Biochimica et biophysica acta. Molecular cell research最新文献

{"title":"Intracellular calcium-induced ROS generation promotes squaraine phototoxicity","authors":"Giorgia Chinigò ,&nbsp;Carlotta Pontremoli ,&nbsp;Francesca Bianco ,&nbsp;Alessandra Gilardino ,&nbsp;Maria Jesus Moran Plata ,&nbsp;Alessia Brossa ,&nbsp;Benedetta Bussolati ,&nbsp;Sonja Visentin ,&nbsp;Nadia Barbero ,&nbsp;Alessandra Fiorio Pla","doi":"10.1016/j.bbamcr.2025.120055","DOIUrl":"10.1016/j.bbamcr.2025.120055","url":null,"abstract":"<div><div>Photodynamic therapy (PDT) is a minimally invasive therapeutic modality approved by the Food and Drug Administration (FDA) for the treatment of several pathological conditions, including cancer. Developing new photosensitizers (PSs) for PDT is of great interest to increase the treatment efficacy while minimizing side effects. In this regard, a better understanding of the signal transduction triggered by PS photo-activation may help to optimize PS efficacy.</div><div>In the present work, we synthesized a series of squaraines (SQs) featuring different indolenine ring modifications. Our results show that unsubstituted SQ has significant phototoxic activity, further increased by the introduction of a bromine in the indolenine ring (Br-SQ-C4) as well as the replacement of the squaryl oxygen atoms with sulfur atoms (SQ-S-C4). Phototoxicity positively correlates with higher photo-induced cytoplasmic Ca²⁺ signals as well as reactive oxygen species (ROS) generation. However, the different substituents strongly affect the signaling pathway triggered. The bromine substituent strengthens the localization of the dye in the endoplasmic reticulum (ER), while the sulfur substituent shifts its preferential localization to the mitochondria. Consistently, photo-activation of Br-SQ-C4 induces a larger ER Ca²⁺ release followed by SOCE, which fuels secondary ROS generation able to sustain a remarkable mitochondrial Ca²⁺ uptake and subsequent mitochondrial ROS generation. On the other hand, SQ-S-C4 can induce, already at the basal level, a greater perturbation of the Ca²⁺/ROS dynamics.</div><div>Overall, our results contribute to a deeper understanding of the intracellular signaling triggered by SQs, paving the way for the development of novel strategies aimed at increasing PDT efficacy.</div></div>","PeriodicalId":8754,"journal":{"name":"Biochimica et biophysica acta. Molecular cell research","volume":"1872 8","pages":"Article 120055"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144940718","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"E3 ligase SMURF2 alleviated intrauterine adhesion by stabilizing SMAD6","authors":"Ke Zhou ,&nbsp;Yun Chen ,&nbsp;Lishi Chen ,&nbsp;Zhenfu Wu ,&nbsp;Lirong Zhang ,&nbsp;Jingjing Zheng ,&nbsp;Song Tian ,&nbsp;Mingzhu Wen ,&nbsp;Xin Li ,&nbsp;Huihua Cai","doi":"10.1016/j.bbamcr.2025.120045","DOIUrl":"10.1016/j.bbamcr.2025.120045","url":null,"abstract":"<div><div>Intrauterine adhesion (IUA) is a debilitating uterine disorder characterized by endometrial fibrosis and infertility, for which effective treatments remain limited. Here, we identify the E3 ubiquitin ligase SMURF2 as a critical protective factor against IUA progression. SMURF2 expression was significantly upregulated in endometrial tissues of IUA patients, a murine IUA model, and TGF-β1-treated human endometrial stromal cells (HESCs). Functional analyses revealed that SMURF2 overexpression mitigated fibrosis-associated phenotypes, including enhanced cell proliferation, migration, and extracellular matrix accumulation, both <em>in vitro</em> and <em>in vivo</em>, whereas SMURF2 knockdown had the opposite effect. Mechanistically, SMURF2 directly interacted with the inhibitory SMAD protein SMAD6 and promoted its stabilization via K63-linked polyubiquitination. Mutation analysis confirmed that disruption of the K63 linkage markedly reduced SMAD6 ubiquitination and destabilized the protein. As a result, SMAD6 accumulation suppressed TGF-β/Smad signaling and downstream fibrotic gene expression. These findings reveal a previously unrecognized SMURF2–SMAD6 axis that counteracts endometrial fibrosis, and suggest that enhancing SMURF2-mediated K63-linked ubiquitination may offer a novel therapeutic avenue for IUA treatment.</div></div>","PeriodicalId":8754,"journal":{"name":"Biochimica et biophysica acta. Molecular cell research","volume":"1872 8","pages":"Article 120045"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144871190","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Loss of Prominin 2 expression inhibits AKT/mTOR signaling to limit glycolysis and drive ferroptosis in breast cancer cells","authors":"Lei Yin ,&nbsp;Yanze Lin ,&nbsp;Zhongdian Yuan ,&nbsp;Rexiati Ruze ,&nbsp;Zhen Yang ,&nbsp;Yingmei Shao","doi":"10.1016/j.bbamcr.2025.120047","DOIUrl":"10.1016/j.bbamcr.2025.120047","url":null,"abstract":"<div><div>This study aimed to characterize the oncogenic functions of Prominin 2 (<em>PROM2</em>), the pro-cancer and ferroptosis resistance gene, in breast cancer (BC). <em>PROM2</em> expression was analyzed using single-cell RNA sequencing and the TCGA database. Its expression was confirmed in BC tissues and cell lines using qRT-PCR, immunohistochemistry, and western blot assays. The effects of <em>PROM2</em> were evaluated <em>in vivo</em> and <em>in vitro</em>. RNA sequencing and GSEA were used to investigate the potential underlying molecular mechanisms of <em>PROM2</em> in BC. Co-immunoprecipitation was used to determine the interaction between AKT and PROM2. <em>PROM2</em> expression was elevated in clinical samples and BC cells and positively correlated with a worse prognosis. Functional experiments demonstrated that <em>PROM2</em> silencing suppressed tumor growth and malignancy. Mechanistically, PROM2 interacts with AKT to activate mTOR signaling, thereby promoting glycolysis and inhibiting ferroptosis. Specifically, for glycolysis, <em>PROM2</em> silencing decreased glucose uptake, extracellular acidification rate, lactate production, and glycolysis-related enzyme expression, while increasing oxygen consumption. For ferroptosis, <em>PROM2</em> silencing upregulated reactive oxygen species, malondialdehyde, iron, Fe²⁺, and downregulated SLC7A11, GPX4, and glutathione levels. Overexpression of AKT or the AKT agonist (SC79) reversed the effects of <em>PROM2</em> silencing on BC cell glycolysis and ferroptosis. Our results suggest that <em>PROM2</em> is an oncogenic gene that supports BC progression by enhancing glycolysis and inhibiting ferroptosis <em>via</em> AKT/mTOR signaling. Therefore, <em>PROM2</em> may be a potential therapeutic target for BC treatment.</div></div>","PeriodicalId":8754,"journal":{"name":"Biochimica et biophysica acta. Molecular cell research","volume":"1872 8","pages":"Article 120047"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144862092","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Calcium-dependent regulation of physiological vs pathological cardiomyocyte hypertrophy","authors":"Joshua Chung ,&nbsp;Nathan Isles ,&nbsp;Stuart Johnston ,&nbsp;David J. Collins ,&nbsp;Julie R. McMullen ,&nbsp;H. Llewelyn Roderick ,&nbsp;Vijay Rajagopal","doi":"10.1016/j.bbamcr.2025.120046","DOIUrl":"10.1016/j.bbamcr.2025.120046","url":null,"abstract":"<div><div>Cardiomyocyte hypertrophic growth contributes to the adaptative response of the heart to meet sustained increases in hemodynamic demand. While hypertrophic responses to physiological cues maintains or enhances cardiac function, when triggered by pathological cues, this response is maladaptive, associated with compromised heart function, although initially, this response maybe adaptive with preserved function. Since cues and activated pathways associated with both forms of hypertrophy overlap, the question arises as to the mechanism that determines these different outcomes. Here we evaluate the hypothesis that cardiomyocyte Ca²⁺ signalling – a regulator of pathological hypertrophy – also signals physiological hypertrophy. We discuss how different Ca²⁺ profiles, in distinct subcellular organelles/microdomains, and interacting with other signalling pathways, provide a mechanism for Ca²⁺ to be decoded to induce distinct hypertrophic phenotypes. We discuss how integration of computational with rich structural and functional cellular measurements can be used to decipher the role of Ca²⁺ in hypertrophic gene programming.</div></div>","PeriodicalId":8754,"journal":{"name":"Biochimica et biophysica acta. Molecular cell research","volume":"1872 8","pages":"Article 120046"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144871189","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"SYT13: An underestimated synaptotagmin","authors":"Johannes Lehmann ,&nbsp;Alberto Catanese","doi":"10.1016/j.bbamcr.2025.120031","DOIUrl":"10.1016/j.bbamcr.2025.120031","url":null,"abstract":"<div><div>Synaptotagmin-13 (SYT13) is a non-canonical member of the of synaptotagmin family that, canonical synaptotagmins, doesn't contain Ca²⁺ binding sites, but still appears to play a key role in the control of different cellular processes such as vesicle transport, cell migration, signaling and cell development. The recent findings associate SYT13 with neuronal survival and development, metabolic homeostasis (especially insulin secretion) and both oncogenic and tumor suppressive function in multiple cancers. And yet all this data is scattered in fields, with no systematic review covering SYT13's detailed biology. A comprehensive literature review is therefore needed to explain SYT13's multifaceted roles, uncover informational gaps and direct future studies to exploit SYT13 as a target for neurodegeneration, metabolic disease and cancer therapy.</div></div>","PeriodicalId":8754,"journal":{"name":"Biochimica et biophysica acta. Molecular cell research","volume":"1872 8","pages":"Article 120031"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144749493","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Heat shock protein 70 regulates m6A modification in response to heat shock in esophageal squamous cell carcinoma.","authors":"Bin Du, Jia Wang, Jun Ma, Pu Wang","doi":"10.1016/j.bbamcr.2025.120027","DOIUrl":"10.1016/j.bbamcr.2025.120027","url":null,"abstract":"<p><p>Heat shock has been known to induce hyperplasia in esophageal epithelial cells. It is widely considered as a crucial risk factor in the initiation and development of esophageal squamous cell carcinoma (ESCC), yet our understanding of the underlying mechanisms remains limited. The m6A modification of mRNA plays a role in mediating several cellular processes and is critical during cell stress. Our study revealed that inhibiting of m6A 'writer' components of ESCC cells exhibit higher death rates and slower recovery after heat shock. After normalization using mRNA expression profiles, 91.08 % of significantly changed m6A modifications aligned with corresponding mRNA abundance changes, with no evidence of over-modification, while the increase in m6A modification of 8.92 % of heat-shock associated genes far exceeded the increase in mRNA (hyper - m6A modification), and A/U rich motifs were commonly observed in the 3'UTR of these gene. Inside the nucleus, the binding of HSP70s in m6A writer complex promote the hyper - m6A modification in specific mRNAs after heat shock. The stronger nuclear localization of HSP70 in ESCC tissues correlates with a poor prognosis for the patients. In conclusion, our research revealed that the nuclear HSP70 protein could bind to the METTL3/14 writer complex and regulate mRNA's m6A modification. Our results provide a new perspective for research into how HSP70 protein regulates mRNA stability and suggests a new direction for the comprehensive prevention and treatment of ESCC.</p>","PeriodicalId":8754,"journal":{"name":"Biochimica et biophysica acta. Molecular cell research","volume":" ","pages":"120027"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144717300","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"TXNIP promotes ferroptosis through NCOA4 mediated ferritinophagy","authors":"Pandian Nagakannan ,&nbsp;Md Imamul Islam ,&nbsp;Shakila Sultana ,&nbsp;Soheila Karimi-Abdolrezaee ,&nbsp;Eftekhar Eftekharpour","doi":"10.1016/j.bbamcr.2025.120054","DOIUrl":"10.1016/j.bbamcr.2025.120054","url":null,"abstract":"<div><div>Ferroptosis is a recently discovered lytic form of cell death that is triggered by iron-driven excessive lipid peroxidation and depletion of glutathione and glutathione peroxidase-4 (GPX4). This form of cell death has been linked to a wide range of conditions from cancer to neurodegenerative diseases. Using murine hippocampal HT22 neurons, we aimed to investigate the underlying mechanisms of glutamate-mediated ferroptosis. A robust increase in Thioredoxin-Inhibiting Protein (TXNIP) prompted us to use genetic approaches and examine the role of this protein in ferroptosis in HT22 neurons, mouse embryonic fibroblasts, and Hela cells. Our results indicate that TXNIP is a key player in ferroptotic pathway, as its deletion conferred resistance to classic ferroptosis-inducing agents (erastin, RSL3, and ML210), while TXNIP overexpression increased their susceptibility to ferroptosis. Notably, TXNIP deletion protected cells from mitochondrial dysfunction induced by ferroptotic agents, independent of GSH and GPX4 levels. We further showed that TXNIP mediates ferroptosis through facilitating degradation of the iron-binding protein ferritin via NCOA4-mediated ferritinophagy. This resulted in elevated cytosolic labile iron levels, therefore amplifying lipid peroxidation, and promoting ferroptosis. Our findings suggest that TXNIP acts as a positive regulator of ferroptosis by modulating autophagy and iron availability. Targeting TXNIP might hold promise in developing drugs for diseases involving the ferroptotic pathway.</div></div>","PeriodicalId":8754,"journal":{"name":"Biochimica et biophysica acta. Molecular cell research","volume":"1872 8","pages":"Article 120054"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145008201","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Hyperosmolarity-induced activation of PIEZO1 engages detrimental calcium/oxidative stress signaling and adaptive catalase response in renal inner medullary collecting duct (mIMCD3) cells","authors":"Stephanie Probst ,&nbsp;Nadiya Romanova ,&nbsp;Robin Herbrechter ,&nbsp;Teresa Kern ,&nbsp;Marie Bergmeier ,&nbsp;Wing-Kee Lee ,&nbsp;Frank Thévenod","doi":"10.1016/j.bbamcr.2025.120041","DOIUrl":"10.1016/j.bbamcr.2025.120041","url":null,"abstract":"<div><div>The collecting duct (CD) is the final segment of the renal nephron and is involved in the fine regulation of osmotic and ionic homeostasis. Its medullary segment is continuously exposed to a wide spectrum of osmotic gradients and resultant osmotic stress. Strikingly, the expression of the mechanically activated non-selective cationic and Ca²⁺-permeable transduction ion channel PIEZO1 is most prominent in inner medullary CD (IMCD) cells, yet its functions there are still not well understood. We hypothesized increased PIEZO1 expression in the IMCD could be linked to its hyperosmotic stress environment. Using the mouse mIMCD₃ cell line, which has been used to characterize hyperosmotic stress-induced cell death, we demonstrate twice as much PIEZO1 expression compared to proximal tubule (WKPT-0293 Cl.2) or cortical CD (mCCD(cl.1)) cell lines. Hyperosmolarity/−tonicity by addition of NaCl ± urea to the culture medium (+ 100–300 mosmol/l) or PIEZO1 agonist Yoda1 (20 μmol/l) decreased mIMCD₃ cell viability assayed by MTT, which were antagonized by PIEZO1 inhibitors GsMTx4 (2.5 μmol/l) and salvianolic acid (SalB, 10 μmol/l). PIEZO1 activation by hyperosmolarity and agonists (Yoda1, Jedi1) increased Ca²⁺ influx, downstream reactive oxygen species (ROS), in particular mitochondrial superoxide (O₂^•-) formation, and subsequent adaptive ROS-decomposing catalase expression and activity that were sensitive to PIEZO1 antagonists (GsMTx4, SalB). Hence, the data demonstrate hyperosmolarity/−tonicity of the kidney elicits PIEZO1 activation, mitochondrial ROS formation and cell death that are partially countered by catalase-mediated stress adaptation.</div></div>","PeriodicalId":8754,"journal":{"name":"Biochimica et biophysica acta. Molecular cell research","volume":"1872 8","pages":"Article 120041"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144803337","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Multiple roles of EML1 in microtubule stabilization and vesicle transport in the nervous system","authors":"Yufang Zhang ,&nbsp;Jing Yu ,&nbsp;Yao Zhou ,&nbsp;Yan Yue ,&nbsp;Yan Liu","doi":"10.1016/j.bbamcr.2025.120048","DOIUrl":"10.1016/j.bbamcr.2025.120048","url":null,"abstract":"<div><div>Microtubule-associated protein EML1 is an important member of the EML family and plays a key role in cytoskeleton regulation and neural development. During neural development, EML1 expression is spatiotemporally specific, and its functional abnormalities are closely associated with neural developmental disorders such as subcortical band heterotopia. This article systematically reviews the structural characteristics and biological functions of EML1. Structural studies have shown that EML1 contains unique HELP-WD and TAPE domains, which underlie its binding to microtubules and functional performance. Functionally, EML1 regulates microtubule stability through multiple mechanisms. Moreover, EML1 is also involved in regulating intracellular material transport—maintaining the stability of transport tracks, coordinating the function of motor proteins, and regulating Golgi-related transport. These findings reveal the multiple roles of EML1 in cellular physiological processes and provide a new perspective for understanding the pathogenesis of related diseases. Future research should focus on elucidating the precise EML1 action mechanisms and its potential as a therapeutic target.</div></div>","PeriodicalId":8754,"journal":{"name":"Biochimica et biophysica acta. Molecular cell research","volume":"1872 8","pages":"Article 120048"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144896506","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"S100A16 knockdown reduces RPN2 expression and inhibits β-catenin/TCF signaling, leading to suppressed metastasis in cervical cancer cells","authors":"Min-Chieh Hsin ,&nbsp;Po-Hui Wang ,&nbsp;Pei-Ni Chen ,&nbsp;Yi-Hsien Hsieh ,&nbsp;Shun-Fa Yang ,&nbsp;Chung-Yuan Lee","doi":"10.1016/j.bbamcr.2025.120053","DOIUrl":"10.1016/j.bbamcr.2025.120053","url":null,"abstract":"<div><div>S100 calcium-binding protein A16 (S100A16), the most recently identified member of the S100 calcium-binding protein family, has been implicated in various cancers. However, its specific role in cervical cancer remains unclear. In this study, we demonstrated that silencing the S100A16 gene inhibits the migratory ability of HeLa and SiHa cells without affecting their viability. RNA sequencing analysis revealed that S100A16 significantly regulates ribophorin II (RPN2). Furthermore, RPN2 knockdown alone effectively suppressed cell migration and overexpression of S100A16 reversed the inhibition of migration caused by RPN2 silencing. Mechanistically, S100A16 was observed to regulate RPN2 through phosphorylated signal transducer and activator of transcription 3 (p-STAT3), which, in turn, modulated the downstream β-catenin/TCF pathway via phosphorylated GSK3β. An analysis of nuclear and cytosolic protein fractions further indicated that S100A16 silencing reduces the ability of β-catenin to translocate into the nucleus. In conclusion, our research revealed that S100A16 silencing downregulated RPN2 levels through p-STAT3, thereby inhibiting the p-GSK3β/β-catenin/TCF signaling pathway. These findings highlight S100A16 as a potential therapeutic target for cervical cancer.</div></div>","PeriodicalId":8754,"journal":{"name":"Biochimica et biophysica acta. Molecular cell research","volume":"1872 8","pages":"Article 120053"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144988545","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}