Journal of Molecular Recognition最新文献

{"title":"Computational Insights Into the Conformational Dynamics of the Dengue Virus Capsid Protein","authors":"Dwaipayan Chaudhuri,&nbsp;Kalyan Giri","doi":"10.1002/jmr.70046","DOIUrl":"https://doi.org/10.1002/jmr.70046","url":null,"abstract":"<div>\u0000 \u0000 <p>The Dengue virus (DENV) capsid protein plays an important role in the viral lifecycle, including encapsidation of the genome, recruitment of lipid droplets, and assembly of particles. Capsid protein includes a hydrophobic pocket, which plays a central role in these functions and switches between closed and open conformations. This work studies the conformational change pathway of the capsid protein, specifically how the molecular mechanisms controlling the opening and closing of the hydrophobic pocket are controlled. By using a combination of different types of molecular dynamics simulations and enhanced sampling methods, we share insights on the structural rearrangements that play a crucial role in governing these transitions. Our results show that lipid binding modulates the accessibility of the hydrophobic pocket through environmental cues. In the open conformation, the pocket is involved in the interaction with lipids, stabilization of capsid dimers, and the promotion of immature virus assembly. Conversely, the closed conformation protects the hydrophobic pocket from the surrounding aqueous media as also preventing premature interactions in the solution phase that might disrupt protein stability. Such insights allow a deep understanding of capsid protein's conformational dynamics and represent a promising set of potent targets for antiviral strategies aiming to interfere with its functional transitions.</p>\u0000 </div>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"39 6","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149068263","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"BTNL2 As an Immunomodulatory Ligand: Delineating an Orphan Immune Checkpoint","authors":"Ishwar Patidar,&nbsp;Ramya Aswthareddy,&nbsp;Anirudha Lakshminarasimhan,&nbsp;Susan Idicula-Thomas","doi":"10.1002/jmr.70047","DOIUrl":"https://doi.org/10.1002/jmr.70047","url":null,"abstract":"<div>\u0000 \u0000 <p>Butyrophilin-like 2 (BTNL2) is a Type I transmembrane glycoprotein of the immunoglobulin superfamily (IgSF) that functions as a tissue-specific immune checkpoint regulator with structural homology to B7 ligands. BTNL2 suppresses T cell activation by attenuating IL-2 secretion through the AP-1, NFAT, and NF-κB pathways. Functional and in vivo studies have established BTNL2 as a regulator of immune responses and have implicated it in tumor immune evasion and cancer progression. Therapeutically, BTNL2 modulation offers dual opportunities: agonists to restore tolerance in autoimmunity and transplantation, and antagonists to overcome tumor immune evasion. Structurally, BTNL2 differs from other canonical checkpoint ligands of the IgSF superfamily, as it contains two sets of IgV and IgC domains connected by a heptameric linker sequence. However, even after two decades of research, its cognate receptor remains unidentified.</p>\u0000 </div>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"39 6","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149068111","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis and Binding Affinity Insights of 2-Phenyl-1H-Benzimidazole Inhibitors Targeting FTO by Spectroscopic Characterization and Molecular Docking","authors":"Jing Wang,&nbsp;Yahong Chen,&nbsp;Ruiyong Wang","doi":"10.1002/jmr.70045","DOIUrl":"10.1002/jmr.70045","url":null,"abstract":"<div>\u0000 \u0000 <p>In this work, we designed and synthesized 28 structural analogs of 2-phenyl-1<i>H</i>-benzimidazole. Three of these compounds exhibited stronger binding affinity to FTO, as determined by fluorescence spectroscopy. The results indicate that the binding process is spontaneous and occurs primarily via a static quenching mechanism, driven mainly by hydrogen bonding and van der Waals forces. The interactions of these three lead analogs with FTO were further investigated using UV–visible absorption spectroscopy, circular dichroism spectroscopy, and molecular docking. The docking results are consistent with the thermodynamic data. Among the 28 synthesized derivatives, compounds <b>7</b>, <b>8</b>, and <b>11</b> exhibited the strongest predicted binding affinities toward FTO and were selected for further spectroscopic and molecular docking studies. In preliminary biological evaluation, compound <b>7</b> showed antiproliferative activity against K562 cells with an IC₅₀ value of 18.11 μM. This study provides valuable insights into the interaction mechanisms between 2-phenyl-1<i>H</i>-benzimidazole analogs and FTO.</p>\u0000 </div>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"39 5","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148969465","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Inhibition and Molecular Recognition of Lactoperoxidase by Acetohydrazide-Based Sulfonamide Derivatives","authors":"Başak Gökçe,&nbsp;Gülnur Arslan,&nbsp;Muhammed Tilahun Muhammed,&nbsp;Özlem Albayrak","doi":"10.1002/jmr.70044","DOIUrl":"https://doi.org/10.1002/jmr.70044","url":null,"abstract":"<div>\u0000 \u0000 <p>Lactoperoxidase (LPO) is a heme-containing enzyme widely distributed in mammalian secretions, contributing to host defense through the generation of antimicrobial oxidants. Unintended inhibition of LPO by therapeutic agents may impair mucosal immunity, making the investigation of potential inhibitors clinically relevant. In this study, the inhibitory effects of 11 acetohydrazide-based sulfonamide derivatives on bovine milk LPO were investigated using combined biochemical and computational approaches. The compounds exhibited diverse inhibition profiles, with IC₅₀ values ranging from 2.32 ± 0.14 to 13.4 ± 2.05 μM. The corresponding <i>Kᵢ</i> values were determined in the low micromolar range, varying from 1.25 ± 0.05 to 7.53 ± 0.03 μM. Among them, <b>4b-2</b> (3-pyridyl) and 4a-5 (2-naphthyl) derivatives were identified as the most potent inhibitors, acting through a competitive inhibition mechanism with low micromolar <i>Kᵢ</i> values. The binding mechanisms of relatively active compounds in the enzymatic assay were explored through molecular modeling. The docking study disclosed that compounds <b>4a-5</b> and <b>4b-2</b> would show higher binding potential to the LPO structure. The two compounds formed stable complexes with the enzyme structure according to the molecular dynamics (MD) simulation study. These interactions were mainly governed by hydrogen bonding and π–π stacking interactions involving key residues in the heme-containing active site, supporting a competitive binding mode consistent with the kinetic data. Overall, the combined biochemical and computational findings suggest that acetohydrazide-based sulfonamides represent promising scaffolds for the development of potent and selective LPO inhibitors and provide new insights into the molecular recognition patterns governing their interaction with the LPO active site.</p>\u0000 </div>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"39 5","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148753846","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Inhibition and Molecular Recognition of Lactoperoxidase by Acetohydrazide-Based Sulfonamide Derivatives","authors":"Başak Gökçe,&nbsp;Gülnur Arslan,&nbsp;Muhammed Tilahun Muhammed,&nbsp;Özlem Albayrak","doi":"10.1002/jmr.70044","DOIUrl":"https://doi.org/10.1002/jmr.70044","url":null,"abstract":"<div>\u0000 \u0000 <p>Lactoperoxidase (LPO) is a heme-containing enzyme widely distributed in mammalian secretions, contributing to host defense through the generation of antimicrobial oxidants. Unintended inhibition of LPO by therapeutic agents may impair mucosal immunity, making the investigation of potential inhibitors clinically relevant. In this study, the inhibitory effects of 11 acetohydrazide-based sulfonamide derivatives on bovine milk LPO were investigated using combined biochemical and computational approaches. The compounds exhibited diverse inhibition profiles, with IC₅₀ values ranging from 2.32 ± 0.14 to 13.4 ± 2.05 μM. The corresponding <i>Kᵢ</i> values were determined in the low micromolar range, varying from 1.25 ± 0.05 to 7.53 ± 0.03 μM. Among them, <b>4b-2</b> (3-pyridyl) and 4a-5 (2-naphthyl) derivatives were identified as the most potent inhibitors, acting through a competitive inhibition mechanism with low micromolar <i>Kᵢ</i> values. The binding mechanisms of relatively active compounds in the enzymatic assay were explored through molecular modeling. The docking study disclosed that compounds <b>4a-5</b> and <b>4b-2</b> would show higher binding potential to the LPO structure. The two compounds formed stable complexes with the enzyme structure according to the molecular dynamics (MD) simulation study. These interactions were mainly governed by hydrogen bonding and π–π stacking interactions involving key residues in the heme-containing active site, supporting a competitive binding mode consistent with the kinetic data. Overall, the combined biochemical and computational findings suggest that acetohydrazide-based sulfonamides represent promising scaffolds for the development of potent and selective LPO inhibitors and provide new insights into the molecular recognition patterns governing their interaction with the LPO active site.</p>\u0000 </div>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"39 5","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148753845","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Prediction-Based Algorithms for Long-Range High-Speed Force Spectroscopy","authors":"Lorenzo Villanueva,&nbsp;Yogesh Saravanan,&nbsp;Mar Eroles,&nbsp;Antoine Couderc,&nbsp;Jorge Rodriguez-Ramos,&nbsp;Qingze Zou,&nbsp;Felix Rico","doi":"10.1002/jmr.70043","DOIUrl":"https://doi.org/10.1002/jmr.70043","url":null,"abstract":"<p>We present a high-speed force microscopy platform mounted on a confocal microscope with a <i>z</i> sample stage enabling long-range, high-speed force spectroscopy measurements on biological samples. The control software is built on a field-programmable gate array (FPGA)-based data acquisition and processing system, complemented with a custom graphical user insterface (GUI). We introduce smart algorithms based on probe-engagement prediction algorithms that leverage previously measured probe-sample contact to accelerate the probe engagement to mm/s and decelerate it in proximity of contact to user-defined μm/s velocities. This significantly reduces long-range force curve acquisition time and data density. Using this system, we provide proof-of-concept mechanical maps of cell clusters to extract topography and viscoelastic parameters. To further explore the versatility of our system, we probed the forces required to extract membrane tethers from monocytic cells using ultrashort cantilevers functionalised with adhesion molecules. Our system allowed us to cover retract velocities from ~1 μm/s up to ~6000 μm/s, and to explore the dynamics of tether formation at physiologically relevant velocities. Our results show that coupling extended <i>z</i> displacement with the prediction-based engagement algorithms enables rapid, quantitative mechanical mapping of heterogeneous biological samples with large topography variation and supports measurements requiring long distances at high velocities.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"39 5","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-08-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.70043","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148662128","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Prediction-Based Algorithms for Long-Range High-Speed Force Spectroscopy","authors":"Lorenzo Villanueva,&nbsp;Yogesh Saravanan,&nbsp;Mar Eroles,&nbsp;Antoine Couderc,&nbsp;Jorge Rodriguez-Ramos,&nbsp;Qingze Zou,&nbsp;Felix Rico","doi":"10.1002/jmr.70043","DOIUrl":"https://doi.org/10.1002/jmr.70043","url":null,"abstract":"<p>We present a high-speed force microscopy platform mounted on a confocal microscope with a <i>z</i> sample stage enabling long-range, high-speed force spectroscopy measurements on biological samples. The control software is built on a field-programmable gate array (FPGA)-based data acquisition and processing system, complemented with a custom graphical user insterface (GUI). We introduce smart algorithms based on probe-engagement prediction algorithms that leverage previously measured probe-sample contact to accelerate the probe engagement to mm/s and decelerate it in proximity of contact to user-defined μm/s velocities. This significantly reduces long-range force curve acquisition time and data density. Using this system, we provide proof-of-concept mechanical maps of cell clusters to extract topography and viscoelastic parameters. To further explore the versatility of our system, we probed the forces required to extract membrane tethers from monocytic cells using ultrashort cantilevers functionalised with adhesion molecules. Our system allowed us to cover retract velocities from ~1 μm/s up to ~6000 μm/s, and to explore the dynamics of tether formation at physiologically relevant velocities. Our results show that coupling extended <i>z</i> displacement with the prediction-based engagement algorithms enables rapid, quantitative mechanical mapping of heterogeneous biological samples with large topography variation and supports measurements requiring long distances at high velocities.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"39 5","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-08-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.70043","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148662130","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Reconstruction of the Flexible IgM Fc Core Using Atomic Force Microscopy Topography and the AFM-Assembly Pipeline","authors":"Harinderbir Kaur,&nbsp;Andrea J. Pinto,&nbsp;Jean-Baptiste Reiser,&nbsp;Wai Li Ling,&nbsp;Jean-Luc Pellequer","doi":"10.1002/jmr.70041","DOIUrl":"10.1002/jmr.70041","url":null,"abstract":"<p>Immunoglobulin M (IgM) is the first class of antibody produced in response to pathogens. It also plays an important role in regulating the immune response, including in autoimmunity. IgM pentamers consist of an Fc core composed of Cμ2, Cμ3, and Cμ4 domains, as well as 10 Fab domains composed of Cμ1 and a variable domain. In this study, we use high-resolution atomic force microscopy (AFM) topography to constrain the reconstruction of pentameric IgM Fc core pseudo-atomic model (without Fabs). Reconstruction is performed in two stages using the AFM-Assembly pipeline. First, we fit the known cryo-EM structure of the inner core of the IgM Fc (Cμ3-Cμ4) and the known x-ray structure of Cμ2 beneath the AFM topographs using the DockAFM tool. Second, the two structural units are assembled to generate a complete pentameric IgM Fc core structure. The experimentally constrained reconstruction of the IgM Fc core reveals a divergence in the assembly of the five Cμ2 monomers: the first and last monomers (M1 and M5) are tightly attached to the inner core, while the remaining monomers (M2–M4) are more loosely bound. This reconstruction describes multiple alternative conformations for the attachment of the Cμ2 domains, suggesting that the reconstruction protocol integrates molecular flexibility present in molecules individually deposited on the AFM substrate.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"39 4","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-07-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13395525/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148579081","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Atomic Force Microscopy Based Single Molecule Recognition: Deciphering Biological Interactions at the Nanoscale","authors":"Huaiwei Zhang,&nbsp;Qianhui Xu,&nbsp;Junmei Chen,&nbsp;Danhong Chen,&nbsp;Haijian Zhong,&nbsp;Weidong Zhao","doi":"10.1002/jmr.70042","DOIUrl":"10.1002/jmr.70042","url":null,"abstract":"<div>\u0000 \u0000 <p>Atomic Force Microscopy (AFM) based single molecule recognition has emerged as a transformative paradigm in nanoscale biology, enabling direct investigation of biological interactions under physiological conditions. This technology bridges critical gaps between structural characterization and functional analysis by providing unparalleled capabilities for quantifying binding forces, mapping molecular distributions, and resolving kinetic parameters at the single molecule level. The core methodology relies on precision probe functionalization strategies, such as oriented immobilization and polyethylene glycol (PEG) linkers, to ensure specific recognition while minimizing nonspecific interactions. Advanced techniques, including single molecule force spectroscopy (SMFS) and topography and recognition imaging (TREC), allow simultaneous acquisition of morphological and binding data with nanometer resolution, revealing insights into molecular organization and dynamics. Applications span diverse domains, from fundamental studies of antigen-antibody interactions and DNA-protein binding to clinical investigations of membrane receptor distributions in cancer cells and pathological diagnosis based on mechanical properties. Despite challenges in throughput, signal resolution, and standardization, integration with super-resolution microscopy and spectroscopic techniques demonstrates significant potential. Future developments emphasize multimodal correlation, artificial intelligence-assisted data analysis, and clinical translation toward nano biopsy, positioning AFM as a highly valuable and complementary platform for advancing molecular biophysics, drug discovery, and personalized medicine, notably due to its unique capability to combine nanoscale imaging with single-molecule force measurement on the same sample under physiological conditions.</p>\u0000 </div>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"39 4","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148421172","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"3D-Printed Structures Versus Drilled Cavities: A Comparison of Microconfinement Methods for Rheological Characterisation of Multicellular Aggregates","authors":"Isis V. M. Lima,&nbsp;Chukwuma Chris Muoghalu,&nbsp;Shruti G. Kulkarni,&nbsp;Mènie Wiemer,&nbsp;Jonas Michalewski,&nbsp;Sander van den Driesche,&nbsp;Wiebke Gehlken,&nbsp;Michael J. Vellekoop,&nbsp;Manfred Radmacher","doi":"10.1002/jmr.70040","DOIUrl":"10.1002/jmr.70040","url":null,"abstract":"<p>Three-dimensional (3D) cell culture systems are increasingly recognised as more physiologically relevant models than traditional two-dimensional cultures, as they better mimic the native tumour microenvironment and enable the study of complex cellular behaviour. However, applying atomic force microscopy (AFM) to these models is challenging due to the inherent instability of multicellular aggregates, which complicates reproducible mechanical property measurements. To address this, we developed and evaluated two distinct strategies for confining multicellular aggregates for AFM analysis. In the first approach, aggregates were encapsulated in porous 3D-printed truncated conical microstructures fabricated by two-photon polymerisation. These structures were designed to allow medium perfusion, which is hypothesised to improve nutrient and metabolite exchange by enhancing fluid accessibility within the confined environment. In the second, cylindrical cavities were microfabricated into the base of PolyHEMA-coated Petri dishes to provide a simple yet robust platform for aggregate retention. Both methods successfully confined aggregates without compromising cellular integrity, enabling reproducible and reliable measurements of stiffness and viscoelasticity. Human pancreatic cancer cells (PANC-1) were used both as single cells and as monotypic aggregates. Aggregates confined in either system were consistently softer than substrate-attached single cells, indicating reduced cytoskeletal tension and altered remodelling in 3D environments. Among the two approaches, cylindrical cavities provided more reliable aggregate retention, whereas the 3D-printed truncated conical structures may possibly facilitate improved medium access through their porous architecture. Together, these microconfinement strategies enable reproducible mechanical characterisation of multicellular aggregates and extend the applicability of AFM to tumour mechanobiology and the assessment of anticancer therapies.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"39 4","pages":""},"PeriodicalIF":2.7,"publicationDate":"2026-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.70040","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148368685","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}