo efficacy is facilitated by high N-glycan sialylation of the IgA","volume":"8","author":"Rouwendal","year":"2016","journal-title":"MAbs"},{"issue":"15","key":"10.1016\/j.xphs.2025.103771_bib0216","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.4155\/bio-2019-0124","article-title":"Effects of sialic acid linkage on antibody-fragment crystallizable receptor binding and antibody dependent cytotoxicity depend on levels of fucosylation\/bisecting","volume":"11","author":"Thomann","year":"2019","journal-title":"Bioanalysis"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0217","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1073\/pnas.1417508112","article-title":"A red meat-derived glycan promotes inflammation and cancer progression","volume":"112","author":"Samraj","year":"2015","journal-title":"Proc Natl Acad Sci USA"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0218","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1016\/j.copbio.2009.10.008","article-title":"Expression systems for therapeutic glycoprotein production","volume":"20","author":"Durocher","year":"2009","journal-title":"Curr Opin Biotechnol"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0219","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1016\/j.jaci.2014.12.1947","article-title":"The alpha-gal story: lessons learned from connecting the dots","volume":"135","author":"Steinke","year":"2015","journal-title":"J Allergy Clin Immun"},{"issue":"13","key":"10.1016\/j.xphs.2025.103771_bib0220","doi-asserted-by":"crossref","first-page":"3485","DOI":"10.1073\/pnas.1702173114","article-title":"Modulating IgG effector function by fc glycan engineering","volume":"114","author":"Li","year":"2017","journal-title":"Proc Natl Acad Sci USA"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0221","doi-asserted-by":"crossref","first-page":"3466","DOI":"10.1074\/jbc.M210665200","article-title":"The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity","volume":"278","author":"Shinkawa","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.xphs.2025.103771_bib0222","article-title":"Glycoengineering of pertuzumab and its impact on the pharmacokinetic\/pharmacodynamic properties","volume":"7","author":"Luo","year":"2017","journal-title":"Sci Rep"},{"key":"10.1016\/j.xphs.2025.103771_bib0223","first-page":"1","article-title":"Targeted treatment for chronic lymphocytic leukemia: clinical potential of obinutuzumab","volume":"8","author":"Smolej","year":"2015","journal-title":"Pharmgenomics Pers Med"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0224","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1016\/j.intimp.2007.01.014","article-title":"Quantitative in vivo comparisons of the Fc gamma receptor-dependent agonist activities of different fucosylation variants of an immunoglobulin G antibody","volume":"7","author":"Scallon","year":"2007","journal-title":"Int Immunopharmacol"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0225","doi-asserted-by":"crossref","DOI":"10.3390\/antib9020022","article-title":"Principles of N-linked glycosylation variations of IgG-based therapeutics: pharmacokinetic and functional considerations","volume":"9","author":"Boune","year":"2020","journal-title":"Antibodies"},{"key":"10.1016\/j.xphs.2025.103771_bib0226","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.mam.2016.04.004","article-title":"Emerging roles of protein mannosylation in inflammation and infection","volume":"51","author":"Loke","year":"2016","journal-title":"Mol Aspects Med"},{"key":"10.1016\/j.xphs.2025.103771_bib0227","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.jbiotec.2021.04.005","article-title":"Strategic feeding of NS0 and CHO cell cultures to control glycan profiles and immunogenic epitopes of monoclonal antibodies","volume":"333","author":"Villacres","year":"2021","journal-title":"J Biotechnol"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0228","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1038\/nri2762","article-title":"FcgammaRIIB in autoimmunity and infection: evolutionary and therapeutic implications","volume":"10","author":"Smith","year":"2010","journal-title":"Nat Rev Immunol"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0229","doi-asserted-by":"crossref","first-page":"798","DOI":"10.1016\/S0952-7915(02)00409-0","article-title":"Fc receptors are major mediators of antibody based inflammation in autoimmunity","volume":"14","author":"Hogarth","year":"2002","journal-title":"Curr Opin Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0230","doi-asserted-by":"crossref","first-page":"21","DOI":"10.3389\/fimmu.2016.00021","article-title":"Immunogenicity to biotherapeutics - the role of anti-drug immune complexes","volume":"7","author":"Krishna","year":"2016","journal-title":"Front Immunol"},{"issue":"48","key":"10.1016\/j.xphs.2025.103771_bib0231","doi-asserted-by":"crossref","first-page":"50336","DOI":"10.1074\/jbc.M409676200","article-title":"Conjugation of mannose 6-phosphate-containing oligosaccharides to acid alpha-glucosidase improves the clearance of glycogen in pompe mice","volume":"279","author":"Zhu","year":"2004","journal-title":"J Biol Chem"},{"issue":"50","key":"10.1016\/j.xphs.2025.103771_bib0232","doi-asserted-by":"crossref","first-page":"35201","DOI":"10.1074\/jbc.M109.056119","article-title":"Glycan microarray analysis of P-type lectins reveals distinct phosphomannose glycan recognition","volume":"284","author":"Song","year":"2009","journal-title":"J Biol Chem"},{"key":"10.1016\/j.xphs.2025.103771_bib0233","doi-asserted-by":"crossref","DOI":"10.1016\/j.biotechadv.2023.108206","article-title":"Glycosylation shapes the efficacy and safety of diverse protein, gene and cell therapies","volume":"67","author":"Rocamora","year":"2023","journal-title":"Biotechnol Adv"},{"key":"10.1016\/j.xphs.2025.103771_bib0234","doi-asserted-by":"crossref","DOI":"10.1016\/j.biotechadv.2023.108144","article-title":"Immunomodulatory glycomedicine: introducing next generation cancer glycovaccines","volume":"65","author":"Freitas","year":"2023","journal-title":"Biotechnol Adv"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0235","doi-asserted-by":"crossref","first-page":"475","DOI":"10.4161\/mabs.20737","article-title":"Production, characterization, and pharmacokinetic properties of antibodies with N-linked mannose-5 glycans","volume":"4","author":"Yu","year":"2012","journal-title":"MAbs"},{"key":"10.1016\/j.xphs.2025.103771_bib0236","first-page":"251","article-title":"Immunogenicity of therapeutic proteins. Protein-based therapeutics","author":"Yasir","year":"2023","journal-title":"Springer"},{"issue":"20","key":"10.1016\/j.xphs.2025.103771_bib0237","doi-asserted-by":"crossref","DOI":"10.3390\/molecules28207033","article-title":"Mucin glycans: a target for cancer therapy","volume":"28","author":"Sun","year":"2023","journal-title":"Molecules"},{"issue":"31","key":"10.1016\/j.xphs.2025.103771_bib0238","doi-asserted-by":"crossref","first-page":"8360","DOI":"10.1073\/pnas.1707662114","article-title":"Sialylation on O-glycans protects platelets from clearance by liver Kupffer cells","volume":"114","author":"Li","year":"2017","journal-title":"Proc Natl Acad Sci USA"},{"issue":"14","key":"10.1016\/j.xphs.2025.103771_bib0239","doi-asserted-by":"crossref","DOI":"10.3390\/cancers15143536","article-title":"Aberrant glycosylation as immune therapeutic targets for solid tumors","volume":"15","author":"Matsumoto","year":"2023","journal-title":"Cancers"},{"key":"10.1016\/j.xphs.2025.103771_bib0240","doi-asserted-by":"crossref","DOI":"10.1016\/j.biotechadv.2023.108174","article-title":"Identification, characterization, and engineering of glycosylation in thrombolytics","volume":"66","author":"Toul","year":"2023","journal-title":"Biotechnol Adv"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0241","doi-asserted-by":"crossref","first-page":"1633","DOI":"10.1021\/acs.bioconjchem.3c00302","article-title":"Site-specific antibody conjugation using modified bisected N-glycans: method development and potential toward tunable effector function","volume":"34","author":"Hsu","year":"2023","journal-title":"Bioconjug Chem"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0242","doi-asserted-by":"crossref","first-page":"915","DOI":"10.4161\/mabs.28808","article-title":"Highly parallel characterization of IgG fc binding interactions","volume":"6","author":"Boesch","year":"2014","journal-title":"MAbs"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0243","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.imlet.2006.05.007","article-title":"Mannan binding lectin and its interaction with immunoglobulins in health and in disease","volume":"106","author":"Arnold","year":"2006","journal-title":"Immunol Lett"},{"issue":"1-2","key":"10.1016\/j.xphs.2025.103771_bib0244","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/S0304-4165(01)00136-2","article-title":"Biological activities of human mannose-binding lectin bound to two different ligand sugar structures, Lewis A and Lewis B antigens and high-mannose type oligosaccharides","volume":"1527","author":"Muto","year":"2001","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.xphs.2025.103771_bib0245","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.3389\/fimmu.2018.01123","article-title":"The C-type lectin receptor DC-SIGN has an anti-inflammatory role in Human M(IL-4) macrophages in response to mycobacterium tuberculosis","volume":"9","author":"Lugo-Villarino","year":"2018","journal-title":"Front Immunol"},{"issue":"12","key":"10.1016\/j.xphs.2025.103771_bib0246","doi-asserted-by":"crossref","first-page":"7606","DOI":"10.1021\/acs.joc.8b02944","article-title":"Synthetic lipomannan glycan microarray reveals the importance of alpha(1,2) mannose branching in DC-SIGN binding","volume":"84","author":"Sawettanai","year":"2019","journal-title":"J Org Chem"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0247","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1093\/glycob\/cwq193","article-title":"Survey of immune-related, mannose\/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities","volume":"21","author":"Lee","year":"2011","journal-title":"Glycobiology"},{"issue":"10","key":"10.1016\/j.xphs.2025.103771_bib0248","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1016\/j.tibtech.2020.05.009","article-title":"The formidable challenge of controlling high Mannose-type N-glycans in therapeutic mAbs","volume":"38","author":"Mastrangeli","year":"2020","journal-title":"Trends Biotechnol"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0249","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1093\/glycob\/cwj077","article-title":"The carbohydrate-recognition domain of Dectin-2 is a C-type lectin with specificity for high mannose","volume":"16","author":"McGreal","year":"2006","journal-title":"Glycobiology"},{"issue":"32","key":"10.1016\/j.xphs.2025.103771_bib0250","doi-asserted-by":"crossref","first-page":"13402","DOI":"10.1074\/jbc.M117.799080","article-title":"Mechanism of pathogen recognition by human dectin-2","volume":"292","author":"Feinberg","year":"2017","journal-title":"J Biol Chem"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0251","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1093\/intimm\/dxt006","article-title":"The Dectin-2 family of C-type lectin-like receptors: an update","volume":"25","author":"Kerscher","year":"2013","journal-title":"Int Immunol"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0252","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1189\/jlb.0512231","article-title":"The mannose receptor","volume":"92","author":"Martinez-Pomares","year":"2012","journal-title":"J Leukoc Biol"},{"issue":"10","key":"10.1016\/j.xphs.2025.103771_bib0253","doi-asserted-by":"crossref","first-page":"5427","DOI":"10.4049\/jimmunol.163.10.5427","article-title":"Binding and uptake of agalactosyl IgG by mannose receptor on macrophages and dendritic cells","volume":"163","author":"Dong","year":"1999","journal-title":"J Immunol"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0254","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1093\/glycob\/cwr027","article-title":"High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans","volume":"21","author":"Goetze","year":"2011","journal-title":"Glycobiology"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0255","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1016\/j.imbio.2008.11.004","article-title":"Influence of the mannose receptor in host immune responses","volume":"214","author":"Gazi","year":"2009","journal-title":"Immunobiology"},{"issue":"21","key":"10.1016\/j.xphs.2025.103771_bib0256","doi-asserted-by":"crossref","first-page":"12156","DOI":"10.1016\/S0021-9258(19)38325-5","article-title":"Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains","volume":"265","author":"Taylor","year":"1990","journal-title":"J Biol Chem"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0257","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/j.jbiosc.2013.11.001","article-title":"Glycosylation analysis of an aggregated antibody produced by Chinese hamster ovary cells in bioreactor culture","volume":"117","author":"Onitsuka","year":"2014","journal-title":"J Biosci Bioeng"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0258","doi-asserted-by":"crossref","first-page":"1072","DOI":"10.1002\/bit.20933","article-title":"Engineering of protein thermodynamic, kinetic, and colloidal stability: chemical glycosylation with monofunctionally activated glycans","volume":"94","author":"Sola","year":"2006","journal-title":"Biotechnol Bioeng"},{"key":"10.1016\/j.xphs.2025.103771_bib0259","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.bbrc.2021.04.070","article-title":"Abolition of aggregation of CH(2) domain of human IgG1 when combining glycosylation and protein stabilization","volume":"558","author":"Oyama","year":"2021","journal-title":"Biochem Biophys Res Commun"},{"issue":"15","key":"10.1016\/j.xphs.2025.103771_bib0260","doi-asserted-by":"crossref","first-page":"3812","DOI":"10.1111\/febs.16783","article-title":"Glycosylation increases active site rigidity leading to improved enzyme stability and turnover","volume":"290","author":"Ramakrishnan","year":"2023","journal-title":"FEBS J"},{"key":"10.1016\/j.xphs.2025.103771_bib0261","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.ijbiomac.2020.04.147","article-title":"Enhancing the stability of adalimumab by engineering additional glycosylation motifs","volume":"158","author":"Reslan","year":"2020","journal-title":"Int J Biol Macromol"},{"issue":"1","key":"10.1016\/j.xphs.2025.103771_bib0262","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1080\/19420862.2015.1112477","article-title":"Rational design of therapeutic mAbs against aggregation through protein engineering and incorporation of glycosylation motifs applied to bevacizumab","volume":"8","author":"Courtois","year":"2016","journal-title":"MAbs"},{"issue":"11","key":"10.1016\/j.xphs.2025.103771_bib0263","doi-asserted-by":"crossref","DOI":"10.3390\/pharmaceutics13111747","article-title":"Glycan profile analysis of engineered trastuzumab with rationally added glycosylation sequons presents significantly increased Glycan complexity","volume":"13","author":"Cruz","year":"2021","journal-title":"Pharmaceutics"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0264","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/j.biochi.2007.10.013","article-title":"Novel long-lasting interferon alpha derivatives designed by glycoengineering","volume":"90","author":"Ceaglio","year":"2008","journal-title":"Biochimie"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0265","doi-asserted-by":"crossref","first-page":"649","DOI":"10.4161\/mabs.28588","article-title":"Influence of glycosylation pattern on the molecular properties of monoclonal antibodies","volume":"6","author":"Zheng","year":"2014","journal-title":"MAbs"},{"issue":"24","key":"10.1016\/j.xphs.2025.103771_bib0266","doi-asserted-by":"crossref","DOI":"10.3390\/molecules27248859","article-title":"Impact of N-linked glycosylation on therapeutic proteins","volume":"27","author":"Chen","year":"2022","journal-title":"Molecules"},{"issue":"2","key":"10.1016\/j.xphs.2025.103771_bib0267","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.ejps.2007.10.008","article-title":"pH dependent effect of glycosylation on protein stability","volume":"33","author":"Wang","year":"2008","journal-title":"Eur J Pharm Sci"},{"issue":"8","key":"10.1016\/j.xphs.2025.103771_bib0268","doi-asserted-by":"crossref","first-page":"3451","DOI":"10.1007\/s00253-016-7388-9","article-title":"Advances in recombinant antibody manufacturing","volume":"100","author":"Kunert","year":"2016","journal-title":"Appl Microbiol Biotechnol"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0269","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1093\/intimm\/dxx038","article-title":"Glycosylation of IgG-Fc: a molecular perspective","volume":"29","author":"Kiyoshi","year":"2017","journal-title":"Int Immunol"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0270","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0132848","article-title":"Glycoengineered monoclonal antibodies with homogeneous glycan (M3, G0, G2, and A2) using a chemoenzymatic approach have different affinities for FcgammaRIIIa and variable antibody-dependent cellular cytotoxicity activities","volume":"10","author":"Kurogochi","year":"2015","journal-title":"PLoS One"},{"issue":"12","key":"10.1016\/j.xphs.2025.103771_bib0271","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0143520","article-title":"Multi-angle effector function analysis of Human monoclonal IgG glycovariants","volume":"10","author":"Dashivets","year":"2015","journal-title":"PLoS One"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0272","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1038\/nri2569","article-title":"Signalling through C-type lectin receptors: shaping immune responses","volume":"9","author":"Geijtenbeek","year":"2009","journal-title":"Nat Rev Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0273","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2021.635411","article-title":"The role of lectin receptors and their ligands in controlling allergic inflammation","volume":"12","author":"Peters","year":"2021","journal-title":"Front Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0274","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2023.1126043","article-title":"The diverse roles of C-type lectin-like receptors in immunity","volume":"14","author":"Scur","year":"2023","journal-title":"Front Immunol"},{"issue":"10","key":"10.1016\/j.xphs.2025.103771_bib0275","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1038\/ni.1778","article-title":"Carbohydrate-specific signaling through the DC-SIGN signalosome tailors immunity to mycobacterium tuberculosis, HIV-1 and Helicobacter pylori","volume":"10","author":"Gringhuis","year":"2009","journal-title":"Nat Immunol"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0276","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.4049\/jimmunol.1502178","article-title":"Allergy-protective arabinogalactan modulates human dendritic cells via C-type lectins and inhibition of NF-kappaB","volume":"196","author":"Peters","year":"2016","journal-title":"J Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0277","doi-asserted-by":"crossref","first-page":"3898","DOI":"10.1038\/ncomms4898","article-title":"Fucose-specific DC-SIGN signalling directs T helper cell type-2 responses via IKKepsilon- and CYLD-dependent Bcl3 activation","volume":"5","author":"Gringhuis","year":"2014","journal-title":"Nat Commun"},{"key":"10.1016\/j.xphs.2025.103771_bib0278","doi-asserted-by":"crossref","DOI":"10.1155\/2019\/9705327","article-title":"Anti-inflammatory property of galectin-1 in a murine model of allergic airway inflammation","author":"Lv","year":"2019","journal-title":"J Immunol Res"},{"issue":"6","key":"10.1016\/j.xphs.2025.103771_bib0279","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1016\/S0002-9440(10)63255-5","article-title":"Critical role for galectin-3 in airway inflammation and bronchial hyperresponsiveness in a murine model of asthma","volume":"165","author":"Zuberi","year":"2004","journal-title":"Am J Pathol"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0280","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1164\/rccm.2111031","article-title":"Gene therapy with galectin-3 inhibits bronchial obstruction and inflammation in antigen-challenged rats through interleukin-5 gene downregulation","volume":"166","author":"del Pozo","year":"2002","journal-title":"Am J Respir Crit Care Med"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0281","doi-asserted-by":"crossref","first-page":"1943","DOI":"10.4049\/jimmunol.176.3.1943","article-title":"Inhibition of chronic airway inflammation and remodeling by galectin-3 gene therapy in a murine model","volume":"176","author":"Lopez","year":"2006","journal-title":"J Immunol"},{"issue":"47","key":"10.1016\/j.xphs.2025.103771_bib0282","doi-asserted-by":"crossref","first-page":"32344","DOI":"10.1074\/jbc.M109.035196","article-title":"Galectin-9 is a high affinity IgE-binding lectin with anti-allergic effect by blocking IgE-antigen complex formation","volume":"284","author":"Niki","year":"2009","journal-title":"J Biol Chem"},{"key":"10.1016\/j.xphs.2025.103771_bib0283","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.jconrel.2016.06.043","article-title":"Mucosal expression of DEC-205 targeted allergen alleviates an asthmatic phenotype in mice","volume":"237","author":"Maaske","year":"2016","journal-title":"J Control Release"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0284","doi-asserted-by":"crossref","first-page":"1973","DOI":"10.4049\/jimmunol.163.4.1973","article-title":"APCs express DCIR, a novel C-type lectin surface receptor containing an immunoreceptor tyrosine-based inhibitory motif","volume":"163","author":"Bates","year":"1999","journal-title":"J Immunol"},{"key":"10.1016\/j.xphs.2025.103771_bib0285","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/j.molimm.2015.10.007","article-title":"DCIR negatively regulates CpG-ODN-induced IL-1\u03b2 and IL-6 production","volume":"68","author":"Zhao","year":"2015","journal-title":"Mol Immunol"},{"issue":"7","key":"10.1016\/j.xphs.2025.103771_bib0286","doi-asserted-by":"crossref","first-page":"1386","DOI":"10.1136\/annrheumdis-2014-206644","article-title":"MICL controls inflammation in rheumatoid arthritis","volume":"75","author":"Redelinghuys","year":"2016","journal-title":"Ann Rheum Dis"},{"key":"10.1016\/j.xphs.2025.103771_bib0287","doi-asserted-by":"crossref","DOI":"10.1016\/j.tube.2022.102294","article-title":"Mycobacterial mycolic acids trigger inhibitory receptor Clec12A to suppress host immune responses","volume":"138","author":"Nishimura","year":"2023","journal-title":"Tuberculosis"},{"issue":"12","key":"10.1016\/j.xphs.2025.103771_bib0288","doi-asserted-by":"crossref","first-page":"7587","DOI":"10.4049\/jimmunol.0900464","article-title":"The C-type lectin Clec12A present on mouse and human dendritic cells can serve as a target for antigen delivery and enhancement of antibody responses","volume":"182","author":"Lahoud","year":"2009","journal-title":"J Immunol"},{"issue":"4","key":"10.1016\/j.xphs.2025.103771_bib0289","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1002\/eji.200738057","article-title":"Characterisation of murine MICL (CLEC12A) and evidence for an endogenous ligand","volume":"38","author":"Pyz","year":"2008","journal-title":"Eur J Immunol"},{"issue":"46","key":"10.1016\/j.xphs.2025.103771_bib0290","doi-asserted-by":"crossref","first-page":"eabo7621","DOI":"10.1126\/sciadv.abo7621","article-title":"CLEC-1 is a death sensor that limits antigen cross-presentation by dendritic cells and represents a target for cancer immunotherapy","volume":"8","author":"Drouin","year":"2022","journal-title":"Sci Adv"},{"issue":"5","key":"10.1016\/j.xphs.2025.103771_bib0291","doi-asserted-by":"crossref","first-page":"3099","DOI":"10.4049\/jimmunol.0803767","article-title":"The C-type lectin-like receptor CLEC-1, expressed by myeloid cells and endothelial cells, is up-regulated by immunoregulatory mediators and moderates T cell activation","volume":"183","author":"Thebault","year":"2009","journal-title":"J Immunol"},{"issue":"9","key":"10.1016\/j.xphs.2025.103771_bib0292","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1182\/bloodadvances.2016002360","article-title":"Cell-surface C-type lectin-like receptor CLEC-1 dampens dendritic cell activation and downstream Th17 responses","volume":"1","author":"Lopez Robles","year":"2017","journal-title":"Blood Adv"},{"issue":"3","key":"10.1016\/j.xphs.2025.103771_bib0293","article-title":"Structural basis of Blastomyces Endoglucanase-2 adjuvancy in anti-fungal and -viral immunity","volume":"17","author":"Dos Santos","year":"2021","journal-title":"PLoS Pathog"}],"container-title":["Journal of Pharmaceutical Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022354925002291?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022354925002291?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,5,30]],"date-time":"2025-05-30T19:31:13Z","timestamp":1748633473000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022354925002291"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,6]]},"references-count":293,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2025,6]]}},"alternative-id":["S0022354925002291"],"URL":"https:\/\/doi.org\/10.1016\/j.xphs.2025.103771","relation":{},"ISSN":["0022-3549"],"issn-type":[{"value":"0022-3549","type":"print"}],"subject":[],"published":{"date-parts":[[2025,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Highly variable aggregation and glycosylation profiles and their roles in immunogenicity to protein-based therapeutics","name":"articletitle","label":"Article Title"},{"value":"Journal of Pharmaceutical Sciences","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.xphs.2025.103771","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 American Pharmacists Association. Published by Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"103771"}}