Open BiologyPub Date : 2025-02-01Epub Date: 2025-02-19DOI: 10.1098/rsob.240225
Sebastian Tanco, Veronique Jonckheere, Arun Kumar Tharkeshwar, Annelies Bogaert, Kris Gevaert, Wim Annaert, Petra Van Damme
{"title":"Proximal partners of the organellar N-terminal acetyltransferase NAA60: insights into Golgi structure and transmembrane protein topology.","authors":"Sebastian Tanco, Veronique Jonckheere, Arun Kumar Tharkeshwar, Annelies Bogaert, Kris Gevaert, Wim Annaert, Petra Van Damme","doi":"10.1098/rsob.240225","DOIUrl":"10.1098/rsob.240225","url":null,"abstract":"<p><p>Biotin identification (BioID) is an interactomics approach that utilizes proximity labelling to map the local interactome or proxeome of proteins within a cell. This study applies BioID to investigate proteins proximal to NAA60 (N-alpha-acetyltransferase 60), an N-terminal acetyltransferase (NAT) of pathological significance in human disease, characterized by its unique Golgi localization. NAA60 is known to N-terminally acetylate transmembrane proteins that present their N-terminus on the cytosolic face of the membrane, and its involvement in maintaining Golgi structure has previously been established. Using a stable cell-line expressing an NAA60-BirA* fusion protein, we isolated biotinylated proteins through streptavidin affinity purification. Mass spectrometry analysis revealed over 100 proximal partners of NAA60, enriched in proteins localized on the <i>trans</i>-side of the Golgi apparatus. High-confidence proximity interactors included golgins and GRASP proteins, essential for Golgi integrity. Considering the transmembrane nature of NAA60, the identification of biotinylated peptides inferred the topology of transmembrane protein interactors within the secretory pathway. Subsequent suborganellar localization analysis revealed a more prominent <i>medial</i>/<i>trans</i>-Golgi localization of NAA60. Our findings underscore the role of NAA60 and its interactors in maintaining Golgi structural integrity and highlight the effectiveness of BioID in generating critical protein topology data, invaluable for enhancing the prediction of protein topology within cellular compartments.</p>","PeriodicalId":19629,"journal":{"name":"Open Biology","volume":"15 2","pages":"240225"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11835485/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143449570","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}
Open BiologyPub Date : 2025-02-01Epub Date: 2025-02-26DOI: 10.1098/rsob.240304
Domenic W Camenzind, Selina Bruckner, Peter Neumann, Annette Van Oystaeyen, Verena Strobl, Geoffrey R Williams, Lars Straub
{"title":"Microsporidian parasite impairs colony fitness in bumblebees.","authors":"Domenic W Camenzind, Selina Bruckner, Peter Neumann, Annette Van Oystaeyen, Verena Strobl, Geoffrey R Williams, Lars Straub","doi":"10.1098/rsob.240304","DOIUrl":"10.1098/rsob.240304","url":null,"abstract":"<p><p>Emerging infectious diseases can have a major impact on fitness of novel hosts, thereby contributing to ongoing species declines. In social insects, collaborative brood care by workers and successful mating of male sexuals are key to colony fitness. The microsporidian endoparasite <i>Nosema ceranae</i> has spread almost globally, shifting across honeybee species and now to bumblebees. However, despite <i>N. ceranae</i> being linked to recent population declines, its possible impact on bumblebee colony fitness remains poorly understood. Here, we show that <i>N. ceranae</i> infections can significantly impact <i>Bombus terrestris</i> worker feeding glands, as well as longevity, sperm quality and mating abilities of drones. In the laboratory, workers and drones were either exposed to the parasite or not. Then, parasite infection rates and loads, as well as lethal and sublethal parameters, were assessed. Infected drones revealed higher parasite infection rates and spore titres, as well as mortality compared with female workers, suggesting sex-specific susceptibility. Furthermore, infections impaired feeding glands, affected sperm traits and altered mating behaviour, all of which are key to colony fitness. Our findings provide a mechanistic explanation on how <i>N. ceranae</i> contributes to the ongoing decline of wild bumblebee populations, calling for respective mitigation measures.</p>","PeriodicalId":19629,"journal":{"name":"Open Biology","volume":"15 2","pages":"240304"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11858756/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143502599","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}
Open BiologyPub Date : 2025-02-01Epub Date: 2025-02-19DOI: 10.1098/rsob.240112
J M Pan, H Betts, A Cubbon, L He, E L Bolt, P Soultanas
{"title":"The human HELQ helicase and XRN2 exoribonuclease cooperate in R-loop resolution.","authors":"J M Pan, H Betts, A Cubbon, L He, E L Bolt, P Soultanas","doi":"10.1098/rsob.240112","DOIUrl":"10.1098/rsob.240112","url":null,"abstract":"<p><p>The human HELQ helicase is a superfamily 2, 3'-5 helicase homologous to POLQ and RNA helicases of the Ski2-like subfamily. It is involved in diverse aspects of DNA repair and is an emerging prognosis biomarker and novel drug target for cancer therapy. HELQ interacts with RPA through its inherently disordered N-HELQ domain and hence is recruited to RPA-bound DNA substrates. Our study reveals a novel role for HELQ in R-loop resolution. We show in cells and <i>in vitro</i> that HELQ is recruited by RPA at R-loops, which are then resolved if HELQ is catalytically active as an ATPase/helicase. Furthermore, we identify a functional interaction of HELQ with XRN2, a nuclear 5' to 3' exoribonuclease, which we suggest coordinates R-loop unwinding by HELQ with RNA digestion by XRN2. Collectively, we assign a new biological function for HELQ in genome stability in metazoans through its involvement with XRN2 in R-loop metabolism.</p>","PeriodicalId":19629,"journal":{"name":"Open Biology","volume":"15 2","pages":"240112"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11835494/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143449642","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}
Open BiologyPub Date : 2025-02-01Epub Date: 2025-02-05DOI: 10.1098/rsob.240239
Maura Rojas-Pirela, Diego Andrade-Alviárez, Verónica Rojas, Miguel Marcos, Daniel Salete-Granado, Marirene Chacón-Arnaude, María Á Pérez-Nieto, Ulrike Kemmerling, Juan Luis Concepción, Paul A M Michels, Wilfredo Quiñones
{"title":"Exploring glycolytic enzymes in disease: potential biomarkers and therapeutic targets in neurodegeneration, cancer and parasitic infections.","authors":"Maura Rojas-Pirela, Diego Andrade-Alviárez, Verónica Rojas, Miguel Marcos, Daniel Salete-Granado, Marirene Chacón-Arnaude, María Á Pérez-Nieto, Ulrike Kemmerling, Juan Luis Concepción, Paul A M Michels, Wilfredo Quiñones","doi":"10.1098/rsob.240239","DOIUrl":"10.1098/rsob.240239","url":null,"abstract":"<p><p>Glycolysis, present in most organisms, is evolutionarily one of the oldest metabolic pathways. It has great relevance at a physiological level because it is responsible for generating ATP in the cell through the conversion of glucose into pyruvate and reducing nicotinamide adenine dinucleotide (NADH) (that may be fed into the electron chain in the mitochondria to produce additional ATP by oxidative phosphorylation), as well as for producing intermediates that can serve as substrates for other metabolic processes. Glycolysis takes place through 10 consecutive chemical reactions, each of which is catalysed by a specific enzyme. Although energy transduction by glucose metabolism is the main function of this pathway, involvement in virulence, growth, pathogen-host interactions, immunomodulation and adaptation to environmental conditions are other functions attributed to this metabolic pathway. In humans, where glycolysis occurs mainly in the cytosol, the mislocalization of some glycolytic enzymes in various other subcellular locations, as well as alterations in their expression and regulation, has been associated with the development and progression of various diseases. In this review, we describe the role of glycolytic enzymes in the pathogenesis of diseases of clinical interest. In addition, the potential role of these enzymes as targets for drug development and their potential for use as diagnostic and prognostic markers of some pathologies are also discussed.</p>","PeriodicalId":19629,"journal":{"name":"Open Biology","volume":"15 2","pages":"240239"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11793985/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143189431","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 high-throughput protein tagging toolkit that retains endogenous untranslated regions for studying gene regulation in kinetoplastids.","authors":"Carla Gilabert Carbajo, Xiaoyang Han, Bhairavi Savur, Arushi Upadhyaya, Fatima Taha, Michele Tinti, Richard J Wheeler, Phillip A Yates, Calvin Tiengwe","doi":"10.1098/rsob.240334","DOIUrl":"10.1098/rsob.240334","url":null,"abstract":"<p><p>Kinetoplastid parasites cause diseases that threaten human and animal health. To survive transitions between vertebrate hosts and insect vectors, these parasites rely on precise regulation of gene expression to adapt to environmental changes. Since gene regulation in kinetoplastids is primarily post-transcriptional, developing efficient genetic tools for modifying genes at their endogenous loci while preserving regulatory mRNA elements is crucial for studying their complex biology. We present a CRISPR/Cas9-based tagging system that preserves untranslated regulatory elements and uses a viral 2A peptide from <i>Thosea asigna</i> to generate two separate proteins from a single transcript: a drug-selectable marker and a tagged protein of interest. This dual-function design maintains native control elements, allowing discrimination between regulation of transcript abundance, translational efficiency, and post-translational events. We validate the system by tagging six <i>Trypanosoma brucei</i> proteins and demonstrate (i) high-efficiency positive selection and separation of drug-selectable marker and target protein, (ii) preservation of regulatory responses to environmental cues like heat shock and iron availability, and (iii) maintenance of stage-specific regulation during developmental transitions. This versatile toolkit is applicable to all kinetoplastids amenable to CRISPR/Cas9 editing, providing a powerful reverse genetic tool for studying post-transcriptional regulation and protein function in organisms where post-transcriptional control is dominant.</p>","PeriodicalId":19629,"journal":{"name":"Open Biology","volume":"15 2","pages":"240334"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11858757/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143502564","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}
Open BiologyPub Date : 2025-02-01Epub Date: 2025-02-19DOI: 10.1098/rsob.240229
Karen Baker, Tara A Eastwood, Esther Garcia, Chris Lennon, Daniel P Mulvihill
{"title":"Simple recombinant monoclonal antibody production from <i>Escherichia coli</i>.","authors":"Karen Baker, Tara A Eastwood, Esther Garcia, Chris Lennon, Daniel P Mulvihill","doi":"10.1098/rsob.240229","DOIUrl":"10.1098/rsob.240229","url":null,"abstract":"<p><p>Antibodies are valuable biological reagents used in a wide range of discovery research, biotechnology, diagnostic and therapeutic applications. Currently, both commercial and laboratory-scale antibody production is reliant on expression from mammalian cells, which can be time-consuming and requires the use of specialist facilities and costly growth reagents. Here, we describe a simple, rapid and cheap method for producing and isolating functional monoclonal antibodies and antibody fragments from bacterial cells that can be used in a range of laboratory applications. This simple method only requires access to basic microbial cell culture and molecular biology equipment, making scalable in-house antibody production accessible to the global diagnostics, therapeutics and molecular bioscience research communities.</p>","PeriodicalId":19629,"journal":{"name":"Open Biology","volume":"15 2","pages":"240229"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11835484/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143449634","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":"AGS3-based optogenetic GDI induces GPCR-independent Gβγ signalling and macrophage migration.","authors":"Waruna Thotamune, Sithurandi Ubeysinghe, Chathuri Rajarathna, Dinesh Kankanamge, Koshala Olupothage, Aditya Chandu, Bryan A Copits, Ajith Karunarathne","doi":"10.1098/rsob.240181","DOIUrl":"10.1098/rsob.240181","url":null,"abstract":"<p><p>G-protein-coupled receptors (GPCRs) are efficient guanine nucleotide exchange factors (GEFs) and exchange GDP to GTP on the Gα subunit of G-protein heterotrimers in response to various extracellular stimuli, including neurotransmitters and light. GPCRs primarily broadcast signals through activated G proteins, GαGTP and free Gβγ and are major disease drivers. Evidence shows that the ambient low threshold signalling required for cells is likely supplemented by signalling regulators such as non-GPCR GEFs and guanine nucleotide dissociation inhibitors (GDIs). Activators of G-protein signalling 3 (AGS3) are recognized as a GDI involved in multiple health and disease-related processes. Nevertheless, understanding of AGS3 is limited, and no significant information is available on its structure-function relationship or signalling regulation in living cells. Here, we employed <i>in silico</i> structure-guided engineering of a novel optogenetic GDI, based on the AGS3's G-protein regulatory motif, to understand its GDI activity and induce standalone Gβγ signalling in living cells on optical command. Our results demonstrate that plasma membrane recruitment of OptoGDI efficiently releases Gβγ, and its subcellular targeting generated localized PIP3 and triggered macrophage migration. Therefore, we propose OptoGDI as a powerful tool for optically dissecting GDI-mediated signalling pathways and triggering GPCR-independent Gβγ signalling in cells and <i>in vivo</i>.</p>","PeriodicalId":19629,"journal":{"name":"Open Biology","volume":"15 2","pages":"240181"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11793977/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143189038","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}
Open BiologyPub Date : 2025-02-01Epub Date: 2025-02-19DOI: 10.1098/rsob.240183
Victoria Sanchez-Martin, Dusan Ruzic, Maria J Tello-Lopez, Andrea Ortiz-Morales, Javier Murciano-Calles, Miguel Soriano, Katarina Nikolic, Jose Antonio Garcia-Salcedo
{"title":"The histone deacetylase inhibitor Scriptaid targets G-quadruplexes.","authors":"Victoria Sanchez-Martin, Dusan Ruzic, Maria J Tello-Lopez, Andrea Ortiz-Morales, Javier Murciano-Calles, Miguel Soriano, Katarina Nikolic, Jose Antonio Garcia-Salcedo","doi":"10.1098/rsob.240183","DOIUrl":"10.1098/rsob.240183","url":null,"abstract":"<p><p>Scriptaid is a chemical compound with anti-tumoural effects due to its role as a histone deacetylase inhibitor. Despite sharing part of the chemical structure with other ligands of G-quadruplexes (G4s), the interaction of Scriptaid with G4s has not been explored before. We synthesized Scriptaid and screened its cytotoxic activity in cellular models of colorectal cancer (CRC). We extensively evaluated its biological activity by cell cycle, immunofluorescence, qRT-PCR and Western blot experiments. To identify the G4 targets of Scriptaid, we conducted a panel of binding assays. Here, we show that Scriptaid induced cytotoxicity, cell cycle arrest and nucleolar stress in CRC cells. Moreover, Scriptaid impaired RNA polymerase I (Pol I) transcription, stabilized G4s and caused DNA damage. Finally, we disclose that these effects were attributable to the binding of Scriptaid to G4s in ribosomal DNA. In conclusion, our work reveals that a primary impact of Scriptaid on human cells is the interaction with G4s.</p>","PeriodicalId":19629,"journal":{"name":"Open Biology","volume":"15 2","pages":"240183"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11835489/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143449639","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}
Open BiologyPub Date : 2025-02-01Epub Date: 2025-02-26DOI: 10.1098/rsob.240267
Anna Frappaolo, Gianluca Zaccagnini, Maria Giovanna Riparbelli, Gianni Colotti, Giuliano Callaini, Maria Grazia Giansanti
{"title":"PACS deficiency disrupts Golgi architecture and causes cytokinesis failures and seizure-like phenotype in <i>Drosophila melanogaster</i>.","authors":"Anna Frappaolo, Gianluca Zaccagnini, Maria Giovanna Riparbelli, Gianni Colotti, Giuliano Callaini, Maria Grazia Giansanti","doi":"10.1098/rsob.240267","DOIUrl":"10.1098/rsob.240267","url":null,"abstract":"<p><p>The PACS (phosphofurin acidic cluster sorting protein) proteins are membrane trafficking regulators, required for maintaining cellular homeostasis and preventing disease states. Mutations in human <i>PACS1</i> and <i>PACS2</i> cause human neurodevelopmental disorders, characterized by epileptic seizures and neurodevelopmental delay. In vertebrates, functional analysis of PACS proteins is complicated by the presence of two paralogues which can compensate for the loss of each other. Here, we characterize the unique fly homologue of human PACS proteins. We demonstrate that Drosophila PACS (dPACS) is required for cell division in dividing spermatocytes and neuroblasts. In primary spermatocytes, dPACS colocalizes with GOLPH3 at the Golgi stacks and is essential for maintaining Golgi architecture. In dividing cells, dPACS is necessary for central spindle stability and contractile ring constriction. dPACS and GOLPH3 proteins form a complex and are mutually dependent for localization to the cleavage site. We propose that dPACS, by associating with GOLPH3, mediates the flow of vesicle trafficking that supports furrow ingression during cytokinesis. Furthermore, loss of dPACS leads to defects in tubulin acetylation and severe bang sensitivity, a phenotype associated with seizures in flies. Together our findings suggest that a Drosophila <i>PACS</i> disease model may contribute to understanding the molecular mechanisms underpinning human PACS syndromes.</p>","PeriodicalId":19629,"journal":{"name":"Open Biology","volume":"15 2","pages":"240267"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11858789/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143502918","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}
Open BiologyPub Date : 2025-02-01Epub Date: 2025-02-26DOI: 10.1098/rsob.240258
Vladimir Mushenkov, Ksenia Zhigalova, Pavel Denisov, Alexey Gordeev, Dmitry Lukyanov, Vladimir Kukushkin, Tatiana Priputnevich, Elena Zavyalova
{"title":"Rapid Raman spectroscopy-based test for antimicrobial resistance.","authors":"Vladimir Mushenkov, Ksenia Zhigalova, Pavel Denisov, Alexey Gordeev, Dmitry Lukyanov, Vladimir Kukushkin, Tatiana Priputnevich, Elena Zavyalova","doi":"10.1098/rsob.240258","DOIUrl":"10.1098/rsob.240258","url":null,"abstract":"<p><p>Antimicrobial resistance (AMR) is one of the top global health threats. In 2019, AMR was associated with 4.95 million deaths, of which 1.97 million were caused by drug-resistant infections directly. The main subset of AMR is antibiotic resistance, that is, the resistance of bacteria to antibiotic treatment. Traditional and most commonly used antibiotic susceptibility tests are based on the detection of bacterial growth and its inhibition in the presence of an antimicrobial. These tests typically take over 1-2 days to perform, so empirical therapy schemes are often administered before proper testing. Rapid tests for AMR are necessary to optimize the treatment of bacterial infection. Here, we combine the MTT test with Raman spectroscopy to provide a 1.5 h long test for minimal inhibitory concentration determination. Several <i>Escherichia coli</i> and <i>Klebsiella pneumoniae</i> strains were tested with three types of antibiotics, including ampicillin from penicillin family, kanamycin from aminoglycoside family and levofloxacin from fluoroquinolone family. The test provided the same minimal inhibitory concentrations as traditional Etest confirming its robustness.</p>","PeriodicalId":19629,"journal":{"name":"Open Biology","volume":"15 2","pages":"240258"},"PeriodicalIF":4.5,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11858750/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143502987","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}