Bioanalysis最新文献

{"title":"18^th GCC Closed Forum: Compliance with FDA Biomarkers Guidance, Novel ELN/LIMS Platforms, Sample Reconciliation, Emerging Technologies, Improvements in ELISpot, Post-extraction Sample Stability, LBA Singlicate, Regulatory Inspections, Chicken anti-Human IgG, Cross-validation Harmonization.","authors":"Shane Karnik, Jennifer Zimmer, Matthias Gutekunst, Shashank Gorityala, Jo Goodman, Erik Jerks, Virginia Litwin, Xiaonan Tang, Amanda Leskovar, Magdalena Tary-Lehmann, Stephen Lowes, Amy Lavelle, Moucun Yuan, Aihua Liu, Kyla O'Brien, Kelly Dong, Kurt Sales, Scott Reuschel, Anahita Keyhani, Derrick Johnson, Mark Odell, Sanofar Jainul Abdeen, Amanda Hays, Dave Beyerlein, Michael Johnson, Mathilde Yu, Sophie Cotton, Philip Joyce, Wendy W T Fang, Wei Garofolo, Sankeetha Nadarajah, Adriane Spytko, Dawn Dufield, Lindsay Rutherford, Todd Pankratz, Allan Xu, Daniel Sikkema, Elizabeth Hyer, Tracy Iles, Eric Bonner, Chantal Dimarco, Georgios Hristopoulos, Kate Patterson, Brad Nash, Vera Bretton, Agostinho Rocha, Christina Satterwhite, Jim Yamashita, Jim McNally, Xinping Fang, Leimin Fan","doi":"10.1080/17576180.2026.2696193","DOIUrl":"10.1080/17576180.2026.2696193","url":null,"abstract":"<p><p>The 18th GCC Closed Forum was held in New Orleans, LA, USA, on 11 April 2025. Representatives from international bioanalytical Contract Research Organizations were in attendance to discuss scientific and regulatory issues specific to bioanalysis. The issues discussed at the meeting included: Compliance with US FDA Guidance for Biomarkers; Emerging Technologies; Sample Reconciliation Efforts; Chicken anti-Human IgG antibody; Post-extraction Sample Stability; Singlicate for LBA; Discrepancies of ELISpot data; Regulatory Inspection Experiences; Cross-validation Harmonization in Regulated Bioanalysis; and ELN/LIMS. Conclusions and consensus from discussions of these topics are included in this article.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"669-689"},"PeriodicalIF":2.1,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13557580/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148629370","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Drawing a line in the sand: impact of analytical choices on anti-drug antibody cut-points and testing outcomes.","authors":"Joshua A Weiner, Linda A Banks, Harini Natarajan, Shu Lin, Samia Sami, Gabriela Kovacikova, Margaret C Carpenter, Margaret E Ackerman","doi":"10.1080/17576180.2026.2698615","DOIUrl":"10.1080/17576180.2026.2698615","url":null,"abstract":"<p><strong>Background: </strong>The identification of anti-drug antibodies (ADA) raised against biologic drugs is important for understanding and ensuring efficacy and safety. Because the immunogenicity of novel biologics is unknown before clinical trials, ADA assays are often developed with positivity thresholds assigned based on statistically determined cut-points defined by testing of samples from treatment-naïve donors.</p><p><strong>Research design and methods: </strong>While the standard approaches are based on reasonable theoretical models, we aimed to identify the impact of alternative analytical pipelines on assignment of ADA positivity by analysis of Tier 1 screening and Tier 2 confirmatory ADA bridging assay data for up to 138 mAbs across up to hundreds of serum samples. We evaluate the utility of data augmentation through bootstrapping and the impact of outlier removal approaches on the consistency of ADA status determinations.</p><p><strong>Results and conclusion: </strong>We find that bootstrapping supports assay development efficiency by improving confidence in threshold setting in the context of limited numbers of test samples and that while outlier exclusion approach led to different apparent levels of ADA positivity, immunogenic drug products were identified by differences in the distribution of sample profiles from naïve and treated participants by each method evaluated.</p><p><strong>Clinical trial registration identifiers include: </strong>NCT02716675 https://clinicaltrials.gov/study/NCT02716675NCT02568215NCT02568215 https://clinicaltrials.gov/study/NCT02568215NCT03875209NCT03875209 https://clinicaltrials.gov/study/NCT03875209NCT04173819NCT04173819 https://clinicaltrials.gov/study/NCT04173819.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"711-722"},"PeriodicalIF":2.1,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13557578/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148435043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Regulated bioanalysis in the age of AI: interpreting the FDA-EMA guiding principles for laboratory practice.","authors":"Scarlett Oxley-King, Mark E Arnold","doi":"10.1080/17576180.2026.2677735","DOIUrl":"10.1080/17576180.2026.2677735","url":null,"abstract":"","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"1-3"},"PeriodicalIF":2.1,"publicationDate":"2026-05-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13321871/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148004348","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dilution displacement enabled measurement of total ligand levels in the presence of an anti-ligand antibody using LBA.","authors":"Catherine Zhang, James P Sheridan, Nils Boehm, Steve Keller, Yuni Fang","doi":"10.1080/17576180.2026.2687590","DOIUrl":"10.1080/17576180.2026.2687590","url":null,"abstract":"<p><strong>Background: </strong>Measurement of soluble ligand targets of biotherapeutics can be challenging, especially when non-competing reagents are unavailable. This study aimed to develop a simple assay to quantify total soluble B-cell Maturation Antigen (sBCMA), including antibody-bound sBCMA, in serum when anti-BCMA antibody is present.</p><p><strong>Research design and methods: </strong>A sample predilution strategy was coupled with a ligand-binding assay (LBA) to dissociate sBCMA from anti-BCMA antibody complexes and enable measurement of total sBCMA.</p><p><strong>Results: </strong>A lower limit of quantitation (LLOQ) of 3 ng/mL in neat serum was achieved in the presence of clinically relevant concentrations of anti-BCMA antibody less than 30 µg/mL. sBCMA serum levels were elevated in patients with multiple myeloma (MM) (mean 198.3 ng/mL; range 3.3-2035.7 ng/mL) compared with healthy subjects (mean 12.4 ng/mL; range 2.9-18.4 ng/mL).</p><p><strong>Conclusions: </strong>This dilution-based approach enabled accurate measurement of total sBCMA despite circulating anti-BCMA antibody. However, this sample predilution approach may or may not have general applicability for similar bioanalytical purposes, when candidate biotherapeutic levels are moderate, assay is highly sensitive, and the target protein levels are substantially elevated, as described in this case.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"585-591"},"PeriodicalIF":2.1,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13349025/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148249110","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeted LC-MS/MS profiling of serum amino acids reveals type 2 diabetes-specific alterations in advanced gastric cancer.","authors":"Mehmet Emrah Yaman, Omer Faruk Kocak, Omer Topdagi, Yucel Kadioglu","doi":"10.1080/17576180.2026.2684669","DOIUrl":"10.1080/17576180.2026.2684669","url":null,"abstract":"<p><strong>Background: </strong>Altered amino acid metabolism is a feature of gastric cancer. Type 2 diabetes (T2D), a prevalent metabolic comorbidity, may affect circulating amino acid profiles; this study aimed to quantify its impact.</p><p><strong>Research design and methods: </strong>A validated targeted LC-MS/MS assay profiled 22 serum amino acids in 156 participants, including gastric cancer patients with and without type 2 diabetes and controls.</p><p><strong>Results: </strong>Adjusted models showed that many observed differences were attributable to type 2 diabetes and body mass index. Type 2 diabetes was associated with lower ornithine (β =  -1.16; q = 0.0019) and interacted with gastric cancer for arginine (β_int =  -1.10; q = 0.0044) and phenylalanine (β_int =  +1.05; q = 0.0112). After adjustment, only valine, taurine, and total amino acids remained lower in gastric cancer. Body mass index was inversely associated with glutamine and positively associated with glutamate.</p><p><strong>Conclusions: </strong>Covariate-adjusted analysis distinguishes cancer-related from comorbidity-driven alterations and identifies type 2 diabetes as a key modifier of amino acid metabolism. Metabolic covariates should be considered when interpreting amino acid alterations in advanced gastric cancer biomarker studies. However, the findings should be interpreted in light of the predominantly advanced-stage gastric cancer cohort and require validation in larger prospective studies.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"571-583"},"PeriodicalIF":2.1,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13393234/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148263153","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"ADA assays for high-dose biologics: redefining drug tolerance through clinical insights.","authors":"Manisha Saxena, David Janik, Carsten Krantz, Annie St-Pierre, Maria Jadhav, Lydia Michaut, Florent Bender","doi":"10.1080/17576180.2026.2690269","DOIUrl":"10.1080/17576180.2026.2690269","url":null,"abstract":"<p><p>The validation of anti-drug antibody (ADA) assays is vital in biologics development, with regulatory bodies like EMA and FDA emphasizing drug tolerance. In patient care, drug tolerance assessments should reflect actual clinical use. We developed an ADA assay for a fully human monoclonal antibody used in oncology, addressing the challenges posed by high circulating drug levels and target biology. Various assay formats were tested using multiple positive controls and drug concentrations that mimic real-world exposure and drug-to-ADA ratios. Assessing different positive controls at various concentrations was key to characterizing sensitivity and drug tolerance. An assay initially showing low drug tolerance with one monoclonal control performed adequately with others. Rather than limiting assessments to a single sensitivity level, we evaluated assay performance using clinically relevant drug and ADA concentrations. This approach ensures the assay's sensitivity and drug tolerance are meaningful for patient management and therapeutic decisions. Early and ongoing collaboration with health authorities supported alignment of clinically relevant performance criteria and interpretation strategies. Ultimately, this patient-oriented strategy guarantees ADA results that inform patient safety and treatment effectiveness for high-dose biologic therapies.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"593-605"},"PeriodicalIF":2.1,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13557555/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148366807","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Vaccine Ligand Binding Assay Life Cycle Management, Assay Maintenance, Monitoring and Transfer.","authors":"Jeroen Stoop, James Huleatt, Luc Gagnon, Alessandra Buoninfante, Meenu Wadhwa, Chad Irwin, Christian Mayer, João Tavares Neto, Joseph Agnes, Anastasia Aksyuk, Angelique Baclin, Marie Bonhomme, Shane Cloney-Clark, Bart Corsaro, Francis Dessy, Louis Fries, Fabio Garofolo, Peter Giardina, Tina Green, Nuria Guimera, Shannon Harris, Roy Helmy, Akiko Ishii-Watabe, Ralf Jaeger, Dewal Jani, Sarah Janssen, Julie Joseph, Lisa Kierstead, Karen Makar, Jean-Claude Marshall, Dulcyane Neiva Mendes, Rocio Murphy, Sankeetha Nadarajah, Katrina Nolan, Joyce Plested, Ingrid Scully, Ivo Sonderegger, Charles Tan, Thorsten Verch, Deidre Wilkins, Arron Xu, Lingyi Zheng, Mingzhu Zhu","doi":"10.1080/17576180.2026.2682709","DOIUrl":"10.1080/17576180.2026.2682709","url":null,"abstract":"<p><p>This white paper focuses on maintenance, monitoring and transfer of Ligand Binding Assays (LBAs) supporting vaccine immunogenicity studies and is part 3 of a series to harmonize method validation and bioanalysis. The objective of this series was identified during the drafting of the 2020 White Paper in Bioanalysis. The Workshop on Recent Issues in Bioanalysis (WRIB) produces the White Paper in Bioanalysis yearly, which is one of the high-profile articles published in the journal, providing detailed discussions and recommendations on Bioanalytical Method Development and Validation. Since 2017, participation by vaccine assay validation experts and regulators in the WRIB working groups has rapidly increased due to its unique format where industry leaders and regulators can meet and exchange ideas on topics of mutual interest. In early 2021, vaccine manufacturers approached WRIB to sponsor and support the authorship and publication of an overarching vaccine assay validation document based on the 2017-2020 discussions and consensus, starting with LBA, then followed by future papers on Molecular Diagnostics (MDx including both PCR and NGS), Biofunctional Assays (BFA) and Cell-Mediated Immunity (CMI) assays validation. Using the industry and WRIB vaccine network, a vaccine immunogenicity assay validation expert working group was assembled representing 16 global companies. The work on the first 3 white papers officially began in April 2021 focusing on vaccine immunogenicity ligand binding assays (Part 1 LBA Validation, Part 2 Assay Development, Part 3 Assay Lifecycle Management, Assay Maintenance, Monitoring and Transfer). In this publication (Part 3), the activities that are required to ensure consistency of assay performance following validation are discussed. In contrast to bioanalytical methods evaluating chemical and biological drugs (ICH-M10), there are no clear guidelines for methods supporting vaccine immunogenicity studies. Hence, the authors of this White Paper hope that this common effort will help close this regulatory gap. These harmonization white papers will collectively be pivotal for whole vaccine development process.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"547-559"},"PeriodicalIF":2.1,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13348908/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148293188","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fit-for-purpose application of LC-MS in protein bioanalysis, case studies shared within the European Bioanalysis Forum Hybrid MS team.","authors":"Amanda Wilson, Richard Lucey, Emmanuel Njumbe Ediage, Katrin Schroeter, Szabolcs Szarka, Peter Blattmann, Paul Boersema, Kees Bronsema, Gregor Jordan, Sebastian Malchow, David Pekar, Heike Wiese, Bryan Marks, Frank Schalk, Marie Reille-Seroussi, Ana Villar Garea, Nico van de Merbel, Lieve Dillen, Philip Timmerman","doi":"10.1080/17576180.2026.2683269","DOIUrl":"10.1080/17576180.2026.2683269","url":null,"abstract":"<p><p>The use of liquid chromatography-mass spectrometry for quantitative large-molecule bioanalysis has increased substantially over the past decade, driven by its ability to address analytical challenges that may be difficult to resolve using traditional ligand-binding assays. In this European Bioanalysis Forum perspective, seven case studies from pharmaceutical companies and contract research organizations illustrate the fit-for-purpose application of LC-MS across different stages of drug development. These include isoform-specific quantification, subclass-resolved immunoglobulin profiling, characterization of post-translational modifications, assessment of <i>in vivo</i> biotherapeutic integrity, and multiplexed analysis in complex biological matrices. Collectively, the examples highlight how LC-MS can support selectivity, structural insight, and analytical flexibility when aligned with the specific context of use. The EBF aims to foster continued scientific exchange by encouraging the sharing of such case studies across its community.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"561-569"},"PeriodicalIF":2.1,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13557579/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148306820","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Simultaneous quantification of D-penicillamine, D-penicillamine disulfide, and L-cysteine-D-penicillamine disulfide in human plasma: optimization of sample preparation and mass spectrometry procedures to support bioequivalence studies.","authors":"Jianghong Gu, Sabrina Li, Guozhang Zou, Nilufer Tampal, Li Xia, Manjinder Kaur, Daniel Seungtaek Oh, Xiaoming Xu, Patrick J Faustino, David A Keire, Diaa Shakleya","doi":"10.1080/17576180.2026.2690263","DOIUrl":"10.1080/17576180.2026.2690263","url":null,"abstract":"<p><strong>Aim: </strong>D-penicillamine (PSH) is an active pharmaceutical ingredient used for the treatment of various diseases, such as Wilson's disease, rheumatoid arthritis, cystinuria, and heavy metal poisoning. However, evaluating PSH in plasma poses substantial analytical challenges due to drug instability, thiol-disulfide exchange reactions with endogenous thiols, and the potential formation of multiple chemical forms of PSH. This study describes the development and validation of an analytical method to ensure the stability of PSH during analysis and enable accurate bioavailability measurements and bioequivalence assessments in human plasma.</p><p><strong>Methods: </strong>An ultra-high performance liquid chromatography-tandem mass spectrometry (UHPLC-MS/MS) method was developed and validated to simultaneously determine PSH and its two major metabolites, D-penicillamine disulfide and L-cysteine-D-penicillamine disulfide, in human plasma. PSH stability was investigated under various experimental conditions to identify the optimal sample preparation procedure. The method was then applied to conduct a 90-day stability study of PSH in human plasma stored at -80°C.</p><p><strong>Results and conclusion: </strong>A sensitive and specific analytical method was developed and validated in accordance with the US FDA M10 guidance. PSH remained stable under optimized conditions for at least 90 days. This method provides pharmaceutical researchers with a standardized approach for PSH pharmacokinetic analysis and bioequivalence evaluations.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"607-617"},"PeriodicalIF":2.1,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13348919/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148315657","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pharmaceutical drug monitoring: the role of oral fluid sampling.","authors":"Sofia Soares, Tiago Rosado, Mário Barroso, Eugenia Gallardo","doi":"10.1080/17576180.2026.2684685","DOIUrl":"10.1080/17576180.2026.2684685","url":null,"abstract":"<p><p>Oral fluid has attracted increasing interest as an alternative biological matrix for monitoring pharmaceutical compounds in clinical and forensic toxicology. Its noninvasive nature, simple collection procedures, and suitability for repeated sampling make it particularly attractive for large-scale drug screening, medical diagnosis, long-term treatment monitoring, and point-of-care applications. Compared with blood sampling, oral fluid collection is better accepted by patients and does not require trained personnel, facilitating its use in decentralized or real-time testing scenarios. In addition, drug concentrations in oral fluid frequently reflect the pharmacologically active unbound fraction of compounds, which may enhance its clinical relevance for individualized dosing and evaluation of therapeutic response. Several studies have reported meaningful correlations between drug concentrations measured in oral fluid and those determined in blood (plasma or serum) for different therapeutic classes, including antiepileptics, antidepressants, analgesics, antibiotics, and immunosuppressants. These characteristics support the growing interest in oral fluid as a useful matrix for therapeutic drug monitoring strategies aimed at optimizing treatment while reducing the risk of adverse effects. This review summarizes and critically discusses recent developments in analytical approaches for the detection of pharmaceutical compounds acting on the central nervous system in oral fluid and their potential application in drug monitoring.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"639-648"},"PeriodicalIF":2.1,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13348911/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148222956","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}