Antibody Therapeutics最新文献

{"title":"Near-infrared photoimmunotherapy: mechanisms, applications, and future perspectives in cancer research.","authors":"Derek Allen, Madeline JoAnna Szoo, Tessa D van Bergen, Ani Seppelin, Jeonghyun Oh, Mohammad A Saad","doi":"10.1093/abt/tbaf001","DOIUrl":"10.1093/abt/tbaf001","url":null,"abstract":"<p><p>Photoimmunotherapy (PIT) involves the targeted delivery of a photosensitizer through antibody conjugation, which, upon binding to its cellular target and activation by external irradiation, induces localized toxicity. This approach addresses several limitations of conventional cancer therapies, such as chemo- and radiotherapies, which result in off-target effects that significantly reduce patient quality of life. Furthermore, PIT improves on the challenges encountered with photodynamic therapy (PDT), such as nonspecific localization of the photosensitizer, which often results in unintended toxicities. Although PIT was first proposed in the early 1980s, its clinical applications have been constrained by limitations in antibody engineering, conjugation chemistries, and optical technologies. However, recent advances in antibody-drug conjugate (ADC) research and the emergence of sophisticated laser technologies have greatly benefited the broader applicability of PIT. Notably, the first near-infrared photoimmunotherapy (NIR-PIT) treatment for head and neck cancer has been approved in Japan and is currently in phase III clinical trials in the USA. A significant advantage of PIT over traditional ADCs in cancer management is the agnostic nature of PDT, making it more adaptable to different tumor types. Specifically, PIT can act on cancer stem cells and cancer cells displaying treatment resistance and aggressive phenotypes-a capability beyond the scope of ADCs alone. This review provides an overview of the mechanism of action of NIR-PIT, highlighting its adaptability and application in cancer therapeutics, and concludes by exploring the potential of PIT in advancing cancer treatments.</p>","PeriodicalId":36655,"journal":{"name":"Antibody Therapeutics","volume":"8 1","pages":"68-85"},"PeriodicalIF":0.0,"publicationDate":"2025-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11826922/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143433820","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Generation of antagonistic biparatopic anti-CD30 antibody from an agonistic antibody by precise epitope determination and utilization of structural characteristics of CD30 molecule.","authors":"Hiroki Akiba, Tomoko Ise, Reiko Satoh, Yasuhiro Abe, Kouhei Tsumoto, Hiroaki Ohno, Haruhiko Kamada, Satoshi Nagata","doi":"10.1093/abt/tbaf002","DOIUrl":"10.1093/abt/tbaf002","url":null,"abstract":"<p><strong>Background: </strong>CD30 is a member of the tumor necrosis factor receptor superfamily. Recently, blocking CD30-dependent intracellular signaling has emerged as potential strategy for immunological regulation. Development of antibody-based CD30 antagonists is therefore of significant interest. However, a key challenge is that the bivalent form of natural antibody can crosslink CD30 molecules, leading to signal transduction even in the absence of specific ligand, CD153. Biparatopic antibodies (BpAbs) offer a solution, using two different variable fragments (Fvs) to bind distinct epitopes on a single antigen molecule. BpAbs format is an attractive alternative of natural antibody by potentially avoiding unwanted crosslinking and signaling induction.</p><p><strong>Methods: </strong>We systematically characterized 36 BpAbs, each designed with pairs of Fvs binding to nine distinct epitopes across the CD30 extracellular domain. We first identified the precise epitope sites of the nine antibodies by assessing the binding to multiple orthologous CD30 proteins and mutants. We then produced the 36 BpAbs and analyzed their biological activities and binding modes.</p><p><strong>Results: </strong>Among 36 BpAbs, we identified both potent ligand-independent agonists and ligand-blocking antagonists, with many displayed reduced signal activation, including 1:1-binding antagonists derived from AC10, a strong agonist developed for lymphoma therapy. Epitope dependency in reduced signaling activity was observed and associated with the flexible nature of CD30 protein.</p><p><strong>Conclusions: </strong>We successfully developed antagonistic BpAbs against CD30 by controlling the stoichiometry of antibody-antigen binding mode. This study elucidated the mechanism of signaling induction, informing the design strategies of the development of biparatopic antibodies.</p>","PeriodicalId":36655,"journal":{"name":"Antibody Therapeutics","volume":"8 1","pages":"56-67"},"PeriodicalIF":0.0,"publicationDate":"2025-01-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11826918/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143433819","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Current use and development of monoclonal antibodies for the treatment of systemic lupus erythematosus: a review.","authors":"Alexander Blagov, Nikolay Orekhov, Alexey Churov, Irina Starodubtseva, Dmitry Beloyartsev, Tatiana Kovyanova, Vasily Sukhorukov, Alexander Orekhov","doi":"10.1093/abt/tbae033","DOIUrl":"10.1093/abt/tbae033","url":null,"abstract":"<p><p>The development of targeted drugs for the treatment of systemic lupus erythematosus (SLE) is a promising area of research because targeted drugs are associated with a lower risk of severe side effects than systemic drugs. There are only two approved drugs based on monoclonal antibodies (a group of targeted drugs) for the treatment of SLE, so there is an unmet need for the development of new and improved antibody analogs. This review analyzes the effectiveness and safety of both already approved antibodies (anifrolumab and belimumab) for the treatment of SLE and antibodies under development with an assessment of their future prospects for entering the pharmaceutical market. In addition to the antibodies themselves, the choice of their therapeutic targets and what role the targets can play in the effectiveness and safety of the antibodies are analyzed here.</p>","PeriodicalId":36655,"journal":{"name":"Antibody Therapeutics","volume":"8 1","pages":"47-55"},"PeriodicalIF":0.0,"publicationDate":"2024-12-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11826920/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143433818","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A bioluminescent reporter bioassay for in-process assessment of chimeric antigen receptor lentiviral vector potency.","authors":"Julia K Gilden, Pete Stecha, Jim Hartnett, Mei Cong","doi":"10.1093/abt/tbae032","DOIUrl":"10.1093/abt/tbae032","url":null,"abstract":"<p><strong>Background: </strong>Chimeric antigen receptor (CAR)-T-cell therapy is a breakthrough in the field of cancer immunotherapy, wherein T cells are genetically modified to recognize and attack cancer cells. Delivery of the CAR gene is a critical step in this therapy and is usually achieved by transducing patient T cells with a lentiviral vector (LV). Because the LV is an essential component of CAR-T manufacturing, there is a need for simple bioassays that reflect the mechanism of action (MOA) of the LV and can measure LV potency with accuracy and specificity. Common methods for LV quantification may overestimate functional titer and lack a functional readout of LV MOA.</p><p><strong>Methods: </strong>We developed a bioluminescent reporter bioassay using Jurkat T cells stably expressing a luciferase reporter under the control of an nuclear factor of activated T cells (NFAT) response element and tested its suitability for measuring LV potency.</p><p><strong>Results: </strong>Jurkat reporter cells can be transduced with CAR LV and combined with target cells, yielding a luminescent signal that is dependent on the identity and potency of the LV used. Bioluminescence was highly correlated with CAR expression. The assay is stability indicating and suitable for use in drug development and quality control settings.</p><p><strong>Conclusions: </strong>We have developed a simple bioassay for potency testing of CAR LV. The bioassay represents a significant improvement over other approaches to LV quantification because it reflects the MOA of the LV and selectively detects fully functional viral particles, making it ideal for inclusion in a matrix of in-process quality control assays for CAR LV.</p>","PeriodicalId":36655,"journal":{"name":"Antibody Therapeutics","volume":"8 1","pages":"40-46"},"PeriodicalIF":0.0,"publicationDate":"2024-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11744306/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143013439","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Humanized anti-CD11d monoclonal antibodies suitable for basic research and therapeutic applications.","authors":"Eoin N Blythe, Christy Barreira, Corby Fink, Arthur Brown, Lynne C Weaver, Gregory A Dekaban","doi":"10.1093/abt/tbae031","DOIUrl":"10.1093/abt/tbae031","url":null,"abstract":"<p><strong>Background: </strong>Immunomodulatory agents targeting the CD11d/CD18 integrin are in development for the treatment of several pathophysiologies including neurotrauma, sepsis, and atherosclerosis. Murine anti-human CD11d therapeutic antibodies have successfully improved neurological and behavioral recovery in rodent neurotrauma models. Here, we present the progression of CD11d-targeted agents with the development of humanized anti-CD11d monoclonal antibodies.</p><p><strong>Methods: </strong>Primary human leukocytes and the THP-1 monocytic cell line were used to determine the binding of the CD11d antibodies, determine binding affinities, and assess outside-in signaling induced by CD11d antibody binding. In addition, a rat model of spinal cord injury was employed to demonstrate that the humanized monoclonal antibodies retained their therapeutic function <i>in vivo</i>. These determinations were made using a combination of flow cytometry, western blotting, immunohistochemistry, biochemical assays, and a locomotor behavioral assessment.</p><p><strong>Results: </strong>Flow cytometric analysis demonstrated that the humanized anti-CD11d clones bind both human monocytes and neutrophils. Using a THP-1 model, the humanized anti-CD11d-2 clone was then determined to bind both the active and inactive CD11d/CD18 conformations without inducing inflammatory cell signaling. Finally, an investigation using anti-CD11d-2 as a detection tool uncovered a mismatch between total and surface-level CD11d and CD18 expression that was not altered by CK2 inhibition.</p><p><strong>Conclusions: </strong>By developing humanized anti-CD11d monoclonal antibodies, new tools are now available to study CD11d biology and potentially treat inflammation arising from acute neurotrauma via CD11d targeting.</p>","PeriodicalId":36655,"journal":{"name":"Antibody Therapeutics","volume":"8 1","pages":"26-39"},"PeriodicalIF":0.0,"publicationDate":"2024-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11744312/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143013374","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Practical advice in the development of a lyophilized protein drug product.","authors":"Yuan Cheng, Huu Thuy Trang Duong, Qingyan Hu, Mohammed Shameem, Xiaolin Charlie Tang","doi":"10.1093/abt/tbae030","DOIUrl":"10.1093/abt/tbae030","url":null,"abstract":"<p><p>The development of lyophilized protein drug products is a critical and complex task in the pharmaceutical industry, requiring a comprehensive understanding of the myriad of factors affecting product quality, stability, and the efficiency and robustness of the lyophilization process. This review offers practical advice on the critical aspects of lyophilized protein drug product development. Practical considerations across both the early and late stages of development are discussed, underscoring the necessity of a strategic approach from initial development through to commercialization. The review then delves into formulation optimization strategies that are essential for enhancing protein stability and the efficiency of the lyophilization process. This section outlines stable formulation design and highlights the unique considerations required for high protein concentration lyophilized drug products. It further explores the formulation strategies to enhance the lyophilization process' efficiency. Moreover, the paper examines the critical elements in selecting primary containers and closures for lyophilized drug products, focusing on vials and dual chamber systems. The analysis encompasses the effects of the container/closure's material, size, geometry, and fill volume on product quality and process efficiency. Lastly, the review provides practical considerations in lyophilization cycle development, including the design and optimization of the freezing, primary drying, and secondary drying stages to achieve a robust, scalable, and efficient lyophilization process. By offering comprehensive insights into these key areas to enhance their understanding and implementation of best practices in the field, this paper serves as a useful resource for researchers, formulators, and process engineers involved in the development of lyophilized protein drug products.</p>","PeriodicalId":36655,"journal":{"name":"Antibody Therapeutics","volume":"8 1","pages":"13-25"},"PeriodicalIF":0.0,"publicationDate":"2024-11-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11744310/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143013379","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Connexin 43 hemichannels and related diseases.","authors":"Yanfeng Zhang, Francisca M Acosta, Jean X Jiang","doi":"10.1093/abt/tbae024","DOIUrl":"10.1093/abt/tbae024","url":null,"abstract":"<p><p>Connexin 43 (Cx43) protein forms hemichannels (connexons) and gap junctions, with hemichannels consisting of six Cx43 molecules and gap junctions formed by two hemichannels. While gap junctions are prevalent in organs like the heart and liver, hemichannels are found in specific cell types, such as astrocytes and osteocytes. They allow the passage of small molecules (<1.5 kDa) between the cytoplasm and extracellular matrix. Cx43 hemichannels have emerged as potential therapeutic targets in various diseases, including central nervous system disorders, bone-related diseases, diabetic complications, wound healing, and cancers. Aberrant hemichannel opening can worsen conditions by releasing inflammatory elements, such as causing gliosis in neuronal cells. Conversely, functional hemichannels may inhibit cancer cell growth and metastasis. Recent studies are revealing new mechanisms of Cx43 hemichannels, broadening their therapeutic applications and highlighting the importance of regulating their activity for improved disease outcomes.</p>","PeriodicalId":36655,"journal":{"name":"Antibody Therapeutics","volume":"7 4","pages":"361-369"},"PeriodicalIF":0.0,"publicationDate":"2024-11-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11646280/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142830127","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Beyond ADCs: harnessing bispecific antibodies to directly induce apoptosis for targeted tumor eradication.","authors":"Victor S Goldmacher, Iosif M Gershteyn, Yelena Kovtun","doi":"10.1093/abt/tbae029","DOIUrl":"https://doi.org/10.1093/abt/tbae029","url":null,"abstract":"<p><p>Bispecific apoptosis triggers (BATs) are innovative bispecific antibodies designed to simultaneously target both a tumor-associated antigen and a cancer cell's death receptor, thereby directly activating the extrinsic apoptotic pathway to induce death of cancer cells. This unique mechanism distinguishes BATs from antibody-drug conjugates (ADCs), which rely on cytotoxic drugs, and bispecific immune cell engagers such as bispecific T-cell engagers (BiTEs) and bispecific natural killer cell engagers (NKCEs), which recruit immune cells to eliminate target cancer cells. BATs offer significant potential advantages in clinical efficacy and safety over ADCs and BiTEs. Although the field is still emerging, recent advancements are highly promising, and analysis of preclinical and clinical data of DR5-targeting antibodies have been pivotal in outlining the criteria for the next generation of effective and safe medicines. Antibodies found inactive in preclinical testing were also found to be clinically ineffective, whereas antibodies with minimal preclinical results demonstrated moderate clinical activity. All clinical DR5-targeting antibodies were well tolerated by patients even at high doses (with the exception of TAS266 due to its unique design). These findings underscore the predictive value of robust preclinical models on clinical outcomes. Notably, first-in-class BAT, Cancerlysin™ IMV-M, demonstrated potent efficacy in diverse xenograft cancer models and safety in non-human primates, marking a significant advancement in developing safe and effective anti-cancer drugs.</p>","PeriodicalId":36655,"journal":{"name":"Antibody Therapeutics","volume":"7 4","pages":"351-360"},"PeriodicalIF":0.0,"publicationDate":"2024-10-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11887037/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143587402","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Leveraging high-throughput analytics and automation to rapidly develop high-concentration mAb formulations: integrated excipient compatibility and viscosity screening.","authors":"Lun Xin, Lan Lan, Mourad Mellal, Nathan McChesney, Robert Vaughan, Claudia Berdugo, Yunsong Li, Jingtao Zhang","doi":"10.1093/abt/tbae028","DOIUrl":"10.1093/abt/tbae028","url":null,"abstract":"<p><strong>Background: </strong>Formulation screening is essential to experimentally balance stability and viscosity in high-concentration mAb formulations. We developed a high-throughput approach with automated sample preparation and analytical workflows to enable the integrated assessment of excipient compatibility and viscosity of mAb formulations.</p><p><strong>Methods: </strong>Ninety-six formulations of a trastuzumab biosimilar were screened by combining 8 types of excipient modifiers with 4 types of buffers across a pH range of 4.5 to 7.5. Key stability risks, including high molecular weight (HMW) aggregation and fragmentation, were thoroughly assessed along with viscosity at high concentrations. Additionally, several biophysical parameters were evaluated for their ability to predict stability or viscosity outcomes. Multiple linear regression was applied to fit the data and identify key factors.</p><p><strong>Results: </strong>The optimal pH range for the trastuzumab biosimilar was found to be 5.0 to 6.5, based on opposing pH dependencies for stability and viscosity. Buffer type had a minor effect on viscosity and fragmentation but played a significant role in influencing HMW aggregates, with Na-acetate and histidine-HCl being the best candidates. The impact of excipient modifiers on viscosity, HMW, and fragmentation depended on both pH and buffer type, showing strong interactions among factors. Arginine-HCl and lysine-HCl effectively lowered viscosity of the trastuzumab biosimilar at pH levels above 6.0, while glycine formulations were more effective at reducing viscosity below pH 6.0. Histidine-HCl, arginine-HCl, and lysine-HCl lowered the risk of HMW aggregation, whereas formulations containing Na-phosphate or NaCl showed higher HMW aggregation. Formulations with arginine-HCl, lysine-HCl, and NaCl demonstrated a rapid increase in fragmentation at pH levels below 5.0, while Na-aspartate formulations showed increased fragmentation at pH levels above 6.5.</p><p><strong>Conclusion: </strong>Hence, it is important to optimize the levels of each chosen excipient in the formulation study to balance their benefits against potential incompatibilities. This study serves as a foundation for identifying high-concentration antibody formulations using a high-throughput approach, where minimal materials are required, and optimized formulation design spaces can be quickly identified.</p>","PeriodicalId":36655,"journal":{"name":"Antibody Therapeutics","volume":"7 4","pages":"335-350"},"PeriodicalIF":0.0,"publicationDate":"2024-10-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11646310/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142830130","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Discovery of a common light chain bispecific antibody targeting PD-1 and PD-L1 by Hybridoma-to-Phage-to-Yeast (H2PtY) platform.","authors":"Peipei Liu, Chunyin Gu, Xiaodan Cao, Huawei Zhang, Zongda Wang, Yukun Yang, KeDong OuYang, Yingying Zhen, Fangfang Jia, Xianqing He, Haixiang Yu, Sujun Deng","doi":"10.1093/abt/tbae027","DOIUrl":"10.1093/abt/tbae027","url":null,"abstract":"<p><strong>Background: </strong>Therapeutic antibody drugs targeting the PD-1 pathway are generally characterized by relatively low response rates and susceptibility to drug resistance during clinical application. Therefore, there is an urgent need for alternative therapeutic strategies to increase the immune response rate. Bispecific antibodies co-targeting PD-1 and PD-L1 may have greater potential to improve the efficacy of the immune checkpoint pathway.</p><p><strong>Method: </strong>In this study, we developed a potent humanized common light chain (CLC) IgG shape bispecific antibody (bsAb), named JMB2005, based on Hybridoma-to-Phage-to-Yeast platform. The platform allowed us to discover CLC bsAb from traditional mice for any pair of given targets.</p><p><strong>Results: </strong>JMB2005 exhibited favorable developability, good manufacturing property, and satisfactory efficacy, which could be given via subcutaneous injection at the concentration of 120 mg/mL. Mechanistically, JMB2005 could bridge tumor cells and T cells with both Fab arms and promote T-cells to function as direct tumor cell killers. It could also promote T cell activation by blocking the binding of PD-L1 to CD80. Furthermore, JMB2005 has exhibited a favorable half-life and has demonstrated promising anti-tumor therapeutic efficacy <i>in vivo</i>.</p><p><strong>Conclusion: </strong>Consequently, the present study showed that the novel humanized CLC bsAb JMB2005 may represent a novel therapeutic agent of great clinical potential.</p>","PeriodicalId":36655,"journal":{"name":"Antibody Therapeutics","volume":"8 1","pages":"1-12"},"PeriodicalIF":0.0,"publicationDate":"2024-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11744305/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143013369","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}