mAbs最新文献

{"title":"What does AlphaFold3 learn about antibody and nanobody docking, and what remains unsolved?","authors":"Fatima N Hitawala, Jeffrey J Gray","doi":"10.1080/19420862.2025.2545601","DOIUrl":"10.1080/19420862.2025.2545601","url":null,"abstract":"<p><p>Antibody therapeutic development is a major focus in healthcare. To accelerate drug development, significant efforts have been directed toward the <i>in silico</i> design and screening of antibodies for which high modeling accuracy is necessary. To probe AlphaFold3's (AF3) capabilities and limitations, we tested AF3's ability to capture the fine details and interplay between antibody structure prediction and antigen docking accuracy. With one seed, AF3 achieves a 10.2% and 13.3% high-accuracy docking success rate for antibodies and nanobodies, respectively. AF3-like models Boltz-1 and Chai-1 achieve 4.08% and 0% high-accuracy rates for antibodies, and 5% and 3.33% for nanobodies, respectively. With twenty seeds, AF3 achieves a median unbound CDR H3 RMSD accuracy of 2.9 Å … and 2.2 Å … for antibodies and nanobodies, respectively. Both AF3-like models Boltz-1 and Chai-1 improve further on antibodies (2.08 Å … and 2.71 Å …, respectively), but do poorly on nanobodies (3.78 Å … , 3.63 Å …). CDR H3 accuracy boosts AF3 complex prediction accuracy, with antigen context improving CDR H3 accuracy, particularly for loops longer than 15 residues. Combining ipTM-HA and I-pLDDT with <math><mi>Δ</mi><mrow><msub><mi>G</mi><mi>B</mi></msub></mrow></math> improves discriminative power for correctly docked antibody and nanobody complexes. However, AF3's 65% failure rate for antibody and nanobody docking (with single seed sampling) demonstrates a need to further improve antibody modeling tools.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2545601"},"PeriodicalIF":7.3,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12360200/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144855726","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Analytical development and application of a targeted liquid chromatography-tandem mass spectrometry assay for chimeric aducanumab.","authors":"Emma H Doud, Kasi Hansen, Kathryn A Haynes, Kierra Eldridge, Jaison Arrivalagan, Nitin Charbe, Lais Da Silva, Sara K Quinney, Amber L Mosley, Stacey J Sukoff Rizzo, Paul R Territo","doi":"10.1080/19420862.2025.2537118","DOIUrl":"10.1080/19420862.2025.2537118","url":null,"abstract":"<p><p>A sensitive and specific liquid chromatography-tandem mass spectrometry assay was developed for the quantification of chimeric aducanumab (chAdu), a therapeutic antibody targeting pathological amyloid plaques in Alzheimer's disease, in murine biological matrices. This method addresses the challenges of quantifying biotherapeutics in multiple tissue types within preclinical animal models with complex genetic backgrounds, where traditional enzyme-linked immunosorbent assay (ELISA) methods may suffer from interference and limited sensitivity. The assay uses parallel reaction monitoring on a Lumos Tribrid Orbitrap mass spectrometer, coupled with an Evosep LC system, and AssayMap Bravo-based automated sample processing. Key features include protein A enrichment for improved sensitivity, optimized peptide selection based on sequence uniqueness and ionization response, and incorporation of stable isotope-labeled peptides for accurate quantification. Assay performance was evaluated for selectivity, repeatability, and stability. The fit-for-purpose assay was successfully applied to quantify chAdu in both mouse cortex and plasma samples obtained from a pilot pharmacokinetic study of a mouse model of amyloid plaque deposition. This targeted mass spectrometry workflow offers a robust and reproducible alternative to ELISA for preclinical biotherapeutic analysis, particularly when dealing with complex biological samples.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2537118"},"PeriodicalIF":7.3,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12296118/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144690676","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Higher order receptor clustering due to the IgG3 subclass is necessary for TLR4 signaling and tolerance induction by novel human anti-TLR4 antibodies.","authors":"Luke S Heuer, Nicolle Sweeney, Manuel Rojas, Weici Zhang, Andrew R Mendelsohn, Manley Huang, Bo Yu, Paulina Ackerman, Qisheng Wei, Andrew B Herr, James W Larrick, William M Ridgway","doi":"10.1080/19420862.2025.2515415","DOIUrl":"10.1080/19420862.2025.2515415","url":null,"abstract":"<p><p>We have previously demonstrated that an IgG3 agonistic TLR4/MD2 antibody reversed acute murine Type 1 diabetes (T1D), induced immune tolerance, and induced long-term endosomal sequestration of TLR4/MD2. We hypothesized that the IgG3 Fc was critical for agonist activity of the mouse TLR4 antibodies, due to the unique IgG3 extended hinge region and enhanced ability to form higher-order oligomeric structures. Here, we prove the essential role of the Fc region using plate-bound antibody and F(ab')2 and F(ab) fragments, which greatly reduced or eliminated TLR4 signaling. Importantly, no agonistic TLR4 antibodies have been described for humans. We developed four novel IgG4 human agonistic TLR4/MD2 antibodies as potential therapeutic candidates for T1D. The human IgG4 anti-TLR4 antibodies failed to activate the TLR4/MD2 pathway. Switching two candidate antibodies from IgG4 to IgG3, however, resulted in robust TLR4 signaling. Cross-linking the IgG4 antibody with an IgG3 secondary antibody also induced robust TLR4 signaling. Based on this result, which suggested that increased TLR4 clustering could increase signaling, we developed tetravalent IgG3 and IgG4 anti-TLR4 antibodies. Tetravalent IgG3, but not IgG4, anti-TLR4 antibodies robustly signaled via the TLR4 pathway. Notably, however, cross-linking human IgG3 antibodies with non-IgG3 secondaries reduced TLR4 signaling, in marked contrast to activation induced by IgG4 isotypes with IgG3 crosslinker, potentially through interference with IgG3 Fc-mediated oligomerization. These results suggest that the IgG3 Fc enhances agonist function of human TLR4 antibodies via aggregation of the TLR4 receptor. Functionally, human IgG3 and IgG3 tetravalent antibodies induced tolerance in primary human monocytes, analogous to the mouse antibody. In conclusion, we developed novel human TLR4 agonistic antibodies, demonstrated that the IgG3 isotype and enhanced multivalency are necessary for their TLR4 signaling, and demonstrated their tolerogenic potential for treating inflammatory diseases.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2515415"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12143713/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144216262","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Building a potent TREM2 agonistic, biparatopic, common light chain antibody.","authors":"Ana da Silva Almeida, Melissa L Geddie, Anil Bhate, Chao Quan, Joseph W Arndt, Yang Jiao, Joseph C Santoro, Liron Noiman, Ramya Vijayakumar, Jorge Sanchez-Salazar, Abhishek Datta, Giovanna Antognetti, Ciputra Adijaya Hartana, Xue Fan Wang, Benjamin A Smith, Dan Bartlett, Danté Duncan, Chia-Chen Liu, Karel Otero Gutierrez, Thomas O Cameron, Samir Koirala, Heather A Cooke","doi":"10.1080/19420862.2025.2546554","DOIUrl":"10.1080/19420862.2025.2546554","url":null,"abstract":"<p><p>Triggering Receptor Expressed on Myeloid cells 2 (TREM2) plays an important role in microglial function and has been genetically linked to Alzheimer's disease. Activation of TREM2 signaling may contribute to protection against neurotoxic effects of amyloid. Numerous TREM2 activating antibodies have been shown to modulate downstream microglial functions to different degrees, with mixed results in preclinical models and in the clinic. We sought to generate an effectorless agonistic antibody that acted solely through TREM2 engagement with sufficient potency to activate TREM2 in the brain. Our approach focused on building a multivalent biparatopic TREM2 antibody that could mimic the higher order clustering induced by native polyanionic ligands of TREM2. We describe our screening strategy and findings that led to the discovery of a potential therapeutic molecule composed of antibodies selected for optimal affinity, binding epitopes, and geometry. The most productive antibody pair was selected from a common light chain yeast-display library, which required multiple rounds of affinity maturation. Lead antibody candidates were converted into asymmetric tetravalent bispecifics via controlled Fab-arm exchange and subsequently screened in signaling assays. The most productive antibody pair was reengineered into a symmetric tetravalent format, increasing potency and simplifying development. This molecule exhibited higher efficacy and potency in signaling assays than other antibody formats tested and elicited TREM2-mediated chemokine responses in vivo. Our results demonstrate a biparatopic strategy for producing a high potency TREM2 agonistic antibody with low effector function that can modulate TREM2 signaling in vitro and brain pharmacodynamic responses in vivo.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2546554"},"PeriodicalIF":7.3,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12351705/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144847279","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Footprinting for fingerprinting: proof-of-concept for the use of hydroxyl radical protein footprinting for structural comparison studies.","authors":"Vanessa A Noreika, Aaron T Wecksler","doi":"10.1080/19420862.2025.2530575","DOIUrl":"10.1080/19420862.2025.2530575","url":null,"abstract":"<p><p>Monoclonal antibodies (mAbs) require extensive physicochemical characterization to ensure product quality. The clinical and pharmacological properties of mAbs are linked to higher order structure (HOS), but high-resolution analytical techniques to evaluate structural conformations and structural comparisons during drug design and process development are limited. Here, we provide proof-of-concept for the use of hydroxyl radical footprinting-mass spectrometry (HRPF-MS) to characterize the average solvent accessible surface area ( < SASA>) of mAbs. The premise is that each mAb exhibits a unique \"oxidative footprint\" that may aid in demonstrating structural similarities and differences between mAbs and support the HOS characterization of a biotherapeutic fingerprint. This work, which includes case studies for comparing oxidative footprints between mAbs, highlights the challenges and future state needed to realize the potential of HRPF for the application of biotherapeutic fingerprinting.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2530575"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12243915/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144591615","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A highly selective TCR-mimic antibody reveals unexpected mechanisms of HBV peptide-MHC recognition and previously unknown target biology.","authors":"Shahzada Khan, Jeremy Lum, Heather Stephenson, Pawan Bir Kohli, David Mortenson, Dhivya Ramakrishnan, Magdeleine Hung, Sheng Ding, Elbert Seto, Sabrina Lu, Randy Yen, Debi Jin, Brian Lee, Sheila Clancy, Nicole Schirle Oakdale, Nikolai Novikov, Don Kang, Ruidong Li, David Pan, Rutwij Dave, Eric Lansdon, Simon P Fletcher, Abhishek V Garg, Nathan Thomsen, Scott Balsitis","doi":"10.1080/19420862.2025.2562998","DOIUrl":"10.1080/19420862.2025.2562998","url":null,"abstract":"<p><p>Curative therapies for chronic hepatitis B virus infection (CHB) are needed, and T-cell redirection is a promising approach, with peptide-MHC complexes (pMHC) being attractive targets. HBV core_18-27 peptide (C18, 10-mer) presented by HLA-A*02:01 (C18-MHC) has two major variants (C18-V or C18-I, differing in the C-terminal residue), both of which are known to be targeted by CD8⁺ T cells in HBV-infected individuals. Through an extensive screening campaign, we identified a highly selective anti-C18-MHC antibody clone MUR35. A MUR35-based T-cell engager (TCE) potently killed HBV-infected hepatocytes but had no activity on uninfected hepatocytes, on other HBV-negative cell types or on host peptides with sequence similarity to C18. Crystal structures of MUR35 bound to both C18-I- and C18-V-MHC revealed a unique binding mode with contacts mediated exclusively by the light chain complementarity-determining regions (CDRs), suggesting that high specificity is achievable without a typical T-cell receptor-like binding mode involving both heavy and light chain CDRs. Although MUR35 exhibits similar binding affinity and structural contacts with C18-V and C18-I, TCE killing was only detected on hepatocytes producing C18-V. To better understand the cause of this discrepancy, we conducted a quantitative proteomics study in an HBV-infected humanized mouse model and found that C18-V was expressed at approximately 300 copies/cell, while C18-I expression was below the limit of detection. Unexpectedly, the proteomics studies revealed that previously unreported 9-mers missing the N-terminal phenylalanine of C18-I and -V were expressed at an average of 508 and 142 copies/cell, respectively, and therefore could be alternative targets for HBV pan genotypic coverage. Our data suggest unexpectedly large differences in antigen presentation efficiency between highly conservative amino acid substitutions in C18 peptide and reveal potentially novel HBV targets for future studies.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2562998"},"PeriodicalIF":7.3,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12461897/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145131244","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A comprehensive strategy for pandemic preparedness with neutralizing monoclonal antibodies.","authors":"Christian Marx, Ralf Piotrowiak, Thomas Schirrmann, Michael Gebinoga, Isabelle Bekeredjian-Ding, Andreas Schober","doi":"10.1080/19420862.2025.2573180","DOIUrl":"10.1080/19420862.2025.2573180","url":null,"abstract":"<p><p>The success of nucleic acid-based vaccines during the COVID-19 pandemic positioned these technologies at the forefront of global preparedness. A retrospective analysis, however, demonstrates that while vaccines play a central role, they do not provide universal protection. Therapeutic interventions, such as monoclonal antibodies (mAbs), are also critical for an effective pandemic response, as they ensure both prophylaxis and treatment of vulnerable populations, prevent overload of healthcare systems, and safeguard the continuity of critical infrastructures. Despite the proven efficacy of antiviral mAbs, the rapid emergence of SARS-CoV-2 variants frequently diminished their effectiveness. Thus, innovative strategies are required to accelerate the development, manufacturing, and adaptation of mAbs to continuously evolving viral targets. Viable approaches consist of targeting conserved viral epitopes and producing multi-mAb formulations to maintain therapeutic efficacy. Notably, the development of prototype mAbs can help to protect high-risk groups and exposed medical personnel early in a pandemic. Here, we propose that a comprehensive mAb strategy - encompassing targeted support for research and development, expansion of resilient manufacturing capacities on a regional level, and collaborative networks integrating standardized procedures for development, production and distribution - should be considered a hallmark of pandemic preparedness, to ensure the rapid and effective deployment of mAbs in future pandemics.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2573180"},"PeriodicalIF":7.3,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145280451","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Temperature and excipient mediated modulation of monoclonal antibody interactions revealed by <i>k</i>D, rheology, and Raman spectroscopy.","authors":"Olivia Noelle Eskens, Sabitoj Singh Virk, Akashdeep Singh Virk, Deepika Venkataramani, Maureen Crames, Maria Calderon Vaca, Matthew Matusewicz, Connor Smith, Joshin George, Collin Taylor, Michael S Marlow, Samiul Amin","doi":"10.1080/19420862.2025.2521511","DOIUrl":"https://doi.org/10.1080/19420862.2025.2521511","url":null,"abstract":"<p><p>High-concentration monoclonal antibody (mAb) formulations are frequently constrained by elevated viscosity and colloidal instability, stemming from enhanced intermolecular interactions under crowded conditions. In this study, we delineate the thermodynamic and rheological consequences of modulating protein-protein interactions through excipient-mediated and temperature-dependent mechanisms. Using an orthogonal analytical framework comprising diffusion interaction parameter (<i>k</i>D) measurements, high-shear rheometry, and Raman spectroscopic profiling, we interrogated mAb solutions at ~ 80 and 160 mg/mL across a physiologically and industrially relevant thermal window (5-45 °C). In the absence of ionic additives, high <i>k</i>D values (~60 mL/g) indicated dominant long-range electrostatic repulsions, resulting in suppressed self-association and lower viscosity. Incorporation of NaCl (0.05% w/v) markedly decreased <i>k</i>D (~16-20 mL/g), consistent with Debye screening of surface charges and a shift toward short-range hydrophobic and van der Waals attractions, which became especially pronounced at elevated protein concentrations and lower temperatures. Polysorbate 20 (0.05% v/v) mitigated these interactions via preferential surface adsorption, while sucrose exhibited a dualistic, concentration-dependent influence on viscosity via preferential exclusion and entropic crowding. The combination of NaCl and PS20 yielded the most pronounced rheological suppression, reflecting synergistic attenuation of both long-range repulsion and short-range association. Raman spectral analysis of Amide I/III regions confirmed structural invariance under thermal and shear stress, attributing viscosity modulation to colloidal rather than conformational perturbations. Collectively, these data elucidate the multivariate control of interparticle potentials in mAb solutions and provide a predictive basis for engineering subcutaneous formulations that optimize manufacturability, physical stability, and injectability through strategic manipulation of colloidal interaction landscapes.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2521511"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144497437","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of free light chain impurity in a bispecific antibody.","authors":"Monica Sadek, Neelima Mantha, Steffen Lippold, Delia Li, Kyle Spitler, Ran Li, Phillip Spinosa, Bob Liu, Steven Luu, Nicholas Woon, Yeying Zhang, Jia Guo, Renee Yang, Jonathan Zarzar, Yi Yang","doi":"10.1080/19420862.2025.2527689","DOIUrl":"10.1080/19420862.2025.2527689","url":null,"abstract":"<p><p>Bispecific antibodies (bsAbs) target two distinct binding sites, which enable novel mechanisms of action for the treatment of disease. Due to this structural complexity, bsAbs exhibit greater heterogeneity as compared to monospecific antibodies and may require nonstandard purification strategies to remove undesired product-related impurities. However, the implementation of unique manufacturing processes may result in the observation of new impurities. When new impurities are identified, comprehensive characterization of these species is needed to understand the potential impact to the safety and efficacy of the product. In this study, the assessment of a unique purification mode, protein L affinity chromatography, for purification of a bsAb resulted in high levels of free light chain (LC) in the final product. It was discovered that the free LC formed oligomers of various sizes upon accelerated stress in a concentration-, time-, and temperature-dependent manner. This is the first time free LC oligomer has been reported as a product-related impurity. Characterization of the free LC and free LC oligomer species was performed using a variety of chromatographic, electrophoretic, and mass spectrometry tools to gain insight on the formation and behavior of these impurities in the product. These studies informed an impact assessment of the observed free LC and free LC oligomer species on safety, immunogenicity, pharmacokinetics, and bioactivity.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2527689"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12233890/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144553935","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction.","authors":"","doi":"10.1080/19420862.2025.2463770","DOIUrl":"10.1080/19420862.2025.2463770","url":null,"abstract":"","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2463770"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11810074/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143255828","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}