Protein Science最新文献

{"title":"A symmetric region produces a novel calcium binding mode in the human Cx46 connexon.","authors":"Cristopher Stepke, Nicolas Espinoza, Fabian Parra, Alvaro Ruiz, Tomas Perez-Acle, Raul Araya-Secchi, Felipe Villanelo, Jose Antonio Garate","doi":"10.1002/pro.70691","DOIUrl":"10.1002/pro.70691","url":null,"abstract":"<p><p>The human connexon formed by connexin 46 (C-hCx46) is a channel with high voltage sensitivity and selective permeability to cations. In this work, we studied the interaction of Ca²⁺ with C-hCx46 and C-hCx26 using molecular dynamics simulations. Unlike other connexons such as the connexon formed by human connexin 26 (C-hCx26), where Ca²⁺ binds to specific sites, in C-hCx46 Ca²⁺ interacts with a toroidal confinement zone limited by negatively charged residues, whose symmetrical distribution allows it to move freely without varying its total attraction potential. This symmetry is lost in C-hCx26 due to the substitution of one of these residues by a lysine, which causes Ca²⁺ to be trapped in specific regions where the electrostatic attraction force is greater. In C-hCx46 a negative electrostatic potential is observed inside the pore, which is screened when interacting with Ca²⁺. In addition, the presence of Ca²⁺ reduces potassium and water permeability.</p>","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"35 8","pages":"e70691"},"PeriodicalIF":5.6,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13347376/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148412648","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Scalable discovery of homomeric protein-protein interactions from cross-linking mass spectrometry data with CLAUDIO 2.0.","authors":"Tobias Löser, Alexander Röhl, Markus Baier, Andrei Lupas, Oliver Kohlbacher, Hadeer Elhabashy","doi":"10.1002/pro.70732","DOIUrl":"10.1002/pro.70732","url":null,"abstract":"<p><p>Cross-linking mass spectrometry (XL-MS) is a powerful biochemical approach for residue-level characterization of protein structures and interactions under near-native conditions. The growing scale of XL-MS datasets demands scalable analysis pipelines that capture signals often overlooked in conventional workflows, including homomeric interactions. Here, we present CLAUDIO 2.0, a next-generation framework for structural analysis of large-scale XL-MS data. CLAUDIO 2.0 identifies homomeric interactions using overlapping peptide sequences and structural evaluation. Our optimized workflow improves computational efficiency, enabling scalable analysis and expanding structural coverage. Applied to a human mitochondrial XL-MS dataset, CLAUDIO 2.0 evaluates over 75% of cross-links using available high-confidence structural models, reduces runtime by over 95% (averaging 5 s per cross-link) compared to its predecessor, and identifies 205 proteins with homomeric interaction signals. CLAUDIO 2.0 is freely available under the MIT License at (https://github.com/ElhabashyLab/CLAUDIO) and as a web server at (https://elhabashylab.org/claudio), providing an accessible platform for scalable structural proteomics.</p>","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"35 8","pages":"e70732"},"PeriodicalIF":5.6,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13410943/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148606914","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction to \"Structure-activity relationship study shows versatility in substrate specificity for heterodisulfide reductase in methanogenic archaea\".","authors":"","doi":"10.1002/pro.70711","DOIUrl":"10.1002/pro.70711","url":null,"abstract":"","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"35 8","pages":"e70711"},"PeriodicalIF":5.6,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13358353/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148430840","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"CoCryoViS: Collaborative online cryo-electron tomography visualization system.","authors":"Omar Mena, Uroš Šmajdek, Weiping Zhang, Piao Yu, Tobias Klein, Stefan T Arold, Sai Li, Ivan Viola, Ciril Bohak","doi":"10.1002/pro.70679","DOIUrl":"10.1002/pro.70679","url":null,"abstract":"<p><p>We present a collaborative, interactive, web-based visualization and processing system for Cryo-Electron Tomography (cryo-ET) data that supports the complete workflow, from raw tilt-series projections to final 3D segmentations. The system integrates tilt-series alignment, motion correction, tomographic reconstruction, manual and pseudo-annotation, deep model training, inference, and visualization, all accessible through a unified web-based interface. The backend manages computationally intensive tasks, including advanced tomographic reconstruction, pseudo-annotation generation, deep learning model training, and large-scale segmentation of new datasets. It features separate queues for CPU and GPU tasks, allowing users to prepare and manage large workloads in advance. The frontend supports lightweight tomographic reconstruction, manual data annotation, segmentation with pretrained models, interactive exploration of pipeline stages, and real-time monitoring of queued tasks. Key processing steps are available on both the client and server sides, providing flexibility for diverse computational environments, enabling visualization of externally hosted datasets, and supporting data privacy when required. The system is designed for collaborative workflows, enabling multiple users to share input data, annotations, and trained models within joint projects. Its modular architecture allows easy extension with additional stages on either the client or server side, making it adaptable to specialized pipelines within individual institutions. We demonstrate the system's capabilities on representative cryo-ET datasets, highlighting its utility for both individual researchers and distributed teams working on structural analysis of complex cellular environments. The initial release of the system is available at https://cocryovis.lgm.fri.uni-lj.si/ (Project repository: https://github.com/nanovis/cocryovis, mirror deploy: https://tomography.kaust.edu.sa/), and the entire system will become open source so that any visualization or domain researcher can further enhance its functionality.</p>","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"35 8","pages":"e70679"},"PeriodicalIF":5.6,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13354744/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148423340","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular and energetic basis of histidine switch dynamics in respiratory complex I.","authors":"Erik Endres, Mahdi Torabi, Mai Jousmäki, Kim Vy Huynh, Cristina Pecorilla, Oleksii Zdorevskyi, Volker Zickermann, Vivek Sharma","doi":"10.1002/pro.70720","DOIUrl":"10.1002/pro.70720","url":null,"abstract":"<p><p>The respiratory complex I in mitochondria and bacteria drives the two-electron reduction of quinone to pump protons across the membrane. The molecular basis of this catalytic reaction remains enigmatic despite significant progress in structural characterization of the complex. A highly conserved histidine residue in the distal antiporter-like subunit of its membrane domain has been shown to undergo conformational changes in molecular simulations and cryo-EM structures. However, the function of histidine switch dynamics and the energetics of its conformational transitions remain unclear. Here, by applying enhanced sampling classical molecular dynamics simulations, we evaluate the energetics of the histidine switch dynamics and demonstrate that it is coupled to the tautomeric state of histidine and to the charge state of lysine residues ca. 10 Å apart, which cause hydrogen bond restructuring and stabilize the histidine residue in specific conformations. Hybrid QM/MM metadynamics-based free energy simulations show that the histidine switch participates in gated proton transfer and may function as a proton confurcation device in complex I and related proteins.</p>","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"35 8","pages":"e70720"},"PeriodicalIF":5.6,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13358369/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148430855","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A cryptic aromatic binding pocket in the highly thermostable GpgS from Mycobacterium hassiacum hints at MGLP pathway crosstalk.","authors":"Daniela Nunes-Costa, Alexandra Silva, Susana Alarico, José A Manso, Nuno Empadinhas, Pedro José Barbosa Pereira, Sandra Macedo-Ribeiro","doi":"10.1002/pro.70713","DOIUrl":"10.1002/pro.70713","url":null,"abstract":"<p><p>Mycobacteria have long posed a threat to human health, being responsible for a range of hard-to-treat infections such as tuberculosis, leprosy, and other chronic diseases caused by nontuberculous mycobacteria. Their intrinsic resistance to antibiotics and resilience when exposed to environmental stress complicate treatment and underscore the need for discovering novel drug targets and developing new therapeutic strategies. Mycobacterium hassiacum, a thermophilic mycobacterium, is a promising source of stable proteins suitable for detailed structural analysis. In this study, we investigated its glucosyl-3-phosphoglycerate synthase (GpgS), an enzyme that plays a key role in the biosynthesis of methylglucose lipopolysaccharides in Mycobacterium tuberculosis and is implicated in responses to nitrogen starvation and thermal stress in different mycobacterial species. We confirmed the potential of M. hassiacum as a source of enzymes amenable to structural studies, as its GpgS ortholog yielded not only the first mycobacterial GpgS crystallographic structure at near-atomic resolution (1.10 Å) but also multiple high-resolution structures under different pH conditions and in complex with various substrates. These structural insights revealed a previously unrecognized aromatic binding pocket that is not only cryptic in nature but also capable of accommodating the substrates p-aminobenzoic acid and p-hydroxybenzaldehyde, which have been found to be relevant in its genetic context, thereby establishing a direct link between GpgS activity and broader metabolic pathways in mycobacteria. Our findings establish M. hassiacum as a valuable model for structural enzymology in mycobacteria and highlight GpgS as a potential drug target. The detailed structural data provided here offer a foundation for rational drug design, opening new avenues for the development of inhibitors targeting this key, potentially pleiotropic enzyme.</p>","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"35 8","pages":"e70713"},"PeriodicalIF":5.6,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13379784/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148471862","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Small electrical field effects on biological polymers.","authors":"Parvin Abazari, Seyed Peyman Shariatpanahi, Bahram Goliaei","doi":"10.1002/pro.70701","DOIUrl":"10.1002/pro.70701","url":null,"abstract":"<p><p>Effects of small-magnitude, long-lasting external electric fields on the mechanical bending response of biological polymers such as microtubule are analyzed. We used coarse-grained Brownian dynamics simulations to model polymers as bead-spring with variable lengths and adjustable bending stiffness that are subject to external forces applied uniformly across the polymer or to the last monomer. Simulations show that, especially when applied over long periods of time, forces as low as 0.001 <math> <semantics> <mrow><msub><mi>k</mi> <mi>B</mi></msub> <mi>T</mi> <mo>/</mo> <mi>σ</mi></mrow> <annotation>$$ {k}_BT/sigma $$</annotation></semantics> </math> ( <math> <semantics><mrow><mi>σ</mi></mrow> <annotation>$$ sigma $$</annotation></semantics> </math> is the length scale of a monomer) can cause detectable curvature variations in polymers. This small force, equivalent to <math> <semantics><mrow><mn>3</mn> <mspace></mspace> <mi>V</mi> <mo>/</mo> <mi>cm</mi></mrow> <annotation>$$ 3kern0.33em mathrm{V}/mathrm{cm} $$</annotation></semantics> </math> for microtubules and <math> <semantics><mrow><mn>6</mn> <mspace></mspace> <mspace></mspace> <mi>V</mi> <mo>/</mo> <mi>cm</mi></mrow> <annotation>$$ 6kern0.43em mathrm{V}/mathrm{cm} $$</annotation></semantics> </math> for actin filaments, when applied to microtubules of lengths 400 and 1600 nm and to actin filaments of length 600 nm for the respective durations of 75, 4.8, and 34 μs, produces significant effects on the polymers. Furthermore a force of 0.01 <math> <semantics> <mrow><msub><mi>k</mi> <mi>B</mi></msub> <mi>T</mi> <mo>/</mo> <mi>σ</mi></mrow> <annotation>$$ {k}_BT/sigma $$</annotation></semantics> </math> <math> <semantics><mrow><mo>≃</mo></mrow> <annotation>$$ simeq $$</annotation></semantics> </math> <math> <semantics><mrow><mn>6</mn> <mspace></mspace> <mspace></mspace> <mi>KV</mi> <mo>/</mo> <mi>cm</mi></mrow> <annotation>$$ 6kern0.35em mathrm{KV}/mathrm{cm} $$</annotation></semantics> </math> for a 50-nm-long amyloid fibril requires a pulse duration of 600 μs to produce a significant change. Bending results are also influenced by the directionality of force application; perpendicular forces result in more angular deformation than parallel forces. A critical duration of force exposure required to induce structural changes was defined by the nonlinear dependence of polymer response on force magnitude and stiffness, as revealed by first passage time analysis. These results provide mechanistic insights into the effects of pulsed or variable electric fields on cytoskeletal deformation by quantifying the effective action time of PEFs in biophysical interventions like electroporation and tumor treating fields.</p>","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"35 8","pages":"e70701"},"PeriodicalIF":5.6,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13347630/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148412802","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Persistent sheaf Laplacian analysis of protein stability and solubility changes upon mutation.","authors":"Yiming Ren, Junjie Wee, Xi Chen, Grace Qian, Guo-Wei Wei","doi":"10.1002/pro.70700","DOIUrl":"10.1002/pro.70700","url":null,"abstract":"<p><p>Genetic mutations frequently disrupt protein structure, stability, and solubility, acting as primary drivers for a wide spectrum of diseases. Despite the critical importance of these molecular alterations, existing computational models often lack interpretability and fail to integrate essential physicochemical interactions. To overcome these limitations, we propose SheafLapNet, a predictive framework grounded in the mathematical theory of Topological Deep Learning (TDL) and Persistent Sheaf Laplacian (PSL). Unlike standard Topological Data Analysis (TDA) tools such as persistent homology, which are often insensitive to heterogeneous information, PSL explicitly encodes specific physical and chemical information such as partial charges directly into the topological analysis. SheafLapNet synergizes these sheaf-theoretic invariants with advanced protein transformer features and auxiliary physical descriptors to capture intrinsic molecular interactions in a multiscale and mechanistic manner. To validate our framework, we employ rigorous benchmarks for both regression and classification tasks. For stability prediction, we utilize the comprehensive S2648 dataset, alongside the independent S350 and strictly non-redundant S669 blind test sets to ensure robust evaluation and thermodynamic consistency. For solubility prediction, we employ the PON-Sol2 dataset, which provides annotations for increased, decreased, or neutral solubility changes. By integrating these multi-perspective features, SheafLapNet achieves state-of-the-art performance across these diverse benchmarks, demonstrating that sheaf-theoretic modeling significantly enhances both interpretability and generalizability in predicting mutation-induced structural and functional changes.</p>","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"35 8","pages":"e70700"},"PeriodicalIF":5.6,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13351944/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148423440","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The characterization of a new stabilized lactonase from the endophytic fungi Aspergillus pseudonomiae with anti-bacterial and anti-fungal properties.","authors":"Dor Ben Tovim, Olena Trofimyuk, Elon Yariv, Gali Prag, Livnat Afriat-Jurnou","doi":"10.1002/pro.70729","DOIUrl":"10.1002/pro.70729","url":null,"abstract":"<p><p>Microorganisms use diverse small-molecule signals to coordinate behavior, supporting interspecies and interkingdom communication. These chemical dialogs shape fundamental biological processes and define interactions from cooperation to antagonism. Quorum-quenching (QQ) enzymes, which degrade or modify quorum sensing (QS) molecules such as N-acyl-homoserine lactones (AHLs), may play a pivotal role in shaping these networks. While bacterial QQ lactonases are well-characterized, fungal lactonases remain undercharacterized, including their potential to target both bacterial QS molecules and fungal secondary metabolites. Using phylogenetic and structural analysis, we identified putative lactonases from the metallo-β-lactamase-like lactonase family in fungi and biochemically validated the activity of one of them, from Aspergillus pseudonomiae. Structural alignment between bacterial lactonases and the AlphaFold-predicted structure of the fungal homolog further supports that the fungal protein is indeed a lactonase. We then applied Protein Repair One-Stop Shop algorithm for stability engineering to design a variant with improved expression in Escherichia coli and thermal stability. Purified enzyme demonstrated broad substrate specificity, effectively degrading various bacterial AHLs, with k_cat/K_M values of up to 1.4 × 10⁵ s^-1M^-1. Both docking analysis and in vitro assays indicated that the enzyme could accommodate and act on the fungal secondary metabolite patulin, a mycotoxin associated with post-harvest disease, showing high catalytic efficiency (1.1 × 10⁴ s^-1M^-1). When added exogenously to microbial cultures, the enzyme reduced bacterial biofilms and impaired fungal hyphal development, with the hyphal inhibition accompanied by a concentration-dependent increase in ROS. Together, these results show that this fungal enzyme functions as a dual-acting lactonase, positioning it as an interference enzyme in chemical signaling of fungi and bacteria and as a means to suppress pathogens and reduce patulin contamination in food.</p>","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"35 8","pages":"e70729"},"PeriodicalIF":5.6,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13413597/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148606958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Damping amyloid-associated conformational fluctuations in a protein by an engineered diselenide bridge.","authors":"Yanwu Yang, Balamurugan Dhayalan, Andreas Ehnbom, Orit Weil-Ktorza, Norman Metanis, Michael A Weiss","doi":"10.1002/pro.70697","DOIUrl":"10.1002/pro.70697","url":null,"abstract":"<p><p>Polypeptide cross-β assembly, characteristic of diverse proteotoxic diseases, defines a general thermodynamic ground state and limits the shelf lives of peptide- and protein therapeutics. A model is provided by insulin. Although the hormone contains a predominance of α-helix, its fibrils exhibit cross-β reorganization. In the real world, aggregation-coupled fibrillation of insulin underlies its degradation above room temperature, impairing activity and imposing a complex global \"cold chain\" of transport and storage. Here, we describe biophysical protection of an insulin analog at an elevated temperature by an engineered diselenide bridge. Our studies focused on insulin glargine, the active ingredient of long-acting formulations in broad clinical use. Insoluble in a subcutaneous depot due to its shifted isoelectric point, the analog dissolves at pH 4.0 and so, unlike neutral formulations of the wild-type hormone, is unprotected by zinc-mediated hexamer assembly. Whereas at 37°C the fibrillation lag time of insulin glargine is accelerated by fourfold relative to WT insulin, such instability is circumvented by pairwise substitution of Cys^A6 and Cys^A11 by selenocysteine. Protection from fibrillation correlates with augmented resistance to pepsin cleavage, guanidine denaturation, and thermal unfolding. Although NMR structures of insulin glargine and its diselenide analog are similar, damping of conformational fluctuations is evidenced by patterns of ¹H-NMR chemical shifts, helix-associated NOEs, amide-resonance line widths, and ¹H-²H amide-proton exchange. Such damping is discussed in relation to molecular dynamics simulations. Demonstrating a likely mechanistic relationship between fibrillation and native-state conformational fluctuations, our findings highlight the translational promise of \"dynamic engineering\" via nonstandard mutagenesis.</p>","PeriodicalId":20761,"journal":{"name":"Protein Science","volume":"35 8","pages":"e70697"},"PeriodicalIF":5.6,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13386395/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148536684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}